Motif 1211 (n=603)
Position-wise Probabilities
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| uniprot | genes | site | source | protein | function |
|---|---|---|---|---|---|
| A0A0B4J1R7 | BORCS7-ASMT | T6 | ochoa | BLOC-1-related complex subunit 7 | None |
| A0A0C4DH35 | IGHV3-35 | S6 | ochoa | Probable non-functional immunoglobulin heavy variable 3-35 | Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin heavy chains (PubMed:24600447). Non-functional ORF generally cannot participate in the synthesis of a productive immunoglobulin chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) (PubMed:9619395). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447, ECO:0000303|PubMed:9619395}. |
| A1KXE4 | FAM168B | S6 | ochoa | Myelin-associated neurite-outgrowth inhibitor (Mani) (p20) | Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27. {ECO:0000250|UniProtKB:D4AEP3}. |
| A2A3N6 | PIPSL | Y7 | ochoa | Putative PIP5K1A and PSMD4-like protein (PIP5K1A-PSMD4) | Has negligible PIP5 kinase activity. Binds to ubiquitinated proteins. |
| A2RRP1 | NBAS | S6 | ochoa | NBAS subunit of NRZ tethering complex (Neuroblastoma-amplified gene protein) (Neuroblastoma-amplified sequence) | Involved in Golgi-to-endoplasmic reticulum (ER) retrograde transport; the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:19369418). Required for normal embryonic development (By similarity). May play a role in the nonsense-mediated decay pathway of mRNAs containing premature stop codons (By similarity). {ECO:0000250|UniProtKB:Q5TYW4, ECO:0000269|PubMed:19369418}. |
| A2RU30 | TESPA1 | S7 | ochoa | Protein TESPA1 (Thymocyte-expressed positive selection-associated protein 1) | Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development (By similarity). Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment. {ECO:0000250, ECO:0000269|PubMed:22561606}. |
| A6NDU8 | RIMOC1 | S7 | ochoa | RAB7A-interacting MON1-CCZ1 complex subunit 1 (UPF0600 protein C5orf51) | Plays an important role in the removal of damaged mitochondria via mitophagy by controlling the stability and localization of RAB7A. Required for the recruitment of RAB7A and ATG9A vesicles to damaged mitochondria and promotes the stability of RAB7A by inhibiting its proteasomal degradation during mitophagy. {ECO:0000269|PubMed:34432599}. |
| A6NFI3 | ZNF316 | T6 | ochoa | Zinc finger protein 316 | May be involved in transcriptional regulation. {ECO:0000250}. |
| A6NFI3 | ZNF316 | T7 | ochoa | Zinc finger protein 316 | May be involved in transcriptional regulation. {ECO:0000250}. |
| B2RU33 | POTEC | S7 | ochoa | POTE ankyrin domain family member C (ANKRD26-like family B member 2) (Prostate, ovary, testis-expressed protein on chromosome 18) (POTE-18) | None |
| B2RUZ4 | SMIM1 | S6 | ochoa | Small integral membrane protein 1 (Vel blood group antigen) | Regulator of red blood cell formation. {ECO:0000250|UniProtKB:B3DHH5}. |
| B4DJY2 | TMEM233 | S7 | ochoa | Transmembrane protein 233 (Dispanin subfamily B member 2) (DSPB2) (Interferon-induced transmembrane domain-containing protein D2) | Probable accessory protein of voltage-gated sodium channels. {ECO:0000269|PubMed:37117223}. |
| B5ME19 | EIF3CL | T6 | ochoa | Eukaryotic translation initiation factor 3 subunit C-like protein | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000250|UniProtKB:Q99613}. |
| B5ME19 | EIF3CL | T7 | ochoa | Eukaryotic translation initiation factor 3 subunit C-like protein | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000250|UniProtKB:Q99613}. |
| B8ZZF3 | None | S7 | ochoa | Mediator of RNA polymerase II transcription subunit 26 (Cofactor required for Sp1 transcriptional activation subunit 7) (Mediator complex subunit 26) | Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. {ECO:0000256|ARBA:ARBA00057523}. |
| C4P0D8 | TSNAX-DISC1 | S7 | ochoa | Disrupted in schizophrenia 1 isoform 51 (TSNAX-DISC1 readthrough (NMD candidate)) | None |
| C9JQL5 | None | T7 | ochoa | Putative dispanin subfamily A member 2d (DSPA2d) | None |
| D3W0D1 | KLRF2 | Y7 | psp | Killer cell lectin-like receptor subfamily F member 2 (Lectin-like receptor F2) (Activating coreceptor NKp65) | C-type lectin-like receptor involved in natural killer cell mediated cytotoxicity and cytokine secretion in keratinocytes via its interaction with CLEC2A (PubMed:20194751, PubMed:25510854). Triggers degranulation in a SYK-dependent manner and stimulates SYK phosphotyrosinylation without recruiting SYK directly (PubMed:28082678). {ECO:0000269|PubMed:20194751, ECO:0000269|PubMed:28082678}. |
| H3BRB1 | None | S6 | ochoa | polynucleotide adenylyltransferase (EC 2.7.7.19) | None |
| H7C1D1 | None | S7 | ochoa | DUF4657 domain-containing protein | None |
| M0R2N4 | None | S7 | ochoa | C3H1-type domain-containing protein | None |
| O00161 | SNAP23 | S6 | ochoa|psp | Synaptosomal-associated protein 23 (SNAP-23) (Vesicle-membrane fusion protein SNAP-23) | Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion. |
| O00178 | GTPBP1 | S6 | ochoa | GTP-binding protein 1 (G-protein 1) (GP-1) (GP1) | Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity). {ECO:0000250|UniProtKB:D2XV59}. |
| O00505 | KPNA3 | S6 | ochoa | Importin subunit alpha-4 (Importin alpha Q2) (Qip2) (Karyopherin subunit alpha-3) (SRP1-gamma) | Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. Recognizes NLSs of influenza A virus nucleoprotein probably through ARM repeats 7-9. |
| O00560 | SDCBP | S6 | ochoa|psp | Syntenin-1 (Melanoma differentiation-associated protein 9) (MDA-9) (Pro-TGF-alpha cytoplasmic domain-interacting protein 18) (TACIP18) (Scaffold protein Pbp1) (Syndecan-binding protein 1) | Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis (PubMed:26291527). Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1 (PubMed:25893292). In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis (PubMed:22660413). Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types (PubMed:26539120). In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA) (PubMed:11498591). May also play a role in vesicular trafficking (PubMed:11179419). Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway (PubMed:10230395). {ECO:0000269|PubMed:10230395, ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:11498591, ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:25893292, ECO:0000269|PubMed:26539120, ECO:0000303|PubMed:26291527}. |
| O14777 | NDC80 | S7 | psp | Kinetochore protein NDC80 homolog (Highly expressed in cancer protein) (Kinetochore protein Hec1) (HsHec1) (Kinetochore-associated protein 2) (Retinoblastoma-associated protein HEC) | Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:12351790, PubMed:14654001, PubMed:14699129, PubMed:15062103, PubMed:15235793, PubMed:15239953, PubMed:15548592, PubMed:16732327, PubMed:30409912, PubMed:9315664). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:15548592, PubMed:30409912). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020). Plays a role in chromosome congression and is essential for the end-on attachment of the kinetochores to spindle microtubules (PubMed:23891108, PubMed:25743205). {ECO:0000269|PubMed:12351790, ECO:0000269|PubMed:14654001, ECO:0000269|PubMed:14699129, ECO:0000269|PubMed:15062103, ECO:0000269|PubMed:15235793, ECO:0000269|PubMed:15239953, ECO:0000269|PubMed:15548592, ECO:0000269|PubMed:16732327, ECO:0000269|PubMed:23085020, ECO:0000269|PubMed:23891108, ECO:0000269|PubMed:25743205, ECO:0000269|PubMed:30409912, ECO:0000269|PubMed:9315664}. |
| O14976 | GAK | S6 | ochoa | Cyclin-G-associated kinase (EC 2.7.11.1) (DnaJ homolog subfamily C member 26) | Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1 (PubMed:10625686). May play a role in clathrin-mediated endocytosis and intracellular trafficking, and in the dynamics of clathrin assembly/disassembly (PubMed:18489706). {ECO:0000269|PubMed:10625686, ECO:0000269|PubMed:18489706}. |
| O14978 | ZNF263 | S7 | ochoa | Zinc finger protein 263 (Zinc finger protein FPM315) (Zinc finger protein with KRAB and SCAN domains 12) | Transcription factor that binds to the consensus sequence 5'-TCCTCCC-3' and acts as a transcriptional repressor (PubMed:32051553). Binds to the promoter region of SIX3 and recruits other proteins involved in chromatin modification and transcriptional corepression, resulting in methylation of the promoter and transcriptional repression (PubMed:32051553). Acts as a transcriptional repressor of HS3ST1 and HS3ST3A1 via binding to gene promoter regions (PubMed:32277030). {ECO:0000269|PubMed:32051553, ECO:0000269|PubMed:32277030}. |
| O15020 | SPTBN2 | S6 | ochoa | Spectrin beta chain, non-erythrocytic 2 (Beta-III spectrin) (Spinocerebellar ataxia 5 protein) | Probably plays an important role in neuronal membrane skeleton. |
| O15126 | SCAMP1 | S6 | ochoa | Secretory carrier-associated membrane protein 1 (Secretory carrier membrane protein 1) | Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface. |
| O15258 | RER1 | S6 | ochoa | Protein RER1 | Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment. {ECO:0000250}. |
| O15287 | FANCG | S7 | psp | Fanconi anemia group G protein (Protein FACG) (DNA repair protein XRCC9) | DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Candidate tumor suppressor gene. |
| O15541 | RNF113A | S6 | ochoa | E3 ubiquitin-protein ligase RNF113A (EC 2.3.2.27) (Cwc24 homolog) (RING finger protein 113A) (Zinc finger protein 183) | Required for pre-mRNA splicing as component of the spliceosome (PubMed:29360106, PubMed:29361316). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). E3 ubiquitin-protein ligase that catalyzes the transfer of ubiquitin onto target proteins (PubMed:28978524, PubMed:29144457). Catalyzes polyubiquitination of SNRNP200/BRR2 with non-canonical 'Lys-63'-linked polyubiquitin chains (PubMed:29144457). Plays a role in DNA repair via its role in the synthesis of 'Lys-63'-linked polyubiquitin chains that recruit ALKBH3 and the ASCC complex to sites of DNA damage by alkylating agents (PubMed:29144457). Ubiquitinates CXCR4, leading to its degradation, and thereby contributes to the termination of CXCR4 signaling (PubMed:28978524). {ECO:0000269|PubMed:28978524, ECO:0000269|PubMed:29144457, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000305|PubMed:33509932}. |
| O43242 | PSMD3 | S6 | psp | 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3) (26S proteasome regulatory subunit S3) (Proteasome subunit p58) | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000269|PubMed:1317798}. |
| O43251 | RBFOX2 | T7 | ochoa | RNA binding protein fox-1 homolog 2 (Fox-1 homolog B) (Hexaribonucleotide-binding protein 2) (RNA-binding motif protein 9) (RNA-binding protein 9) (Repressor of tamoxifen transcriptional activity) | RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis (By similarity). RNA-binding protein that seems to act as a coregulatory factor of ER-alpha. Together with RNA binding proteins RBPMS and MBNL1/2, activates vascular smooth muscle cells alternative splicing events (PubMed:37548402). {ECO:0000250, ECO:0000269|PubMed:11875103, ECO:0000269|PubMed:37548402}. |
| O43252 | PAPSS1 | S6 | ochoa | Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 (PAPS synthase 1) (PAPSS 1) (Sulfurylase kinase 1) (SK 1) (SK1) [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (3'-phosphoadenosine-5'-phosphosulfate synthase) (APS kinase) (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenylylsulfate 3'-phosphotransferase)] | Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway (PubMed:14747722, PubMed:9576487, PubMed:9648242, PubMed:9668121). Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells (PubMed:9576487). {ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242, ECO:0000269|PubMed:9668121}. |
| O43255 | SIAH2 | S6 | ochoa|psp | E3 ubiquitin-protein ligase SIAH2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH2) (Seven in absentia homolog 2) (Siah-2) (hSiah2) | E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:11483518, PubMed:19224863, PubMed:9334332). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:11483518, PubMed:19224863, PubMed:9334332). Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes (PubMed:11483518, PubMed:19224863, PubMed:9334332). Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP) (PubMed:11483518, PubMed:19224863, PubMed:9334332). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia (PubMed:22878263). It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes (PubMed:11483518, PubMed:19224863, PubMed:22878263, PubMed:9334332). Has some overlapping function with SIAH1 (PubMed:11483518, PubMed:19224863, PubMed:9334332). Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not (PubMed:12411493). Promotes monoubiquitination of SNCA (PubMed:19224863). Regulates cellular clock function via ubiquitination of the circadian transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal degradation (PubMed:26392558). Plays an important role in mediating the rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their circadian profile of protein abundance (PubMed:26392558). Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1. {ECO:0000250|UniProtKB:Q06986, ECO:0000269|PubMed:11483518, ECO:0000269|PubMed:12411493, ECO:0000269|PubMed:19224863, ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:26392558, ECO:0000269|PubMed:28546513, ECO:0000269|PubMed:9334332}. |
| O43255 | SIAH2 | T7 | ochoa | E3 ubiquitin-protein ligase SIAH2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH2) (Seven in absentia homolog 2) (Siah-2) (hSiah2) | E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:11483518, PubMed:19224863, PubMed:9334332). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:11483518, PubMed:19224863, PubMed:9334332). Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes (PubMed:11483518, PubMed:19224863, PubMed:9334332). Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP) (PubMed:11483518, PubMed:19224863, PubMed:9334332). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia (PubMed:22878263). It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes (PubMed:11483518, PubMed:19224863, PubMed:22878263, PubMed:9334332). Has some overlapping function with SIAH1 (PubMed:11483518, PubMed:19224863, PubMed:9334332). Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not (PubMed:12411493). Promotes monoubiquitination of SNCA (PubMed:19224863). Regulates cellular clock function via ubiquitination of the circadian transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal degradation (PubMed:26392558). Plays an important role in mediating the rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their circadian profile of protein abundance (PubMed:26392558). Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1. {ECO:0000250|UniProtKB:Q06986, ECO:0000269|PubMed:11483518, ECO:0000269|PubMed:12411493, ECO:0000269|PubMed:19224863, ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:26392558, ECO:0000269|PubMed:28546513, ECO:0000269|PubMed:9334332}. |
| O43379 | WDR62 | S6 | ochoa | WD repeat-containing protein 62 | Required for cerebral cortical development. Plays a role in neuronal proliferation and migration (PubMed:20729831, PubMed:20890278). Plays a role in mother-centriole-dependent centriole duplication; the function also seems to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:26297806}. |
| O43447 | PPIH | S6 | ochoa | Peptidyl-prolyl cis-trans isomerase H (PPIase H) (EC 5.2.1.8) (Rotamase H) (Small nuclear ribonucleoprotein particle-specific cyclophilin H) (CypH) (U-snRNP-associated cyclophilin SnuCyp-20) (USA-CYP) | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. {ECO:0000269|PubMed:11823439, ECO:0000269|PubMed:12875835, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:9570313}. |
| O43447 | PPIH | S7 | ochoa | Peptidyl-prolyl cis-trans isomerase H (PPIase H) (EC 5.2.1.8) (Rotamase H) (Small nuclear ribonucleoprotein particle-specific cyclophilin H) (CypH) (U-snRNP-associated cyclophilin SnuCyp-20) (USA-CYP) | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. {ECO:0000269|PubMed:11823439, ECO:0000269|PubMed:12875835, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:9570313}. |
| O43491 | EPB41L2 | S7 | 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}. |
| O43524 | FOXO3 | S7 | ochoa|psp | Forkhead box protein O3 (AF6q21 protein) (Forkhead in rhabdomyosarcoma-like 1) | Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302). {ECO:0000250|UniProtKB:Q9WVH4, ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:30513302}. |
| O43583 | DENR | S6 | ochoa | Density-regulated protein (DRP) (Protein DRP1) (Smooth muscle cell-associated protein 3) (SMAP-3) | Translation regulator forming a complex with MCTS1 to promote translation reinitiation. Translation reinitiation is the process where the small ribosomal subunit remains attached to the mRNA following termination of translation of a regulatory upstream ORF (uORF), and resume scanning on the same mRNA molecule to initiate translation of a downstream ORF, usually the main ORF (mORF). The MCTS1/DENR complex is pivotal to two linked mechanisms essential for translation reinitiation. Firstly, the dissociation of deacylated tRNAs from post-termination 40S ribosomal complexes during ribosome recycling. Secondly, the recruitment in an EIF2-independent manner of aminoacylated initiator tRNA to P site of 40S ribosomes for a new round of translation. This regulatory mechanism governs the translation of more than 150 genes which translation reinitiation is MCTS1/DENR complex-dependent. {ECO:0000269|PubMed:16982740, ECO:0000269|PubMed:20713520, ECO:0000269|PubMed:37875108}. |
| O43597 | SPRY2 | S7 | psp | Protein sprouty homolog 2 (Spry-2) | Antagonist of fibroblast growth factor (FGF) pathways via inhibition of FGF-mediated phosphorylation of ERK1/2 (By similarity). Thereby acts as an antagonist of FGF-induced retinal lens fiber differentiation, may inhibit limb bud outgrowth and may negatively modulate respiratory organogenesis (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in retinal lens epithelial cells (By similarity). Inhibits CBL/C-CBL-mediated EGFR ubiquitination (PubMed:17974561). {ECO:0000250|UniProtKB:Q9QXV8, ECO:0000269|PubMed:17974561}. |
| O43711 | TLX3 | S6 | ochoa | T-cell leukemia homeobox protein 3 (Homeobox protein Hox-11L2) | None |
| O43760 | SYNGR2 | Y6 | ochoa | Synaptogyrin-2 (Cellugyrin) | May play a role in regulated exocytosis. In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles. May also play a role in GLUT4 storage and transport to the plasma membrane. {ECO:0000250|UniProtKB:O54980}.; FUNCTION: (Microbial infection) May play a role in the assembly of cytoplasmic inclusion bodies required for SFTS phlebovirus replication. {ECO:0000269|PubMed:27226560}. |
| O43791 | SPOP | S6 | ochoa|psp | Speckle-type POZ protein (HIB homolog 1) (Roadkill homolog 1) | Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of MACROH2A1 and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL. Involved in the regulation of bromodomain and extra-terminal motif (BET) proteins BRD2, BRD3, BRD4 stability (PubMed:32109420). Plays an essential role for proper translation, but not for their degradation, of critical DNA replication licensing factors CDT1 and CDC6, thereby participating in DNA synthesis and cell proliferation (PubMed:36791496). Regulates interferon regulatory factor 1/IRF1 proteasomal turnover by targeting S/T-rich degrons in IRF1 (PubMed:37622993). Facilitates the lysosome-dependent degradation of enterovirus EV71 protease 2A by inducing its 'Lys-48'-linked polyubiquitination, which ultimately restricts EV71 replication (PubMed:37796126). Acts as an antiviral factor also against hepatitis B virus/HBV by promoting ubiquitination and subsequent degradation of HNF1A (PubMed:38018242). In turn, inhibits HBV transcription and replication by preventing HNF1A stimulating activity of HBV preS1 promoter and enhancer II (PubMed:38018242). Involved in ubiquitination of BRDT and promotes its degradation, thereby regulates histone removal in early condensing spermatids prior to histone-to-protamine exchange (By similarity). {ECO:0000250|UniProtKB:Q6ZWS8, ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:19818708, ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:22632832, ECO:0000269|PubMed:32109420, ECO:0000269|PubMed:37622993, ECO:0000269|PubMed:37796126, ECO:0000269|PubMed:38018242}. |
| O43929 | ORC4 | S6 | ochoa | Origin recognition complex subunit 4 | Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3. {ECO:0000269|PubMed:22427655}. |
| O60220 | TIMM8A | S6 | ochoa | Mitochondrial import inner membrane translocase subunit Tim8 A (Deafness dystonia protein 1) (X-linked deafness dystonia protein) | Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. Probably necessary for normal neurologic development. {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}. |
| O60220 | TIMM8A | S7 | ochoa | Mitochondrial import inner membrane translocase subunit Tim8 A (Deafness dystonia protein 1) (X-linked deafness dystonia protein) | Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. Probably necessary for normal neurologic development. {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}. |
| O60443 | GSDME | T6 | psp | Gasdermin-E (Inversely correlated with estrogen receptor expression 1) (ICERE-1) (Non-syndromic hearing impairment protein 5) [Cleaved into: Gasdermin-E, N-terminal (GSDME-NT); Gasdermin-E, C-terminal (GSDME-CT)] | [Gasdermin-E]: Precursor of a pore-forming protein that converts non-inflammatory apoptosis to pyroptosis (PubMed:27281216, PubMed:28459430, PubMed:33852854, PubMed:35594856, PubMed:36607699). This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-E, N-terminal) binds to membranes and forms pores, triggering pyroptosis (PubMed:28459430). {ECO:0000269|PubMed:27281216, ECO:0000269|PubMed:28459430, ECO:0000269|PubMed:33852854, ECO:0000269|PubMed:35594856, ECO:0000269|PubMed:36607699}.; FUNCTION: [Gasdermin-E, N-terminal]: Pore-forming protein produced by cleavage by CASP3 or granzyme B (GZMB), which converts non-inflammatory apoptosis to pyroptosis or promotes granzyme-mediated pyroptosis, respectively (PubMed:27281216, PubMed:28459430, PubMed:32188940, PubMed:33852854, PubMed:35594856). After cleavage, moves to the plasma membrane, homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, allowing the release of mature interleukins (IL1B and IL16) and triggering pyroptosis (PubMed:28459430, PubMed:32188940, PubMed:33852854, PubMed:35594856). Binds to inner leaflet lipids, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate (PubMed:28459430). Cleavage by CASP3 switches CASP3-mediated apoptosis induced by TNF or danger signals, such as chemotherapy drugs, to pyroptosis (PubMed:27281216, PubMed:28459430, PubMed:32188940). Mediates secondary necrosis downstream of the mitochondrial apoptotic pathway and CASP3 activation as well as in response to viral agents (PubMed:28045099). Exhibits bactericidal activity (PubMed:27281216). Cleavage by GZMB promotes tumor suppressor activity by triggering robust anti-tumor immunity (PubMed:21522185, PubMed:32188940). Suppresses tumors by mediating granzyme-mediated pyroptosis in target cells of natural killer (NK) cells: cleavage by granzyme B (GZMB), delivered to target cells from NK-cells, triggers pyroptosis of tumor cells and tumor suppression (PubMed:31953257, PubMed:32188940). May play a role in the p53/TP53-regulated cellular response to DNA damage (PubMed:16897187). {ECO:0000269|PubMed:16897187, ECO:0000269|PubMed:21522185, ECO:0000269|PubMed:27281216, ECO:0000269|PubMed:28045099, ECO:0000269|PubMed:28459430, ECO:0000269|PubMed:31953257, ECO:0000269|PubMed:32188940, ECO:0000269|PubMed:33852854, ECO:0000269|PubMed:35594856}.; FUNCTION: [Gasdermin-E, N-terminal]: (Microbial infection) Pore-forming protein, which promotes maternal placental pyroptosis in response to Zika virus infection, contributing to adverse fetal outcomes. {ECO:0000269|PubMed:35972780}. |
| O60502 | OGA | S6 | ochoa | Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylglucosaminidase) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (N-acetyl-beta-glucosaminidase) (Nuclear cytoplasmic O-GlcNAcase and acetyltransferase) (NCOAT) | [Isoform 1]: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins (PubMed:11148210, PubMed:11788610, PubMed:20673219, PubMed:22365600, PubMed:24088714, PubMed:28939839, PubMed:37962578). Deglycosylates a large and diverse number of proteins, such as CRYAB, ELK1, GSDMD, LMNB1 and TAB1 (PubMed:28939839, PubMed:37962578). Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:20673219). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714). {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:20673219, ECO:0000269|PubMed:22365600, ECO:0000269|PubMed:24088714, ECO:0000269|PubMed:28939839, ECO:0000269|PubMed:37962578}.; FUNCTION: [Isoform 3]: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1. {ECO:0000269|PubMed:20673219}. |
| O60524 | NEMF | S6 | ochoa | Ribosome quality control complex subunit NEMF (Antigen NY-CO-1) (Nuclear export mediator factor) (Serologically defined colon cancer antigen 1) | Key component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes as well as their ubiquitin-mediated proteasomal degradation (PubMed:25578875, PubMed:32726578, PubMed:33406423, PubMed:33909987). Thereby, frees 60S subunit ribosomes from the stalled translation complex and prevents the accumulation of nascent polypeptide chains that are potentially toxic for the cell (PubMed:25578875, PubMed:33406423, PubMed:33909987). Within the RQC complex, NEMF specifically binds stalled 60S ribosomal subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety and promotes the recruitment of LTN1 to stalled 60S subunits (PubMed:25578875). Following binding to stalled 60S ribosomal subunits, NEMF mediates CAT tailing by recruiting alanine-charged tRNA to the A-site and directing the elongation of stalled nascent chains independently of mRNA or 40S subunits, leading to non-templated C-terminal alanine extensions (CAT tails) (PubMed:33406423, PubMed:33909987). Mainly recruits alanine-charged tRNAs, but can also other amino acid-charged tRNAs (PubMed:33406423, PubMed:33909987). CAT tailing is required to promote ubiquitination of stalled nascent chains by different E3 ubiquitin-protein ligases (PubMed:33909987). In the canonical RQC pathway (RQC-L), CAT tailing facilitates LTN1-dependent ubiquitination by exposing lysine residues that would otherwise remain buried in the ribosomal exit tunnel (By similarity). In the alternative RQC pathway (RQC-C) CAT tailing creates an C-degron mainly composed of alanine that is recognized by the CRL2(KLHDC10) and RCHY1/PIRH2 E3 ligases, leading to ubiquitination and degradation of stalled nascent chains (PubMed:33909987). NEMF may also indirectly play a role in nuclear export (PubMed:16103875). {ECO:0000250|UniProtKB:Q12532, ECO:0000269|PubMed:16103875, ECO:0000269|PubMed:25578875, ECO:0000269|PubMed:32726578, ECO:0000269|PubMed:33406423, ECO:0000269|PubMed:33909987}. |
| O60682 | MSC | S7 | ochoa | Musculin (Activated B-cell factor 1) (ABF-1) (Class A basic helix-loop-helix protein 22) (bHLHa22) | Transcription repressor capable of inhibiting the transactivation capability of TCF3/E47. May play a role in regulating antigen-dependent B-cell differentiation. |
| O60684 | KPNA6 | S6 | ochoa | Importin subunit alpha-7 (Karyopherin subunit alpha-6) | Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:10523667}. |
| O60762 | DPM1 | S7 | ochoa | Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (Dolichol-phosphate mannose synthase subunit 1) (DPM synthase subunit 1) (Dolichyl-phosphate beta-D-mannosyltransferase subunit 1) (Mannose-P-dolichol synthase subunit 1) (MPD synthase subunit 1) | Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex. {ECO:0000269|PubMed:10835346}. |
| O60814 | H2BC12 | S7 | ochoa | Histone H2B type 1-K (H2B K) (HIRA-interacting protein 1) | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; FUNCTION: Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid. |
| O60825 | PFKFB2 | S6 | ochoa | 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 (6PF-2-K/Fru-2,6-P2ase 2) (PFK/FBPase 2) (6PF-2-K/Fru-2,6-P2ase heart-type isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] | Synthesis and degradation of fructose 2,6-bisphosphate. {ECO:0000269|PubMed:11069105}. |
| O60825 | PFKFB2 | S7 | ochoa | 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 (6PF-2-K/Fru-2,6-P2ase 2) (PFK/FBPase 2) (6PF-2-K/Fru-2,6-P2ase heart-type isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] | Synthesis and degradation of fructose 2,6-bisphosphate. {ECO:0000269|PubMed:11069105}. |
| O75143 | ATG13 | S7 | ochoa | Autophagy-related protein 13 | Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. {ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19225151, ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:21795849, ECO:0000269|PubMed:21855797}. |
| O75382 | TRIM3 | S7 | ochoa | Tripartite motif-containing protein 3 (EC 2.3.2.27) (Brain-expressed RING finger protein) (RING finger protein 22) (RING finger protein 97) | E3 ubiquitin ligase that plays essential roles in neuronal functions such as regulation of neuronal plasticity, learning, and memory (By similarity). In addition to its neuronal functions, participates in other biological processes such as innate immunity or cell cycle regulation. Component of the cytoskeleton-associated recycling or transport complex in neurons, polyubiquitinates gamma-actin, thus regulating neuronal plasticity, learning, and memory (By similarity). Ubiquitinates postsynaptic scaffold GKAP, a neuronal substrate involved in synaptic remodeling and thereby modulates dendritic spine morphology (By similarity). Positively regulates motility of microtubule-dependent motor protein KIF21B (By similarity). Induces growth arrest via its RING-dependent E3 ligase activity and ubiquinates CDKN1A (PubMed:24393003). Positively regulates TLR3-mediated signaling by mediating 'Lys-63'-linked polyubiquitination of TLR3 (PubMed:32878999). In turn, promotes the recognition and sorting of polyubiquitinated TLR3 by the ESCRT complexes (PubMed:32878999). {ECO:0000250|UniProtKB:Q9R1R2, ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:24393003, ECO:0000269|PubMed:32878999}. |
| O75530 | EED | S7 | ochoa | Polycomb protein EED (hEED) (Embryonic ectoderm development protein) (WD protein associating with integrin cytoplasmic tails 1) (WAIT-1) | Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A. {ECO:0000269|PubMed:10581039, ECO:0000269|PubMed:14532106, ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:20974918, ECO:0000269|PubMed:28229514, ECO:0000269|PubMed:9584199}. |
| O75563 | SKAP2 | S6 | ochoa | Src kinase-associated phosphoprotein 2 (Pyk2/RAFTK-associated protein) (Retinoic acid-induced protein 70) (SKAP55 homolog) (SKAP-55HOM) (SKAP-HOM) (Src family-associated phosphoprotein 2) (Src kinase-associated phosphoprotein 55-related protein) (Src-associated adapter protein with PH and SH3 domains) | May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway. {ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:9837776}. |
| O75563 | SKAP2 | T7 | ochoa | Src kinase-associated phosphoprotein 2 (Pyk2/RAFTK-associated protein) (Retinoic acid-induced protein 70) (SKAP55 homolog) (SKAP-55HOM) (SKAP-HOM) (Src family-associated phosphoprotein 2) (Src kinase-associated phosphoprotein 55-related protein) (Src-associated adapter protein with PH and SH3 domains) | May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway. {ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:9837776}. |
| O75995 | SASH3 | S7 | ochoa | SAM and SH3 domain-containing protein 3 (SH3 protein expressed in lymphocytes homolog) | May function as a signaling adapter protein in lymphocytes. {ECO:0000250|UniProtKB:Q8K352}. |
| O76021 | RSL1D1 | S6 | ochoa | Ribosomal L1 domain-containing protein 1 (CATX-11) (Cellular senescence-inhibited gene protein) (Protein PBK1) | Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage. {ECO:0000269|PubMed:18678645, ECO:0000269|PubMed:22419112}. |
| O76094 | SRP72 | S6 | ochoa | Signal recognition particle subunit SRP72 (SRP72) (Signal recognition particle 72 kDa protein) | Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (PubMed:34020957). The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (PubMed:34020957). Binds the signal recognition particle RNA (7SL RNA) in presence of SRP68 (PubMed:21073748, PubMed:27899666). Can bind 7SL RNA with low affinity (PubMed:21073748, PubMed:27899666). The SRP complex possibly participates in the elongation arrest function (By similarity). {ECO:0000250|UniProtKB:P38688, ECO:0000269|PubMed:21073748, ECO:0000269|PubMed:27899666, ECO:0000269|PubMed:34020957}. |
| O94782 | USP1 | S7 | ochoa | Ubiquitin carboxyl-terminal hydrolase 1 (EC 3.4.19.12) (Deubiquitinating enzyme 1) (hUBP) (Ubiquitin thioesterase 1) (Ubiquitin-specific-processing protease 1) [Cleaved into: Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment] | Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2 (PubMed:15694335). Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA (PubMed:16531995, PubMed:20147293). Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity (PubMed:18082604, PubMed:26388029). {ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:26388029}. |
| O94806 | PRKD3 | S6 | ochoa | Serine/threonine-protein kinase D3 (EC 2.7.11.13) (Protein kinase C nu type) (Protein kinase EPK2) (nPKC-nu) | Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity). {ECO:0000250}. |
| O94888 | UBXN7 | S7 | ochoa | UBX domain-containing protein 7 | Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates. {ECO:0000269|PubMed:22537386}. |
| O94903 | PLPBP | S6 | ochoa | Pyridoxal phosphate homeostasis protein (PLP homeostasis protein) (Proline synthase co-transcribed bacterial homolog protein) (Pyridoxal phosphate-binding protein) | Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6. {ECO:0000255|HAMAP-Rule:MF_03225, ECO:0000269|PubMed:27912044}. |
| O95231 | VENTX | S6 | ochoa | Homeobox protein VENTX (VENT homeobox homolog) (VENT-like homeobox protein 2) | May be involved in ventralization. |
| O95235 | KIF20A | S7 | ochoa|psp | Kinesin-like protein KIF20A (GG10_2) (Mitotic kinesin-like protein 2) (MKlp2) (Rab6-interacting kinesin-like protein) (Rabkinesin-6) | Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. {ECO:0000269|PubMed:12939256}. |
| O95295 | SNAPIN | S6 | ochoa | SNARE-associated protein Snapin (Biogenesis of lysosome-related organelles complex 1 subunit 7) (BLOC-1 subunit 7) (Synaptosomal-associated protein 25-binding protein) (SNAP-associated protein) | Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells (PubMed:17182842, PubMed:18167355). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (PubMed:25898167). {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:25898167}. |
| O95402 | MED26 | S7 | ochoa | Mediator of RNA polymerase II transcription subunit 26 (Activator-recruited cofactor 70 kDa component) (ARC70) (Cofactor required for Sp1 transcriptional activation subunit 7) (CRSP complex subunit 7) (Mediator complex subunit 26) (Transcriptional coactivator CRSP70) | Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. |
| O95429 | BAG4 | S7 | ochoa | BAG family molecular chaperone regulator 4 (BAG-4) (Bcl-2-associated athanogene 4) (Silencer of death domains) | Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (By similarity). Prevents constitutive TNFRSF1A signaling. Negative regulator of PRKN translocation to damaged mitochondria. {ECO:0000250, ECO:0000269|PubMed:24270810}. |
| O95707 | POP4 | Y6 | ochoa | Ribonuclease P protein subunit p29 (hPOP4) | Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000269|PubMed:10024167, ECO:0000269|PubMed:10352175, ECO:0000269|PubMed:30454648}. |
| O95817 | BAG3 | S7 | ochoa | BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1) | Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269|PubMed:10597216, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:27474739, ECO:0000269|PubMed:27884606, ECO:0000269|PubMed:30559338, ECO:0000269|PubMed:9873016}. |
| O95999 | BCL10 | S7 | ochoa | B-cell lymphoma/leukemia 10 (B-cell CLL/lymphoma 10) (Bcl-10) (CARD-containing molecule enhancing NF-kappa-B) (CARD-like apoptotic protein) (hCLAP) (CED-3/ICH-1 prodomain homologous E10-like regulator) (CIPER) (Cellular homolog of vCARMEN) (cCARMEN) (Cellular-E10) (c-E10) (Mammalian CARD-containing adapter molecule E10) (mE10) | Plays a key role in both adaptive and innate immune signaling by bridging CARD domain-containing proteins to immune activation (PubMed:10187770, PubMed:10364242, PubMed:10400625, PubMed:24074955, PubMed:25365219). Acts by channeling adaptive and innate immune signaling downstream of CARD domain-containing proteins CARD9, CARD11 and CARD14 to activate NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:24074955). Recruited by activated CARD domain-containing proteins: homooligomerized CARD domain-containing proteins form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10, subsequent recruitment of MALT1 and formation of a CBM complex (PubMed:24074955). This leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:18287044, PubMed:24074955, PubMed:27777308). Activated by CARD9 downstream of C-type lectin receptors; CARD9-mediated signals are essential for antifungal immunity (PubMed:26488816). Activated by CARD11 downstream of T-cell receptor (TCR) and B-cell receptor (BCR) (PubMed:18264101, PubMed:18287044, PubMed:24074955, PubMed:27777308). Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK (PubMed:10187815). {ECO:0000269|PubMed:10187770, ECO:0000269|PubMed:10187815, ECO:0000269|PubMed:10364242, ECO:0000269|PubMed:10400625, ECO:0000269|PubMed:18264101, ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:24074955, ECO:0000269|PubMed:25365219, ECO:0000269|PubMed:26488816, ECO:0000269|PubMed:27777308}. |
| O96018 | APBA3 | S7 | ochoa|psp | Amyloid-beta A4 precursor protein-binding family A member 3 (Adapter protein X11gamma) (Neuron-specific X11L2 protein) (Neuronal Munc18-1-interacting protein 3) (Mint-3) | May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN. {ECO:0000269|PubMed:19726677}. |
| P00352 | ALDH1A1 | T6 | ochoa | Aldehyde dehydrogenase 1A1 (EC 1.2.1.19) (EC 1.2.1.28) (EC 1.2.1.3) (EC 1.2.1.36) (3-deoxyglucosone dehydrogenase) (ALDH-E1) (ALHDII) (Aldehyde dehydrogenase family 1 member A1) (Aldehyde dehydrogenase, cytosolic) (Retinal dehydrogenase 1) (RALDH 1) (RalDH1) | Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:12941160, PubMed:15623782, PubMed:17175089, PubMed:19296407, PubMed:25450233, PubMed:26373694). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid (By similarity). This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification (PubMed:12941160, PubMed:15623782, PubMed:19296407). Also functions downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (PubMed:17175089). Also has an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity). {ECO:0000250|UniProtKB:P24549, ECO:0000269|PubMed:12941160, ECO:0000269|PubMed:15623782, ECO:0000269|PubMed:17175089, ECO:0000269|PubMed:19296407, ECO:0000269|PubMed:25450233, ECO:0000269|PubMed:26373694}. |
| P02786 | TFRC | S7 | ochoa | Transferrin receptor protein 1 (TR) (TfR) (TfR1) (Trfr) (T9) (p90) (CD antigen CD71) [Cleaved into: Transferrin receptor protein 1, serum form (sTfR)] | Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production (By similarity). {ECO:0000250|UniProtKB:Q62351, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:26642240, ECO:0000269|PubMed:3568132}.; FUNCTION: (Microbial infection) Acts as a receptor for new-world arenaviruses: Guanarito, Junin and Machupo virus. {ECO:0000269|PubMed:17287727, ECO:0000269|PubMed:18268337}.; FUNCTION: (Microbial infection) Acts as a host entry factor for rabies virus that hijacks the endocytosis of TFRC to enter cells. {ECO:0000269|PubMed:36779762, ECO:0000269|PubMed:36779763}.; FUNCTION: (Microbial infection) Acts as a host entry factor for SARS-CoV, MERS-CoV and SARS-CoV-2 viruses that hijack the endocytosis of TFRC to enter cells. {ECO:0000269|PubMed:36779762}. |
| P02795 | MT2A | S6 | ochoa | Metallothionein-2 (MT-2) (Metallothionein-2A) (Metallothionein-II) (MT-II) | Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. |
| P04080 | CSTB | S7 | ochoa | Cystatin-B (CPI-B) (Liver thiol proteinase inhibitor) (Stefin-B) | This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. |
| P04150 | NR3C1 | S6 | ochoa | Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1) | Receptor for glucocorticoids (GC) (PubMed:27120390, PubMed:37478846). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors (PubMed:28139699). Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:9590696). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (PubMed:25775514). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:25775514, ECO:0000269|PubMed:27120390, ECO:0000269|PubMed:28139699, ECO:0000269|PubMed:37478846, ECO:0000269|PubMed:9590696}.; FUNCTION: [Isoform Alpha]: Has transcriptional activation and repression activity (PubMed:11435610, PubMed:15769988, PubMed:15866175, PubMed:17635946, PubMed:19141540, PubMed:19248771, PubMed:20484466, PubMed:21664385, PubMed:23820903). Mediates glucocorticoid-induced apoptosis (PubMed:23303127). Promotes accurate chromosome segregation during mitosis (PubMed:25847991). May act as a tumor suppressor (PubMed:25847991). May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (By similarity). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:20484466, ECO:0000269|PubMed:21664385, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903, ECO:0000269|PubMed:25847991}.; FUNCTION: [Isoform Beta]: Acts as a dominant negative inhibitor of isoform Alpha (PubMed:20484466, PubMed:7769088, PubMed:8621628). Has intrinsic transcriptional activity independent of isoform Alpha when both isoforms are coexpressed (PubMed:19248771, PubMed:26711253). Loses this transcription modulator function on its own (PubMed:20484466). Has no hormone-binding activity (PubMed:8621628). May play a role in controlling glucose metabolism by maintaining insulin sensitivity (By similarity). Reduces hepatic gluconeogenesis through down-regulation of PEPCK in an isoform Alpha-dependent manner (PubMed:26711253). Directly regulates STAT1 expression in isoform Alpha-independent manner (PubMed:26711253). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:20484466, ECO:0000269|PubMed:26711253, ECO:0000269|PubMed:7769088, ECO:0000269|PubMed:8621628}.; FUNCTION: [Isoform Alpha-2]: Has lower transcriptional activation activity than isoform Alpha. Exerts a dominant negative effect on isoform Alpha trans-repression mechanism (PubMed:20484466).; FUNCTION: [Isoform GR-P]: Increases activity of isoform Alpha. {ECO:0000269|PubMed:11358809}.; FUNCTION: [Isoform Alpha-B]: More effective than isoform Alpha in transcriptional activation, but not repression activity. {ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform 10]: Has transcriptional activation activity. {ECO:0000269|PubMed:20484466}.; FUNCTION: [Isoform Alpha-C1]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-C2]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-C3]: Has highest transcriptional activation activity of all isoforms created by alternative initiation (PubMed:15866175, PubMed:23820903). Has transcriptional repression activity (PubMed:23303127). Mediates glucocorticoid-induced apoptosis (PubMed:23303127, PubMed:23820903). {ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903}.; FUNCTION: [Isoform Alpha-D1]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-D2]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-D3]: Has lowest transcriptional activation activity of all isoforms created by alternative initiation (PubMed:15866175, PubMed:23820903). Has transcriptional repression activity (PubMed:23303127). {ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903}. |
| P04632 | CAPNS1 | S6 | ochoa | 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}. |
| P04637 | TP53 | S6 | ochoa|psp | Cellular tumor antigen p53 (Antigen NY-CO-13) (Phosphoprotein p53) (Tumor suppressor p53) | Multifunctional transcription factor that induces cell cycle arrest, DNA repair or apoptosis upon binding to its target DNA sequence (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:35618207, PubMed:36634798, PubMed:38653238, PubMed:9840937). Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17189187, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:38653238, PubMed:9840937). Negatively regulates cell division by controlling expression of a set of genes required for this process (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:9840937). One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression (PubMed:12524540, PubMed:17189187). Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (PubMed:12524540). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (PubMed:12524540). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492). {ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:17317671, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24051492, ECO:0000269|PubMed:24652652, ECO:0000269|PubMed:35618207, ECO:0000269|PubMed:36634798, ECO:0000269|PubMed:38653238, ECO:0000269|PubMed:9840937}. |
| P05114 | HMGN1 | S7 | ochoa|psp | Non-histone chromosomal protein HMG-14 (High mobility group nucleosome-binding domain-containing protein 1) | Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2 (By similarity). {ECO:0000250}. |
| P05387 | RPLP2 | S6 | ochoa | Large ribosomal subunit protein P2 (60S acidic ribosomal protein P2) (Renal carcinoma antigen NY-REN-44) | Plays an important role in the elongation step of protein synthesis. |
| P05387 | RPLP2 | Y7 | ochoa | Large ribosomal subunit protein P2 (60S acidic ribosomal protein P2) (Renal carcinoma antigen NY-REN-44) | Plays an important role in the elongation step of protein synthesis. |
| P05783 | KRT18 | S7 | ochoa | Keratin, type I cytoskeletal 18 (Cell proliferation-inducing gene 46 protein) (Cytokeratin-18) (CK-18) (Keratin-18) (K18) | Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}. |
| P07384 | CAPN1 | T7 | ochoa | Calpain-1 catalytic subunit (EC 3.4.22.52) (Calcium-activated neutral proteinase 1) (CANP 1) (Calpain mu-type) (Calpain-1 large subunit) (Cell proliferation-inducing gene 30 protein) (Micromolar-calpain) (muCANP) | Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction (PubMed:19617626, PubMed:21531719, PubMed:2400579). Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-387' and 'His-409' (PubMed:23707407). Cleaves and activates caspase-7 (CASP7) (PubMed:19617626). {ECO:0000269|PubMed:19617626, ECO:0000269|PubMed:21531719, ECO:0000269|PubMed:23707407, ECO:0000269|PubMed:2400579}. |
| P07900 | HSP90AA1 | T7 | ochoa|psp | Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Heat shock protein family C member 1) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38) | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812). {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:12526792, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123, ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155, ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.; FUNCTION: (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion. {ECO:0000305|PubMed:22066472}. |
| P08047 | SP1 | S7 | ochoa|psp | Transcription factor Sp1 | Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Also binds the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component BMAL1 (PubMed:10391891, PubMed:11371615, PubMed:11904305, PubMed:14593115, PubMed:16377629, PubMed:16478997, PubMed:16943418, PubMed:17049555, PubMed:18171990, PubMed:18199680, PubMed:18239466, PubMed:18513490, PubMed:18619531, PubMed:19193796, PubMed:20091743, PubMed:21046154, PubMed:21798247). Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity). {ECO:0000250|UniProtKB:O89090, ECO:0000250|UniProtKB:Q01714, ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:11371615, ECO:0000269|PubMed:11904305, ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16377629, ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16943418, ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18171990, ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466, ECO:0000269|PubMed:18513490, ECO:0000269|PubMed:18619531, ECO:0000269|PubMed:19193796, ECO:0000269|PubMed:20091743, ECO:0000269|PubMed:21046154, ECO:0000269|PubMed:21798247}. |
| P08473 | MME | S6 | ochoa|psp | Neprilysin (EC 3.4.24.11) (Atriopeptidase) (Common acute lymphocytic leukemia antigen) (CALLA) (Enkephalinase) (Neutral endopeptidase 24.11) (NEP) (Neutral endopeptidase) (Skin fibroblast elastase) (SFE) (CD antigen CD10) | Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:6208535, PubMed:6349683, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991, PubMed:6349683). Catalyzes cleavage of bradykinin, substance P and neurotensin peptides (PubMed:6208535). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675, PubMed:6349683). Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)) (PubMed:16254193, PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573). {ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:17101991, ECO:0000269|PubMed:20876573, ECO:0000269|PubMed:2531377, ECO:0000269|PubMed:27588448, ECO:0000269|PubMed:2972276, ECO:0000269|PubMed:6208535, ECO:0000269|PubMed:6349683}. |
| P08670 | VIM | S7 | ochoa|psp | Vimentin | Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). {ECO:0000250|UniProtKB:A0A8C0N8E3, ECO:0000250|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269|PubMed:21746880}. |
| P09543 | CNP | S6 | ochoa | 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) (CNPase) (EC 3.1.4.37) | Catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates (By similarity). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity). {ECO:0000250|UniProtKB:P06623, ECO:0000250|UniProtKB:P16330}. |
| P09651 | HNRNPA1 | S6 | ochoa|psp | Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) (Helix-destabilizing protein) (Single-strand RNA-binding protein) (hnRNP core protein A1) [Cleaved into: Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed] | Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection (PubMed:17371836). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1 (PubMed:31498791). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:31498791}.; FUNCTION: (Microbial infection) May play a role in HCV RNA replication. {ECO:0000269|PubMed:17229681}.; FUNCTION: (Microbial infection) Cleavage by Enterovirus 71 protease 3C results in increased translation of apoptosis protease activating factor APAF1, leading to apoptosis. {ECO:0000269|PubMed:17229681}. |
| P0C264 | SBK3 | S6 | ochoa | Uncharacterized serine/threonine-protein kinase SBK3 (EC 2.7.11.1) (SH3 domain-binding kinase family member 3) (Sugen kinase 110) | None |
| P10073 | ZSCAN22 | S7 | ochoa | Zinc finger and SCAN domain-containing protein 22 (Krueppel-related zinc finger protein 2) (Protein HKR2) (Zinc finger protein 50) | May be involved in transcriptional regulation. |
| P10243 | MYBL1 | S7 | ochoa|psp | Myb-related protein A (A-Myb) (Myb-like protein 1) | Transcription factor that specifically recognizes the sequence 5'-YAAC[GT]G-3' (PubMed:7987850, PubMed:8058310). Acts as a master regulator of male meiosis by promoting expression of piRNAs: activates expression of both piRNA precursor RNAs and expression of protein-coding genes involved in piRNA metabolism (By similarity). The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons, which is essential for the germline integrity (By similarity). Transcriptional activator of SOX30 (By similarity). {ECO:0000250|UniProtKB:P51960, ECO:0000269|PubMed:7987850, ECO:0000269|PubMed:8058310}. |
| P10301 | RRAS | S7 | ochoa | Ras-related protein R-Ras (EC 3.6.5.2) (p23) | GTP-binding protein with GTPase activity, likely involved in the regulation of MAPK signaling pathway and thereby controlling multiple cellular processes (PubMed:39809765). Regulates the organization of the actin cytoskeleton (PubMed:16537651, PubMed:18270267). With OSPBL3, modulates integrin beta-1 (ITGB1) activity (PubMed:18270267). {ECO:0000269|PubMed:16537651, ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:39809765}. |
| P11086 | PNMT | S7 | ochoa | Phenylethanolamine N-methyltransferase (PNMTase) (EC 2.1.1.28) (Noradrenaline N-methyltransferase) | Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor (PubMed:20496117). Other substrates include phenylethanolamine and octopamine (PubMed:16277617, PubMed:16363801, PubMed:8812853). Also methylates normetanephrine (By similarity). {ECO:0000250|UniProtKB:P10937, ECO:0000269|PubMed:16277617, ECO:0000269|PubMed:16363801, ECO:0000269|PubMed:20496117, ECO:0000269|PubMed:8812853}. |
| P11171 | EPB41 | S6 | 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}. |
| P11836 | MS4A1 | S7 | ochoa | B-lymphocyte antigen CD20 (B-lymphocyte surface antigen B1) (Bp35) (Leukocyte surface antigen Leu-16) (Membrane-spanning 4-domains subfamily A member 1) (CD antigen CD20) | B-lymphocyte-specific membrane protein that plays a role in the regulation of cellular calcium influx necessary for the development, differentiation, and activation of B-lymphocytes (PubMed:12920111, PubMed:3925015, PubMed:7684739). Functions as a store-operated calcium (SOC) channel component promoting calcium influx after activation by the B-cell receptor/BCR (PubMed:12920111, PubMed:18474602, PubMed:7684739). {ECO:0000269|PubMed:12920111, ECO:0000269|PubMed:18474602, ECO:0000269|PubMed:3925015, ECO:0000269|PubMed:7684739}. |
| P12235 | SLC25A4 | S7 | ochoa | ADP/ATP translocase 1 (ADP,ATP carrier protein 1) (ADP,ATP carrier protein, heart/skeletal muscle isoform T1) (Adenine nucleotide translocator 1) (ANT 1) (Solute carrier family 25 member 4) | ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:21586654, PubMed:27693233). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity (PubMed:31883789). Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis (By similarity). Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A4/ANT1 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity) (By similarity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it (By similarity). Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death (PubMed:31883789). It is however unclear if SLC25A4/ANT1 constitutes a pore-forming component of mPTP or regulates it (By similarity). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (By similarity). {ECO:0000250|UniProtKB:G2QNH0, ECO:0000250|UniProtKB:P48962, ECO:0000269|PubMed:21586654, ECO:0000269|PubMed:27693233, ECO:0000269|PubMed:31883789}. |
| P12277 | CKB | S6 | ochoa | Creatine kinase B-type (EC 2.7.3.2) (Brain creatine kinase) (B-CK) (Creatine kinase B chain) (Creatine phosphokinase B-type) (CPK-B) | Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate) (PubMed:8186255). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (Probable). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating phosphorylation of creatine to initiate a futile cycle of creatine phosphorylation and dephosphorylation (By similarity). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity). {ECO:0000250|UniProtKB:Q04447, ECO:0000269|PubMed:8186255, ECO:0000305}. |
| P12814 | ACTN1 | S6 | ochoa | Alpha-actinin-1 (Alpha-actinin cytoskeletal isoform) (F-actin cross-linking protein) (Non-muscle alpha-actinin-1) | F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation (PubMed:22689882). {ECO:0000269|PubMed:22689882}. |
| P12956 | XRCC6 | S6 | ochoa|psp | X-ray repair cross-complementing protein 6 (EC 3.6.4.-) (EC 4.2.99.-) (5'-deoxyribose-5-phosphate lyase Ku70) (5'-dRP lyase Ku70) (70 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (CTC box-binding factor 75 kDa subunit) (CTC75) (CTCBF) (DNA repair protein XRCC6) (Lupus Ku autoantigen protein p70) (Ku70) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 6) | Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Required for double-strand break repair and V(D)J recombination (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Also has a role in chromosome translocation (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Has a role in chromosome translocation (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). It works in the 3'-5' direction (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and binds to the broken ends of the DNA and protects them from further resection (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Binding to DNA may be mediated by XRCC6 (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The XRCC5-XRRC6 dimer acts as a regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks (PubMed:20383123). 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined (PubMed:20383123). The XRCC5-XRRC6 dimer together with APEX1 acts as a negative regulator of transcription (PubMed:8621488). In association with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin promoter and activates osteocalcin expression (PubMed:12145306). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Negatively regulates apoptosis by interacting with BAX and sequestering it from the mitochondria (PubMed:15023334). Might have deubiquitination activity, acting on BAX (PubMed:18362350). {ECO:0000269|PubMed:11493912, ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:15023334, ECO:0000269|PubMed:18362350, ECO:0000269|PubMed:20383123, ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:2466842, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:7957065, ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:9742108}. |
| P13051 | UNG | T6 | ochoa|psp | Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) | Uracil-DNA glycosylase that hydrolyzes the N-glycosidic bond between uracil and deoxyribose in single- and double-stranded DNA (ssDNA and dsDNA) to release a free uracil residue and form an abasic (apurinic/apyrimidinic; AP) site. Excises uracil residues arising as a result of misincorporation of dUMP residues by DNA polymerase during replication or due to spontaneous or enzymatic deamination of cytosine (PubMed:12958596, PubMed:15967827, PubMed:17101234, PubMed:22521144, PubMed:7671300, PubMed:8900285, PubMed:9016624, PubMed:9776759). Mediates error-free base excision repair (BER) of uracil at replication forks. According to the model, it is recruited by PCNA to S-phase replication forks to remove misincorporated uracil at U:A base mispairs in nascent DNA strands. Via trimeric RPA it is recruited to ssDNA stretches ahead of the polymerase to allow detection and excision of deaminated cytosines prior to replication. The resultant AP sites temporarily stall replication, allowing time to repair the lesion (PubMed:22521144). Mediates mutagenic uracil processing involved in antibody affinity maturation. Processes AICDA-induced U:G base mispairs at variable immunoglobulin (Ig) regions leading to the generation of transversion mutations (PubMed:12958596). Operates at switch sites of Ig constant regions where it mediates Ig isotype class switch recombination. Excises AICDA-induced uracil residues forming AP sites that are subsequently nicked by APEX1 endonuclease. The accumulation of staggered nicks in opposite strands results in double strand DNA breaks that are finally resolved via non-homologous end joining repair pathway (By similarity) (PubMed:12958596). {ECO:0000250|UniProtKB:P97931, ECO:0000269|PubMed:12958596, ECO:0000269|PubMed:15967827, ECO:0000269|PubMed:17101234, ECO:0000269|PubMed:22521144, ECO:0000269|PubMed:7671300, ECO:0000269|PubMed:8900285, ECO:0000269|PubMed:9016624, ECO:0000269|PubMed:9776759}. |
| P13489 | RNH1 | S7 | ochoa | Ribonuclease inhibitor (Placental ribonuclease inhibitor) (Placental RNase inhibitor) (Ribonuclease/angiogenin inhibitor 1) (RAI) | Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and angiogenin (ANG) (PubMed:12578357, PubMed:14515218, PubMed:3219362, PubMed:3243277, PubMed:3470787, PubMed:9050852). May play a role in redox homeostasis (PubMed:17292889). Required to inhibit the cytotoxic tRNA ribonuclease activity of ANG in the cytoplasm in absence of stress (PubMed:23843625, PubMed:32510170). Relocates to the nucleus in response to stress, relieving inhibition of ANG in the cytoplasm, and inhibiting the angiogenic activity of ANG in the nucleus (PubMed:23843625). {ECO:0000269|PubMed:12578357, ECO:0000269|PubMed:14515218, ECO:0000269|PubMed:17292889, ECO:0000269|PubMed:23843625, ECO:0000269|PubMed:3219362, ECO:0000269|PubMed:3243277, ECO:0000269|PubMed:32510170, ECO:0000269|PubMed:3470787, ECO:0000269|PubMed:9050852}. |
| P13796 | LCP1 | S7 | ochoa | Plastin-2 (L-plastin) (LC64P) (Lymphocyte cytosolic protein 1) (LCP-1) | Actin-binding protein (PubMed:16636079, PubMed:17294403, PubMed:28493397). Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28 (PubMed:17294403). Modulates the cell surface expression of IL2RA/CD25 and CD69 (PubMed:17294403). {ECO:0000269|PubMed:16636079, ECO:0000269|PubMed:17294403, ECO:0000269|PubMed:28493397}. |
| P14136 | GFAP | T7 | psp | Glial fibrillary acidic protein (GFAP) | GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells. |
| P14618 | PKM | S6 | ochoa | Pyruvate kinase PKM (EC 2.7.1.40) (Cytosolic thyroid hormone-binding protein) (CTHBP) (Opa-interacting protein 3) (OIP-3) (Pyruvate kinase 2/3) (Pyruvate kinase muscle isozyme) (Threonine-protein kinase PKM2) (EC 2.7.11.1) (Thyroid hormone-binding protein 1) (THBP1) (Tumor M2-PK) (Tyrosine-protein kinase PKM2) (EC 2.7.10.2) (p58) | Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:15996096, PubMed:1854723, PubMed:20847263). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed:15996096, PubMed:1854723, PubMed:20847263). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:15996096, PubMed:1854723, PubMed:20847263). {ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723, ECO:0000269|PubMed:20847263}.; FUNCTION: [Isoform M2]: Isoform specifically expressed during embryogenesis that has low pyruvate kinase activity by itself and requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for pyruvate kinase activity (PubMed:18337823, PubMed:20847263). In addition to its pyruvate kinase activity in the cytoplasm, also acts as a regulator of transcription in the nucleus by acting as a protein kinase (PubMed:18191611, PubMed:21620138, PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661). Translocates into the nucleus in response to various signals, such as EGF receptor activation, and homodimerizes, leading to its conversion into a protein threonine- and tyrosine-protein kinase (PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661, PubMed:26787900). Catalyzes phosphorylation of STAT3 at 'Tyr-705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate transcription (PubMed:22306293, PubMed:22901803, PubMed:24120661). Its ability to activate transcription plays a role in cancer cells by promoting cell proliferation and promote tumorigenesis (PubMed:18337823, PubMed:22901803, PubMed:26787900). Promotes the expression of the immune checkpoint protein CD274 in BMAL1-deficient macrophages (By similarity). May also act as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs (By similarity). Plays a role in caspase independent cell death of tumor cells (PubMed:17308100). {ECO:0000250|UniProtKB:P52480, ECO:0000269|PubMed:17308100, ECO:0000269|PubMed:18191611, ECO:0000269|PubMed:18337823, ECO:0000269|PubMed:20847263, ECO:0000269|PubMed:21620138, ECO:0000269|PubMed:22056988, ECO:0000269|PubMed:22306293, ECO:0000269|PubMed:22901803, ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900}.; FUNCTION: [Isoform M1]: Pyruvate kinase isoform expressed in adult tissues, which replaces isoform M2 after birth (PubMed:18337823). In contrast to isoform M2, has high pyruvate kinase activity by itself and does not require allosteric activation by D-fructose 1,6-bisphosphate (FBP) for activity (PubMed:20847263). {ECO:0000269|PubMed:18337823, ECO:0000269|PubMed:20847263}. |
| P14621 | ACYP2 | S6 | ochoa | Acylphosphatase-2 (EC 3.6.1.7) (Acylphosphatase, muscle type isozyme) (Acylphosphate phosphohydrolase 2) | Its physiological role is not yet clear. |
| P15144 | ANPEP | Y6 | psp | Aminopeptidase N (AP-N) (hAPN) (EC 3.4.11.2) (Alanyl aminopeptidase) (Aminopeptidase M) (AP-M) (Microsomal aminopeptidase) (Myeloid plasma membrane glycoprotein CD13) (gp150) (CD antigen CD13) | Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization. May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity (By similarity). {ECO:0000250|UniProtKB:P97449, ECO:0000269|PubMed:10605003, ECO:0000269|PubMed:10676659, ECO:0000269|PubMed:11384645, ECO:0000269|PubMed:12473585, ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8102610, ECO:0000269|PubMed:9056417}.; FUNCTION: (Microbial infection) Acts as a receptor for human coronavirus 229E/HCoV-229E. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. {ECO:0000269|PubMed:12551991, ECO:0000269|PubMed:1350662, ECO:0000269|PubMed:8887485, ECO:0000269|PubMed:9367365}.; FUNCTION: (Microbial infection) Mediates as well Human cytomegalovirus (HCMV) infection. {ECO:0000269|PubMed:8105105}. |
| P15531 | NME1 | T7 | ochoa | Nucleoside diphosphate kinase A (NDK A) (NDP kinase A) (EC 2.7.4.6) (Granzyme A-activated DNase) (GAAD) (Metastasis inhibition factor nm23) (NM23-H1) (Tumor metastatic process-associated protein) | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair. {ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:8810265}. |
| P15924 | DSP | S7 | ochoa | Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen) | Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250|UniProtKB:F1LMV6}. |
| P17096 | HMGA1 | S6 | ochoa | High mobility group protein HMG-I/HMG-Y (HMG-I(Y)) (High mobility group AT-hook protein 1) (High mobility group protein A1) (High mobility group protein R) | HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions. |
| P17844 | DDX5 | S6 | ochoa | Probable ATP-dependent RNA helicase DDX5 (EC 3.6.4.13) (DEAD box protein 5) (RNA helicase p68) | Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as a transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. {ECO:0000269|PubMed:12527917, ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:15660129, ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:17960593, ECO:0000269|PubMed:18829551, ECO:0000269|PubMed:19718048, ECO:0000269|PubMed:21343338}. |
| P17931 | LGALS3 | S6 | psp | Galectin-3 (Gal-3) (35 kDa lectin) (Carbohydrate-binding protein 35) (CBP 35) (Galactose-specific lectin 3) (Galactoside-binding protein) (GALBP) (IgE-binding protein) (L-31) (Laminin-binding protein) (Lectin L-29) (Mac-2 antigen) | Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes. {ECO:0000250, ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:19594635, ECO:0000269|PubMed:19616076, ECO:0000269|PubMed:27693506}. |
| P17987 | TCP1 | S6 | ochoa | T-complex protein 1 subunit alpha (TCP-1-alpha) (EC 3.6.1.-) (CCT-alpha) (Chaperonin containing T-complex polypeptide 1 subunit 1) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
| P19174 | PLCG1 | S6 | ochoa | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC 3.1.4.11) (PLC-148) (Phosphoinositide phospholipase C-gamma-1) (Phospholipase C-II) (PLC-II) (Phospholipase C-gamma-1) (PLC-gamma-1) | Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, EGFR, FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Plays a role in actin reorganization and cell migration (PubMed:17229814). Guanine nucleotide exchange factor that binds the GTPase DNM1 and catalyzes the dissociation of GDP, allowing a GTP molecule to bind in its place, therefore enhancing DNM1-dependent endocytosis (By similarity). {ECO:0000250|UniProtKB:P10686, ECO:0000269|PubMed:17229814, ECO:0000269|PubMed:37422272}. |
| P19388 | POLR2E | T7 | ochoa | DNA-directed RNA polymerases I, II, and III subunit RPABC1 (RNA polymerases I, II, and III subunit ABC1) (DNA-directed RNA polymerase II 23 kDa polypeptide) (DNA-directed RNA polymerase II subunit E) (RPB5 homolog) (XAP4) | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPABC1 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. {ECO:0000250|UniProtKB:P20434, ECO:0000269|PubMed:16809778, ECO:0000269|PubMed:20413673, ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596, ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492, ECO:0000269|PubMed:9852112}. |
| P19525 | EIF2AK2 | S6 | psp | Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase) | IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (PubMed:18835251, PubMed:19189853, PubMed:19507191, PubMed:21072047, PubMed:21123651, PubMed:22381929, PubMed:22948139, PubMed:23229543). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (PubMed:19189853, PubMed:21123651, PubMed:22948139, PubMed:23229543). Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1) (PubMed:11836380, PubMed:19189853, PubMed:19840259, PubMed:20171114, PubMed:21710204, PubMed:23115276, PubMed:23399035). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11 (PubMed:11836380, PubMed:19229320, PubMed:22214662). In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteasomal degradation (PubMed:20395957). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (PubMed:22948139, PubMed:23084476, PubMed:23372823). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (PubMed:10848580, PubMed:15121867, PubMed:15229216). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (PubMed:20685959). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (PubMed:20685959). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (PubMed:22801494). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (By similarity). {ECO:0000250|UniProtKB:Q03963, ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:11836380, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15229216, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:19189853, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19507191, ECO:0000269|PubMed:19840259, ECO:0000269|PubMed:20171114, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20685959, ECO:0000269|PubMed:21072047, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21710204, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:22381929, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948139, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:23115276, ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:23372823, ECO:0000269|PubMed:23399035, ECO:0000269|PubMed:32197074}. |
| P19971 | TYMP | T6 | ochoa | Thymidine phosphorylase (TP) (EC 2.4.2.4) (Gliostatin) (Platelet-derived endothelial cell growth factor) (PD-ECGF) (TdRPase) | May have a role in maintaining the integrity of the blood vessels. Has growth promoting activity on endothelial cells, angiogenic activity in vivo and chemotactic activity on endothelial cells in vitro. {ECO:0000269|PubMed:1590793}.; FUNCTION: Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. {ECO:0000269|PubMed:1590793}. |
| P20339 | RAB5A | T7 | psp | Ras-related protein Rab-5A (EC 3.6.5.2) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes (PubMed:10818110, PubMed:14617813, PubMed:15378032, PubMed:16410077). Contributes to the regulation of filopodia extension (PubMed:14978216). Required for the exosomal release of SDCBP, CD63, PDCD6IP and syndecan (PubMed:22660413). Regulates maturation of apoptotic cell-containing phagosomes, probably downstream of DYN2 and PIK3C3 (By similarity). {ECO:0000250|UniProtKB:Q9CQD1, ECO:0000269|PubMed:10818110, ECO:0000269|PubMed:14617813, ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:16410077, ECO:0000269|PubMed:22660413}. |
| P20648 | ATP4A | Y7 | psp | Potassium-transporting ATPase alpha chain 1 (EC 7.2.2.19) (Gastric H(+)/K(+) ATPase subunit alpha) (Proton pump) | The catalytic subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Uses ATP as an energy source to pump H(+) ions to the gastric lumen while transporting K(+) ion from the lumen into the cell (By similarity). Remarkably generates a million-fold proton gradient across the gastric parietal cell membrane, acidifying the gastric juice down to pH 1 (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). The release of the H(+) ion in the stomach lumen is followed by binding of K(+) ion converting the pump conformation back to the E1 state (By similarity). {ECO:0000250|UniProtKB:P09626, ECO:0000250|UniProtKB:P19156, ECO:0000250|UniProtKB:Q64436}. |
| P22392 | NME2 | T7 | ochoa | Nucleoside diphosphate kinase B (NDK B) (NDP kinase B) (EC 2.7.4.6) (C-myc purine-binding transcription factor PUF) (Histidine protein kinase NDKB) (EC 2.7.13.3) (nm23-H2) | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Negatively regulates Rho activity by interacting with AKAP13/LBC (PubMed:15249197). Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:19435876, PubMed:8392752). Binds to both single-stranded guanine- and cytosine-rich strands within the nuclease hypersensitive element (NHE) III(1) region of the MYC gene promoter. Does not bind to duplex NHE III(1) (PubMed:19435876). Has G-quadruplex (G4) DNA-binding activity, which is independent of its nucleotide-binding and kinase activity. Binds both folded and unfolded G4 with similar low nanomolar affinities. Stabilizes folded G4s regardless of whether they are prefolded or not (PubMed:25679041). Exhibits histidine protein kinase activity (PubMed:20946858). {ECO:0000250|UniProtKB:P36010, ECO:0000269|PubMed:15249197, ECO:0000269|PubMed:19435876, ECO:0000269|PubMed:20946858, ECO:0000269|PubMed:25679041, ECO:0000269|PubMed:8392752}. |
| P23396 | RPS3 | S6 | 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}. |
| P25440 | BRD2 | T6 | ochoa | Bromodomain-containing protein 2 (O27.1.1) | Chromatin reader protein that specifically recognizes and binds histone H4 acetylated at 'Lys-5' and 'Lys-12' (H4K5ac and H4K12ac, respectively), thereby controlling gene expression and remodeling chromatin structures (PubMed:17148447, PubMed:17848202, PubMed:18406326, PubMed:20048151, PubMed:20709061, PubMed:20871596). Recruits transcription factors and coactivators to target gene sites, and activates RNA polymerase II machinery for transcriptional elongation (PubMed:28262505). Plays a key role in genome compartmentalization via its association with CTCF and cohesin: recruited to chromatin by CTCF and promotes formation of topologically associating domains (TADs) via its ability to bind acetylated histones, contributing to CTCF boundary formation and enhancer insulation (PubMed:35410381). Also recognizes and binds acetylated non-histone proteins, such as STAT3 (PubMed:28262505). Involved in inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17: recognizes and binds STAT3 acetylated at 'Lys-87', promoting STAT3 recruitment to chromatin (PubMed:28262505). In addition to acetylated lysines, also recognizes and binds lysine residues on histones that are both methylated and acetylated on the same side chain to form N6-acetyl-N6-methyllysine (Kacme), an epigenetic mark of active chromatin associated with increased transcriptional initiation (PubMed:37731000). Specifically binds histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively) (PubMed:37731000). {ECO:0000269|PubMed:17148447, ECO:0000269|PubMed:17848202, ECO:0000269|PubMed:18406326, ECO:0000269|PubMed:20048151, ECO:0000269|PubMed:20709061, ECO:0000269|PubMed:20871596, ECO:0000269|PubMed:28262505, ECO:0000269|PubMed:35410381, ECO:0000269|PubMed:37731000}. |
| P25787 | PSMA2 | S7 | ochoa | Proteasome subunit alpha type-2 (Macropain subunit C3) (Multicatalytic endopeptidase complex subunit C3) (Proteasome component C3) (Proteasome subunit alpha-2) (alpha-2) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
| P26232 | CTNNA2 | S6 | ochoa | Catenin alpha-2 (Alpha N-catenin) (Alpha-catenin-related protein) | May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system (By similarity). Required for proper regulation of cortical neuronal migration and neurite growth (PubMed:30013181). It acts as a negative regulator of Arp2/3 complex activity and Arp2/3-mediated actin polymerization (PubMed:30013181). It thereby suppresses excessive actin branching which would impair neurite growth and stability (PubMed:30013181). Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation (By similarity). {ECO:0000250|UniProtKB:Q61301, ECO:0000269|PubMed:30013181}. |
| P26639 | TARS1 | S7 | ochoa | Threonine--tRNA ligase 1, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase 1) | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (PubMed:25824639, PubMed:31374204). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage (By similarity). {ECO:0000250|UniProtKB:Q9D0R2, ECO:0000269|PubMed:25824639, ECO:0000269|PubMed:31374204}. |
| P26641 | EEF1G | Y7 | ochoa | Elongation factor 1-gamma (EF-1-gamma) (eEF-1B gamma) | Probably plays a role in anchoring the complex to other cellular components. |
| P28290 | ITPRID2 | S6 | ochoa | Protein ITPRID2 (Cleavage signal-1 protein) (CS-1) (ITPR-interacting domain-containing protein 2) (Ki-ras-induced actin-interacting protein) (Sperm-specific antigen 2) | None |
| P28290 | ITPRID2 | S7 | ochoa | Protein ITPRID2 (Cleavage signal-1 protein) (CS-1) (ITPR-interacting domain-containing protein 2) (Ki-ras-induced actin-interacting protein) (Sperm-specific antigen 2) | None |
| P28347 | TEAD1 | S7 | ochoa | Transcriptional enhancer factor TEF-1 (NTEF-1) (Protein GT-IIC) (TEA domain family member 1) (TEAD-1) (Transcription factor 13) (TCF-13) | Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and cooperatively to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription in vivo in a cell-specific manner. The activation function appears to be mediated by a limiting cell-specific transcriptional intermediary factor (TIF). Involved in cardiac development. Binds to the M-CAT motif. {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}. |
| P30519 | HMOX2 | T7 | ochoa | Heme oxygenase 2 (HO-2) (EC 1.14.14.18) [Cleaved into: Heme oxygenase 2 soluble form] | [Heme oxygenase 2]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. {ECO:0000269|PubMed:1575508, ECO:0000269|PubMed:7890772}.; FUNCTION: [Heme oxygenase 2 soluble form]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. {ECO:0000269|PubMed:7890772}. |
| P30520 | ADSS2 | Y7 | ochoa | Adenylosuccinate synthetase isozyme 2 (AMPSase 2) (AdSS 2) (EC 6.3.4.4) (Adenylosuccinate synthetase, acidic isozyme) (Adenylosuccinate synthetase, liver isozyme) (L-type adenylosuccinate synthetase) (IMP--aspartate ligase 2) | Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000250|UniProtKB:P46664}. |
| P31946 | YWHAB | S6 | ochoa | 14-3-3 protein beta/alpha (Protein 1054) (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein beta/alpha, N-terminally processed] | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13. {ECO:0000269|PubMed:17717073, ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21224381}. |
| P31949 | S100A11 | S6 | ochoa | Protein S100-A11 (Calgizzarin) (Metastatic lymph node gene 70 protein) (MLN 70) (Protein S100-C) (S100 calcium-binding protein A11) [Cleaved into: Protein S100-A11, N-terminally processed] | Facilitates the differentiation and the cornification of keratinocytes. {ECO:0000269|PubMed:18618420}. |
| P33241 | LSP1 | S6 | ochoa | Lymphocyte-specific protein 1 (47 kDa actin-binding protein) (52 kDa phosphoprotein) (pp52) (Lymphocyte-specific antigen WP34) | May play a role in mediating neutrophil activation and chemotaxis. {ECO:0000250}. |
| P33981 | TTK | S7 | ochoa|psp | Dual specificity protein kinase TTK (EC 2.7.12.1) (Phosphotyrosine picked threonine-protein kinase) (PYT) | Involved in mitotic spindle assembly checkpoint signaling, a process that delays anaphase until chromosomes are bioriented on the spindle, and in the repair of incorrect mitotic kinetochore-spindle microtubule attachments (PubMed:18243099, PubMed:28441529, PubMed:29162720). Phosphorylates MAD1L1 to promote the mitotic spindle assembly checkpoint (PubMed:18243099, PubMed:29162720). Phosphorylates CDCA8/Borealin leading to enhanced AURKB activity at the kinetochore (PubMed:18243099). Phosphorylates SKA3 at 'Ser-34' leading to dissociation of the SKA complex from microtubules and destabilization of microtubule-kinetochore attachments (PubMed:28441529). Phosphorylates KNL1, KNTC1 and autophosphorylates (PubMed:28441529). Phosphorylates MCRS1 which enhances recruitment of KIF2A to the minus end of spindle microtubules and promotes chromosome alignment (PubMed:30785839). {ECO:0000269|PubMed:18243099, ECO:0000269|PubMed:28441529, ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:30785839}. |
| P33991 | MCM4 | S6 | ochoa | DNA replication licensing factor MCM4 (EC 3.6.4.12) (CDC21 homolog) (P1-CDC21) | Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:16899510, PubMed:25661590, PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232, PubMed:9305914). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:16899510, PubMed:25661590, PubMed:32453425, PubMed:9305914). {ECO:0000269|PubMed:16899510, ECO:0000269|PubMed:25661590, ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232, ECO:0000269|PubMed:9305914}. |
| P33991 | MCM4 | T7 | ochoa|psp | DNA replication licensing factor MCM4 (EC 3.6.4.12) (CDC21 homolog) (P1-CDC21) | Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:16899510, PubMed:25661590, PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232, PubMed:9305914). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:16899510, PubMed:25661590, PubMed:32453425, PubMed:9305914). {ECO:0000269|PubMed:16899510, ECO:0000269|PubMed:25661590, ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232, ECO:0000269|PubMed:9305914}. |
| P35568 | IRS1 | S7 | psp | Insulin receptor substrate 1 (IRS-1) | Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:7541045, PubMed:33991522, PubMed:38625937). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:19639489). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:11171109, PubMed:8265614). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100). {ECO:0000250|UniProtKB:P35570, ECO:0000269|PubMed:11171109, ECO:0000269|PubMed:16878150, ECO:0000269|PubMed:19639489, ECO:0000269|PubMed:38625937, ECO:0000269|PubMed:7541045, ECO:0000269|PubMed:8265614}. |
| P35637 | FUS | T7 | psp | RNA-binding protein FUS (75 kDa DNA-pairing protein) (Oncogene FUS) (Oncogene TLS) (POMp75) (Translocated in liposarcoma protein) | DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response (PubMed:27731383). Binds to ssRNA containing the consensus sequence 5'-AGGUAA-3' (PubMed:21256132). Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing (PubMed:26124092). Also binds its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay (PubMed:24204307). Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous recombination during DNA double-strand break repair (PubMed:10567410). In neuronal cells, plays crucial roles in dendritic spine formation and stability, RNA transport, mRNA stability and synaptic homeostasis (By similarity). {ECO:0000250|UniProtKB:P56959, ECO:0000269|PubMed:10567410, ECO:0000269|PubMed:21256132, ECO:0000269|PubMed:24204307, ECO:0000269|PubMed:26124092, ECO:0000269|PubMed:27731383}. |
| P35712 | SOX6 | T7 | ochoa | Transcription factor SOX-6 | Transcription factor that plays a key role in several developmental processes, including neurogenesis, chondrocytes differentiation and cartilage formation (Probable). Specifically binds the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis. Required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on active enhancers and super-enhancers associated with cartilage-specific genes, and thereby potentiate SOX9's ability to transactivate. Not involved in precartilaginous condensation, the first step in chondrogenesis, during which skeletal progenitors differentiate into prechondrocytes. Together with SOX5, required to form and maintain a pool of highly proliferating chondroblasts between epiphyses and metaphyses, to form columnar chondroblasts, delay chondrocyte prehypertrophy but promote hypertrophy, and to delay terminal differentiation of chondrocytes on contact with ossification fronts. Binds to the proximal promoter region of the myelin protein MPZ gene, and is thereby involved in the differentiation of oligodendroglia in the developing spinal tube. Binds to the gene promoter of MBP and acts as a transcriptional repressor (By similarity). {ECO:0000250|UniProtKB:P40645, ECO:0000305|PubMed:32442410}. |
| P35716 | SOX11 | S7 | ochoa | Transcription factor SOX-11 | Transcription factor that acts as a transcriptional activator (PubMed:24886874, PubMed:26543203). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (By similarity). Acts as a transcriptional activator of TEAD2 by binding to its gene promoter and first intron (By similarity). Plays a redundant role with SOX4 and SOX12 in cell survival of developing tissues such as the neural tube, branchial arches and somites, thereby contributing to organogenesis (By similarity). {ECO:0000250|UniProtKB:Q7M6Y2, ECO:0000269|PubMed:24886874, ECO:0000269|PubMed:26543203}. |
| P38435 | GGCX | S7 | ochoa | Vitamin K-dependent gamma-carboxylase (EC 4.1.1.90) (Gamma-glutamyl carboxylase) (Peptidyl-glutamate 4-carboxylase) (Vitamin K gamma glutamyl carboxylase) | Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide (PubMed:17073445). Catalyzes gamma-carboxylation of various proteins, such as blood coagulation factors (F2, F7, F9 and F10), osteocalcin (BGLAP) or matrix Gla protein (MGP) (PubMed:17073445). {ECO:0000269|PubMed:17073445}. |
| P40227 | CCT6A | T6 | psp | 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}. |
| P41236 | PPP1R2 | S7 | ochoa | Protein phosphatase inhibitor 2 (IPP-2) | Inhibitor of protein-phosphatase 1. |
| P41743 | PRKCI | S7 | ochoa | Protein kinase C iota type (EC 2.7.11.13) (Atypical protein kinase C-lambda/iota) (PRKC-lambda/iota) (aPKC-lambda/iota) (nPKC-iota) | Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (By similarity). {ECO:0000250|UniProtKB:F1M7Y5, ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10467349, ECO:0000269|PubMed:10906326, ECO:0000269|PubMed:11042363, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:12871960, ECO:0000269|PubMed:14684752, ECO:0000269|PubMed:15994303, ECO:0000269|PubMed:18270268, ECO:0000269|PubMed:19327373, ECO:0000269|PubMed:21189248, ECO:0000269|PubMed:21419810, ECO:0000269|PubMed:8226978, ECO:0000269|PubMed:9346882}. |
| P42771 | CDKN2A | S7 | psp | Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (Multiple tumor suppressor 1) (MTS-1) (p16-INK4a) (p16-INK4) (p16INK4A) | Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein. {ECO:0000269|PubMed:16782892, ECO:0000269|PubMed:7972006}. |
| P43007 | SLC1A4 | T7 | ochoa | Neutral amino acid transporter A (Alanine/serine/cysteine/threonine transporter 1) (ASCT-1) (Solute carrier family 1 member 4) | Sodium-dependent neutral amino-acid transporter that mediates transport of alanine, serine, cysteine, proline, hydroxyproline and threonine. {ECO:0000269|PubMed:14502423, ECO:0000269|PubMed:26041762, ECO:0000269|PubMed:8101838, ECO:0000269|PubMed:8340364}. |
| P43487 | RANBP1 | T7 | ochoa | Ran-specific GTPase-activating protein (Ran-binding protein 1) (RanBP1) | Plays a role in RAN-dependent nucleocytoplasmic transport. Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and mediates the dissociation of RAN from proteins involved in transport into the nucleus (By similarity). Induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (PubMed:20485264). Promotes the disassembly of the complex formed by RAN and importin beta. Promotes dissociation of RAN from a complex with KPNA2 and CSE1L (By similarity). Required for normal mitotic spindle assembly and normal progress through mitosis via its effect on RAN (PubMed:17671426). Does not increase the RAN GTPase activity by itself, but increases GTP hydrolysis mediated by RANGAP1 (PubMed:7882974). Inhibits RCC1-dependent exchange of RAN-bound GDP by GTP (PubMed:7616957, PubMed:7882974). {ECO:0000250|UniProtKB:P34022, ECO:0000269|PubMed:17671426, ECO:0000269|PubMed:20485264, ECO:0000269|PubMed:7616957, ECO:0000269|PubMed:7882974}. |
| P45985 | MAP2K4 | S7 | ochoa | Dual specificity mitogen-activated protein kinase kinase 4 (MAP kinase kinase 4) (MAPKK 4) (EC 2.7.12.2) (JNK-activating kinase 1) (MAPK/ERK kinase 4) (MEK 4) (SAPK/ERK kinase 1) (SEK1) (Stress-activated protein kinase kinase 1) (SAPK kinase 1) (SAPKK-1) (SAPKK1) (c-Jun N-terminal kinase kinase 1) (JNKK) | Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K7/MKK7, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The phosphorylation of the Thr residue by MAP2K7/MKK7 seems to be the prerequisite for JNK activation at least in response to pro-inflammatory cytokines, while other stimuli activate both MAP2K4/MKK4 and MAP2K7/MKK7 which synergistically phosphorylate JNKs. MAP2K4 is required for maintaining peripheral lymphoid homeostasis. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7 exclusively activates JNKs, MAP2K4/MKK4 additionally activates the p38 MAPKs MAPK11, MAPK12, MAPK13 and MAPK14. {ECO:0000269|PubMed:7716521}. |
| P46019 | PHKA2 | S7 | ochoa | Phosphorylase b kinase regulatory subunit alpha, liver isoform (Phosphorylase kinase alpha L subunit) | Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin. |
| P46020 | PHKA1 | S7 | ochoa | Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform (Phosphorylase kinase alpha M subunit) | Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin. |
| P46379 | BAG6 | S6 | ochoa | Large proline-rich protein BAG6 (BAG family molecular chaperone regulator 6) (BCL2-associated athanogene 6) (BAG-6) (HLA-B-associated transcript 3) (Protein G3) (Protein Scythe) | ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins (PubMed:21636303). Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation (PubMed:20516149, PubMed:21636303, PubMed:21743475, PubMed:28104892). The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum (PubMed:20516149, PubMed:20676083, PubMed:25535373, PubMed:28104892). Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome (PubMed:24981174, PubMed:27193484, PubMed:28104892). SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins (PubMed:23129660, PubMed:25179605, PubMed:27193484). Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum (PubMed:21743475). The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome (PubMed:21636303). BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response (By similarity). BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress (PubMed:26565908). By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis (By similarity). Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1 (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). {ECO:0000250|UniProtKB:Q9Z1R2, ECO:0000269|PubMed:20516149, ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:21743475, ECO:0000269|PubMed:23129660, ECO:0000269|PubMed:24981174, ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:26565908, ECO:0000269|PubMed:26692333, ECO:0000269|PubMed:27193484, ECO:0000269|PubMed:28104892}.; FUNCTION: Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity (PubMed:17403783). When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2) (PubMed:18765639). {ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:18765639}.; FUNCTION: Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC). {ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}.; FUNCTION: Mediates ricin-induced apoptosis. {ECO:0000269|PubMed:14960581}. |
| P46379 | BAG6 | T7 | ochoa | Large proline-rich protein BAG6 (BAG family molecular chaperone regulator 6) (BCL2-associated athanogene 6) (BAG-6) (HLA-B-associated transcript 3) (Protein G3) (Protein Scythe) | ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins (PubMed:21636303). Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation (PubMed:20516149, PubMed:21636303, PubMed:21743475, PubMed:28104892). The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum (PubMed:20516149, PubMed:20676083, PubMed:25535373, PubMed:28104892). Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome (PubMed:24981174, PubMed:27193484, PubMed:28104892). SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins (PubMed:23129660, PubMed:25179605, PubMed:27193484). Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum (PubMed:21743475). The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome (PubMed:21636303). BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response (By similarity). BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress (PubMed:26565908). By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis (By similarity). Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1 (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). {ECO:0000250|UniProtKB:Q9Z1R2, ECO:0000269|PubMed:20516149, ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:21743475, ECO:0000269|PubMed:23129660, ECO:0000269|PubMed:24981174, ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:26565908, ECO:0000269|PubMed:26692333, ECO:0000269|PubMed:27193484, ECO:0000269|PubMed:28104892}.; FUNCTION: Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity (PubMed:17403783). When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2) (PubMed:18765639). {ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:18765639}.; FUNCTION: Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC). {ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}.; FUNCTION: Mediates ricin-induced apoptosis. {ECO:0000269|PubMed:14960581}. |
| P46734 | MAP2K3 | S6 | ochoa | Dual specificity mitogen-activated protein kinase kinase 3 (MAP kinase kinase 3) (MAPKK 3) (EC 2.7.12.2) (MAPK/ERK kinase 3) (MEK 3) (Stress-activated protein kinase kinase 2) (SAPK kinase 2) (SAPKK-2) (SAPKK2) | Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. {ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:8622669}. |
| P46734 | MAP2K3 | S7 | ochoa | Dual specificity mitogen-activated protein kinase kinase 3 (MAP kinase kinase 3) (MAPKK 3) (EC 2.7.12.2) (MAPK/ERK kinase 3) (MEK 3) (Stress-activated protein kinase kinase 2) (SAPK kinase 2) (SAPKK-2) (SAPKK2) | Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. {ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:8622669}. |
| P47712 | PLA2G4A | Y7 | ochoa | Cytosolic phospholipase A2 (cPLA2) (Phospholipase A2 group IVA) [Includes: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase); Lysophospholipase (EC 3.1.1.5)] | Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (PubMed:10358058, PubMed:14709560, PubMed:16617059, PubMed:17472963, PubMed:18451993, PubMed:27642067, PubMed:7794891, PubMed:8619991, PubMed:8702602, PubMed:9425121). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:10358058, PubMed:17472963, PubMed:18451993, PubMed:7794891, PubMed:8619991, PubMed:9425121). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway (PubMed:10358058, PubMed:17472963, PubMed:18451993, PubMed:7794891, PubMed:9425121). In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids (PubMed:27642067). Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific (PubMed:7794891). Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides (PubMed:12672805). Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (PubMed:7794891). {ECO:0000250|UniProtKB:P47713, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:14709560, ECO:0000269|PubMed:16617059, ECO:0000269|PubMed:17472963, ECO:0000269|PubMed:18451993, ECO:0000269|PubMed:27642067, ECO:0000269|PubMed:7794891, ECO:0000269|PubMed:8619991, ECO:0000269|PubMed:8702602, ECO:0000269|PubMed:9425121}. |
| P48059 | LIMS1 | S7 | ochoa | LIM and senescent cell antigen-like-containing domain protein 1 (Particularly interesting new Cys-His protein 1) (PINCH-1) (Renal carcinoma antigen NY-REN-48) | Within the IPP (ILK-PINCH-PARVIN) complex, binds to F-actin, promoting F-actin bundling, a process required to generate force for actin cytoskeleton reorganization and subsequent dynamic cell adhesion events such as cell spreading and migration. {ECO:0000269|PubMed:30367047}. |
| P48651 | PTDSS1 | S7 | ochoa | Phosphatidylserine synthase 1 (PSS-1) (PtdSer synthase 1) (EC 2.7.8.29) (Serine-exchange enzyme I) | Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine (PubMed:19014349, PubMed:24241535). Catalyzes mainly the conversion of phosphatidylcholine (PubMed:19014349, PubMed:24241535). Also converts, in vitro and to a lesser extent, phosphatidylethanolamine (PubMed:19014349, PubMed:24241535). {ECO:0000269|PubMed:19014349, ECO:0000269|PubMed:24241535}. |
| P49321 | NASP | T6 | ochoa | Nuclear autoantigenic sperm protein (NASP) | Component of the histone chaperone network (PubMed:22195965). Binds and stabilizes histone H3-H4 not bound to chromatin to maintain a soluble reservoir and modulate degradation by chaperone-mediated autophagy (PubMed:22195965). Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA. {ECO:0000250|UniProtKB:Q99MD9, ECO:0000269|PubMed:22195965}.; FUNCTION: [Isoform 1]: Stabilizes soluble histone H3-H4. {ECO:0000269|PubMed:22195965}.; FUNCTION: [Isoform 2]: Stabilizes soluble histone H3-H4. {ECO:0000269|PubMed:22195965}. |
| P49356 | FNTB | S6 | ochoa | Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Ras proteins prenyltransferase subunit beta) | Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8494894}. |
| P49450 | CENPA | S7 | psp | Histone H3-like centromeric protein A (Centromere autoantigen A) (Centromere protein A) (CENP-A) | Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes (PubMed:11756469, PubMed:14667408, PubMed:15282608, PubMed:15475964, PubMed:15702419, PubMed:17651496, PubMed:19114591, PubMed:20739937, PubMed:27499292, PubMed:7962047, PubMed:9024683). Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore (PubMed:18072184). The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wrapped around the nucleosome and gives rise to protruding DNA ends that are less well-ordered and rigid compared to nucleosomes containing histone H3 (PubMed:26878239, PubMed:27499292). May serve as an epigenetic mark that propagates centromere identity through replication and cell division (PubMed:15282608, PubMed:15475964, PubMed:20739937, PubMed:21478274, PubMed:26878239). Required for recruitment and assembly of kinetochore proteins, and as a consequence required for progress through mitosis, chromosome segregation and cytokinesis (PubMed:11756469, PubMed:14667408, PubMed:18072184, PubMed:23818633, PubMed:25556658, PubMed:27499292). {ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:14667408, ECO:0000269|PubMed:15282608, ECO:0000269|PubMed:15475964, ECO:0000269|PubMed:15702419, ECO:0000269|PubMed:17651496, ECO:0000269|PubMed:18072184, ECO:0000269|PubMed:19114591, ECO:0000269|PubMed:21478274, ECO:0000269|PubMed:23818633, ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:26878239, ECO:0000269|PubMed:27499292, ECO:0000269|PubMed:7962047, ECO:0000269|PubMed:9024683, ECO:0000305|PubMed:20739937}. |
| P49736 | MCM2 | S7 | ochoa|psp | DNA replication licensing factor MCM2 (EC 3.6.4.12) (Minichromosome maintenance protein 2 homolog) (Nuclear protein BM28) | Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:32453425). Required for the entry in S phase and for cell division (PubMed:8175912). Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis (PubMed:26196677). {ECO:0000269|PubMed:26196677, ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232, ECO:0000269|PubMed:8175912}. |
| P49753 | ACOT2 | S7 | ochoa | Acyl-coenzyme A thioesterase 2, mitochondrial (Acyl-CoA thioesterase 2) (EC 3.1.2.2) (Acyl-coenzyme A thioester hydrolase 2a) (CTE-Ia) (Long-chain acyl-CoA thioesterase 2) (ZAP128) | Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:10944470, PubMed:16940157). Displays higher activity toward long chain acyl CoAs (C14-C20) (PubMed:10944470, PubMed:16940157). The enzyme is involved in enhancing the hepatic fatty acid oxidation in mitochondria (By similarity). {ECO:0000250|UniProtKB:Q9QYR9, ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:16940157}. |
| P49757 | NUMB | S7 | psp | Protein numb homolog (h-Numb) (Protein S171) | Regulates clathrin-mediated receptor endocytosis (PubMed:18657069). Plays a role in the process of neurogenesis (By similarity). Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate (By similarity). Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity (By similarity). May also mediate local repair of brain ventricular wall damage (By similarity). {ECO:0000250|UniProtKB:Q9QZS3, ECO:0000269|PubMed:18657069}. |
| P49810 | PSEN2 | S7 | psp | Presenilin-2 (PS-2) (EC 3.4.23.-) (AD3LP) (AD5) (E5-1) (STM-2) [Cleaved into: Presenilin-2 NTF subunit; Presenilin-2 CTF subunit] | Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is involved in calcium homeostasis (PubMed:16959576). Is a regulator of mitochondrion-endoplasmic reticulum membrane tethering and modulates calcium ions shuttling between ER and mitochondria (PubMed:21285369). {ECO:0000269|PubMed:10497236, ECO:0000269|PubMed:10652302, ECO:0000269|PubMed:16959576, ECO:0000269|PubMed:21285369}. |
| P49840 | GSK3A | S7 | ochoa | Glycogen synthase kinase-3 alpha (GSK-3 alpha) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3A) (EC 2.7.11.1) | Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1 (PubMed:11749387, PubMed:17478001, PubMed:19366350). Requires primed phosphorylation of the majority of its substrates (PubMed:11749387, PubMed:17478001, PubMed:19366350). Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (PubMed:11749387, PubMed:17478001, PubMed:19366350). Regulates glycogen metabolism in liver, but not in muscle (By similarity). May also mediate the development of insulin resistance by regulating activation of transcription factors (PubMed:10868943, PubMed:17478001). In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin (PubMed:17229088). Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease (PubMed:12761548). May be involved in the regulation of replication in pancreatic beta-cells (By similarity). Is necessary for the establishment of neuronal polarity and axon outgrowth (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions which activates KAT5/TIP60 acetyltransferase activity and promotes acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (By similarity). Phosphorylates mTORC2 complex component RICTOR at 'Thr-1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR (PubMed:25897075). {ECO:0000250|UniProtKB:P18265, ECO:0000250|UniProtKB:P49841, ECO:0000250|UniProtKB:Q2NL51, ECO:0000269|PubMed:10868943, ECO:0000269|PubMed:12761548, ECO:0000269|PubMed:17229088, ECO:0000269|PubMed:25897075, ECO:0000269|PubMed:30704899, ECO:0000303|PubMed:11749387, ECO:0000303|PubMed:17478001, ECO:0000303|PubMed:19366350}. |
| P49841 | GSK3B | T7 | ochoa | Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1) | Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1 (PubMed:11430833, PubMed:12554650, PubMed:14690523, PubMed:16484495, PubMed:1846781, PubMed:20937854, PubMed:9072970). Requires primed phosphorylation of the majority of its substrates (PubMed:11430833, PubMed:16484495). In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (PubMed:8397507). May also mediate the development of insulin resistance by regulating activation of transcription factors (PubMed:8397507). Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase (PubMed:8397507). In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes (PubMed:12554650). Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA (PubMed:1846781). Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin (PubMed:9072970). Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules (PubMed:14690523). MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease (PubMed:14690523). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair (By similarity). Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA) (By similarity). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin (PubMed:9819408). Is necessary for the establishment of neuronal polarity and axon outgrowth (PubMed:20067585). Phosphorylates MARK2, leading to inhibition of its activity (By similarity). Phosphorylates SIK1 at 'Thr-182', leading to sustainment of its activity (PubMed:18348280). Phosphorylates ZC3HAV1 which enhances its antiviral activity (PubMed:22514281). Phosphorylates SNAI1, leading to its ubiquitination and proteasomal degradation (PubMed:15448698, PubMed:15647282, PubMed:25827072, PubMed:29059170). Phosphorylates SFPQ at 'Thr-687' upon T-cell activation (PubMed:20932480). Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including BMAL1, CLOCK and PER2 (PubMed:19946213, PubMed:28903391). Phosphorylates FBXL2 at 'Thr-404' and primes it for ubiquitination by the SCF(FBXO3) complex and proteasomal degradation (By similarity). Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation (PubMed:19946213). Phosphorylates BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation (PubMed:28903391). Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation (PubMed:24391509). Regulates the circadian rhythmicity of hippocampal long-term potentiation and BMAL1 and PER2 expression (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, activating KAT5/TIP60 acetyltransferase activity and promoting acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (PubMed:18846110). Phosphorylates E2F1, promoting the interaction between E2F1 and USP11, stabilizing E2F1 and promoting its activity (PubMed:17050006, PubMed:28992046). Phosphorylates mTORC2 complex component RICTOR at 'Ser-1235' in response to endoplasmic stress, inhibiting mTORC2 (PubMed:21343617). Phosphorylates mTORC2 complex component RICTOR at 'Thr-1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR (PubMed:25897075). Phosphorylates FXR1, promoting FXR1 ubiquitination by the SCF(FBXO4) complex and FXR1 degradation by the proteasome (By similarity). Phosphorylates interleukin-22 receptor subunit IL22RA1, preventing its proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P18266, ECO:0000250|UniProtKB:Q9WV60, ECO:0000269|PubMed:11430833, ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15448698, ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:17050006, ECO:0000269|PubMed:18348280, ECO:0000269|PubMed:1846781, ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20067585, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:21343617, ECO:0000269|PubMed:22514281, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:25827072, ECO:0000269|PubMed:25897075, ECO:0000269|PubMed:28903391, ECO:0000269|PubMed:28992046, ECO:0000269|PubMed:29059170, ECO:0000269|PubMed:30704899, ECO:0000269|PubMed:8397507, ECO:0000269|PubMed:9072970, ECO:0000269|PubMed:9819408}. |
| P49902 | NT5C2 | S6 | ochoa | Cytosolic purine 5'-nucleotidase (EC 3.1.3.5) (EC 3.1.3.99) (Cytosolic 5'-nucleotidase II) (cN-II) (Cytosolic IMP/GMP-specific 5'-nucleotidase) (Cytosolic nucleoside phosphotransferase 5'N) (EC 2.7.1.77) (High Km 5'-nucleotidase) | Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates (PubMed:10092873, PubMed:12907246, PubMed:1659319, PubMed:9371705). In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferably inosine, deoxyinosine and guanosine (PubMed:1659319, PubMed:9371705). Has the highest activities for IMP and GMP followed by dIMP, dGMP and XMP (PubMed:10092873, PubMed:12907246, PubMed:1659319, PubMed:9371705). Could also catalyze the transfer of phosphates from pyrimidine monophosphates but with lower efficiency (PubMed:1659319, PubMed:9371705). Through these activities regulates the purine nucleoside/nucleotide pools within the cell (PubMed:10092873, PubMed:12907246, PubMed:1659319, PubMed:9371705). {ECO:0000269|PubMed:10092873, ECO:0000269|PubMed:12907246, ECO:0000269|PubMed:1659319, ECO:0000269|PubMed:9371705}. |
| P49903 | SEPHS1 | S6 | ochoa | Selenide, water dikinase 1 (EC 2.7.9.3) (Selenium donor protein 1) (Selenophosphate synthase 1) | Synthesizes selenophosphate from selenide and ATP. {ECO:0000269|PubMed:7665581}. |
| P50151 | GNG10 | S6 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10 | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Interacts with beta-1 and beta-2, but not with beta-3. |
| P50548 | ERF | T7 | ochoa | ETS domain-containing transcription factor ERF (Ets2 repressor factor) (PE-2) | Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. May regulate other genes involved in cellular proliferation. Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment (By similarity). May be important for regulating trophoblast stem cell differentiation (By similarity). {ECO:0000250}. |
| P50750 | CDK9 | S7 | psp | Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit) | Protein kinase involved in the regulation of transcription (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:20930849, PubMed:28426094, PubMed:29335245). Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:16427012, PubMed:20930849, PubMed:28426094, PubMed:30134174). This complex is inactive when in the 7SK snRNP complex form (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:20930849, PubMed:28426094). Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR and the negative elongation factors DSIF and NELFE (PubMed:10912001, PubMed:11112772, PubMed:12037670, PubMed:16427012, PubMed:20081228, PubMed:20980437, PubMed:21127351, PubMed:9857195). Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling) (PubMed:17956865, PubMed:18362169). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis (PubMed:10393184, PubMed:11112772). P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export (PubMed:15564463, PubMed:19575011, PubMed:19844166). Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing (PubMed:15564463, PubMed:19575011, PubMed:19844166). The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro (PubMed:21127351). Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage (PubMed:20493174). In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6 (PubMed:20493174). Promotes cardiac myocyte enlargement (PubMed:20081228). RPB1/POLR2A phosphorylation on 'Ser-2' in CTD activates transcription (PubMed:21127351). AR phosphorylation modulates AR transcription factor promoter selectivity and cell growth. DSIF and NELF phosphorylation promotes transcription by inhibiting their negative effect (PubMed:10912001, PubMed:11112772, PubMed:9857195). The phosphorylation of MYOD1 enhances its transcriptional activity and thus promotes muscle differentiation (PubMed:12037670). Catalyzes phosphorylation of KAT5, promoting KAT5 recruitment to chromatin and histone acetyltransferase activity (PubMed:29335245). {ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11145967, ECO:0000269|PubMed:11575923, ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:11884399, ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:14701750, ECO:0000269|PubMed:15564463, ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:16427012, ECO:0000269|PubMed:17956865, ECO:0000269|PubMed:18362169, ECO:0000269|PubMed:19575011, ECO:0000269|PubMed:19844166, ECO:0000269|PubMed:20081228, ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:20930849, ECO:0000269|PubMed:20980437, ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:28426094, ECO:0000269|PubMed:29335245, ECO:0000269|PubMed:30134174, ECO:0000269|PubMed:9857195}. |
| P51610 | HCFC1 | S6 | ochoa | Host cell factor 1 (HCF) (HCF-1) (C1 factor) (CFF) (VCAF) (VP16 accessory protein) [Cleaved into: HCF N-terminal chain 1; HCF N-terminal chain 2; HCF N-terminal chain 3; HCF N-terminal chain 4; HCF N-terminal chain 5; HCF N-terminal chain 6; HCF C-terminal chain 1; HCF C-terminal chain 2; HCF C-terminal chain 3; HCF C-terminal chain 4; HCF C-terminal chain 5; HCF C-terminal chain 6] | Transcriptional coregulator (By similarity). Serves as a scaffold protein, bridging interactions between transcription factors, including THAP11 and ZNF143, and transcriptional coregulators (PubMed:26416877). Involved in control of the cell cycle (PubMed:10629049, PubMed:10779346, PubMed:15190068, PubMed:16624878, PubMed:23629655). Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300 (PubMed:10675337, PubMed:12244100). Coactivator for EGR2 and GABP2 (PubMed:12244100, PubMed:14532282). Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together (PubMed:12670868). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (PubMed:20200153). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852). Recruits KMT2E/MLL5 to E2F1 responsive promoters promoting transcriptional activation and thereby facilitates G1 to S phase transition (PubMed:23629655). Modulates expression of homeobox protein PDX1, perhaps acting in concert with transcription factor E2F1, thereby regulating pancreatic beta-cell growth and glucose-stimulated insulin secretion (By similarity). May negatively modulate transcriptional activity of FOXO3 (By similarity). {ECO:0000250|UniProtKB:D3ZN95, ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:10675337, ECO:0000269|PubMed:10779346, ECO:0000269|PubMed:12244100, ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:14532282, ECO:0000269|PubMed:15190068, ECO:0000269|PubMed:16624878, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:23629655, ECO:0000269|PubMed:26416877}.; FUNCTION: (Microbial infection) In case of human herpes simplex virus (HSV) infection, HCFC1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and POU2F1 thereby enabling the transcription of the viral immediate early genes. {ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:17578910}. |
| P51965 | UBE2E1 | S6 | ochoa | Ubiquitin-conjugating enzyme E2 E1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme E1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme E1) (UbcH6) (Ubiquitin carrier protein E1) (Ubiquitin-protein ligase E1) | Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination. Catalyzes monoubiquitination of other proteins in both an E3-dependent and E3-independent manner (PubMed:27237050). {ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:27237050}. |
| P52701 | MSH6 | T6 | ochoa | DNA mismatch repair protein Msh6 (hMSH6) (G/T mismatch-binding protein) (GTBP) (GTMBP) (MutS protein homolog 6) (MutS-alpha 160 kDa subunit) (p160) | Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction. {ECO:0000269|PubMed:10078208, ECO:0000269|PubMed:10660545, ECO:0000269|PubMed:15064730, ECO:0000269|PubMed:21120944, ECO:0000269|PubMed:23622243, ECO:0000269|PubMed:9564049, ECO:0000269|PubMed:9822679, ECO:0000269|PubMed:9822680}. |
| P52732 | KIF11 | S7 | ochoa | Kinesin-like protein KIF11 (Kinesin-like protein 1) (Kinesin-like spindle protein HKSP) (Kinesin-related motor protein Eg5) (Thyroid receptor-interacting protein 5) (TR-interacting protein 5) (TRIP-5) | Motor protein required for establishing a bipolar spindle and thus contributing to chromosome congression during mitosis (PubMed:19001501, PubMed:37728657). Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface (PubMed:23857769). {ECO:0000269|PubMed:19001501, ECO:0000269|PubMed:23857769}. |
| P52757 | CHN2 | S7 | ochoa | Beta-chimaerin (Beta-chimerin) (Rho GTPase-activating protein 3) | GTPase-activating protein for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors. |
| P54274 | TERF1 | S6 | ochoa | Telomeric repeat-binding factor 1 (NIMA-interacting protein 2) (TTAGGG repeat-binding factor 1) (Telomeric protein Pin2/TRF1) | Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. {ECO:0000269|PubMed:16166375}. |
| P54274 | TERF1 | S7 | ochoa | Telomeric repeat-binding factor 1 (NIMA-interacting protein 2) (TTAGGG repeat-binding factor 1) (Telomeric protein Pin2/TRF1) | Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. {ECO:0000269|PubMed:16166375}. |
| P54278 | PMS2 | S6 | ochoa | Mismatch repair endonuclease PMS2 (EC 3.1.-.-) (DNA mismatch repair protein PMS2) (PMS1 protein homolog 2) | Component of the post-replicative DNA mismatch repair system (MMR) (PubMed:30653781, PubMed:35189042). Heterodimerizes with MLH1 to form MutL alpha. DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Possesses an ATPase activity, but in the absence of gross structural changes, ATP hydrolysis may not be necessary for proficient mismatch repair (PubMed:35189042). {ECO:0000269|PubMed:16873062, ECO:0000269|PubMed:18206974, ECO:0000269|PubMed:23709753, ECO:0000269|PubMed:30653781, ECO:0000269|PubMed:35189042}. |
| P54619 | PRKAG1 | S6 | ochoa | 5'-AMP-activated protein kinase subunit gamma-1 (AMPK gamma1) (AMPK subunit gamma-1) (AMPKg) | AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:21680840, PubMed:24563466). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:21680840, PubMed:24563466). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:21680840, PubMed:24563466). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:21680840, PubMed:24563466). Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits (PubMed:21680840, PubMed:24563466). ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit (PubMed:21680840, PubMed:24563466). ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (PubMed:21680840, PubMed:24563466). {ECO:0000269|PubMed:21680840, ECO:0000269|PubMed:24563466}. |
| P54619 | PRKAG1 | S7 | ochoa | 5'-AMP-activated protein kinase subunit gamma-1 (AMPK gamma1) (AMPK subunit gamma-1) (AMPKg) | AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:21680840, PubMed:24563466). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:21680840, PubMed:24563466). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:21680840, PubMed:24563466). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:21680840, PubMed:24563466). Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits (PubMed:21680840, PubMed:24563466). ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit (PubMed:21680840, PubMed:24563466). ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (PubMed:21680840, PubMed:24563466). {ECO:0000269|PubMed:21680840, ECO:0000269|PubMed:24563466}. |
| P55055 | NR1H2 | T6 | ochoa | Oxysterols receptor LXR-beta (Liver X receptor beta) (Nuclear receptor NER) (Nuclear receptor subfamily 1 group H member 2) (Ubiquitously-expressed nuclear receptor) | Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:25661920). Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles (By similarity). Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators (By similarity). Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex (PubMed:20159957). {ECO:0000250|UniProtKB:Q60644, ECO:0000269|PubMed:20159957, ECO:0000269|PubMed:25661920}. |
| P55055 | NR1H2 | S7 | ochoa | Oxysterols receptor LXR-beta (Liver X receptor beta) (Nuclear receptor NER) (Nuclear receptor subfamily 1 group H member 2) (Ubiquitously-expressed nuclear receptor) | Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:25661920). Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles (By similarity). Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators (By similarity). Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex (PubMed:20159957). {ECO:0000250|UniProtKB:Q60644, ECO:0000269|PubMed:20159957, ECO:0000269|PubMed:25661920}. |
| P55072 | VCP | S7 | ochoa | Transitional endoplasmic reticulum ATPase (TER ATPase) (EC 3.6.4.6) (15S Mg(2+)-ATPase p97 subunit) (Valosin-containing protein) (VCP) | Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Mediates the endoplasmic reticulum-associated degradation of CHRNA3 in cortical neurons as part of the STUB1-VCP-UBXN2A complex (PubMed:26265139). Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:26565908). Involved in clearance process by mediating G3BP1 extraction from stress granules (PubMed:29804830, PubMed:34739333). Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites (PubMed:22020440, PubMed:22120668). Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage (PubMed:23042605, PubMed:23042607). Together with SPRTN metalloprotease, involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis (PubMed:32152270). Involved in interstrand cross-link repair in response to replication stress by mediating unloading of the ubiquitinated CMG helicase complex (By similarity). Mediates extraction of PARP1 trapped to chromatin: recognizes and binds ubiquitinated PARP1 and promotes its removal (PubMed:35013556). Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation (PubMed:16186510, PubMed:21118995). Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy (PubMed:20104022, PubMed:27753622). Acts as a negative regulator of type I interferon production by interacting with RIGI: interaction takes place when RIGI is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of RIGI (PubMed:26471729). May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation (PubMed:21822278). May more particularly play a role in caveolins sorting in cells (PubMed:21822278, PubMed:23335559). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). {ECO:0000250|UniProtKB:P23787, ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:16186510, ECO:0000269|PubMed:20104022, ECO:0000269|PubMed:21118995, ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:22020440, ECO:0000269|PubMed:22120668, ECO:0000269|PubMed:22607976, ECO:0000269|PubMed:23042605, ECO:0000269|PubMed:23042607, ECO:0000269|PubMed:23335559, ECO:0000269|PubMed:26265139, ECO:0000269|PubMed:26471729, ECO:0000269|PubMed:26565908, ECO:0000269|PubMed:26692333, ECO:0000269|PubMed:27753622, ECO:0000269|PubMed:29804830, ECO:0000269|PubMed:32152270, ECO:0000269|PubMed:34739333, ECO:0000269|PubMed:35013556}. |
| P57053 | H2BC12L | S7 | ochoa | Histone H2B type F-S (H2B-clustered histone 12 like) (H2B.S histone 1) (Histone H2B.s) (H2B/s) | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; FUNCTION: Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid. |
| P58005 | SESN3 | S7 | ochoa | Sestrin-3 (EC 1.11.1.-) | May function as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway (PubMed:25263562). May also regulate the insulin-receptor signaling pathway through activation of TORC2 (By similarity). This metabolic regulator may also play a role in protection against oxidative and genotoxic stresses (By similarity). May prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (By similarity). {ECO:0000250|UniProtKB:P58004, ECO:0000250|UniProtKB:Q9CYP7, ECO:0000269|PubMed:25263562}. |
| P58340 | MLF1 | S7 | ochoa | Myeloid leukemia factor 1 (Myelodysplasia-myeloid leukemia factor 1) | Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus. {ECO:0000269|PubMed:15861129}. |
| P59768 | GNG2 | T6 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (G gamma-I) | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems (PubMed:29925951, PubMed:33762731, PubMed:34239069, PubMed:35610220, PubMed:35714614, PubMed:35835867, PubMed:36087581, PubMed:36989299, PubMed:37327704, PubMed:37935376, PubMed:37935377, PubMed:37963465, PubMed:38168118, PubMed:38552625). The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (PubMed:29925951, PubMed:33762731, PubMed:34239069, PubMed:35610220, PubMed:35714614, PubMed:35835867, PubMed:36087581, PubMed:36989299, PubMed:37327704, PubMed:37935376, PubMed:37935377, PubMed:37963465, PubMed:38168118, PubMed:38552625). {ECO:0000269|PubMed:29925951, ECO:0000269|PubMed:33762731, ECO:0000269|PubMed:34239069, ECO:0000269|PubMed:35610220, ECO:0000269|PubMed:35714614, ECO:0000269|PubMed:35835867, ECO:0000269|PubMed:36087581, ECO:0000269|PubMed:36989299, ECO:0000269|PubMed:37327704, ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37935377, ECO:0000269|PubMed:37963465, ECO:0000269|PubMed:38168118, ECO:0000269|PubMed:38552625}. |
| P60468 | SEC61B | S7 | ochoa | Protein transport protein Sec61 subunit beta | Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (PubMed:12475939). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (PubMed:12475939). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (PubMed:32820719, PubMed:36261522). The SEC61 channel cooperates with the translocating protein TRAM1 to import nascent proteins into the ER (PubMed:19121997). {ECO:0000269|PubMed:12475939, ECO:0000269|PubMed:19121997, ECO:0000269|PubMed:32820719, ECO:0000269|PubMed:36261522}. |
| P60842 | EIF4A1 | S7 | ochoa | Eukaryotic initiation factor 4A-I (eIF-4A-I) (eIF4A-I) (EC 3.6.4.13) (ATP-dependent RNA helicase eIF4A-1) | ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome (PubMed:20156963). In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. As a result, promotes cell proliferation and growth (PubMed:20156963). {ECO:0000269|PubMed:19153607, ECO:0000269|PubMed:19204291, ECO:0000269|PubMed:20156963}. |
| P60866 | RPS20 | T6 | ochoa | Small ribosomal subunit protein uS10 (40S ribosomal protein S20) | Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). {ECO:0000269|PubMed:23636399}. |
| P60900 | PSMA6 | S6 | ochoa | Proteasome subunit alpha type-6 (27 kDa prosomal protein) (PROS-27) (p27K) (Macropain iota chain) (Multicatalytic endopeptidase complex iota chain) (Proteasome iota chain) (Proteasome subunit alpha-1) (alpha-1) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
| P61020 | RAB5B | T6 | ochoa|psp | Ras-related protein Rab-5B (EC 3.6.5.2) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. {ECO:0000250|UniProtKB:P20339}. |
| P61026 | RAB10 | Y6 | ochoa | Ras-related protein Rab-10 (EC 3.6.5.2) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:21248164). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:21248164). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane (PubMed:21248164). Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane (By similarity). In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response (By similarity). Also plays a specific role in asymmetric protein transport to the plasma membrane (PubMed:16641372). In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane (By similarity). In epithelial cells, it regulates transport from the Golgi to the basolateral membrane (PubMed:16641372). May play a role in the basolateral recycling pathway and in phagosome maturation (By similarity). May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (PubMed:23263280). Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis (PubMed:30398148). When phosphorylated by LRRK2 on Thr-73, binds RILPL1 and inhibits ciliogenesis (PubMed:30398148). Participates in the export of a subset of neosynthesized proteins through a Rab8-Rab10-Rab11-dependent endososomal export route (PubMed:32344433). Targeted to and stabilized on stressed lysosomes through LRRK2 phosphorylation where it promotes the extracellular release of lysosomal content through EHBP1 and EHNP1L1 effector proteins (PubMed:30209220). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61027, ECO:0000269|PubMed:16641372, ECO:0000269|PubMed:21248164, ECO:0000269|PubMed:23263280, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:32344433}.; FUNCTION: (Microbial infection) Upon Legionella pneumophila infection promotes endoplasmic reticulum recruitment and bacterial replication. Plays a role in remodeling the Legionella-containing vacuole (LCV) into an endoplasmic reticulum-like vacuole. {ECO:0000269|PubMed:31540829}. |
| P61081 | UBE2M | S6 | ochoa | NEDD8-conjugating enzyme Ubc12 (EC 2.3.2.34) (NEDD8 carrier protein) (Ubiquitin-conjugating enzyme E2 M) | Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation. {ECO:0000269|PubMed:10207026, ECO:0000269|PubMed:15361859}. |
| P61587 | RND3 | S7 | psp | Rho-related GTP-binding protein RhoE (Protein MemB) (Rho family GTPase 3) (Rho-related GTP-binding protein Rho8) (Rnd3) | Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. |
| P61758 | VBP1 | S7 | ochoa | 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}. |
| P62273 | RPS29 | Y7 | ochoa | Small ribosomal subunit protein uS14 (40S ribosomal protein S29) | Component of the small ribosomal subunit (PubMed:23636399, PubMed:25901680, PubMed:25957688). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:25901680, PubMed:25957688). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680, ECO:0000269|PubMed:25957688}. |
| P62753 | RPS6 | S6 | ochoa | Small ribosomal subunit protein eS6 (40S ribosomal protein S6) (Phosphoprotein NP33) | Component of the 40S small ribosomal subunit (PubMed:23636399, PubMed:8706699). Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA (PubMed:17220279). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:17220279, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:8706699}. |
| P62807 | H2BC4 | S7 | ochoa | Histone H2B type 1-C/E/F/G/I (Histone H2B.1 A) (Histone H2B.a) (H2B/a) (Histone H2B.g) (H2B/g) (Histone H2B.h) (H2B/h) (Histone H2B.k) (H2B/k) (Histone H2B.l) (H2B/l) | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; FUNCTION: Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid. |
| P62993 | GRB2 | Y7 | psp | Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2) | Non-enzymatic adapter protein that plays a pivotal role in precisely regulated signaling cascades from cell surface receptors to cellular responses, including signaling transduction and gene expression (PubMed:11726515, PubMed:37626338). Thus, participates in many biological processes including regulation of innate and adaptive immunity, autophagy, DNA repair or necroptosis (PubMed:35831301, PubMed:37626338, PubMed:38182563). Controls signaling complexes at the T-cell antigen receptor to facilitate the activation, differentiation, and function of T-cells (PubMed:36864087, PubMed:9489702). Mechanistically, engagement of the TCR leads to phosphorylation of the adapter protein LAT, which serves as docking site for GRB2 (PubMed:9489702). In turn, GRB2 establishes a a connection with SOS1 that acts as a guanine nucleotide exchange factor and serves as a critical regulator of KRAS/RAF1 leading to MAPKs translocation to the nucleus and activation (PubMed:12171928, PubMed:25870599). Functions also a role in B-cell activation by amplifying Ca(2+) mobilization and activation of the ERK MAP kinase pathway upon recruitment to the phosphorylated B-cell antigen receptor (BCR) (PubMed:25413232, PubMed:29523808). Plays a role in switching between autophagy and programmed necrosis upstream of EGFR by interacting with components of necrosomes including RIPK1 and with autophagy regulators SQSTM1 and BECN1 (PubMed:35831301, PubMed:38182563). Regulates miRNA biogenesis by forming a functional ternary complex with AGO2 and DICER1 (PubMed:37328606). Functions in the replication stress response by protecting DNA at stalled replication forks from MRE11-mediated degradation. Mechanistically, inhibits RAD51 ATPase activity to stabilize RAD51 on stalled replication forks (PubMed:38459011). Additionally, directly recruits and later releases MRE11 at DNA damage sites during the homology-directed repair (HDR) process (PubMed:34348893). {ECO:0000269|PubMed:11726515, ECO:0000269|PubMed:12171928, ECO:0000269|PubMed:1322798, ECO:0000269|PubMed:19815557, ECO:0000269|PubMed:25413232, ECO:0000269|PubMed:25870599, ECO:0000269|PubMed:29523808, ECO:0000269|PubMed:34348893, ECO:0000269|PubMed:35831301, ECO:0000269|PubMed:36864087, ECO:0000269|PubMed:37328606, ECO:0000269|PubMed:37626338, ECO:0000269|PubMed:38182563, ECO:0000269|PubMed:38459011, ECO:0000269|PubMed:9489702}.; FUNCTION: [Isoform 2]: Does not bind to phosphorylated epidermal growth factor receptor (EGFR) but inhibits EGF-induced transactivation of a RAS-responsive element. Acts as a dominant negative protein over GRB2 and by suppressing proliferative signals, may trigger active programmed cell death. Mechanistically, inhibits RAS-ERK signaling and downstream cell proliferation by competing with GRB2 for SOS1 binding and thus by regulating SOS1 membrane recruitment (PubMed:36171279). {ECO:0000269|PubMed:36171279, ECO:0000269|PubMed:8178156}. |
| P63010 | AP2B1 | Y6 | ochoa|psp | AP-2 complex subunit beta (AP105B) (Adaptor protein complex AP-2 subunit beta) (Adaptor-related protein complex 2 subunit beta) (Beta-2-adaptin) (Beta-adaptin) (Clathrin assembly protein complex 2 beta large chain) (Plasma membrane adaptor HA2/AP2 adaptin beta subunit) | Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly. {ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:14985334, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23676497}. |
| P63218 | GNG5 | S6 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5 | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. |
| P63244 | RACK1 | T6 | ochoa | Small ribosomal subunit protein RACK1 (Cell proliferation-inducing gene 21 protein) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Guanine nucleotide-binding protein subunit beta-like protein 12.3) (Human lung cancer oncogene 7 protein) (HLC-7) (Receptor for activated C kinase) (Receptor of activated protein C kinase 1) [Cleaved into: Small ribosomal subunit protein RACK1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed) (Receptor of activated protein C kinase 1, N-terminally processed)] | Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158). Acts as an adapter for the dephosphorylation and inactivation of AKT1 by promoting recruitment of PP2A phosphatase to AKT1 (By similarity). {ECO:0000250|UniProtKB:P68040, ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:12589061, ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17108144, ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:18621736, ECO:0000269|PubMed:19423701, ECO:0000269|PubMed:19674157, ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20541605, ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:20976005, ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:21347310, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:28132843, ECO:0000269|PubMed:9584165}.; FUNCTION: (Microbial infection) Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells. {ECO:0000269|PubMed:21347310}.; FUNCTION: (Microbial infection) Enhances phosphorylation of HIV-1 Nef by PKCs. {ECO:0000269|PubMed:11312657}.; FUNCTION: (Microbial infection) In case of poxvirus infection, remodels the ribosomes so that they become optimal for the viral mRNAs (containing poly-A leaders) translation but not for host mRNAs. {ECO:0000269|PubMed:28636603}.; FUNCTION: (Microbial infection) Contributes to the cap-independent internal ribosome entry site (IRES)-mediated translation by some RNA viruses. {ECO:0000269|PubMed:25416947}. |
| P67809 | YBX1 | T7 | 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}. |
| P67936 | TPM4 | S6 | ochoa | Tropomyosin alpha-4 chain (TM30p1) (Tropomyosin-4) | Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments (By similarity). Binds calcium (PubMed:1836432). Plays a role in platelet biogenesis. {ECO:0000250|UniProtKB:P09495, ECO:0000269|PubMed:1836432, ECO:0000269|PubMed:28134622, ECO:0000269|PubMed:35170221}. |
| P68104 | EEF1A1 | T6 | ochoa | Elongation factor 1-alpha 1 (EF-1-alpha-1) (EC 3.6.5.-) (Elongation factor Tu) (EF-Tu) (Eukaryotic elongation factor 1 A-1) (eEF1A-1) (Leukocyte receptor cluster member 7) | Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623). Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976). Also plays a role in cytoskeleton organization by promoting actin bundling (By similarity). {ECO:0000250|UniProtKB:P68105, ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:26593721, ECO:0000269|PubMed:26651998, ECO:0000269|PubMed:36123449, ECO:0000269|PubMed:36264623, ECO:0000269|PubMed:36638793}.; FUNCTION: (Microbial infection) Required for the translation of viral proteins and viral replication during human coronavirus SARS-CoV-2 infection. {ECO:0000269|PubMed:33495306}. |
| P68402 | PAFAH1B2 | S6 | ochoa | Platelet-activating factor acetylhydrolase IB subunit alpha2 (EC 3.1.1.47) (PAF acetylhydrolase 30 kDa subunit) (PAF-AH 30 kDa subunit) (PAF-AH subunit beta) (PAFAH subunit beta) | Alpha2 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA). In contrast, the alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes AAGPA more efficiently than PAF, but has little hydrolytic activity towards AAGPE (By similarity). May play a role in male germ cell meiosis during the late pachytenestage and meiotic divisions as well as early spermiogenesis (By similarity). {ECO:0000250|UniProtKB:P68401, ECO:0000250|UniProtKB:Q61206}. |
| P78347 | GTF2I | S7 | ochoa | General transcription factor II-I (GTFII-I) (TFII-I) (Bruton tyrosine kinase-associated protein 135) (BAP-135) (BTK-associated protein 135) (SRF-Phox1-interacting protein) (SPIN) (Williams-Beuren syndrome chromosomal region 6 protein) | Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. {ECO:0000269|PubMed:10373551, ECO:0000269|PubMed:11373296, ECO:0000269|PubMed:16738337}. |
| P83731 | RPL24 | S7 | ochoa | Large ribosomal subunit protein eL24 (60S ribosomal protein L24) (60S ribosomal protein L30) | Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}. |
| P98082 | DAB2 | T7 | ochoa | Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Differentially-expressed protein 2) | Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. {ECO:0000269|PubMed:11387212, ECO:0000269|PubMed:12805222, ECO:0000269|PubMed:16267015, ECO:0000269|PubMed:16984970, ECO:0000269|PubMed:19306879, ECO:0000269|PubMed:21995445, ECO:0000269|PubMed:22323290, ECO:0000269|PubMed:22491013}. |
| Q01081 | U2AF1 | S7 | ochoa | Splicing factor U2AF 35 kDa subunit (U2 auxiliary factor 35 kDa subunit) (U2 small nuclear RNA auxiliary factor 1) (U2 snRNP auxiliary factor small subunit) | Plays a critical role in both constitutive and enhancer-dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Recruits U2 snRNP to the branch point. Directly mediates interactions between U2AF2 and proteins bound to the enhancers and thus may function as a bridge between U2AF2 and the enhancer complex to recruit it to the adjacent intron. {ECO:0000269|PubMed:22158538, ECO:0000269|PubMed:25311244, ECO:0000269|PubMed:8647433}. |
| Q01105 | SET | S7 | ochoa|psp | Protein SET (HLA-DR-associated protein II) (Inhibitor of granzyme A-activated DNase) (IGAAD) (PHAPII) (Phosphatase 2A inhibitor I2PP2A) (I-2PP2A) (Template-activating factor I) (TAF-I) | Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher. {ECO:0000269|PubMed:11555662, ECO:0000269|PubMed:12628186}. |
| Q01628 | IFITM3 | T7 | ochoa | Interferon-induced transmembrane protein 3 (Dispanin subfamily A member 2b) (DSPA2b) (Interferon-inducible protein 1-8U) | IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) (PubMed:26354436, PubMed:33239446, PubMed:33270927). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-2 S protein-mediated viral entry and VSV G protein-mediated viral entry (PubMed:33270927). Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation (PubMed:26354436). IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome (PubMed:26354436). Exerts opposing activities on SARS-CoV-2, including amphipathicity-dependent restriction of virus at endosomes and amphipathicity-independent enhancement of infection at the plasma membrane (PubMed:33270927). {ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20534863, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22046135, ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:23601107, ECO:0000269|PubMed:26354436, ECO:0000269|PubMed:33239446, ECO:0000269|PubMed:33270927}. |
| Q01629 | IFITM2 | T7 | ochoa | Interferon-induced transmembrane protein 2 (Dispanin subfamily A member 2c) (DSPA2c) (Interferon-inducible protein 1-8D) | IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol (PubMed:26354436, PubMed:33563656). Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) (PubMed:26354436, PubMed:33239446, PubMed:33270927, PubMed:33563656). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-2 S protein-mediated viral entry and VSV G protein-mediated viral entry (PubMed:33563656). Induces cell cycle arrest and mediates apoptosis by caspase activation and in p53-independent manner. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation (PubMed:26354436). IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome (PubMed:26354436). {ECO:0000269|PubMed:19544527, ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20534863, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:26354436, ECO:0000269|PubMed:33239446, ECO:0000269|PubMed:33270927, ECO:0000269|PubMed:33563656}. |
| Q01959 | SLC6A3 | S7 | psp | Sodium-dependent dopamine transporter (DA transporter) (DAT) (Solute carrier family 6 member 3) | Mediates sodium- and chloride-dependent transport of dopamine (PubMed:10375632, PubMed:11093780, PubMed:1406597, PubMed:15505207, PubMed:19478460, PubMed:39112701, PubMed:39112703, PubMed:39112705, PubMed:8302271). Also mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline) (By similarity). Regulator of light-dependent retinal hyaloid vessel regression, downstream of OPN5 signaling (By similarity). {ECO:0000250|UniProtKB:P23977, ECO:0000250|UniProtKB:Q61327, ECO:0000269|PubMed:10375632, ECO:0000269|PubMed:11093780, ECO:0000269|PubMed:1406597, ECO:0000269|PubMed:15505207, ECO:0000269|PubMed:19478460, ECO:0000269|PubMed:39112701, ECO:0000269|PubMed:39112703, ECO:0000269|PubMed:39112705, ECO:0000269|PubMed:8302271}. |
| Q01995 | TAGLN | S7 | ochoa | Transgelin (22 kDa actin-binding protein) (Protein WS3-10) (Smooth muscle protein 22-alpha) (SM22-alpha) | Actin cross-linking/gelling protein (By similarity). Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence. {ECO:0000250}. |
| Q02978 | SLC25A11 | S6 | ochoa | Mitochondrial 2-oxoglutarate/malate carrier protein (OGCP) (alpha-oxoglutarate carrier) (Solute carrier family 25 member 11) (SLC25A11) | Catalyzes the transport of 2-oxoglutarate (alpha-oxoglutarate) across the inner mitochondrial membrane in an electroneutral exchange for malate. Can also exchange 2-oxoglutarate for other dicarboxylic acids such as malonate, succinate, maleate and oxaloacetate, although with lower affinity. Contributes to several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism (By similarity). Maintains mitochondrial fusion and fission events, and the organization and morphology of cristae (PubMed:21448454). Involved in the regulation of apoptosis (By similarity). Helps protect from cytotoxic-induced apoptosis by modulating glutathione levels in mitochondria (By similarity). {ECO:0000250|UniProtKB:P22292, ECO:0000250|UniProtKB:P97700, ECO:0000250|UniProtKB:Q9CR62, ECO:0000269|PubMed:21448454}. |
| Q03135 | CAV1 | Y6 | ochoa|psp | Caveolin-1 | May act as a scaffolding protein within caveolar membranes (PubMed:11751885). Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (PubMed:19262564). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (PubMed:25893292). Binds 20(S)-hydroxycholesterol (20(S)-OHC) (By similarity). {ECO:0000250|UniProtKB:P49817, ECO:0000269|PubMed:11751885, ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:19262564, ECO:0000269|PubMed:25893292}. |
| Q03169 | TNFAIP2 | S6 | ochoa | Tumor necrosis factor alpha-induced protein 2 (TNF alpha-induced protein 2) (Primary response gene B94 protein) | May play a role as a mediator of inflammation and angiogenesis. |
| Q04446 | GBE1 | T6 | ochoa | 1,4-alpha-glucan-branching enzyme (EC 2.4.1.18) (Brancher enzyme) (Glycogen-branching enzyme) | Glycogen-branching enzyme participates in the glycogen biosynthetic process along with glycogenin and glycogen synthase. Generates alpha-1,6-glucosidic branches from alpha-1,4-linked glucose chains, to increase solubility of the glycogen polymer (PubMed:26199317, PubMed:8463281, PubMed:8613547). {ECO:0000269|PubMed:26199317, ECO:0000269|PubMed:8463281, ECO:0000269|PubMed:8613547}. |
| Q05329 | GAD2 | S6 | psp | Glutamate decarboxylase 2 (EC 4.1.1.15) (65 kDa glutamic acid decarboxylase) (GAD-65) (Glutamate decarboxylase 65 kDa isoform) | Catalyzes the production of GABA. {ECO:0000305|PubMed:8999827}. |
| Q05639 | EEF1A2 | T6 | ochoa | Elongation factor 1-alpha 2 (EF-1-alpha-2) (EC 3.6.5.-) (Eukaryotic elongation factor 1 A-2) (eEF1A-2) (Statin-S1) | Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis. Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (By similarity). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (By similarity). {ECO:0000250|UniProtKB:P68104, ECO:0000250|UniProtKB:Q71V39}. |
| Q06330 | RBPJ | S7 | ochoa | Recombining binding protein suppressor of hairless (CBF-1) (J kappa-recombination signal-binding protein) (RBP-J kappa) (RBP-J) (RBP-JK) (Renal carcinoma antigen NY-REN-30) | Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations. Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some NICD product of Notch proteins (Notch intracellular domain), it acts as a transcriptional activator that activates transcription of Notch target genes. Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively. Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence. Binds specifically to methylated DNA (PubMed:21991380). Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen) (PubMed:23303788). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by repressing transcription of NADPH oxidase subunits (By similarity). {ECO:0000250|UniProtKB:P31266, ECO:0000269|PubMed:21991380, ECO:0000269|PubMed:23303788}. |
| Q07869 | PPARA | S6 | psp | Peroxisome proliferator-activated receptor alpha (PPAR-alpha) (Nuclear receptor subfamily 1 group C member 1) | Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as a transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2. {ECO:0000269|PubMed:10195690, ECO:0000269|PubMed:24043310, ECO:0000269|PubMed:7629123, ECO:0000269|PubMed:7684926, ECO:0000269|PubMed:9556573}. |
| Q08117 | TLE5 | S6 | ochoa | TLE family member 5 (Amino-terminal enhancer of split) (Amino enhancer of split) (Gp130-associated protein GAM) (Grg-5) (Groucho-related protein 5) (Protein ESP1) (Protein GRG) (TLE family member 5, transcriptional modulator) | Transcriptional corepressor. Acts as a dominant repressor towards other family members. Inhibits NF-kappa-B-regulated gene expression. May be required for the initiation and maintenance of the differentiated state. Essential for the transcriptional repressor activity of SIX3 during retina and lens development. {ECO:0000269|PubMed:10660609, ECO:0000269|PubMed:10748198}. |
| Q09161 | NCBP1 | S7 | ochoa|psp | Nuclear cap-binding protein subunit 1 (80 kDa nuclear cap-binding protein) (CBP80) (NCBP 80 kDa subunit) | Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Associates with NCBP3 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export and is particularly important in cellular stress situations such as virus infections. The conventional CBC with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus whereas the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role only in mRNA export. NCBP1/CBP80 is required for cell growth and viability (PubMed:26382858). {ECO:0000269|PubMed:11551508, ECO:0000269|PubMed:12093754, ECO:0000269|PubMed:15059963, ECO:0000269|PubMed:15361857, ECO:0000269|PubMed:16186820, ECO:0000269|PubMed:16317009, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17873884, ECO:0000269|PubMed:18369367, ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:19648179, ECO:0000269|PubMed:26382858, ECO:0000269|PubMed:7651522, ECO:0000269|PubMed:8069914}. |
| Q10567 | AP1B1 | Y6 | ochoa | AP-1 complex subunit beta-1 (Adaptor protein complex AP-1 subunit beta-1) (Adaptor-related protein complex 1 subunit beta-1) (Beta-1-adaptin) (Beta-adaptin 1) (Clathrin assembly protein complex 1 beta large chain) (Golgi adaptor HA1/AP1 adaptin beta subunit) | Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes (PubMed:31630791). The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. {ECO:0000269|PubMed:31630791}. |
| Q12888 | TP53BP1 | S6 | psp | TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1) | Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250|UniProtKB:P70399, ECO:0000269|PubMed:12364621, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:22553214, ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112, ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:31135337, ECO:0000269|PubMed:37696958}. |
| Q12933 | TRAF2 | T7 | ochoa | TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2) (Tumor necrosis factor type 2 receptor-associated protein 3) | E3 ubiquitin-protein ligase that regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis (PubMed:10346818, PubMed:11784851, PubMed:12917689, PubMed:15383523, PubMed:18981220, PubMed:19150425, PubMed:19810754, PubMed:19918265, PubMed:19937093, PubMed:20047764, PubMed:20064526, PubMed:20385093, PubMed:20577214, PubMed:22212761). Catalyzes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, IKBKE, MLST8, RIPK1 and TICAM1 (PubMed:23453969, PubMed:28489822). Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases (PubMed:15383523, PubMed:18981220). Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain (PubMed:11907583, PubMed:19506082). Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR (PubMed:15121867). In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE (PubMed:23453969). Acts as a regulator of mTORC1 and mTORC2 assembly by mediating 'Lys-63'-linked ubiquitination of MLST8, thereby inhibiting formation of the mTORC2 complex, while facilitating assembly of the mTORC1 complex (PubMed:28489822). Required for normal antibody isotype switching from IgM to IgG (By similarity). {ECO:0000250|UniProtKB:P39429, ECO:0000269|PubMed:10346818, ECO:0000269|PubMed:11784851, ECO:0000269|PubMed:11907583, ECO:0000269|PubMed:12917689, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15383523, ECO:0000269|PubMed:18981220, ECO:0000269|PubMed:19150425, ECO:0000269|PubMed:19506082, ECO:0000269|PubMed:19810754, ECO:0000269|PubMed:19918265, ECO:0000269|PubMed:19937093, ECO:0000269|PubMed:20047764, ECO:0000269|PubMed:20064526, ECO:0000269|PubMed:20385093, ECO:0000269|PubMed:20577214, ECO:0000269|PubMed:22212761, ECO:0000269|PubMed:23453969, ECO:0000269|PubMed:28489822}. |
| Q12948 | FOXC1 | S6 | ochoa | Forkhead box protein C1 (Forkhead-related protein FKHL7) (Forkhead-related transcription factor 3) (FREAC-3) | DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as eye, bones, cardiovascular, kidney and skin development (PubMed:11782474, PubMed:14506133, PubMed:14578375, PubMed:15277473, PubMed:15299087, PubMed:15684392, PubMed:16449236, PubMed:16492674, PubMed:17210863, PubMed:19279310, PubMed:19793056, PubMed:25786029, PubMed:27804176, PubMed:27907090). Acts either as a transcriptional activator or repressor (PubMed:11782474). Binds to the consensus binding site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes (PubMed:11782474, PubMed:12533514, PubMed:14506133, PubMed:19793056, PubMed:27804176, PubMed:7957066). Upon DNA-binding, promotes DNA bending (PubMed:14506133, PubMed:7957066). Acts as a transcriptional coactivator (PubMed:26565916). Stimulates Indian hedgehog (Ihh)-induced target gene expression mediated by the transcription factor GLI2, and hence regulates endochondral ossification (By similarity). Also acts as a transcriptional coregulator by increasing DNA-binding capacity of GLI2 in breast cancer cells (PubMed:26565916). Regulates FOXO1 through binding to a conserved element, 5'-GTAAACAAA-3' in its promoter region, implicating FOXC1 as an important regulator of cell viability and resistance to oxidative stress in the eye (PubMed:17993506). Cooperates with transcription factor FOXC2 in regulating expression of genes that maintain podocyte integrity (By similarity). Promotes cell growth inhibition by stopping the cell cycle in the G1 phase through TGFB1-mediated signals (PubMed:12408963). Involved in epithelial-mesenchymal transition (EMT) induction by increasing cell proliferation, migration and invasion (PubMed:20406990, PubMed:22991501). Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression (By similarity). Plays a role in the gene regulatory network essential for epidermal keratinocyte terminal differentiation (PubMed:27907090). Essential developmental transcriptional factor required for mesoderm-derived tissues, such as the somites, skin, bone and cartilage. Positively regulates CXCL12 and stem cell factor expression in bone marrow mesenchymal progenitor cells, and hence plays a role in the development and maintenance of mesenchymal niches for haematopoietic stem and progenitor cells (HSPC). Plays a role in corneal transparency by preventing both blood vessel and lymphatic vessel growth during embryonic development in a VEGF-dependent manner. Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression (By similarity). May function as a tumor suppressor (PubMed:12408963). {ECO:0000250|UniProtKB:Q61572, ECO:0000269|PubMed:11782474, ECO:0000269|PubMed:12408963, ECO:0000269|PubMed:12533514, ECO:0000269|PubMed:14506133, ECO:0000269|PubMed:14578375, ECO:0000269|PubMed:15277473, ECO:0000269|PubMed:15299087, ECO:0000269|PubMed:15684392, ECO:0000269|PubMed:16449236, ECO:0000269|PubMed:16492674, ECO:0000269|PubMed:17210863, ECO:0000269|PubMed:17993506, ECO:0000269|PubMed:19279310, ECO:0000269|PubMed:19793056, ECO:0000269|PubMed:20406990, ECO:0000269|PubMed:22991501, ECO:0000269|PubMed:25786029, ECO:0000269|PubMed:26565916, ECO:0000269|PubMed:27804176, ECO:0000269|PubMed:27907090, ECO:0000269|PubMed:7957066}. |
| Q12965 | MYO1E | Y7 | ochoa | Unconventional myosin-Ie (Myosin-Ic) (Unconventional myosin 1E) | Actin-based motor molecule with ATPase activity (PubMed:11940582, PubMed:36316095). Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Involved in clathrin-mediated endocytosis and intracellular movement of clathrin-coated vesicles (PubMed:36316095). Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14. {ECO:0000269|PubMed:11940582, ECO:0000269|PubMed:17257598, ECO:0000269|PubMed:20860408, ECO:0000269|PubMed:36316095}. |
| Q12996 | CSTF3 | T7 | ochoa | Cleavage stimulation factor subunit 3 (CF-1 77 kDa subunit) (Cleavage stimulation factor 77 kDa subunit) (CSTF 77 kDa subunit) (CstF-77) | One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. |
| Q13049 | TRIM32 | S7 | ochoa | E3 ubiquitin-protein ligase TRIM32 (EC 2.3.2.27) (72 kDa Tat-interacting protein) (RING-type E3 ubiquitin transferase TRIM32) (Tripartite motif-containing protein 32) (Zinc finger protein HT2A) | E3 ubiquitin ligase that plays a role in various biological processes including neural stem cell differentiation, innate immunity, inflammatory resonse and autophagy (PubMed:19349376, PubMed:31123703). Plays a role in virus-triggered induction of IFN-beta and TNF-alpha by mediating the ubiquitination of STING1. Mechanistically, targets STING1 for 'Lys-63'-linked ubiquitination which promotes the interaction of STING1 with TBK1 (PubMed:22745133). Regulates bacterial clearance and promotes autophagy in Mycobacterium tuberculosis-infected macrophages (PubMed:37543647). Negatively regulates TLR3/4-mediated innate immune and inflammatory response by triggering the autophagic degradation of TICAM1 in an E3 activity-independent manner (PubMed:28898289). Plays an essential role in oxidative stress induced cell death by inducing loss of transmembrane potential and enhancing mitochondrial reactive oxygen species (ROS) production during oxidative stress conditions (PubMed:32918979). Ubiquitinates XIAP and targets it for proteasomal degradation (PubMed:21628460). Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation (PubMed:19349376). May ubiquitinate BBS2 (PubMed:22500027). Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes treated with UVB and TNF-alpha (By similarity). Also acts as a regulator of autophagy by mediating formation of unanchored 'Lys-63'-linked polyubiquitin chains that activate ULK1: interaction with AMBRA1 is required for ULK1 activation (PubMed:31123703). Positively regulates dendritic branching by promoting ubiquitination and subsequent degradation of the epigenetic factor CDYL (PubMed:34888944). Under metabolic stress and phosphorylation by CHK2, mediates 'Lys-63'-linked ubiquitination of ATG7 at 'Lys-45' to initiate autophagy (PubMed:37943659). {ECO:0000250|UniProtKB:Q8CH72, ECO:0000269|PubMed:19349376, ECO:0000269|PubMed:21628460, ECO:0000269|PubMed:22500027, ECO:0000269|PubMed:22745133, ECO:0000269|PubMed:28898289, ECO:0000269|PubMed:31123703, ECO:0000269|PubMed:32918979, ECO:0000269|PubMed:34888944, ECO:0000269|PubMed:37543647, ECO:0000269|PubMed:37943659}.; FUNCTION: (Microbial infection) May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo (PubMed:7778269). Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo (PubMed:7778269). {ECO:0000269|PubMed:7778269}. |
| Q13077 | TRAF1 | S7 | ochoa | TNF receptor-associated factor 1 (Epstein-Barr virus-induced protein 6) | Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2. {ECO:0000269|PubMed:10692572, ECO:0000269|PubMed:16323247, ECO:0000269|PubMed:18429822, ECO:0000269|PubMed:19287455, ECO:0000269|PubMed:19698991, ECO:0000269|PubMed:20385093}. |
| Q13123 | IK | S6 | ochoa | Protein Red (Cytokine IK) (IK factor) (Protein RER) | Involved in pre-mRNA splicing as a component of the spliceosome (PubMed:28781166). Auxiliary spliceosomal protein that regulates selection of alternative splice sites in a small set of target pre-mRNA species (Probable). Required for normal mitotic cell cycle progression (PubMed:22351768, PubMed:24252166). Recruits MAD1L1 and MAD2L1 to kinetochores, and is required to trigger the spindle assembly checkpoint (PubMed:22351768). Required for normal accumulation of SMU1 (PubMed:24945353). {ECO:0000269|PubMed:22351768, ECO:0000269|PubMed:24252166, ECO:0000269|PubMed:24945353, ECO:0000269|PubMed:28781166, ECO:0000305}.; FUNCTION: (Microbial infection) Required, together with SMU1, for normal splicing of influenza A virus NS1 pre-mRNA, which is required for the production of the exportin NS2 and for the production of influenza A virus particles. Not required for the production of VSV virus particles. {ECO:0000269|PubMed:24945353}. |
| Q13185 | CBX3 | T6 | ochoa | Chromobox protein homolog 3 (HECH) (Heterochromatin protein 1 homolog gamma) (HP1 gamma) (Modifier 2 protein) | Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the methyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1. Mediates the recruitment of NIPBL to sites of DNA damage at double-strand breaks (DSBs) (PubMed:28167679). {ECO:0000250|UniProtKB:P23198, ECO:0000269|PubMed:28167679}. |
| Q13206 | DDX10 | S7 | ochoa | Probable ATP-dependent RNA helicase DDX10 (EC 3.6.4.13) (DEAD box protein 10) | Putative ATP-dependent RNA helicase that plays various role in innate immunity or inflammation. Plays a role in the enhancement of AIM2-induced inflammasome activation by interacting with AIM2 and stabilizing its protein level (PubMed:32519665). Negatively regulates viral infection by promoting interferon beta production and interferon stimulated genes/ISGs expression (PubMed:36779599). {ECO:0000269|PubMed:32519665, ECO:0000269|PubMed:36779599}. |
| Q13283 | G3BP1 | S7 | ochoa | Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (hDH VIII) (GAP SH3 domain-binding protein 1) | Protein involved in various processes, such as stress granule formation and innate immunity (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:30510222, PubMed:30804210). Plays an essential role in stress granule formation (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:35977029, PubMed:36183834, PubMed:36279435, PubMed:36692217, PubMed:37379838). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:27022092, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:36279435, PubMed:37379838). Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding: functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:36279435, PubMed:36692217). Also acts as an ATP- and magnesium-dependent helicase: unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency (PubMed:9889278). Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA (PubMed:9889278). Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends (PubMed:9889278). Plays an essential role in innate immunity by promoting CGAS and RIGI activity (PubMed:30510222, PubMed:30804210). Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS (PubMed:30510222). Triggers the condensation of cGAS, a process probably linked to the formation of membrane-less organelles (PubMed:34779554). Also enhances RIGI-induced type I interferon production probably by helping RIGI at sensing pathogenic RNA (PubMed:30804210). May also act as a phosphorylation-dependent sequence-specific endoribonuclease in vitro: Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR (PubMed:11604510). {ECO:0000269|PubMed:11604510, ECO:0000269|PubMed:12642610, ECO:0000269|PubMed:20180778, ECO:0000269|PubMed:23279204, ECO:0000269|PubMed:27022092, ECO:0000269|PubMed:30510222, ECO:0000269|PubMed:30804210, ECO:0000269|PubMed:32302570, ECO:0000269|PubMed:32302571, ECO:0000269|PubMed:32302572, ECO:0000269|PubMed:34739333, ECO:0000269|PubMed:34779554, ECO:0000269|PubMed:35977029, ECO:0000269|PubMed:36183834, ECO:0000269|PubMed:36279435, ECO:0000269|PubMed:36692217, ECO:0000269|PubMed:37379838, ECO:0000269|PubMed:9889278}. |
| Q13303 | KCNAB2 | T6 | ochoa|psp | Voltage-gated potassium channel subunit beta-2 (EC 1.1.1.-) (K(+) channel subunit beta-2) (Kv-beta-2) (hKvbeta2) | Regulatory subunit of the voltage-gated potassium (Kv) Shaker channels composed of pore-forming and potassium-conducting alpha subunits and of regulatory beta subunits (PubMed:11825900, PubMed:7649300). The beta-2/KCNAB2 cytoplasmic subunit promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore (PubMed:11825900, PubMed:7649300). Promotes the inactivation of Kv1.4/KCNA4 and Kv1.5/KCNA5 alpha subunit-containing channels (PubMed:11825900, PubMed:7649300). Displays nicotinamide adenine dinucleotide phosphate (NADPH)-dependent aldoketoreductase activity by catalyzing the NADPH-dependent reduction of a wide range of aldehyde and ketone substrates (By similarity). Substrate specificity includes methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro, no physiological substrate identified yet) (By similarity). The binding of oxidized and reduced nucleotide alters Kv channel gating and may contribute to dynamic fine tuning of cell excitability (By similarity). Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (By similarity). {ECO:0000250|UniProtKB:P62482, ECO:0000250|UniProtKB:P62483, ECO:0000269|PubMed:11825900, ECO:0000269|PubMed:7649300}. |
| Q13303 | KCNAB2 | T7 | ochoa|psp | Voltage-gated potassium channel subunit beta-2 (EC 1.1.1.-) (K(+) channel subunit beta-2) (Kv-beta-2) (hKvbeta2) | Regulatory subunit of the voltage-gated potassium (Kv) Shaker channels composed of pore-forming and potassium-conducting alpha subunits and of regulatory beta subunits (PubMed:11825900, PubMed:7649300). The beta-2/KCNAB2 cytoplasmic subunit promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore (PubMed:11825900, PubMed:7649300). Promotes the inactivation of Kv1.4/KCNA4 and Kv1.5/KCNA5 alpha subunit-containing channels (PubMed:11825900, PubMed:7649300). Displays nicotinamide adenine dinucleotide phosphate (NADPH)-dependent aldoketoreductase activity by catalyzing the NADPH-dependent reduction of a wide range of aldehyde and ketone substrates (By similarity). Substrate specificity includes methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro, no physiological substrate identified yet) (By similarity). The binding of oxidized and reduced nucleotide alters Kv channel gating and may contribute to dynamic fine tuning of cell excitability (By similarity). Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (By similarity). {ECO:0000250|UniProtKB:P62482, ECO:0000250|UniProtKB:P62483, ECO:0000269|PubMed:11825900, ECO:0000269|PubMed:7649300}. |
| Q13404 | UBE2V1 | S7 | ochoa | Ubiquitin-conjugating enzyme E2 variant 1 (UEV-1) (CROC-1) (TRAF6-regulated IKK activator 1 beta Uev1A) | Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. Together with RNF135 and UBE2N, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (PubMed:31006531). UBE2V1-UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway. {ECO:0000269|PubMed:11057907, ECO:0000269|PubMed:19825828, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:31006531, ECO:0000269|PubMed:9305758, ECO:0000269|PubMed:9418904, ECO:0000269|PubMed:9580084, ECO:0000269|PubMed:9705497}. |
| Q13522 | PPP1R1A | S6 | ochoa | Protein phosphatase 1 regulatory subunit 1A (Protein phosphatase inhibitor 1) (I-1) (IPP-1) | Inhibitor of protein-phosphatase 1. This protein may be important in hormonal control of glycogen metabolism. Hormones that elevate intracellular cAMP increase I-1 activity in many tissues. I-1 activation may impose cAMP control over proteins that are not directly phosphorylated by PKA. Following a rise in intracellular calcium, I-1 is inactivated by calcineurin (or PP2B). Does not inhibit type-2 phosphatases. |
| Q13541 | EIF4EBP1 | S6 | ochoa | Eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) (eIF4E-binding protein 1) (Phosphorylated heat- and acid-stable protein regulated by insulin 1) (PHAS-I) | Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. {ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22684010, ECO:0000269|PubMed:7935836}. |
| Q13542 | EIF4EBP2 | S7 | ochoa | Eukaryotic translation initiation factor 4E-binding protein 2 (4E-BP2) (eIF4E-binding protein 2) | Repressor of translation initiation involved in synaptic plasticity, learning and memory formation (PubMed:30765518). Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (PubMed:25533957, PubMed:30765518). EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation (By similarity). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (By similarity). {ECO:0000250|UniProtKB:P70445, ECO:0000269|PubMed:25533957, ECO:0000269|PubMed:30765518}. |
| Q13561 | DCTN2 | Y6 | ochoa | Dynactin subunit 2 (50 kDa dynein-associated polypeptide) (Dynactin complex 50 kDa subunit) (DCTN-50) (p50 dynamitin) | Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In the dynactin soulder domain, binds the ACTR1A filament and acts as a molecular ruler to determine the length (By similarity). Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development (By similarity). {ECO:0000250|UniProtKB:A0A5G2QD80, ECO:0000250|UniProtKB:Q99KJ8}. |
| Q13614 | MTMR2 | S6 | ochoa | Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2 (EC 3.1.3.95) (Myotubularin-related protein 2) (Phosphatidylinositol-3-phosphate phosphatase) | Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate (PubMed:11733541, PubMed:12668758, PubMed:14690594, PubMed:21372139). Regulates the level of these phosphoinositides critical for various biological processes including autophagy initiation and autophagosome maturation (PubMed:35580604). {ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:14690594, ECO:0000269|PubMed:21372139, ECO:0000269|PubMed:35580604}. |
| Q13671 | RIN1 | S7 | ochoa | Ras and Rab interactor 1 (Ras inhibitor JC99) (Ras interaction/interference protein 1) | Ras effector protein, which may serve as an inhibitory modulator of neuronal plasticity in aversive memory formation. Can affect Ras signaling at different levels. First, by competing with RAF1 protein for binding to activated Ras. Second, by enhancing signaling from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by activating RAB5A, possibly by functioning as a guanine nucleotide exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP, and facilitating Ras-activated receptor endocytosis. {ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9208849}. |
| Q13769 | THOC5 | S6 | psp | THO complex subunit 5 (Functional spliceosome-associated protein 79) (fSAP79) (NF2/meningioma region protein pK1.3) (Placental protein 39.2) (PP39.2) (hTREX90) | Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Plays a key structural role in the oligomerization of the THO-DDX39B complex (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in transcription elongation and genome stability (PubMed:18974867). Involved in alternative polyadenylation site choice by recruiting CPSF6 to 5' region of target genes; probably mediates association of the TREX and CFIm complexes (PubMed:23685434). {ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:18974867, ECO:0000269|PubMed:23685434, ECO:0000269|PubMed:33191911}.; FUNCTION: Regulates the expression of myeloid transcription factors CEBPA, CEBPB and GAB2 by enhancing the levels of phosphatidylinositol 3,4,5-trisphosphate. May be involved in the differentiation of granulocytes and adipocytes. Essential for hematopoietic primitive cell survival and plays an integral role in monocytic development. {ECO:0000250|UniProtKB:Q8BKT7}.; 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}. |
| Q14004 | CDK13 | T7 | ochoa | Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller) | Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. {ECO:0000269|PubMed:16721827, ECO:0000269|PubMed:1731328, ECO:0000269|PubMed:18480452, ECO:0000269|PubMed:20952539}. |
| Q14061 | COX17 | S7 | ochoa | Cytochrome c oxidase copper chaperone | Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2). {ECO:0000269|PubMed:19393246}. |
| Q14134 | TRIM29 | S7 | ochoa | Tripartite motif-containing protein 29 (Ataxia telangiectasia group D-associated protein) | Plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. Mechanistically, TRIM29 interacts with IKBKG/NEMO in the lysosome where it induces its 'Lys-48' ubiquitination and subsequent degradation. In turn, the expression of type I interferons and the production of pro-inflammatory cytokines are inhibited. Additionally, induces the 'Lys-48' ubiquitination of STING1 in a similar way, leading to its degradation. {ECO:0000269|PubMed:27695001, ECO:0000269|PubMed:29038422}. |
| Q14161 | GIT2 | S7 | ochoa | ARF GTPase-activating protein GIT2 (ARF GAP GIT2) (Cool-interacting tyrosine-phosphorylated protein 2) (CAT-2) (CAT2) (G protein-coupled receptor kinase-interactor 2) (GRK-interacting protein 2) | GTPase-activating protein for ADP ribosylation factor family members, including ARF1. {ECO:0000269|PubMed:10896954}. |
| Q14315 | FLNC | Y7 | ochoa | Filamin-C (FLN-C) (FLNc) (ABP-280-like protein) (ABP-L) (Actin-binding-like protein) (Filamin-2) (Gamma-filamin) | Muscle-specific filamin, which plays a central role in sarcomere assembly and organization (PubMed:34405687). Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events (By similarity). {ECO:0000250|UniProtKB:Q8VHX6, ECO:0000269|PubMed:34405687}. |
| Q14451 | GRB7 | S6 | ochoa | Growth factor receptor-bound protein 7 (B47) (Epidermal growth factor receptor GRB-7) (GRB7 adapter protein) | Adapter protein that interacts with the cytoplasmic domain of numerous receptor kinases and modulates down-stream signaling. Promotes activation of down-stream protein kinases, including STAT3, AKT1, MAPK1 and/or MAPK3. Promotes activation of HRAS. Plays a role in signal transduction in response to EGF. Plays a role in the regulation of cell proliferation and cell migration. Plays a role in the assembly and stability of RNA stress granules. Binds to the 5'UTR of target mRNA molecules and represses translation of target mRNA species, when not phosphorylated. Phosphorylation impairs RNA binding and promotes stress granule disassembly during recovery after cellular stress (By similarity). {ECO:0000250, ECO:0000269|PubMed:10893408, ECO:0000269|PubMed:12021278, ECO:0000269|PubMed:12223469, ECO:0000269|PubMed:20622016}. |
| Q14493 | SLBP | S7 | ochoa|psp | Histone RNA hairpin-binding protein (Histone stem-loop-binding protein) | RNA-binding protein involved in the histone pre-mRNA processing (PubMed:12588979, PubMed:19155325, PubMed:8957003, PubMed:9049306). Binds the stem-loop structure of replication-dependent histone pre-mRNAs and contributes to efficient 3'-end processing by stabilizing the complex between histone pre-mRNA and U7 small nuclear ribonucleoprotein (snRNP), via the histone downstream element (HDE) (PubMed:12588979, PubMed:19155325, PubMed:8957003, PubMed:9049306). Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery (PubMed:12588979, PubMed:19155325, PubMed:8957003, PubMed:9049306). Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression (PubMed:12588979, PubMed:19155325, PubMed:8957003, PubMed:9049306). Involved in the mechanism by which growing oocytes accumulate histone proteins that support early embryogenesis (By similarity). Binds to the 5' side of the stem-loop structure of histone pre-mRNAs (By similarity). {ECO:0000250|UniProtKB:P97440, ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:19155325, ECO:0000269|PubMed:8957003, ECO:0000269|PubMed:9049306}. |
| Q14568 | HSP90AA2P | T7 | ochoa | Heat shock protein HSP 90-alpha A2 (Heat shock 90 kDa protein 1 alpha-like 3) (Heat shock protein HSP 90-alpha A2 pseudogene) (Heat shock protein family C member 2) | Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}. |
| Q14690 | PDCD11 | S7 | ochoa | Protein RRP5 homolog (NF-kappa-B-binding protein) (NFBP) (Programmed cell death protein 11) | Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA. {ECO:0000269|PubMed:17654514}.; FUNCTION: Involved in the biogenesis of rRNA. {ECO:0000250}. |
| Q14789 | GOLGB1 | S6 | ochoa | Golgin subfamily B member 1 (372 kDa Golgi complex-associated protein) (GCP372) (Giantin) (Macrogolgin) | May participate in forming intercisternal cross-bridges of the Golgi complex. |
| Q14CB8 | ARHGAP19 | S7 | ochoa | Rho GTPase-activating protein 19 (Rho-type GTPase-activating protein 19) | GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. |
| Q15019 | SEPTIN2 | T7 | ochoa | Septin-2 (Neural precursor cell expressed developmentally down-regulated protein 5) (NEDD-5) | Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (PubMed:25588830). Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements. In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri. {ECO:0000269|PubMed:15774761, ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18209106, ECO:0000269|PubMed:19145258, ECO:0000305|PubMed:25588830}. |
| Q15020 | SART3 | T7 | ochoa | Spliceosome associated factor 3, U4/U6 recycling protein (Squamous cell carcinoma antigen recognized by T-cells 3) (SART-3) (Tat-interacting protein of 110 kDa) (Tip110) (p110 nuclear RNA-binding protein) | U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation (PubMed:12032085). Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites (PubMed:14749385). May also function as a substrate-targeting factor for deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3 deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly (PubMed:20595234). May also recruit the deubiquitinase USP15 to histone H2B and mediate histone deubiquitination, thereby regulating gene expression and/or DNA repair (PubMed:24526689). May play a role in hematopoiesis probably through transcription regulation of specific genes including MYC (By similarity). {ECO:0000250|UniProtKB:Q9JLI8, ECO:0000269|PubMed:12032085, ECO:0000269|PubMed:14749385, ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:24526689}.; FUNCTION: Regulates Tat transactivation activity through direct interaction. May be a cellular factor for HIV-1 gene expression and viral replication. {ECO:0000269|PubMed:11959860}. |
| Q15056 | EIF4H | T6 | ochoa | 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}. |
| Q15056 | EIF4H | Y7 | ochoa | 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}. |
| Q15058 | KIF14 | T6 | 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}. |
| Q15208 | STK38 | S6 | ochoa|psp | Serine/threonine-protein kinase 38 (EC 2.7.11.1) (NDR1 protein kinase) (Nuclear Dbf2-related kinase 1) | Serine/threonine-protein kinase that acts as a negative regulator of MAP3K1/2 signaling (PubMed:12493777, PubMed:15197186, PubMed:17906693, PubMed:7761441). Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2 (PubMed:12493777, PubMed:15197186, PubMed:17906693, PubMed:7761441). Acts as an ufmylation 'reader' in a kinase-independent manner: specifically recognizes and binds mono-ufmylated histone H4 in response to DNA damage, promoting the recruitment of SUV39H1 to the double-strand breaks, resulting in ATM activation (PubMed:32537488). {ECO:0000269|PubMed:12493777, ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:17906693, ECO:0000269|PubMed:32537488, ECO:0000269|PubMed:7761441}. |
| Q15208 | STK38 | T7 | ochoa|psp | Serine/threonine-protein kinase 38 (EC 2.7.11.1) (NDR1 protein kinase) (Nuclear Dbf2-related kinase 1) | Serine/threonine-protein kinase that acts as a negative regulator of MAP3K1/2 signaling (PubMed:12493777, PubMed:15197186, PubMed:17906693, PubMed:7761441). Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2 (PubMed:12493777, PubMed:15197186, PubMed:17906693, PubMed:7761441). Acts as an ufmylation 'reader' in a kinase-independent manner: specifically recognizes and binds mono-ufmylated histone H4 in response to DNA damage, promoting the recruitment of SUV39H1 to the double-strand breaks, resulting in ATM activation (PubMed:32537488). {ECO:0000269|PubMed:12493777, ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:17906693, ECO:0000269|PubMed:32537488, ECO:0000269|PubMed:7761441}. |
| Q15424 | SAFB | S6 | ochoa | Scaffold attachment factor B1 (SAF-B) (SAF-B1) (HSP27 estrogen response element-TATA box-binding protein) (HSP27 ERE-TATA-binding protein) | Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (PubMed:9671816). Functions as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription (PubMed:12660241). Thereby acts as a negative regulator of cell proliferation (PubMed:12660241). When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (By similarity). {ECO:0000250|UniProtKB:D3YXK2, ECO:0000269|PubMed:12660241, ECO:0000269|PubMed:9671816}. |
| Q15544 | TAF11 | S7 | ochoa | Transcription initiation factor TFIID subunit 11 (TFIID subunit p30-beta) (Transcription initiation factor TFIID 28 kDa subunit) (TAF(II)28) (TAFII-28) (TAFII28) | 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). TAF11, together with TAF13 and TBP, play key roles during promoter binding by the TFIID and TFIIA transcription factor complexes (PubMed:33795473). {ECO:0000269|PubMed:33795473}. |
| Q15555 | MAPRE2 | T7 | ochoa | Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2) (End-binding protein 2) (EB2) | Adapter protein that is involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. Therefore, ensures mitotic progression and genome stability (PubMed:27030108). Acts as a central regulator of microtubule reorganization in apico-basal epithelial differentiation (By similarity). Plays a role during oocyte meiosis by regulating microtubule dynamics (By similarity). Participates in neurite growth by interacting with plexin B3/PLXNB3 and microtubule reorganization during apico-basal epithelial differentiation (PubMed:22373814). Also plays an essential role for cell migration and focal adhesion dynamics. Mechanistically, recruits HAX1 to microtubules in order to regulate focal adhesion dynamics (PubMed:26527684). {ECO:0000250|UniProtKB:Q8R001, ECO:0000269|PubMed:22373814, ECO:0000269|PubMed:23844040, ECO:0000269|PubMed:26527684, ECO:0000269|PubMed:27030108}. |
| Q15651 | HMGN3 | S6 | ochoa | High mobility group nucleosome-binding domain-containing protein 3 (Thyroid receptor-interacting protein 7) (TR-interacting protein 7) (TRIP-7) | Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function (By similarity). {ECO:0000250}. |
| Q15691 | MAPRE1 | Y6 | ochoa | Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1) (End-binding protein 1) (EB1) | Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:23001180, PubMed:28726242, PubMed:28814570, PubMed:34608293). Recruits other +TIP proteins to microtubules by binding to a conserved Ser-X-Leu-Pro (SXLP) motif in their polypeptide chains (PubMed:19632184, PubMed:36592928). Promotes cytoplasmic microtubule nucleation and elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). Involved in mitotic spindle positioning by stabilizing microtubules and promoting dynamic connection between astral microtubules and the cortex during mitotic chromosome segregation (PubMed:12388762, PubMed:34608293). Assists chromosome alignment in metaphase by recruiting the SKA complex to the spindle and stabilizing its interactions with microtubule bundles (K-fibers) (PubMed:27225956, PubMed:36592928). Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:28814570). Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (PubMed:28814570). Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (PubMed:28726242). Functions downstream of Rho GTPases and DIAPH1 in stable microtubule formation (By similarity). May play a role in cell migration (By similarity). {ECO:0000250|UniProtKB:Q61166, ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:16109370, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:23001180, ECO:0000269|PubMed:27225956, ECO:0000269|PubMed:28726242, ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:34608293, ECO:0000269|PubMed:36592928}. |
| Q15742 | NAB2 | S6 | ochoa | NGFI-A-binding protein 2 (EGR-1-binding protein 2) (Melanoma-associated delayed early response protein) (Protein MADER) | Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability (By similarity). {ECO:0000250}. |
| Q15750 | TAB1 | S7 | ochoa | TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 1) (TGF-beta-activated kinase 1-binding protein 1) (TAK1-binding protein 1) | Key adapter protein that plays an essential role in JNK and NF-kappa-B activation and proinflammatory cytokines production in response to stimulation with TLRs and cytokines (PubMed:22307082, PubMed:24403530). Mechanistically, associates with the catalytic domain of MAP3K7/TAK1 to trigger MAP3K7/TAK1 autophosphorylation leading to its full activation (PubMed:10838074, PubMed:25260751, PubMed:37832545). Similarly, associates with MAPK14 and triggers its autophosphorylation and subsequent activation (PubMed:11847341, PubMed:29229647). In turn, MAPK14 phosphorylates TAB1 and inhibits MAP3K7/TAK1 activation in a feedback control mechanism (PubMed:14592977). Also plays a role in recruiting MAPK14 to the TAK1 complex for the phosphorylation of the TAB2 and TAB3 regulatory subunits (PubMed:18021073). {ECO:0000269|PubMed:10838074, ECO:0000269|PubMed:11847341, ECO:0000269|PubMed:14592977, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:22307082, ECO:0000269|PubMed:24403530, ECO:0000269|PubMed:25260751, ECO:0000269|PubMed:29229647, ECO:0000269|PubMed:37832545}. |
| Q15788 | NCOA1 | S7 | ochoa | Nuclear receptor coactivator 1 (NCoA-1) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 74) (bHLHe74) (Protein Hin-2) (RIP160) (Renal carcinoma antigen NY-REN-52) (Steroid receptor coactivator 1) (SRC-1) | Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3. {ECO:0000269|PubMed:10449719, ECO:0000269|PubMed:12954634, ECO:0000269|PubMed:7481822, ECO:0000269|PubMed:9223281, ECO:0000269|PubMed:9223431, ECO:0000269|PubMed:9296499, ECO:0000269|PubMed:9427757}. |
| Q15836 | VAMP3 | T6 | ochoa | Vesicle-associated membrane protein 3 (VAMP-3) (Cellubrevin) (CEB) (Synaptobrevin-3) | SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269|PubMed:18195106}. |
| Q15911 | ZFHX3 | S6 | ochoa | Zinc finger homeobox protein 3 (AT motif-binding factor 1) (AT-binding transcription factor 1) (Alpha-fetoprotein enhancer-binding protein) (Zinc finger homeodomain protein 3) (ZFH-3) | Transcriptional regulator which can act as an activator or a repressor. Inhibits the enhancer element of the AFP gene by binding to its AT-rich core sequence. In concert with SMAD-dependent TGF-beta signaling can repress the transcription of AFP via its interaction with SMAD2/3 (PubMed:25105025). Regulates the circadian locomotor rhythms via transcriptional activation of neuropeptidergic genes which are essential for intercellular synchrony and rhythm amplitude in the suprachiasmatic nucleus (SCN) of the brain (By similarity). Regulator of myoblasts differentiation through the binding to the AT-rich sequence of MYF6 promoter and promoter repression (PubMed:11312261). Down-regulates the MUC5AC promoter in gastric cancer (PubMed:17330845). In association with RUNX3, up-regulates CDKN1A promoter activity following TGF-beta stimulation (PubMed:20599712). Inhibits estrogen receptor (ESR1) function by selectively competing with coactivator NCOA3 for binding to ESR1 in ESR1-positive breast cancer cells (PubMed:20720010). {ECO:0000250|UniProtKB:Q61329, ECO:0000269|PubMed:11312261, ECO:0000269|PubMed:17330845, ECO:0000269|PubMed:20599712, ECO:0000269|PubMed:20720010, ECO:0000269|PubMed:25105025}. |
| Q15942 | ZYX | S7 | ochoa | Zyxin (Zyxin-2) | Adhesion plaque protein. Binds alpha-actinin and the CRP protein. Important for targeting TES and ENA/VASP family members to focal adhesions and for the formation of actin-rich structures. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity). {ECO:0000250}. |
| Q16537 | PPP2R5E | T7 | ochoa | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform (PP2A B subunit isoform B'-epsilon) (PP2A B subunit isoform B56-epsilon) (PP2A B subunit isoform PR61-epsilon) (PP2A B subunit isoform R5-epsilon) | The B regulatory subunit might modulate substrate selectivity and catalytic activity, and might also direct the localization of the catalytic enzyme to a particular subcellular compartment. |
| Q16619 | CTF1 | S7 | ochoa | Cardiotrophin-1 (CT-1) | Induces cardiac myocyte hypertrophy in vitro. Binds to and activates the ILST/gp130 receptor. |
| Q16643 | DBN1 | S7 | ochoa | Drebrin (Developmentally-regulated brain protein) | Actin cytoskeleton-organizing protein that plays a role in the formation of cell projections (PubMed:20215400). Required for actin polymerization at immunological synapses (IS) and for the recruitment of the chemokine receptor CXCR4 to IS (PubMed:20215400). Plays a role in dendritic spine morphogenesis and organization, including the localization of the dopamine receptor DRD1 to the dendritic spines (By similarity). Involved in memory-related synaptic plasticity in the hippocampus (By similarity). {ECO:0000250|UniProtKB:Q9QXS6, ECO:0000269|PubMed:20215400}. |
| Q16778 | H2BC21 | S7 | ochoa | Histone H2B type 2-E (H2B-clustered histone 21) (Histone H2B-GL105) (Histone H2B.q) (H2B/q) | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; FUNCTION: Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid. |
| Q2HXU8 | CLEC12B | Y7 | psp | C-type lectin domain family 12 member B (Macrophage antigen H) | Inhibitory receptor postulated to negatively regulate immune and non-immune functions (PubMed:17562706, PubMed:34310951). Upon phosphorylation, recruits SH2 domain-containing PTPN6 and PTPN11 phosphatases to its ITIM motif and antagonizes activation signals (PubMed:17562706, PubMed:34310951). Although it inhibits KLRK1/NKG2D-mediated signaling, it does not bind known ligands of KLRK1/NKG2D and therefore is not its inhibitory counterpart (PubMed:17562706). May limit activation of myeloid cell subsets in response to infection or tissue inflammation (PubMed:17562706). May protect target cells against natural killer cell-mediated lysis (PubMed:17562706). May negatively regulate cell cycle and differentiation of melanocytes via inactivation of STAT3 (PubMed:34310951). {ECO:0000269|PubMed:17562706, ECO:0000269|PubMed:34310951}. |
| Q2M389 | WASHC4 | S7 | ochoa | WASH complex subunit 4 (Strumpellin and WASH-interacting protein) (SWIP) (WASH complex subunit SWIP) | Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. {ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093, ECO:0000303|PubMed:21498477}. |
| Q4V339 | ZNG1F | S7 | ochoa | Zinc-regulated GTPase metalloprotein activator 1F (EC 3.6.5.-) (Cobalamin synthase W domain-containing protein 6) (COBW domain-containing protein 6) | Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them (By similarity). Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation (PubMed:35584702). Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1 (By similarity). After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1F to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis (By similarity). GTP/GDP exchange is required for release of active METAP1 (By similarity). {ECO:0000250|UniProtKB:Q8VEH6, ECO:0000269|PubMed:35584702}. |
| Q4VC44 | FLYWCH1 | S7 | ochoa | FLYWCH-type zinc finger-containing protein 1 | Transcription cofactor (PubMed:30097457). Negatively regulates transcription activation by catenin beta-1 CTNNB1, perhaps acting by competing with TCF4 for CTNNB1 binding (PubMed:30097457). May play a role in DNA-damage response signaling (PubMed:33924684). Binds specifically to DNA sequences at peri-centromeric chromatin loci. {ECO:0000269|PubMed:30097457, ECO:0000269|PubMed:33924684, ECO:0000269|PubMed:34408139}. |
| Q52LA3 | LIN52 | S7 | psp | Protein lin-52 homolog | None |
| Q53QZ3 | ARHGAP15 | S7 | ochoa | Rho GTPase-activating protein 15 (ArhGAP15) (Rho-type GTPase-activating protein 15) | GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction. {ECO:0000269|PubMed:12650940}. |
| Q5BKX5 | ACTMAP | S6 | ochoa | Actin maturation protease (EC 3.4.11.-) (Actin aminopeptidase ACTMAP) | Actin maturation protease that specifically mediates the cleavage of immature acetylated N-terminal actin, thereby contributing to actin maturation (PubMed:36173861). Cleaves N-terminal acetylated methionine of immature cytoplasmic beta- and gamma-actins ACTB and ACTG1 after translation (PubMed:36173861). Cleaves N-terminal acetylated cysteine of muscle alpha-actins ACTA1, ACTC1 and ACTA2 after canonical removal of N-terminal methionine (By similarity). {ECO:0000250|UniProtKB:J3QPC3, ECO:0000269|PubMed:36173861}. |
| Q5BKZ1 | ZNF326 | Y7 | ochoa | DBIRD complex subunit ZNF326 (Zinc finger protein 326) (Zinc finger protein interacting with mRNPs and DBC1) | Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro. {ECO:0000269|PubMed:22446626}. |
| Q5EBL8 | PDZD11 | Y7 | ochoa | PDZ domain-containing protein 11 (ATPase-interacting PDZ protein) (Plasma membrane calcium ATPase-interacting single-PDZ protein) (PMCA-interacting single-PDZ protein) | Mediates docking of ADAM10 to zonula adherens by interacting with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10-binding protein TSPAN33. {ECO:0000269|PubMed:30463011}. |
| Q5I0X4 | PEX39 | S6 | ochoa | Peroxisomal biogenesis factor 39 | May be a peroxin involved in the PTS2-mediated protein import pathway. {ECO:0000305|PubMed:37160800}. |
| Q5JSH3 | WDR44 | T7 | ochoa | WD repeat-containing protein 44 (Rab11-binding protein) (Rab11BP) (Rabphilin-11) | Downstream effector for Rab11 which regulates Rab11 intracellular membrane trafficking functions such as endocytic recycling, intracellular ciliogenesis and protein export (PubMed:31204173, PubMed:32344433). ATK1-mediated phosphorylation of WDR44 induces binding to Rab11 which activates endocytic recycling of transferrin receptor back to the plasma membrane (PubMed:31204173). When bound to Rab11, prevents the formation of the ciliogenic Rab11-Rabin8/RAB3IP-RAB11FIP3 complex, therefore inhibiting preciliary trafficking and ciliogenesis (PubMed:31204173). Participates in neo-synthesized protein export by connecting the endoplasmic reticulum (ER) with the endosomal tubule via direct interactions with the integral ER proteins VAPA or VAPB and the endosomal protein GRAFs (GRAF1/ARHGAP26 or GRAF2/ARHGAP10), which facilitates the transfer of proteins such as E-cadherin, MPP14 and CFTR into a Rab8-Rab10-Rab11-dependent export route (PubMed:32344433). {ECO:0000269|PubMed:31204173, ECO:0000269|PubMed:32344433}. |
| Q5JSP0 | FGD3 | S7 | ochoa | FYVE, RhoGEF and PH domain-containing protein 3 (Zinc finger FYVE domain-containing protein 5) | Promotes the formation of filopodia. May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape (By similarity). {ECO:0000250}. |
| Q5JTY5 | ZNG1C | S7 | ochoa | Zinc-regulated GTPase metalloprotein activator 1C (EC 3.6.5.-) (Cobalamin synthase W domain-containing protein 3) (COBW domain-containing protein 3) | Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1C to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1. {ECO:0000250|UniProtKB:Q8VEH6}. |
| Q5JVS0 | HABP4 | S7 | ochoa | Intracellular hyaluronan-binding protein 4 (IHABP-4) (IHABP4) (Hyaluronan-binding protein 4) (Ki-1/57 intracellular antigen) | Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with EEF2/eEF2 factor at the A-site of the ribosome, promoting ribosome stabilization in an inactive state compatible with storage (By similarity). Plays a key role in ribosome hibernation in the mature oocyte by promoting ribosome stabilization (By similarity). Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the oocyte and early embryo (By similarity). Also binds RNA, regulating transcription and pre-mRNA splicing (PubMed:14699138, PubMed:16455055, PubMed:19523114, PubMed:21771594). Binds (via C-terminus) to poly(U) RNA (PubMed:19523114). Seems to play a role in PML-nuclear bodies formation (PubMed:28695742). Negatively regulates DNA-binding activity of the transcription factor MEF2C in myocardial cells in response to mechanical stress (By similarity). {ECO:0000250|UniProtKB:A1L1K8, ECO:0000250|UniProtKB:Q5XJA5, ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:16455055, ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:21771594, ECO:0000269|PubMed:28695742}. |
| Q5QGZ9 | CLEC12A | Y7 | ochoa | C-type lectin domain family 12 member A (C-type lectin-like molecule 1) (CLL-1) (Dendritic cell-associated lectin 2) (DCAL-2) (Killer cell C-type lectin-like receptor L1) (hKLRL1) (Myeloid inhibitory C-type lectin-like receptor) (MICL) (CD antigen CD371) | Myeloid inhibitory C-type lectin receptor that acts as a negative regulator of myeloid cell activation (PubMed:14739280, PubMed:15238421, PubMed:16239426, PubMed:34234773, PubMed:38367667, PubMed:38386511, PubMed:39143217). Myeloid cell inhibition is required to limit proinflammatory pathways and protect against excessive inflammation (By similarity). Specifically recognizes and binds various structures, such as neutrophil extracellular traps (NETs) or monosodium urate crystals (PubMed:38367667, PubMed:38386511, PubMed:39143217). Also acts as a pattern-recognition receptor for pathogen-associated molecules, such as plasmodium hemozoin or mycobacterial micolic acid (PubMed:31269448, PubMed:36542980). Ligand-binding induces phosphorylation of its ITIM motif, followed by recruitment of tyrosine-protein phosphatases PTPN6 and PTPN11, which counteract tyrosine-protein kinase SYK, thereby preventing myeloid cell activation (PubMed:14739280, PubMed:16239426, PubMed:34234773). Acts as a pattern-recognition receptor for NETs in neutrophils: specifically recognizes DNA in NETs, leading to inhibit neutrophil activation and limit further NET formation (PubMed:39143217). This regulation is essential for controlling key neutrophil responses and limit NET-mediated inflammatory conditions (By similarity). Also recognizes dead cells by acting as a receptor for monosodium urate crystals, leading to down-regulate neutrophil activation (PubMed:38367667, PubMed:38386511). Binding to monosodium urate crystals also promotes the type I interferon response (By similarity). Acts as an inhibitor of natural killer (NK) cell cytotoxicity (PubMed:15238421). Also acts as an ihibitor of dendritic cell maturation in an IL10-dependent manner (PubMed:16239426). {ECO:0000250|UniProtKB:Q504P2, ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:15238421, ECO:0000269|PubMed:16239426, ECO:0000269|PubMed:31269448, ECO:0000269|PubMed:34234773, ECO:0000269|PubMed:36542980, ECO:0000269|PubMed:38367667, ECO:0000269|PubMed:38386511, ECO:0000269|PubMed:39143217}. |
| Q5RIA9 | ZNG1E | S7 | ochoa | Zinc-regulated GTPase metalloprotein activator 1E (EC 3.6.5.-) (Cobalamin synthase W domain-containing protein 5) (COBW domain-containing protein 5) | Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1E to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1. {ECO:0000250|UniProtKB:Q8VEH6}. |
| Q5SGD2 | PPM1L | T7 | ochoa | Protein phosphatase 1L (EC 3.1.3.16) (Protein phosphatase 1-like) (Protein phosphatase 2C isoform epsilon) (PP2C-epsilon) | Acts as a suppressor of the SAPK signaling pathways by associating with and dephosphorylating MAP3K7/TAK1 and MAP3K5, and by attenuating the association between MAP3K7/TAK1 and MAP2K4 or MAP2K6. {ECO:0000269|PubMed:17456047}. |
| Q5SSJ5 | HP1BP3 | S6 | ochoa | Heterochromatin protein 1-binding protein 3 (Protein HP1-BP74) | Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity (PubMed:24830416). Mediates chromatin condensation during hypoxia, leading to increased tumor cell viability, radio-resistance, chemo-resistance and self-renewal (PubMed:25100860). {ECO:0000269|PubMed:24830416, ECO:0000269|PubMed:25100860}. |
| Q5T7W7 | TSTD2 | S6 | ochoa | Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 2 (Rhodanese domain-containing protein 2) | None |
| Q5UIP0 | RIF1 | S7 | 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}. |
| Q5VTE0 | EEF1A1P5 | T6 | 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}. |
| Q5VV41 | ARHGEF16 | S6 | ochoa | Rho guanine nucleotide exchange factor 16 (Ephexin-4) | Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 and mediate activation of CDC42 by the viral protein HPV16 E6. {ECO:0000269|PubMed:20679435}. |
| Q5VWZ2 | LYPLAL1 | S7 | ochoa | Lysophospholipase-like protein 1 (EC 3.1.2.22) | Palmitoyl thioesterase that catalyzes depalmitoylation of CGAS and KCNMA1 (PubMed:22052940, PubMed:22399288, PubMed:37802025). Acts as a regulator of innate immunity by mediating depalmitoylation of CGAS, thereby preventing CGAS homodimerization and cyclic GMP-AMP synthase activity (PubMed:37802025). Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site (PubMed:22052940). {ECO:0000269|PubMed:22052940, ECO:0000269|PubMed:22399288, ECO:0000269|PubMed:37802025}. |
| Q5VZE5 | NAA35 | S6 | ochoa | N-alpha-acetyltransferase 35, NatC auxiliary subunit (Embryonic growth-associated protein homolog) (Protein MAK10 homolog) | Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues (PubMed:19398576, PubMed:37891180). N-terminal acetylation protects proteins from ubiquitination and degradation by the N-end rule pathway (PubMed:37891180). Involved in regulation of apoptosis and proliferation of smooth muscle cells (PubMed:19398576). {ECO:0000269|PubMed:19398576, ECO:0000269|PubMed:37891180}. |
| Q5XXA6 | ANO1 | Y7 | ochoa | Anoctamin-1 (Discovered on gastrointestinal stromal tumors protein 1) (Oral cancer overexpressed protein 2) (Transmembrane protein 16A) (Tumor-amplified and overexpressed sequence 2) | Calcium-activated chloride channel (CaCC) (PubMed:20056604, PubMed:22178883, PubMed:22946059, PubMed:32487539). Plays a role in transepithelial anion transport and smooth muscle contraction. Required for the normal functioning of the interstitial cells of Cajal (ICCs) which generate electrical pacemaker activity in gastrointestinal smooth muscles. Acts as a major contributor to basal and stimulated chloride conductance in airway epithelial cells and plays an important role in tracheal cartilage development. Required for CFTR activation by enhancing endoplasmic reticulum Ca(2+) store release and is also required for CFTR membrane expression (PubMed:28963502). Required for basal and ATP-dependent mucus secretion in airways and intestine, probably by controlling exocytosis of mucus-filled granules by providing Ca(2+) to an apical signaling compartment (By similarity). Contributes to airway mucus expression induced by interleukins IL3 and IL8 and by the asthma-associated protein CLCA1 and is required for expression of mucin MUC5AC (PubMed:33026825). However, was shown in another study not to be required for MUC5AC expression (PubMed:31732694). Plays a role in the propagation of Ca(2+) waves in Kolliker's organ in the cochlea and contributes to the refinement of auditory brainstem circuitries prior to hearing onset (By similarity). In vomeronasal sensory neurons, modulates spontaneous firing patterns in the absence of stimuli as well as the firing pattern of pheromone-evoked activity (By similarity). Responsible for calcium-activated chloride channel activity in type I taste cells of the vallate papillae (By similarity). Acts as a heat sensor in nociceptive neurons (By similarity). In dorsal root ganglion neurons, plays a role in mediating non-histaminergic Mas-related G-protein coupled receptor (MRGPR)-dependent itching, acting as a downstream effector of MRGPRs (By similarity). In the developing brain, required for the Ca(2+)-dependent process extension of radial glial cells (By similarity). {ECO:0000250|UniProtKB:Q8BHY3, ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22178883, ECO:0000269|PubMed:22946059, ECO:0000269|PubMed:28963502, ECO:0000269|PubMed:31732694, ECO:0000269|PubMed:32487539, ECO:0000269|PubMed:33026825, ECO:0000269|PubMed:37253099}.; FUNCTION: [Isoform 4]: Calcium-activated chloride channel (CaCC). Contributes to calcium-activated chloride secretion in human sweat gland epithelial cells. Shows increased basal chloride permeability and decreased Ca(2+)-induced chloride permeability. {ECO:0000269|PubMed:25220078}.; FUNCTION: [Isoform 5]: Calcium-activated chloride channel (CaCC). Shows increased sensitivity to intracellular Ca(2+). {ECO:0000269|PubMed:26359375}. |
| Q641Q2 | WASHC2A | T6 | ochoa | WASH complex subunit 2A | Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes inhibits WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization and is involved in the fission of tubules that serve as transport intermediates during endosome sorting. Mediates the recruitment of the WASH core complex to endosome membranes via binding to phospholipids and VPS35 of the retromer CSC. Mediates the recruitment of the F-actin-capping protein dimer to the WASH core complex probably promoting localized F-actin polymerization needed for vesicle scission. Via its C-terminus binds various phospholipids, most strongly phosphatidylinositol 4-phosphate (PtdIns-(4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Required for the association of DNAJC13, ENTR1, ANKRD50 with retromer CSC subunit VPS35. Required for the endosomal recruitment of CCC complex subunits COMMD1 and CCDC93 as well as the retriever complex subunit VPS35L. {ECO:0000269|PubMed:25355947, ECO:0000269|PubMed:28892079}. |
| Q66K64 | DCAF15 | S7 | ochoa | 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}. |
| Q684P5 | RAP1GAP2 | S7 | ochoa|psp | Rap1 GTPase-activating protein 2 (Rap1GAP2) (GTPase-activating Rap/Ran-GAP domain-like protein 4) | GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. {ECO:0000269|PubMed:15632203}. |
| Q6AWC2 | WWC2 | S7 | ochoa | Protein WWC2 (BH-3-only member B) (WW domain-containing protein 2) | Regulator of the Hippo signaling pathway, also known as the Salvador-Warts-Hippo (SWH) pathway. Enhances phosphorylation of LATS1 and YAP1 and negatively regulates cell proliferation and organ growth due to a suppression of the transcriptional activity of YAP1, the major effector of the Hippo pathway. {ECO:0000269|PubMed:24682284}. |
| Q6NSJ2 | PHLDB3 | S6 | ochoa | Pleckstrin homology-like domain family B member 3 | None |
| Q6NXS1 | PPP1R2B | S7 | ochoa | Protein phosphatase inhibitor 2 family member B (PPP1R2 family member B) (Protein phosphatase 1, regulatory subunit 2 pseudogene 3) (Protein phosphatase inhibitor 2-like protein 3) | Inhibitor of protein-phosphatase 1. {ECO:0000269|PubMed:23506001}. |
| Q6P1K2 | PMF1 | S6 | ochoa | Polyamine-modulated factor 1 (PMF-1) | Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT. {ECO:0000269|PubMed:10419538, ECO:0000269|PubMed:11256947, ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}. |
| Q6P2D8 | XRRA1 | Y7 | ochoa | X-ray radiation resistance-associated protein 1 | May be involved in the response of cells to X-ray radiation. {ECO:0000269|PubMed:12908878}. |
| Q6P2E9 | EDC4 | S6 | ochoa | Enhancer of mRNA-decapping protein 4 (Autoantigen Ge-1) (Autoantigen RCD-8) (Human enhancer of decapping large subunit) (Hedls) | In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro). {ECO:0000269|PubMed:16364915}. |
| Q6P3V2 | ZNF585A | S7 | ochoa | Zinc finger protein 585A | May be involved in transcriptional regulation. |
| Q6PCB5 | RSBN1L | S6 | ochoa | Lysine-specific demethylase RSBN1L (EC 1.14.11.-) (Round spermatid basic protein 1-like protein) | Lysine-specific demethylase that specifically demethylates methylated lysine residues of proteins. {ECO:0000250|UniProtKB:Q80T69}. |
| Q6UXN9 | WDR82 | S6 | ochoa | WD repeat-containing protein 82 | Regulatory component of the SET1/COMPASS complex implicated in the tethering of this complex to transcriptional start sites of active genes (PubMed:17998332, PubMed:18838538, PubMed:20516061). Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) (PubMed:17998332, PubMed:18838538). Component of the PNUTS-PP1 protein phosphatase complex, a protein phosphatase 1 (PP1) complex that promotes RNA polymerase II transcription pause-release, allowing transcription elongation (PubMed:39603240, PubMed:39603239). PNUTS-PP1 also plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061). Together with ZC3H4, but independently of the SET1 complex, part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs and promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452). {ECO:0000269|PubMed:17998332, ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:33767452, ECO:0000269|PubMed:33913806, ECO:0000269|PubMed:39603239, ECO:0000269|PubMed:39603240}. |
| Q6ZMZ0 | RNF19B | S7 | ochoa | E3 ubiquitin-protein ligase RNF19B (EC 2.3.2.31) (IBR domain-containing protein 3) (Natural killer lytic-associated molecule) (RING finger protein 19B) | E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1 (PubMed:16709802, PubMed:27485036). Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells (PubMed:10438909). Protects against staurosporin-induced cell death (PubMed:27485036). {ECO:0000269|PubMed:10438909, ECO:0000269|PubMed:16709802, ECO:0000269|PubMed:27485036}. |
| Q6ZN18 | AEBP2 | T6 | ochoa | Zinc finger protein AEBP2 (Adipocyte enhancer-binding protein 2) (AE-binding protein 2) | Acts as an accessory subunit for the core Polycomb repressive complex 2 (PRC2), which mediates histone H3K27 (H3K27me3) trimethylation on chromatin leading to transcriptional repression of the affected target gene (PubMed:15225548, PubMed:29499137, PubMed:31959557). Plays a role in nucleosome localization of the PRC2 complex (PubMed:29499137). {ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:31959557}. |
| Q6ZN30 | BNC2 | T7 | ochoa | Zinc finger protein basonuclin-2 | Probable transcription factor specific for skin keratinocytes. May play a role in the differentiation of spermatozoa and oocytes (PubMed:14988505). May also play an important role in early urinary-tract development (PubMed:31051115). {ECO:0000269|PubMed:14988505, ECO:0000269|PubMed:31051115}. |
| Q6ZRV2 | FAM83H | S7 | ochoa | Protein FAM83H | May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688). {ECO:0000269|PubMed:18252228, ECO:0000269|PubMed:23902688}. |
| Q6ZTU2 | EP400P1 | S7 | ochoa | Putative EP400-like protein (EP400 pseudogene 1) | None |
| Q6ZU35 | CRACD | S7 | ochoa | Capping protein-inhibiting regulator of actin dynamics (Cancer-related regulator of actin dynamics) | Involved in epithelial cell integrity by acting on the maintenance of the actin cytoskeleton. Positively regulates the actin polymerization, by inhibiting the interaction of actin-capping proteins with actin. {ECO:0000269|PubMed:30361697}. |
| Q6ZWJ1 | STXBP4 | S6 | ochoa | Syntaxin-binding protein 4 (Syntaxin 4-interacting protein) (STX4-interacting protein) (Synip) | Plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane. Inhibits the translocation of SLC2A4 from intracellular vesicles to the plasma membrane by STX4A binding and preventing the interaction between STX4A and VAMP2. Stimulation with insulin disrupts the interaction with STX4A, leading to increased levels of SLC2A4 at the plasma membrane. May also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose (By similarity). {ECO:0000250}. |
| Q6ZWJ1 | STXBP4 | T7 | ochoa | Syntaxin-binding protein 4 (Syntaxin 4-interacting protein) (STX4-interacting protein) (Synip) | Plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane. Inhibits the translocation of SLC2A4 from intracellular vesicles to the plasma membrane by STX4A binding and preventing the interaction between STX4A and VAMP2. Stimulation with insulin disrupts the interaction with STX4A, leading to increased levels of SLC2A4 at the plasma membrane. May also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose (By similarity). {ECO:0000250}. |
| Q719H9 | KCTD1 | T7 | ochoa | BTB/POZ domain-containing protein KCTD1 (Potassium channel tetramerization domain-containing protein 1) | May repress the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C to various extent. {ECO:0000269|PubMed:18358072, ECO:0000269|PubMed:19115315}. |
| Q7KZ85 | SUPT6H | S7 | ochoa | Transcription elongation factor SPT6 (hSPT6) (Histone chaperone suppressor of Ty6) (Tat-cotransactivator 2 protein) (Tat-CT2 protein) | Histone H3-H4 chaperone that plays a key role in the regulation of transcription elongation and mRNA processing. Enhances the transcription elongation by RNA polymerase II (RNAPII) and is also required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. Besides chaperoning histones in transcription, acts to transport and splice mRNA by forming a complex with IWS1 and the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2), to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. SUPT6H via its association with SETD1A, regulates both class-switch recombination and somatic hypermutation through formation of H3K4me3 epigenetic marks on activation-induced cytidine deaminase (AICDA) target loci. Promotes the activation of the myogenic gene program by entailing erasure of the repressive H3K27me3 epigenetic mark through stabilization of the chromatin interaction of the H3K27 demethylase KDM6A. {ECO:0000269|PubMed:15060154, ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:22316138, ECO:0000269|PubMed:23503590, ECO:0000269|PubMed:9514752}. |
| Q7KZF4 | SND1 | S7 | ochoa | Staphylococcal nuclease domain-containing protein 1 (EC 3.1.31.1) (100 kDa coactivator) (EBNA2 coactivator p100) (Tudor domain-containing protein 11) (p100 co-activator) | Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (PubMed:18453631, PubMed:28546213). As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (PubMed:28546213). Functions as a bridging factor between STAT6 and the basal transcription factor (PubMed:12234934). Plays a role in PIM1 regulation of MYB activity (PubMed:9809063). Functions as a transcriptional coactivator for STAT5 (By similarity). {ECO:0000250|UniProtKB:Q78PY7, ECO:0000269|PubMed:12234934, ECO:0000269|PubMed:18453631, ECO:0000269|PubMed:28546213, ECO:0000269|PubMed:9809063}.; FUNCTION: (Microbial infection) Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2). {ECO:0000269|PubMed:7651391}.; FUNCTION: (Microbial infection) Promotes SARS-CoV-2 RNA synthesis by binding to negative-sense RNA and the viral protein nsp9. {ECO:0000269|PubMed:37794589}. |
| Q7KZI7 | MARK2 | T6 | ochoa | Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2) (PAR1 homolog) (PAR1 homolog b) (Par-1b) (Par1b) | Serine/threonine-protein kinase (PubMed:23666762). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells. {ECO:0000269|PubMed:11433294, ECO:0000269|PubMed:12429843, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15158914, ECO:0000269|PubMed:15324659, ECO:0000269|PubMed:15365179, ECO:0000269|PubMed:16775013, ECO:0000269|PubMed:16980613, ECO:0000269|PubMed:18626018, ECO:0000269|PubMed:20194617, ECO:0000269|PubMed:23666762}. |
| Q7L4I2 | RSRC2 | T6 | ochoa | Arginine/serine-rich coiled-coil protein 2 | None |
| Q7L9L4 | MOB1B | S7 | ochoa | MOB kinase activator 1B (Mob1 homolog 1A) (Mob1A) (Mob1B) (Mps one binder kinase activator-like 1A) | Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38L. {ECO:0000269|PubMed:15067004, ECO:0000269|PubMed:19739119}. |
| Q7Z3U7 | MON2 | S6 | ochoa | Protein MON2 homolog (Protein SF21) | Plays a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and DOP1B, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation. {ECO:0000269|PubMed:30213940}. |
| Q7Z4H3 | HDDC2 | S6 | ochoa | 5'-deoxynucleotidase HDDC2 (EC 3.1.3.89) (HD domain-containing protein 2) (Hepatitis C virus NS5A-transactivated protein 2) (HCV NS5A-transactivated protein 2) | Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP). {ECO:0000250|UniProtKB:P53144}. |
| Q86TI2 | DPP9 | T6 | ochoa | Dipeptidyl peptidase 9 (DP9) (EC 3.4.14.5) (Dipeptidyl peptidase IV-related protein 2) (DPRP-2) (Dipeptidyl peptidase IX) (DPP IX) (Dipeptidyl peptidase-like protein 9) (DPLP9) | Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:12662155, PubMed:16475979, PubMed:19667070, PubMed:29382749, PubMed:30291141, PubMed:33731929, PubMed:36112693). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed:27820798, PubMed:29967349, PubMed:30291141, PubMed:31525884, PubMed:32796818, PubMed:36112693, PubMed:36357533). Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation (PubMed:33731929, PubMed:33731932, PubMed:34019797). The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP9, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (PubMed:33731929). {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:16475979, ECO:0000269|PubMed:19667070, ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29382749, ECO:0000269|PubMed:29967349, ECO:0000269|PubMed:30291141, ECO:0000269|PubMed:31525884, ECO:0000269|PubMed:32796818, ECO:0000269|PubMed:33731929, ECO:0000269|PubMed:33731932, ECO:0000269|PubMed:34019797, ECO:0000269|PubMed:36112693, ECO:0000269|PubMed:36357533}. |
| Q86U38 | NOP9 | S7 | ochoa | Nucleolar protein 9 | None |
| Q86UA6 | RPAIN | S7 | ochoa | RPA-interacting protein (hRIP) | Mediates the import of RPA complex into the nucleus, possibly via some interaction with importin beta. Isoform 2 is sumoylated and mediates the localization of RPA complex into the PML body of the nucleus, thereby participating in RPA function in DNA metabolism. {ECO:0000269|PubMed:16135809}. |
| Q86UE8 | TLK2 | S7 | ochoa | Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (HsHPK) (PKU-alpha) (Tousled-like kinase 2) | Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (PubMed:10523312, PubMed:11470414, PubMed:12660173, PubMed:12955071, PubMed:29955062, PubMed:33323470, PubMed:9427565). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (PubMed:11470414, PubMed:20016786, PubMed:29955062, PubMed:35136069). Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (PubMed:20016786). Negative regulator of amino acid starvation-induced autophagy (PubMed:22354037). {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12955071, ECO:0000269|PubMed:20016786, ECO:0000269|PubMed:22354037, ECO:0000269|PubMed:29955062, ECO:0000269|PubMed:33323470, ECO:0000269|PubMed:35136069, ECO:0000269|PubMed:9427565}. |
| Q86UP3 | ZFHX4 | S6 | ochoa | Zinc finger homeobox protein 4 (Zinc finger homeodomain protein 4) (ZFH-4) | May play a role in neural and muscle differentiation (By similarity). May be involved in transcriptional regulation. {ECO:0000250}. |
| Q86UX7 | FERMT3 | T6 | ochoa | Fermitin family homolog 3 (Kindlin-3) (MIG2-like protein) (Unc-112-related protein 2) | Plays a central role in cell adhesion in hematopoietic cells (PubMed:19234463, PubMed:26359933). Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3) (By similarity). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells (PubMed:19234460). Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By similarity). {ECO:0000250|UniProtKB:Q8K1B8, ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463, ECO:0000269|PubMed:26359933}.; FUNCTION: Isoform 2 may act as a repressor of NF-kappa-B and apoptosis. {ECO:0000269|PubMed:19064721, ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463}. |
| Q86VM9 | ZC3H18 | S6 | ochoa | Zinc finger CCCH domain-containing protein 18 (Nuclear protein NHN1) | None |
| Q86VP6 | CAND1 | Y6 | ochoa | Cullin-associated NEDD8-dissociated protein 1 (Cullin-associated and neddylation-dissociated protein 1) (TBP-interacting protein of 120 kDa A) (TBP-interacting protein 120A) (p120 CAND1) | Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes. {ECO:0000269|PubMed:12504025, ECO:0000269|PubMed:12504026, ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:16449638, ECO:0000269|PubMed:21249194, ECO:0000269|PubMed:23453757}. |
| Q86VQ0 | LCA5 | S7 | ochoa | Lebercilin (Leber congenital amaurosis 5 protein) | Involved in intraflagellar protein (IFT) transport in photoreceptor cilia. {ECO:0000250|UniProtKB:Q80ST9}. |
| Q86VS8 | HOOK3 | S6 | ochoa | Protein Hook homolog 3 (h-hook3) (hHK3) | Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Predominantly recruits 2 dyneins, which increases both the force and speed of the microtubule motor (PubMed:25035494, PubMed:33734450). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell (PubMed:32073997). {ECO:0000250|UniProtKB:Q8BUK6, ECO:0000269|PubMed:11238449, ECO:0000269|PubMed:17237231, ECO:0000269|PubMed:18799622, ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:32073997, ECO:0000269|PubMed:33734450}.; FUNCTION: (Microbial infection) May serve as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking. {ECO:0000305}. |
| Q86WH2 | RASSF3 | S6 | ochoa | Ras association domain-containing protein 3 | None |
| Q86WH2 | RASSF3 | S7 | ochoa | Ras association domain-containing protein 3 | None |
| Q86YV0 | RASAL3 | S7 | ochoa | RAS protein activator like-3 | Functions as a Ras GTPase-activating protein. Plays an important role in the expansion and functions of natural killer T (NKT) cells in the liver by negatively regulating RAS activity and the down-stream ERK signaling pathway. {ECO:0000250|UniProtKB:Q8C2K5}. |
| Q8IU68 | TMC8 | S6 | ochoa | Transmembrane channel-like protein 8 (Epidermodysplasia verruciformis protein 2) | Acts as a regulatory protein involved in the regulation of numerous cellular processes (PubMed:18158319, PubMed:23429285, PubMed:30068544, PubMed:32917726). Together with its homolog TMC6/EVER1, forms a complex with calcium-binding protein CIB1 in lymphocytes and keratynocytes where TMC6 and TMC8 stabilize CIB1 levels and reciprocally (PubMed:30068544, PubMed:32917726). Together with TMC6, also forms a complex with and activates zinc transporter ZNT1 at the ER membrane of keratynocytes, thereby facilitating zinc uptake into the ER (PubMed:18158319). Also inhibits receptor-mediated calcium release from ER stores and calcium activated and volume regulated chloride channels (PubMed:25220380). Down-regulates the activity of transcription factors induced by zinc and cytokines (PubMed:18158319). Also sequesters TRADD which impairs the recruitment of TRAF2 and RIPK1 in the pro-survival complex I and promotes proapoptotic complex II formation, and may therefore be involved in TNF-induced cell death/survival decisions (PubMed:23429285). {ECO:0000269|PubMed:18158319, ECO:0000269|PubMed:23429285, ECO:0000269|PubMed:25220380, ECO:0000269|PubMed:30068544, ECO:0000269|PubMed:32917726}. |
| Q8IUD2 | ERC1 | S7 | ochoa | ELKS/Rab6-interacting/CAST family member 1 (ERC-1) (Rab6-interacting protein 2) | Regulatory subunit of the IKK complex. Probably recruits IkappaBalpha/NFKBIA to the complex. May be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. May be involved in vesicle trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to Golgi transport. {ECO:0000269|PubMed:15218148}. |
| Q8IV08 | PLD3 | Y7 | ochoa | 5'-3' exonuclease PLD3 (EC 3.1.16.1) ((S,S)-bis(monoacylglycero)phosphate synthase PLD3) (EC 3.1.4.-) (HindIII K4L homolog) (Hu-K4) (Phospholipase D3) | 5'->3' exonuclease that hydrolyzes the phosphodiester bond of single-stranded DNA (ssDNA) and RNA molecules to form nucleoside 3'-monophosphates and 5'-end 5'-hydroxy deoxyribonucleotide/ribonucleotide fragments (PubMed:30111894, PubMed:30312375, PubMed:34620855, PubMed:37225734, PubMed:37994783, PubMed:38537643, PubMed:38697119). Partially redundant with PLD4, can cleave all four nucleotides displaying higher efficiency for ssDNA and RNA fragments initiated with uridine and guanosine residues and lower efficiency for cytidine-initiated substrates (PubMed:30111894, PubMed:30312375, PubMed:34620855, PubMed:37225734, PubMed:37994783, PubMed:38537643, PubMed:38697119). As a result, it does not always degrade polynucleotides to the single nucleotide level, it can stall at specific sites sparing certain fragments from exonucleolytic degradation (PubMed:30111894, PubMed:30312375, PubMed:34620855, PubMed:37225734, PubMed:37994783, PubMed:38537643, PubMed:38697119). Processes self and pathogenic ssDNA and RNA molecules that reach the endolysosomal compartment via phagocytosis or autophagy and may serve as 'danger' signals for recognition by innate immune receptors such as toll-like receptors (TLRs) (PubMed:34620855, PubMed:37225734, PubMed:38697119). Degrades mitochondrial CpG-rich ssDNA fragments to prevent TLR9 activation and autoinflammatory response, but it can cleave viral RNA to generate ligands for TLR7 activation and initiate antiviral immune responses (PubMed:34620855, PubMed:37225734, PubMed:38697119). In plasmacytoid dendritic cells, it cooperates with endonuclease RNASET2 to release 2',3'-cyclic guanosine monophosphate (2',3'-cGMP), a potent stimulatory ligand for TLR7 (PubMed:34620855, PubMed:37225734, PubMed:38697119). Produces 2',3'-cGMPs and cytidine-rich RNA fragments that occupy TLR7 ligand-binding pockets and trigger a signaling-competent state (PubMed:34620855, PubMed:37225734, PubMed:38697119). Can exert polynucleotide phosphatase activity toward 5'-phosphorylated ssDNA substrates although at a slow rate (PubMed:38537643). Transphosphatidylase that catalyzes the exchange with R to S stereo-inversion of the glycerol moiety between (S,R)-lysophosphatidylglycerol (LPG) and monoacylglycerol (MAG) substrates to yield (S,S)-bis(monoacylglycero)phosphate (BMP) (PubMed:39423811). Can synthesize a variety of (S,S)-BMPs representing the main phospholipid constituent of lysosomal intralumenal vesicle (ILV) membranes that bind acid hydrolases for lipid degradation (PubMed:39423811). Regulates the homeostasis and interorganellar communication of the endolysosomal system with an overall impact on cellular removal of dysfunctional organelles via autophagy as well as proper protein and lipid turnover (PubMed:28128235, PubMed:29368044, PubMed:37225734). May play a role in myotube formation in response to ER stress (PubMed:22428023). {ECO:0000269|PubMed:22428023, ECO:0000269|PubMed:28128235, ECO:0000269|PubMed:29368044, ECO:0000269|PubMed:30111894, ECO:0000269|PubMed:30312375, ECO:0000269|PubMed:34620855, ECO:0000269|PubMed:37225734, ECO:0000269|PubMed:37994783, ECO:0000269|PubMed:38537643, ECO:0000269|PubMed:38697119, ECO:0000269|PubMed:39423811}. |
| Q8IWA4 | MFN1 | S6 | ochoa | Mitofusin-1 (EC 3.6.5.-) (Fzo homolog) (Transmembrane GTPase MFN1) | Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:12475957, PubMed:12759376, PubMed:27920125, PubMed:28114303). Membrane clustering requires GTPase activity (PubMed:27920125). It may involve a major rearrangement of the coiled coil domains (PubMed:27920125, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:12475957, PubMed:12759376). Overexpression induces the formation of mitochondrial networks (in vitro) (PubMed:12759376). Has low GTPase activity (PubMed:27920125, PubMed:28114303). {ECO:0000269|PubMed:12475957, ECO:0000269|PubMed:12759376, ECO:0000269|PubMed:27920125, ECO:0000269|PubMed:28114303}. |
| Q8IY26 | PLPP6 | S7 | ochoa | Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6 (EC 3.1.3.-) (EC 3.6.1.-) (EC 3.6.1.68) (Lipid phosphatase-related protein-B) (LPRP-B) (PA-PSP) (Phosphatidic acid phosphatase type 2 domain-containing protein 2) (PPAP2 domain-containing protein 2) (Phospholipid phosphatase 6) (Presqualene diphosphate phosphatase) (Type 1 polyisoprenoid diphosphate phosphatase) | Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates (PubMed:16464866, PubMed:19220020, PubMed:20110354). Functions in the innate immune response through the dephosphorylation of presqualene diphosphate which acts as a potent inhibitor of the signaling pathways contributing to polymorphonuclear neutrophils activation (PubMed:16464866, PubMed:23568778). May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway (PubMed:20110354). May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins (PubMed:20110354). Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols (PubMed:18930839). May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine-1-phosphate (PubMed:18930839, PubMed:20110354). {ECO:0000269|PubMed:16464866, ECO:0000269|PubMed:18930839, ECO:0000269|PubMed:19220020, ECO:0000269|PubMed:20110354, ECO:0000269|PubMed:23568778}. |
| Q8IY67 | RAVER1 | S6 | ochoa | Ribonucleoprotein PTB-binding 1 (Protein raver-1) | Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA (By similarity). {ECO:0000250}. |
| Q8IZW8 | TNS4 | S6 | ochoa | Tensin-4 (C-terminal tensin-like protein) | Promotes EGF-induced cell migration by displacing tensin TNS3 from the cytoplasmic tail of integrin ITGB1 which results in dissociation of TNS3 from focal adhesions, disassembly of actin stress fibers and initiation of cell migration (PubMed:17643115). Suppresses ligand-induced degradation of EGFR by reducing EGFR ubiquitination in the presence of EGF (PubMed:23774213). Increases MET protein stability by inhibiting MET endocytosis and subsequent lysosomal degradation which leads to increased cell survival, proliferation and migration (PubMed:24814316). {ECO:0000269|PubMed:17643115, ECO:0000269|PubMed:23774213, ECO:0000269|PubMed:24814316}. |
| Q8IZW8 | TNS4 | S7 | ochoa | Tensin-4 (C-terminal tensin-like protein) | Promotes EGF-induced cell migration by displacing tensin TNS3 from the cytoplasmic tail of integrin ITGB1 which results in dissociation of TNS3 from focal adhesions, disassembly of actin stress fibers and initiation of cell migration (PubMed:17643115). Suppresses ligand-induced degradation of EGFR by reducing EGFR ubiquitination in the presence of EGF (PubMed:23774213). Increases MET protein stability by inhibiting MET endocytosis and subsequent lysosomal degradation which leads to increased cell survival, proliferation and migration (PubMed:24814316). {ECO:0000269|PubMed:17643115, ECO:0000269|PubMed:23774213, ECO:0000269|PubMed:24814316}. |
| Q8N302 | AGGF1 | S7 | ochoa | Angiogenic factor with G patch and FHA domains 1 (Angiogenic factor VG5Q) (hVG5Q) (G patch domain-containing protein 7) (Vasculogenesis gene on 5q protein) | Promotes angiogenesis and the proliferation of endothelial cells. Able to bind to endothelial cells and promote cell proliferation, suggesting that it may act in an autocrine fashion. {ECO:0000269|PubMed:14961121}. |
| Q8N344 | MIER2 | S6 | ochoa | Mesoderm induction early response protein 2 (Mi-er2) | Transcriptional repressor. {ECO:0000250}. |
| Q8N568 | DCLK2 | S6 | ochoa | Serine/threonine-protein kinase DCLK2 (EC 2.7.11.1) (CaMK-like CREB regulatory kinase 2) (CL2) (CLICK-II) (CLICK2) (Doublecortin domain-containing protein 3B) (Doublecortin-like and CAM kinase-like 2) (Doublecortin-like kinase 2) | Protein kinase with a significantly reduced C(a2+)/CAM affinity and dependence compared to other members of the CaMK family. May play a role in the down-regulation of CRE-dependent gene activation probably by phosphorylation of the CREB coactivator CRTC2/TORC2 and the resulting retention of TORC2 in the cytoplasm (By similarity). {ECO:0000250}. |
| Q8N5F7 | NKAP | S7 | ochoa | NF-kappa-B-activating protein | Acts as a transcriptional repressor (PubMed:14550261, PubMed:19409814, PubMed:31587868). Plays a role as a transcriptional corepressor of the Notch-mediated signaling required for T-cell development (PubMed:19409814). Also involved in the TNF and IL-1 induced NF-kappa-B activation. Associates with chromatin at the Notch-regulated SKP2 promoter. {ECO:0000269|PubMed:14550261, ECO:0000269|PubMed:19409814, ECO:0000269|PubMed:31587868}. |
| Q8N5W9 | RFLNB | S6 | ochoa | Refilin-B (Regulator of filamin protein B) (RefilinB) | Involved in the regulation of the perinuclear actin network and nuclear shape through interaction with filamins. Plays an essential role in the formation of cartilaginous skeletal elements. {ECO:0000250|UniProtKB:Q5SVD0}. |
| Q8NBL1 | POGLUT1 | S6 | ochoa | Protein O-glucosyltransferase 1 (EC 2.4.1.376) (CAP10-like 46 kDa protein) (hCLP46) (KTEL motif-containing protein 1) (Myelodysplastic syndromes relative protein) (O-glucosyltransferase Rumi homolog) (hRumi) (Protein O-xylosyltransferase POGLUT1) (EC 2.4.2.63) | Dual specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to a serine residue found in the consensus sequence of C-X-S-X-P-C (PubMed:21081508, PubMed:21490058, PubMed:21949356, PubMed:27807076, PubMed:28775322). Specifically targets extracellular EGF repeats of protein such as CRB2, F7, F9 and NOTCH2 (PubMed:21081508, PubMed:21490058, PubMed:21949356, PubMed:27807076, PubMed:28775322). Acts as a positive regulator of Notch signaling by mediating O-glucosylation of Notch, leading to regulate muscle development (PubMed:27807076). Notch glucosylation does not affect Notch ligand binding (PubMed:21490058). Required during early development to promote gastrulation: acts by mediating O-glucosylation of CRB2, which is required for CRB2 localization to the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q8BYB9, ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:21490058, ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:27807076, ECO:0000269|PubMed:28775322}. |
| Q8NBL1 | POGLUT1 | S7 | ochoa | Protein O-glucosyltransferase 1 (EC 2.4.1.376) (CAP10-like 46 kDa protein) (hCLP46) (KTEL motif-containing protein 1) (Myelodysplastic syndromes relative protein) (O-glucosyltransferase Rumi homolog) (hRumi) (Protein O-xylosyltransferase POGLUT1) (EC 2.4.2.63) | Dual specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to a serine residue found in the consensus sequence of C-X-S-X-P-C (PubMed:21081508, PubMed:21490058, PubMed:21949356, PubMed:27807076, PubMed:28775322). Specifically targets extracellular EGF repeats of protein such as CRB2, F7, F9 and NOTCH2 (PubMed:21081508, PubMed:21490058, PubMed:21949356, PubMed:27807076, PubMed:28775322). Acts as a positive regulator of Notch signaling by mediating O-glucosylation of Notch, leading to regulate muscle development (PubMed:27807076). Notch glucosylation does not affect Notch ligand binding (PubMed:21490058). Required during early development to promote gastrulation: acts by mediating O-glucosylation of CRB2, which is required for CRB2 localization to the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q8BYB9, ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:21490058, ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:27807076, ECO:0000269|PubMed:28775322}. |
| Q8NCH0 | CHST14 | T7 | ochoa | Carbohydrate sulfotransferase 14 (EC 2.8.2.35) (Dermatan 4-sulfotransferase 1) (D4ST-1) (hD4ST1) | Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of dermatan sulfate. Plays a pivotal role in the formation of 4-0-sulfated IdoA blocks in dermatan sulfate. Transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with an alpha-linked iduronic acid (IdoUA) at the C-3 hydroxyl. Transfers sulfate more efficiently to GalNAc residues in -IdoUA-GalNAc-IdoUA- than in -GlcUA-GalNAc-GlcUA-sequences. Has preference for partially desulfated dermatan sulfate. Addition of sulfate to GalNAc may occur immediately after epimerization of GlcUA to IdoUA. Appears to have an important role in the formation of the cerebellar neural network during postnatal brain development. {ECO:0000269|PubMed:19661164}. |
| Q8NDC0 | MAPK1IP1L | S6 | ochoa | MAPK-interacting and spindle-stabilizing protein-like (Mitogen-activated protein kinase 1-interacting protein 1-like) | None |
| Q8NEM2 | SHCBP1 | T7 | ochoa | SHC SH2 domain-binding protein 1 | May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc. Acts as a positive regulator of FGF signaling in neural progenitor cells. {ECO:0000250|UniProtKB:Q9Z179}. |
| Q8NFU5 | IPMK | S7 | ochoa | Inositol polyphosphate multikinase (EC 2.7.1.140) (EC 2.7.1.151) (EC 2.7.1.153) (Inositol 1,3,4,6-tetrakisphosphate 5-kinase) | Inositol phosphate kinase with a broad substrate specificity (PubMed:12027805, PubMed:12223481, PubMed:28882892, PubMed:30420721, PubMed:30624931). Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) first to inositol 1,3,4,5-tetrakisphosphate and then to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) (PubMed:12027805, PubMed:12223481, PubMed:28882892, PubMed:30624931). Phosphorylates inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4) (PubMed:12223481). Phosphorylates inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4) (By similarity). Phosphorylates glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate to glycero-3-phospho-1D-myo-inositol 3,4,5-trisphosphate (PubMed:28882892, PubMed:30420721). Plays an important role in MLKL-mediated necroptosis via its role in the biosynthesis of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Binding of these highly phosphorylated inositol phosphates to MLKL mediates the release of an N-terminal auto-inhibitory region, leading to activation of the kinase. Essential for activated phospho-MLKL to oligomerize and localize to the cell membrane during necroptosis (PubMed:29883610). Required for normal embryonic development, probably via its role in the biosynthesis of inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) and inositol hexakisphosphate (InsP6) (By similarity). {ECO:0000250|UniProtKB:Q7TT16, ECO:0000269|PubMed:12027805, ECO:0000269|PubMed:12223481, ECO:0000269|PubMed:28882892, ECO:0000269|PubMed:29883610, ECO:0000269|PubMed:30420721, ECO:0000269|PubMed:30624931}. |
| Q8NFZ5 | TNIP2 | S7 | ochoa | TNFAIP3-interacting protein 2 (A20-binding inhibitor of NF-kappa-B activation 2) (ABIN-2) (Fetal liver LKB1-interacting protein) | Inhibits NF-kappa-B activation by blocking the interaction of RIPK1 with its downstream effector NEMO/IKBKG. Forms a ternary complex with NFKB1 and MAP3K8 but appears to function upstream of MAP3K8 in the TLR4 signaling pathway that regulates MAP3K8 activation. Involved in activation of the MEK/ERK signaling pathway during innate immune response; this function seems to be stimulus- and cell type specific. Required for stability of MAP3K8. Involved in regulation of apoptosis in endothelial cells; promotes TEK agonist-stimulated endothelial survival. May act as transcriptional coactivator when translocated to the nucleus. Enhances CHUK-mediated NF-kappa-B activation involving NF-kappa-B p50-p65 and p50-c-Rel complexes. {ECO:0000269|PubMed:11389905, ECO:0000269|PubMed:12595760, ECO:0000269|PubMed:12753905, ECO:0000269|PubMed:12933576, ECO:0000269|PubMed:14653779, ECO:0000269|PubMed:15169888, ECO:0000269|PubMed:21784860}. |
| Q8NHZ8 | CDC26 | T7 | psp | Anaphase-promoting complex subunit CDC26 (Anaphase-promoting complex subunit 12) (APC12) (Cell division cycle protein 26 homolog) | Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). May recruit the E2 ubiquitin-conjugating enzymes to the complex (PubMed:18485873). {ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:29033132}. |
| Q8TAA9 | VANGL1 | T6 | ochoa | Vang-like protein 1 (Loop-tail protein 2 homolog) (LPP2) (Strabismus 2) (Van Gogh-like protein 1) | None |
| Q8TAA9 | VANGL1 | Y7 | ochoa | Vang-like protein 1 (Loop-tail protein 2 homolog) (LPP2) (Strabismus 2) (Van Gogh-like protein 1) | None |
| Q8TAG9 | EXOC6 | S7 | ochoa | Exocyst complex component 6 (Exocyst complex component Sec15A) (SEC15-like protein 1) | Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (By similarity). {ECO:0000250}. |
| Q8TB45 | DEPTOR | S6 | psp | DEP domain-containing mTOR-interacting protein (hDEPTOR) (DEP domain-containing protein 6) | Negative regulator of the mTORC1 and mTORC2 complexes: inhibits the protein kinase activity of MTOR, thereby inactivating both complexes (PubMed:19446321, PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:25936805, PubMed:29382726, PubMed:34519268, PubMed:34519269). DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy (PubMed:22017875, PubMed:22017876, PubMed:22017877). In contrast to AKT1S1/PRAS40, only partially inhibits mTORC1 activity (PubMed:34519268, PubMed:34519269). {ECO:0000269|PubMed:19446321, ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:22017877, ECO:0000269|PubMed:25936805, ECO:0000269|PubMed:29382726, ECO:0000269|PubMed:34519268, ECO:0000269|PubMed:34519269}. |
| Q8TB45 | DEPTOR | T7 | psp | DEP domain-containing mTOR-interacting protein (hDEPTOR) (DEP domain-containing protein 6) | Negative regulator of the mTORC1 and mTORC2 complexes: inhibits the protein kinase activity of MTOR, thereby inactivating both complexes (PubMed:19446321, PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:25936805, PubMed:29382726, PubMed:34519268, PubMed:34519269). DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy (PubMed:22017875, PubMed:22017876, PubMed:22017877). In contrast to AKT1S1/PRAS40, only partially inhibits mTORC1 activity (PubMed:34519268, PubMed:34519269). {ECO:0000269|PubMed:19446321, ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:22017877, ECO:0000269|PubMed:25936805, ECO:0000269|PubMed:29382726, ECO:0000269|PubMed:34519268, ECO:0000269|PubMed:34519269}. |
| Q8TDH9 | BLOC1S5 | T6 | ochoa | Biogenesis of lysosome-related organelles complex 1 subunit 5 (BLOC-1 subunit 5) (Protein Muted homolog) | Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes (PubMed:32565547). In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:32565547}. |
| Q8TDR2 | STK35 | S6 | ochoa | Serine/threonine-protein kinase 35 (EC 2.7.11.1) (CLP-36-interacting kinase 1) (CLIK-1) (PDLIM1-interacting kinase 1) (Serine/threonine-protein kinase 35 L1) | None |
| Q8TE77 | SSH3 | S7 | ochoa | Protein phosphatase Slingshot homolog 3 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 3) (SSH-3L) (hSSH-3L) | Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly (By similarity). {ECO:0000250}. |
| Q8TEB1 | DCAF11 | S6 | ochoa | DDB1- and CUL4-associated factor 11 (WD repeat-containing protein 23) | May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}. |
| Q8TEB1 | DCAF11 | S7 | ochoa | DDB1- and CUL4-associated factor 11 (WD repeat-containing protein 23) | May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}. |
| Q8WTW3 | COG1 | T6 | ochoa | Conserved oligomeric Golgi complex subunit 1 (COG complex subunit 1) (Component of oligomeric Golgi complex 1) | Required for normal Golgi function. {ECO:0000250}. |
| Q8WTW3 | COG1 | S7 | ochoa | Conserved oligomeric Golgi complex subunit 1 (COG complex subunit 1) (Component of oligomeric Golgi complex 1) | Required for normal Golgi function. {ECO:0000250}. |
| Q8WU68 | U2AF1L4 | S7 | ochoa | Splicing factor U2AF 26 kDa subunit (U2 auxiliary factor 26) (U2 small nuclear RNA auxiliary factor 1-like protein 4) (U2AF1-like 4) (U2(RNU2) small nuclear RNA auxiliary factor 1-like protein 3) (U2 small nuclear RNA auxiliary factor 1-like protein 3) (U2AF1-like protein 3) | RNA-binding protein that function as a pre-mRNA splicing factor. Plays a critical role in both constitutive and enhancer-dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Acts by enhancing the binding of U2AF2 to weak pyrimidine tracts. Also participates in the regulation of alternative pre-mRNA splicing. Activates exon 5 skipping of PTPRC during T-cell activation; an event reversed by GFI1. Binds to RNA at the AG dinucleotide at the 3'-splice site (By similarity). Shows a preference for AGC or AGA (By similarity). {ECO:0000250|UniProtKB:Q8BGJ9}. |
| Q8WUM0 | NUP133 | S7 | ochoa | Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133) | Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222). {ECO:0000269|PubMed:11684705, ECO:0000269|PubMed:30179222}. |
| Q8WVV9 | HNRNPLL | S6 | ochoa | Heterogeneous nuclear ribonucleoprotein L-like (hnRNPLL) (Stromal RNA-regulating factor) | RNA-binding protein that functions as a regulator of alternative splicing for multiple target mRNAs, including PTPRC/CD45 and STAT5A. Required for alternative splicing of PTPRC. {ECO:0000269|PubMed:18669861}. |
| Q8WVV9 | HNRNPLL | S7 | ochoa | Heterogeneous nuclear ribonucleoprotein L-like (hnRNPLL) (Stromal RNA-regulating factor) | RNA-binding protein that functions as a regulator of alternative splicing for multiple target mRNAs, including PTPRC/CD45 and STAT5A. Required for alternative splicing of PTPRC. {ECO:0000269|PubMed:18669861}. |
| Q8WW01 | TSEN15 | S7 | ochoa | tRNA-splicing endonuclease subunit Sen15 (SEN15 homolog) (HsSEN15) (tRNA-intron endonuclease Sen15) | Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini (PubMed:15109492, PubMed:27392077). There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events (PubMed:15109492). {ECO:0000269|PubMed:15109492, ECO:0000269|PubMed:27392077}. |
| Q8WYQ5 | DGCR8 | S6 | ochoa | Microprocessor complex subunit DGCR8 (DiGeorge syndrome critical region 8) | Component of the microprocessor complex that acts as a RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs (PubMed:26027739, PubMed:26748718). The heme-bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is active in triggering pri-miRNA cleavage, whereas the heme-free DGCR8 monomer binds pri-miRNAs as a dimer and is much less active. Both double-stranded and single-stranded regions of a pri-miRNA are required for its binding (PubMed:15531877, PubMed:15574589, PubMed:15589161, PubMed:16751099, PubMed:16906129, PubMed:16963499, PubMed:17159994). Specifically recognizes and binds N6-methyladenosine (m6A)-containing pri-miRNAs, a modification required for pri-miRNAs processing (PubMed:25799998). Involved in the silencing of embryonic stem cell self-renewal (By similarity). Also plays a role in DNA repair by promoting the recruitment of RNF168 to RNF8 and MDC1 at DNA double-strand breaks and subsequently the clearance of DNA breaks (PubMed:34188037). {ECO:0000250|UniProtKB:Q9EQM6, ECO:0000269|PubMed:15531877, ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:15589161, ECO:0000269|PubMed:16751099, ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:16963499, ECO:0000269|PubMed:17159994, ECO:0000269|PubMed:25799998, ECO:0000269|PubMed:26027739, ECO:0000269|PubMed:26748718}. |
| Q8WZA1 | POMGNT1 | S7 | ochoa | Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (POMGnT1) (EC 2.4.1.-) (UDP-GlcNAc:alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.2) (GnT I.2) | Participates in O-mannosyl glycosylation by catalyzing the addition of N-acetylglucosamine to O-linked mannose on glycoproteins (PubMed:11709191, PubMed:27493216, PubMed:28512129). Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins, providing the necessary basis for the addition of further carbohydrate moieties (PubMed:11709191, PubMed:27493216). Is specific for alpha linked terminal mannose and does not have MGAT3, MGAT4, MGAT5, MGAT7 or MGAT8 activity. {ECO:0000269|PubMed:11709191, ECO:0000269|PubMed:11742540, ECO:0000269|PubMed:26908613, ECO:0000269|PubMed:27391550, ECO:0000269|PubMed:27493216, ECO:0000269|PubMed:28512129}. |
| Q92567 | FAM168A | S6 | ochoa | Protein FAM168A (Tongue cancer chemotherapy resistance-associated protein 1) | In cancer context, protects cells from induced-DNA damage and apoptosis. Acts, at least in part, through PI3K/AKT/NFKB signaling pathway and by preventing POLB degradation. Decreases POLB ubiquitation and stabilizes its protein levels. {ECO:0000269|PubMed:21334329, ECO:0000269|PubMed:21603883, ECO:0000269|PubMed:23251525, ECO:0000269|PubMed:25260657}. |
| Q92609 | TBC1D5 | S6 | ochoa | TBC1 domain family member 5 | May act as a GTPase-activating protein (GAP) for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity (PubMed:19531583, PubMed:20923837). Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy (PubMed:22354992). May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes (PubMed:24603492). {ECO:0000269|PubMed:19531583, ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:24603492, ECO:0000305|PubMed:19531583, ECO:0000305|PubMed:22354992, ECO:0000305|PubMed:24603492}. |
| Q92610 | ZNF592 | T6 | ochoa | Zinc finger protein 592 | May be involved in transcriptional regulation. {ECO:0000269|PubMed:20531441}. |
| Q92900 | UPF1 | Y6 | ochoa | Regulator of nonsense transcripts 1 (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent helicase RENT1) (Nonsense mRNA reducing factor 1) (NORF1) (Up-frameshift suppressor 1 homolog) (hUpf1) | RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs (PubMed:11163187, PubMed:16086026, PubMed:18172165, PubMed:21145460, PubMed:21419344, PubMed:24726324). Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD (PubMed:11544179, PubMed:25220460). Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (PubMed:19417104). In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD (PubMed:21419344). Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation and allowing the recycling of NMD factors (PubMed:12554878). UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways (PubMed:18447585). Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2 (PubMed:16086026, PubMed:18172165). For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed (PubMed:18447585, PubMed:25220460). The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD (PubMed:21145460). Together with UPF2 and dependent on TDRD6, mediates the degradation of mRNA harboring long 3'UTR by inducing the NMD machinery (By similarity). Also capable of unwinding double-stranded DNA and translocating on single-stranded DNA (PubMed:30218034). {ECO:0000250|UniProtKB:Q9EPU0, ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:11544179, ECO:0000269|PubMed:12554878, ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:18447585, ECO:0000269|PubMed:19417104, ECO:0000269|PubMed:21145460, ECO:0000269|PubMed:21419344, ECO:0000269|PubMed:24726324, ECO:0000269|PubMed:25220460, ECO:0000269|PubMed:30218034}. |
| Q93015 | NAA80 | S6 | ochoa | N-alpha-acetyltransferase 80 (HsNAAA80) (EC 2.3.1.-) (N-acetyltransferase 6) (Protein fusion-2) (Protein fus-2) | N-alpha-acetyltransferase that specifically mediates the acetylation of the acidic amino terminus of processed forms of beta- and gamma-actin (ACTB and ACTG, respectively) (PubMed:29581253, PubMed:30028079). N-terminal acetylation of processed beta- and gamma-actin regulates actin filament depolymerization and elongation (PubMed:29581253). In vivo, preferentially displays N-terminal acetyltransferase activity towards acid N-terminal sequences starting with Asp-Asp-Asp and Glu-Glu-Glu (PubMed:29581253, PubMed:30028079). In vitro, shows high activity towards Met-Asp-Glu-Leu and Met-Asp-Asp-Asp (PubMed:10644992, PubMed:29581307). May act as a tumor suppressor (PubMed:10644992). {ECO:0000269|PubMed:10644992, ECO:0000269|PubMed:29581253, ECO:0000269|PubMed:29581307, ECO:0000269|PubMed:30028079}. |
| Q93015 | NAA80 | T7 | ochoa | N-alpha-acetyltransferase 80 (HsNAAA80) (EC 2.3.1.-) (N-acetyltransferase 6) (Protein fusion-2) (Protein fus-2) | N-alpha-acetyltransferase that specifically mediates the acetylation of the acidic amino terminus of processed forms of beta- and gamma-actin (ACTB and ACTG, respectively) (PubMed:29581253, PubMed:30028079). N-terminal acetylation of processed beta- and gamma-actin regulates actin filament depolymerization and elongation (PubMed:29581253). In vivo, preferentially displays N-terminal acetyltransferase activity towards acid N-terminal sequences starting with Asp-Asp-Asp and Glu-Glu-Glu (PubMed:29581253, PubMed:30028079). In vitro, shows high activity towards Met-Asp-Glu-Leu and Met-Asp-Asp-Asp (PubMed:10644992, PubMed:29581307). May act as a tumor suppressor (PubMed:10644992). {ECO:0000269|PubMed:10644992, ECO:0000269|PubMed:29581253, ECO:0000269|PubMed:29581307, ECO:0000269|PubMed:30028079}. |
| Q969G3 | SMARCE1 | S6 | ochoa | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 (BRG1-associated factor 57) (BAF57) | 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. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Required for the coactivation of estrogen responsive promoters by SWI/SNF complexes and the SRC/p160 family of histone acetyltransferases (HATs). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells. {ECO:0000250|UniProtKB:O54941, ECO:0000303|PubMed:12672490, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
| Q969L2 | MAL2 | S7 | ochoa | Protein MAL2 | Member of the machinery of polarized transport. Required for the indirect transcytotic route at the step of the egress of the transcytosing cargo from perinuclear endosomes in order for it to travel to the apical surface via a raft-dependent pathway. {ECO:0000269|PubMed:12370246}. |
| Q96A54 | ADIPOR1 | S7 | psp | Adiponectin receptor protein 1 (Progestin and adipoQ receptor family member 1) (Progestin and adipoQ receptor family member I) | Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:12802337, PubMed:25855295). Required for normal glucose and fat homeostasis and for maintaining a normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Has high affinity for globular adiponectin and low affinity for full-length adiponectin (By similarity). {ECO:0000250|UniProtKB:Q91VH1, ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}. |
| Q96A57 | TMEM230 | T6 | ochoa | Transmembrane protein 230 | Involved in trafficking and recycling of synaptic vesicles. {ECO:0000269|PubMed:27270108}. |
| Q96AB3 | ISOC2 | S7 | ochoa | Isochorismatase domain-containing protein 2 | None |
| Q96AE4 | FUBP1 | T6 | ochoa | Far upstream element-binding protein 1 (FBP) (FUSE-binding protein 1) (DNA helicase V) (hDH V) | Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription. {ECO:0000269|PubMed:8125259}. |
| Q96AY2 | EME1 | S6 | ochoa | Structure-specific endonuclease subunit EME1 (Crossover junction endonuclease EME1) (Essential meiotic structure-specific endonuclease 1) (MMS4 homolog) (hMMS4) | Non-catalytic subunit of the structure-specific, heterodimeric DNA endonuclease MUS81-EME1 which is involved in the maintenance of genome stability. In the complex, EME1 is required for DNA cleavage, participating in DNA recognition and bending (PubMed:12686547, PubMed:12721304, PubMed:14617801, PubMed:17289582, PubMed:24733841, PubMed:24813886, PubMed:35290797, PubMed:39015284). MUS81-EME1 cleaves 3'-flaps and nicked Holliday junctions, and exhibit limited endonuclease activity with 5' flaps and nicked double-stranded DNAs (PubMed:24733841, PubMed:35290797). Active during prometaphase, MUS81-EME1 resolves mitotic recombination intermediates, including Holliday junctions, which form during homologous recombination (PubMed:14617801, PubMed:24813886). {ECO:0000269|PubMed:12686547, ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:17289582, ECO:0000269|PubMed:24733841, ECO:0000269|PubMed:24813886, ECO:0000269|PubMed:35290797, ECO:0000269|PubMed:39015284}. |
| Q96AY2 | EME1 | S7 | ochoa | Structure-specific endonuclease subunit EME1 (Crossover junction endonuclease EME1) (Essential meiotic structure-specific endonuclease 1) (MMS4 homolog) (hMMS4) | Non-catalytic subunit of the structure-specific, heterodimeric DNA endonuclease MUS81-EME1 which is involved in the maintenance of genome stability. In the complex, EME1 is required for DNA cleavage, participating in DNA recognition and bending (PubMed:12686547, PubMed:12721304, PubMed:14617801, PubMed:17289582, PubMed:24733841, PubMed:24813886, PubMed:35290797, PubMed:39015284). MUS81-EME1 cleaves 3'-flaps and nicked Holliday junctions, and exhibit limited endonuclease activity with 5' flaps and nicked double-stranded DNAs (PubMed:24733841, PubMed:35290797). Active during prometaphase, MUS81-EME1 resolves mitotic recombination intermediates, including Holliday junctions, which form during homologous recombination (PubMed:14617801, PubMed:24813886). {ECO:0000269|PubMed:12686547, ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:17289582, ECO:0000269|PubMed:24733841, ECO:0000269|PubMed:24813886, ECO:0000269|PubMed:35290797, ECO:0000269|PubMed:39015284}. |
| Q96B18 | DACT3 | S6 | ochoa | Dapper homolog 3 (Antagonist of beta-catenin Dapper homolog 3) (Arginine-rich region 1 protein) (Dapper antagonist of catenin 3) | May be involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. {ECO:0000269|PubMed:18538736}. |
| Q96C90 | PPP1R14B | T6 | ochoa | Protein phosphatase 1 regulatory subunit 14B (Phospholipase C-beta-3 neighbouring gene protein) | Inhibitor of PPP1CA. Has over 50-fold higher inhibitory activity when phosphorylated (By similarity). {ECO:0000250}. |
| Q96CP2 | FLYWCH2 | S7 | ochoa | FLYWCH family member 2 | None |
| Q96D46 | NMD3 | S7 | ochoa | 60S ribosomal export protein NMD3 (hNMD3) | Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit. {ECO:0000269|PubMed:12724356, ECO:0000269|PubMed:12773398}. |
| Q96DE5 | ANAPC16 | S6 | ochoa | Anaphase-promoting complex subunit 16 (APC16) (Cyclosome subunit 16) | Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:20360068). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:20360068). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269|PubMed:20360068, ECO:0000269|PubMed:29033132}. |
| Q96DF8 | ESS2 | S7 | ochoa | Splicing factor ESS-2 homolog (DiGeorge syndrome critical region 13) (DiGeorge syndrome critical region 14) (DiGeorge syndrome protein H) (DGS-H) (Protein ES2) | May be involved in pre-mRNA splicing. {ECO:0000250|UniProtKB:P34420}. |
| Q96DG6 | CMBL | Y6 | ochoa | Carboxymethylenebutenolidase homolog (EC 3.1.-.-) | Cysteine hydrolase. Can convert the prodrug olmesartan medoxomil into its pharmacologically active metabolite olmerstatan, an angiotensin receptor blocker, in liver and intestine. May also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin. {ECO:0000269|PubMed:20177059}. |
| Q96DH6 | MSI2 | S6 | ochoa | RNA-binding protein Musashi homolog 2 (Musashi-2) | RNA binding protein that regulates the expression of target mRNAs at the translation level. May play a role in the proliferation and maintenance of stem cells in the central nervous system (By similarity). {ECO:0000250}. |
| Q96E14 | RMI2 | S7 | ochoa | RecQ-mediated genome instability protein 2 (hRMI2) (BLM-associated protein of 18 kDa) (BLAP18) | Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates. It is required to regulate sister chromatid segregation and to limit DNA crossover. Essential for the stability, localization, and function of BLM, TOP3A, and complexes containing BLM. In the RMI complex, it is required to target BLM to chromatin and stress-induced nuclear foci and mitotic phosphorylation of BLM. {ECO:0000269|PubMed:18923082, ECO:0000269|PubMed:18923083, ECO:0000269|PubMed:27977684}. |
| Q96EC8 | YIPF6 | S7 | ochoa | Protein YIPF6 (YIP1 family member 6) | May be required for stable YIPF1 and YIPF2 protein expression. {ECO:0000269|PubMed:28286305}. |
| Q96ER3 | SAAL1 | S6 | ochoa | Protein SAAL1 (Synoviocyte proliferation-associated in collagen-induced arthritis protein 1) (SPACIA1) | Plays a role in promoting the proliferation of synovial fibroblasts in response to pro-inflammatory stimuli. {ECO:0000269|PubMed:22127701}. |
| Q96ET8 | TVP23C | S6 | ochoa | Golgi apparatus membrane protein TVP23 homolog C | None |
| Q96GD4 | AURKB | S7 | ochoa | Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (AIM-1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B) | Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis (PubMed:11516652, PubMed:12925766, PubMed:14610074, PubMed:14722118, PubMed:29449677). The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly (PubMed:11516652, PubMed:12925766, PubMed:14610074, PubMed:14722118, PubMed:26829474). Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis (PubMed:15249581). Required for central/midzone spindle assembly and cleavage furrow formation (PubMed:12458200, PubMed:12686604). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP (PubMed:11516652, PubMed:12925766, PubMed:14610074). Phosphorylation of INCENP leads to increased AURKB activity (PubMed:11516652, PubMed:12925766, PubMed:14610074). Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1, VIM/vimentin, HASPIN, and histone H3 (PubMed:11756469, PubMed:11784863, PubMed:11856369, PubMed:12689593, PubMed:14602875, PubMed:16103226, PubMed:21658950). A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres (PubMed:21658950). Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively) (PubMed:11784863, PubMed:11856369). AURKB is also required for kinetochore localization of BUB1 and SGO1 (PubMed:15020684, PubMed:17617734). Phosphorylation of p53/TP53 negatively regulates its transcriptional activity (PubMed:20959462). Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes (By similarity). Acts as an inhibitor of CGAS during mitosis: catalyzes phosphorylation of the N-terminus of CGAS during the G2-M transition, blocking CGAS liquid phase separation and activation, and thereby preventing CGAS-induced autoimmunity (PubMed:33542149). Phosphorylates KRT5 during anaphase and telophase (By similarity). Phosphorylates ATXN10 which promotes phosphorylation of ATXN10 by PLK1 and may play a role in the regulation of cytokinesis and stimulating the proteasomal degradation of ATXN10 (PubMed:25666058). {ECO:0000250|UniProtKB:O70126, ECO:0000269|PubMed:11516652, ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:11784863, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12458200, ECO:0000269|PubMed:12686604, ECO:0000269|PubMed:12689593, ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14602875, ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21658950, ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:24814515, ECO:0000269|PubMed:25666058, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:29449677, ECO:0000269|PubMed:33542149}. |
| Q96HU1 | SGSM3 | T6 | ochoa | Small G protein signaling modulator 3 (Merlin-associated protein) (RUN and TBC1 domain-containing protein 3) (Rab-GTPase-activating protein-like protein) (RabGAPLP) | May play a cooperative role in NF2-mediated growth suppression of cells. {ECO:0000269|PubMed:15541357}. |
| Q96IZ7 | RSRC1 | S6 | ochoa | Serine/Arginine-related protein 53 (SRrp53) (Arginine/serine-rich coiled-coil protein 1) | Has a role in alternative splicing and transcription regulation (PubMed:29522154). Involved in both constitutive and alternative pre-mRNA splicing. May have a role in the recognition of the 3' splice site during the second step of splicing. {ECO:0000269|PubMed:15798186, ECO:0000269|PubMed:29522154}. |
| Q96J02 | ITCH | S6 | ochoa | E3 ubiquitin-protein ligase Itchy homolog (Itch) (EC 2.3.2.26) (Atrophin-1-interacting protein 4) (AIP4) (HECT-type E3 ubiquitin transferase Itchy homolog) (NFE2-associated polypeptide 1) (NAPP1) | Acts as an Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:11046148, PubMed:14602072, PubMed:15051726, PubMed:16387660, PubMed:17028573, PubMed:18718448, PubMed:18718449, PubMed:19116316, PubMed:19592251, PubMed:19881509, PubMed:20068034, PubMed:20392206, PubMed:20491914, PubMed:23146885, PubMed:24790097, PubMed:25631046). Catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation (PubMed:17028573, PubMed:18718448, PubMed:19131965, PubMed:19881509). Involved in the control of inflammatory signaling pathways (PubMed:19131965). Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways (PubMed:19131965). Promotes the association of the complex after TNF stimulation (PubMed:19131965). Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains (PubMed:19131965). This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1 (PubMed:19131965). Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways (PubMed:19592251). Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response (PubMed:18718448, PubMed:20491914). Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages (PubMed:18718448). Mediates JUN ubiquitination and degradation (By similarity). Mediates JUNB ubiquitination and degradation (PubMed:16387660). Critical regulator of type 2 helper T (Th2) cell cytokine production by inducing JUNB ubiquitination and degradation (By similarity). Involved in the negative regulation of MAVS-dependent cellular antiviral responses (PubMed:19881509). Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation (PubMed:19881509). Following ligand stimulation, regulates sorting of Wnt receptor FZD4 to the degradative endocytic pathway probably by modulating PI42KA activity (PubMed:23146885). Ubiquitinates PI4K2A and negatively regulates its catalytic activity (PubMed:23146885). Ubiquitinates chemokine receptor CXCR4 and regulates sorting of CXCR4 to the degradative endocytic pathway following ligand stimulation by ubiquitinating endosomal sorting complex required for transport ESCRT-0 components HGS and STAM (PubMed:14602072, PubMed:23146885, PubMed:34927784). Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination (PubMed:17028573, PubMed:18628966, PubMed:23886940). Ubiquitinates SNX9 (PubMed:20491914). Ubiquitinates MAP3K7 through 'Lys-48'-linked conjugation (By similarity). Together with UBR5, involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP: catalyzes 'Lys-48'-/'Lys-63'-branched ubiquitination of TXNIP (PubMed:20068034, PubMed:29378950). ITCH synthesizes 'Lys-63'-linked chains, while UBR5 is branching multiple 'Lys-48'-linked chains of substrate initially modified (PubMed:29378950). Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID (PubMed:20392206). Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). Inhibits the replication of influenza A virus (IAV) via ubiquitination of IAV matrix protein 1 (M1) through 'Lys-48'-linked conjugation resulting in M1 proteasomal degradation (PubMed:30328013). Ubiquitinates NEDD9/HEF1, resulting in proteasomal degradation of NEDD9/HEF1 (PubMed:15051726). {ECO:0000250|UniProtKB:Q8C863, ECO:0000269|PubMed:14602072, ECO:0000269|PubMed:15051726, ECO:0000269|PubMed:16387660, ECO:0000269|PubMed:17028573, ECO:0000269|PubMed:18628966, ECO:0000269|PubMed:18718448, ECO:0000269|PubMed:18718449, ECO:0000269|PubMed:19116316, ECO:0000269|PubMed:19131965, ECO:0000269|PubMed:19592251, ECO:0000269|PubMed:19881509, ECO:0000269|PubMed:20068034, ECO:0000269|PubMed:20392206, ECO:0000269|PubMed:20491914, ECO:0000269|PubMed:23146885, ECO:0000269|PubMed:23886940, ECO:0000269|PubMed:24790097, ECO:0000269|PubMed:25631046, ECO:0000269|PubMed:29378950, ECO:0000269|PubMed:30328013}. |
| Q96MF7 | NSMCE2 | S6 | ochoa | E3 SUMO-protein ligase NSE2 (EC 2.3.2.-) (E3 SUMO-protein transferase NSE2) (MMS21 homolog) (hMMS21) (Non-structural maintenance of chromosomes element 2 homolog) (Non-SMC element 2 homolog) | E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination (PubMed:16055714, PubMed:16810316). Is not be required for the stability of the complex (PubMed:16055714, PubMed:16810316). The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks (PubMed:16055714, PubMed:16810316). The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs) (PubMed:17589526). Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and STAG2 (PubMed:16055714, PubMed:16810316, PubMed:17589526, PubMed:31400850). Required for recruitment of telomeres to PML nuclear bodies (PubMed:17589526). SUMO protein-ligase activity is required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair, and for formation of APBs in ALT cell lines (PubMed:17589526). Required for sister chromatid cohesion during prometaphase and mitotic progression (PubMed:19502785). {ECO:0000269|PubMed:16055714, ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:19502785, ECO:0000269|PubMed:31400850}. |
| Q96MF7 | NSMCE2 | S7 | ochoa | E3 SUMO-protein ligase NSE2 (EC 2.3.2.-) (E3 SUMO-protein transferase NSE2) (MMS21 homolog) (hMMS21) (Non-structural maintenance of chromosomes element 2 homolog) (Non-SMC element 2 homolog) | E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination (PubMed:16055714, PubMed:16810316). Is not be required for the stability of the complex (PubMed:16055714, PubMed:16810316). The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks (PubMed:16055714, PubMed:16810316). The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs) (PubMed:17589526). Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and STAG2 (PubMed:16055714, PubMed:16810316, PubMed:17589526, PubMed:31400850). Required for recruitment of telomeres to PML nuclear bodies (PubMed:17589526). SUMO protein-ligase activity is required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair, and for formation of APBs in ALT cell lines (PubMed:17589526). Required for sister chromatid cohesion during prometaphase and mitotic progression (PubMed:19502785). {ECO:0000269|PubMed:16055714, ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:19502785, ECO:0000269|PubMed:31400850}. |
| Q96MG8 | PCMTD1 | S6 | ochoa | Protein-L-isoaspartate O-methyltransferase domain-containing protein 1 | Substrate recognition component of an ECS (Elongin BC-CUL5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:35486881). Specifically binds to the methyltransferase cofactor S-adenosylmethionine (AdoMet) via the N-terminal AdoMet binding motif, but does not display methyltransferase activity (PubMed:35486881). May provide an alternate maintenance pathway for modified proteins by acting as a damage-specific E3 ubiquitin ligase adaptor protein (PubMed:35486881). {ECO:0000269|PubMed:35486881}. |
| Q96NB3 | ZNF830 | S6 | ochoa | Zinc finger protein 830 (Coiled-coil domain-containing protein 16) | May play a role in pre-mRNA splicing as component of the spliceosome (PubMed:25599396). Acts as an important regulator of the cell cycle that participates in the maintenance of genome integrity. During cell cycle progression in embryonic fibroblast, prevents replication fork collapse, double-strand break formation and cell cycle checkpoint activation. Controls mitotic cell cycle progression and cell survival in rapidly proliferating intestinal epithelium and embryonic stem cells. During the embryo preimplantation, controls different aspects of M phase. During early oocyte growth, plays a role in oocyte survival by preventing chromosomal breaks formation, activation of TP63 and reduction of transcription (By similarity). {ECO:0000250|UniProtKB:Q8R1N0, ECO:0000305|PubMed:25599396}. |
| Q96NT5 | SLC46A1 | S6 | ochoa | Proton-coupled folate transporter (HsPCFT) (hPCFT) (Heme carrier protein 1) (PCFT/HCP1) (Solute carrier family 46 member 1) | Proton-coupled folate symporter that mediates folate absorption using an H(+) gradient as a driving force (PubMed:17129779, PubMed:17446347, PubMed:17475902, PubMed:19389703, PubMed:19762432, PubMed:25504888, PubMed:29344585, PubMed:30858177, PubMed:31494288, PubMed:31792273, PubMed:32893190, PubMed:34619546). Involved in the intestinal absorption of folates at the brush-border membrane of the proximal jejunum, and the transport from blood to cerebrospinal fluid across the choroid plexus (PubMed:17129779, PubMed:17446347, PubMed:17475902, PubMed:19389703, PubMed:25504888, PubMed:29344585, PubMed:30858177, PubMed:31494288, PubMed:32893190). Functions at acidic pH via alternate outward- and inward-open conformation states (PubMed:32893190, PubMed:34040256). Protonation of residues in the outward open state primes the protein for transport (PubMed:34040256). Binding of folate promotes breaking of salt bridge network and subsequent closure of the extracellular gate, leading to the inward-open state and release of protons and folate (PubMed:34040256). Also able to transport antifolate drugs, such as methotrexate and pemetrexed, which are established treatments for cancer and autoimmune diseases (PubMed:18524888, PubMed:19762432, PubMed:22345511, PubMed:25608532, PubMed:28802835, PubMed:29326243, PubMed:34040256, PubMed:34619546). Involved in FOLR1-mediated endocytosis by serving as a route of export of folates from acidified endosomes (PubMed:19074442). Also acts as a lower-affinity, pH-independent heme carrier protein and constitutes the main importer of heme in the intestine (PubMed:17156779). Imports heme in the retina and retinal pigment epithelium, in neurons of the hippocampus, in hepatocytes and in the renal epithelial cells (PubMed:32621820). Hence, participates in the trafficking of heme and increases intracellular iron content (PubMed:32621820). {ECO:0000269|PubMed:17129779, ECO:0000269|PubMed:17156779, ECO:0000269|PubMed:17446347, ECO:0000269|PubMed:17475902, ECO:0000269|PubMed:18524888, ECO:0000269|PubMed:19074442, ECO:0000269|PubMed:19389703, ECO:0000269|PubMed:19762432, ECO:0000269|PubMed:22345511, ECO:0000269|PubMed:25504888, ECO:0000269|PubMed:25608532, ECO:0000269|PubMed:28802835, ECO:0000269|PubMed:29326243, ECO:0000269|PubMed:29344585, ECO:0000269|PubMed:30858177, ECO:0000269|PubMed:31494288, ECO:0000269|PubMed:31792273, ECO:0000269|PubMed:32621820, ECO:0000269|PubMed:32893190, ECO:0000269|PubMed:34040256, ECO:0000269|PubMed:34619546}.; FUNCTION: [Isoform 2]: Inactive isoform which is not able to mediate proton-coupled folate transport. {ECO:0000269|PubMed:17129779}. |
| Q96QE2 | SLC2A13 | S6 | ochoa | Proton myo-inositol cotransporter (H(+)-myo-inositol cotransporter) (Hmit) (H(+)-myo-inositol symporter) (Solute carrier family 2 member 13) | H(+)-myo-inositol cotransporter (PubMed:11500374). Can also transport related stereoisomers (PubMed:11500374). {ECO:0000269|PubMed:11500374}. |
| Q96QK1 | VPS35 | S7 | ochoa | Vacuolar protein sorting-associated protein 35 (hVPS35) (Maternal-embryonic 3) (Vesicle protein sorting 35) | Acts as a component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (PubMed:30213940). The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (PubMed:15078903, PubMed:15247922, PubMed:20164305). Required for endosomal localization of WASHC2C (PubMed:22070227, PubMed:28892079). Mediates the association of the CSC with the WASH complex via WASHC2 (PubMed:22070227, PubMed:24819384, PubMed:24980502). Required for the endosomal localization of TBC1D5 (PubMed:20923837). {ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:15247922, ECO:0000269|PubMed:20164305, ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22070227, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24819384, ECO:0000269|PubMed:24980502, ECO:0000269|PubMed:28892079, ECO:0000269|PubMed:30213940, ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:22070227, ECO:0000303|PubMed:22513087, ECO:0000303|PubMed:23563491}.; FUNCTION: (Microbial infection) The heterotrimeric retromer cargo-selective complex (CSC) mediates the exit of human papillomavirus from the early endosome and the delivery to the Golgi apparatus. {ECO:0000269|PubMed:25693203, ECO:0000269|PubMed:30122350}. |
| Q96QR8 | PURB | S6 | ochoa | Transcriptional regulator protein Pur-beta (Purine-rich element-binding protein B) | Transcriptional regulator which can act as an activator or a repressor. Represses the transcription of ACTA2 in fibroblasts and smooth muscle cells via its ability to interact with the purine-rich strand of a MCAT- containing element in the 5' flanking region of the gene. Represses the transcription of MYOCD, capable of repressing all isoforms of MYOCD but the magnitude of the repressive effects is most notable for the SMC- specific isoforms. Promotes hepatic glucose production by activating the transcription of ADCY6, leading to cAMP accumulation, increased PKA activity, CREB activation, and increased transcription of PCK1 and G6PC genes (By similarity). Has capacity to bind repeated elements in single-stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene (PubMed:1448097). Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine-rich negative regulatory (PNR) element Modulates constitutive liver galectin-3 gene transcription by binding to its promoter. May play a role in the dendritic transport of a subset of mRNAs (By similarity). {ECO:0000250|UniProtKB:O35295, ECO:0000250|UniProtKB:Q68A21, ECO:0000269|PubMed:1448097}. |
| Q96S21 | RAB40C | S6 | ochoa | Ras-related protein Rab-40C (EC 3.6.5.2) (Rar-like protein) (Ras-like protein family member 8C) (SOCS box-containing protein RAR3) | RAB40C small GTPase acts as substrate-recognition component of the ECS(RAB40C) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15601820, PubMed:35512830). The Rab40 subfamily belongs to the Rab family that are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:29156729). As part of the ECS(RAB40C) complex, mediates ANKRD28 ubiquitination and degradation, thereby inhibiting protein phosphatase 6 (PP6) complex activity and focal adhesion assembly during cell migration (PubMed:35512830). Also negatively regulate lipid droplets accumulation in a GTP-dependent manner (PubMed:29156729). {ECO:0000269|PubMed:15601820, ECO:0000269|PubMed:29156729, ECO:0000269|PubMed:35512830}. |
| Q96S44 | TP53RK | T7 | ochoa | EKC/KEOPS complex subunit TP53RK (EC 3.6.-.-) (Atypical serine/threonine protein kinase TP53RK) (Nori-2) (TP53-regulating kinase) (EC 2.7.11.1) (p53-related protein kinase) | Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine (PubMed:22912744, PubMed:27903914). The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37 (PubMed:22912744, PubMed:27903914). TP53RK has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit OSGEP (By similarity). Atypical protein kinase that phosphorylates 'Ser-15' of p53/TP53 protein and may therefore participate in its activation (PubMed:11546806). {ECO:0000250|UniProtKB:P53323, ECO:0000250|UniProtKB:Q9UYB9, ECO:0000269|PubMed:11546806, ECO:0000305|PubMed:22912744, ECO:0000305|PubMed:27903914}. |
| Q96SF7 | TBX15 | S7 | ochoa | T-box transcription factor TBX15 (T-box protein 15) (T-box transcription factor TBX14) (T-box protein 14) | Probable transcriptional regulator involved in the development of the skeleton of the limb, vertebral column and head. Acts by controlling the number of mesenchymal precursor cells and chondrocytes (By similarity). {ECO:0000250}. |
| Q99598 | TSNAX | S7 | ochoa | Translin-associated protein X (Translin-associated factor X) | Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis. {ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:21552258}. |
| Q99613 | EIF3C | T6 | ochoa | Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 subunit 8) (eIF3 p110) | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. |
| Q99613 | EIF3C | T7 | ochoa | Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 subunit 8) (eIF3 p110) | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. |
| Q99622 | C12orf57 | T6 | ochoa | Protein C10 | In brain, may be required for corpus callosum development. {ECO:0000269|PubMed:23453666}. |
| Q99653 | CHP1 | S6 | ochoa | Calcineurin B homologous protein 1 (Calcineurin B-like protein) (Calcium-binding protein CHP) (Calcium-binding protein p22) (EF-hand calcium-binding domain-containing protein p22) | Calcium-binding protein involved in different processes such as regulation of vesicular trafficking, plasma membrane Na(+)/H(+) exchanger and gene transcription. Involved in the constitutive exocytic membrane traffic. Mediates the association between microtubules and membrane-bound organelles of the endoplasmic reticulum and Golgi apparatus and is also required for the targeting and fusion of transcytotic vesicles (TCV) with the plasma membrane. Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Affects the pH sensitivity of SLC9A1/NHE1 by increasing its sensitivity at acidic pH. Required for the stabilization and localization of SLC9A1/NHE1 at the plasma membrane. Inhibits serum- and GTPase-stimulated Na(+)/H(+) exchange. Plays a role as an inhibitor of ribosomal RNA transcription by repressing the nucleolar UBF1 transcriptional activity. May sequester UBF1 in the nucleoplasm and limit its translocation to the nucleolus. Associates to the ribosomal gene promoter. Acts as a negative regulator of the calcineurin/NFAT signaling pathway. Inhibits NFAT nuclear translocation and transcriptional activity by suppressing the calcium-dependent calcineurin phosphatase activity. Also negatively regulates the kinase activity of the apoptosis-induced kinase STK17B. Inhibits both STK17B auto- and substrate-phosphorylations in a calcium-dependent manner. {ECO:0000269|PubMed:10593895, ECO:0000269|PubMed:11350981, ECO:0000269|PubMed:15035633, ECO:0000269|PubMed:8901634}. |
| Q99653 | CHP1 | T7 | ochoa | Calcineurin B homologous protein 1 (Calcineurin B-like protein) (Calcium-binding protein CHP) (Calcium-binding protein p22) (EF-hand calcium-binding domain-containing protein p22) | Calcium-binding protein involved in different processes such as regulation of vesicular trafficking, plasma membrane Na(+)/H(+) exchanger and gene transcription. Involved in the constitutive exocytic membrane traffic. Mediates the association between microtubules and membrane-bound organelles of the endoplasmic reticulum and Golgi apparatus and is also required for the targeting and fusion of transcytotic vesicles (TCV) with the plasma membrane. Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Affects the pH sensitivity of SLC9A1/NHE1 by increasing its sensitivity at acidic pH. Required for the stabilization and localization of SLC9A1/NHE1 at the plasma membrane. Inhibits serum- and GTPase-stimulated Na(+)/H(+) exchange. Plays a role as an inhibitor of ribosomal RNA transcription by repressing the nucleolar UBF1 transcriptional activity. May sequester UBF1 in the nucleoplasm and limit its translocation to the nucleolus. Associates to the ribosomal gene promoter. Acts as a negative regulator of the calcineurin/NFAT signaling pathway. Inhibits NFAT nuclear translocation and transcriptional activity by suppressing the calcium-dependent calcineurin phosphatase activity. Also negatively regulates the kinase activity of the apoptosis-induced kinase STK17B. Inhibits both STK17B auto- and substrate-phosphorylations in a calcium-dependent manner. {ECO:0000269|PubMed:10593895, ECO:0000269|PubMed:11350981, ECO:0000269|PubMed:15035633, ECO:0000269|PubMed:8901634}. |
| Q99661 | KIF2C | S6 | ochoa | Kinesin-like protein KIF2C (Kinesin-like protein 6) (Mitotic centromere-associated kinesin) (MCAK) | In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (PubMed:21820309). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis (PubMed:19060894). Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment (PubMed:23891108). {ECO:0000269|PubMed:19060894, ECO:0000269|PubMed:21820309, ECO:0000269|PubMed:23891108}. |
| Q99685 | MGLL | S6 | ochoa | Monoglyceride lipase (MGL) (EC 3.1.1.23) (HU-K5) (Lysophospholipase homolog) (Lysophospholipase-like) (Monoacylglycerol lipase) (MAGL) | Converts monoacylglycerides to free fatty acids and glycerol (PubMed:19029917, PubMed:20079333, PubMed:21049984, PubMed:22969151, PubMed:24368842). Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain (PubMed:19029917, PubMed:20079333, PubMed:21049984, PubMed:22969151, PubMed:24368842). Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (PubMed:20079333). {ECO:0000269|PubMed:19029917, ECO:0000269|PubMed:20079333, ECO:0000269|PubMed:21049984, ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:24368842}. |
| Q99708 | RBBP8 | S6 | ochoa | DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2) | Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway (PubMed:17965729, PubMed:19202191, PubMed:19759395, PubMed:20064462, PubMed:23273981, PubMed:26721387, PubMed:27814491, PubMed:27889449, PubMed:30787182). HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse (PubMed:17965729, PubMed:19202191, PubMed:23273981, PubMed:27814491, PubMed:27889449, PubMed:30787182). Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ) (PubMed:19202191). Specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts: recruited to DSBs by NBN following phosphorylation by CDK1, and promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:33836577). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA (PubMed:16581787, PubMed:17965729, PubMed:19759395, PubMed:20064462). Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (PubMed:15485915, PubMed:16818604). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity). Binds preferentially to DNA Y-junctions and to DNA substrates with blocked ends and promotes intermolecular DNA bridging (PubMed:30601117). {ECO:0000250|UniProtKB:Q80YR6, ECO:0000269|PubMed:15485915, ECO:0000269|PubMed:16581787, ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19202191, ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:20064462, ECO:0000269|PubMed:23273981, ECO:0000269|PubMed:26721387, ECO:0000269|PubMed:27814491, ECO:0000269|PubMed:27889449, ECO:0000269|PubMed:30601117, ECO:0000269|PubMed:30787182, ECO:0000269|PubMed:33836577}. |
| Q99708 | RBBP8 | S7 | ochoa | DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2) | Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway (PubMed:17965729, PubMed:19202191, PubMed:19759395, PubMed:20064462, PubMed:23273981, PubMed:26721387, PubMed:27814491, PubMed:27889449, PubMed:30787182). HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse (PubMed:17965729, PubMed:19202191, PubMed:23273981, PubMed:27814491, PubMed:27889449, PubMed:30787182). Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ) (PubMed:19202191). Specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts: recruited to DSBs by NBN following phosphorylation by CDK1, and promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:33836577). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA (PubMed:16581787, PubMed:17965729, PubMed:19759395, PubMed:20064462). Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (PubMed:15485915, PubMed:16818604). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity). Binds preferentially to DNA Y-junctions and to DNA substrates with blocked ends and promotes intermolecular DNA bridging (PubMed:30601117). {ECO:0000250|UniProtKB:Q80YR6, ECO:0000269|PubMed:15485915, ECO:0000269|PubMed:16581787, ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19202191, ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:20064462, ECO:0000269|PubMed:23273981, ECO:0000269|PubMed:26721387, ECO:0000269|PubMed:27814491, ECO:0000269|PubMed:27889449, ECO:0000269|PubMed:30601117, ECO:0000269|PubMed:30787182, ECO:0000269|PubMed:33836577}. |
| Q99733 | NAP1L4 | S7 | ochoa | Nucleosome assembly protein 1-like 4 (Nucleosome assembly protein 2) (NAP-2) | Acts as a histone chaperone in nucleosome assembly. {ECO:0000269|PubMed:9325046}. |
| Q99816 | TSG101 | S6 | ochoa | Tumor susceptibility gene 101 protein (ESCRT-I complex subunit TSG101) | Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). It may also play a role in the extracellular release of microvesicles that differ from the exosomes (PubMed:22315426). {ECO:0000269|PubMed:11916981, ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:21070952, ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22315426, ECO:0000269|PubMed:22660413}. |
| Q99879 | H2BC14 | S7 | ochoa | Histone H2B type 1-M (Histone H2B.e) (H2B/e) | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. |
| Q9BPY3 | FAM118B | S6 | ochoa | Protein FAM118B | May play a role in Cajal bodies formation. {ECO:0000269|PubMed:24569877}. |
| Q9BPY8 | HOPX | S7 | ochoa | Homeodomain-only protein (Lung cancer-associated Y protein) (Not expressed in choriocarcinoma protein 1) (Odd homeobox protein 1) | Atypical homeodomain protein which does not bind DNA and is required to modulate cardiac growth and development. Acts via its interaction with SRF, thereby modulating the expression of SRF-dependent cardiac-specific genes and cardiac development. Prevents SRF-dependent transcription either by inhibiting SRF binding to DNA or by recruiting histone deacetylase (HDAC) proteins that prevent transcription by SRF. Overexpression causes cardiac hypertrophy (By similarity). May act as a tumor suppressor. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and assists in chaperone-mediated protein refolding (PubMed:27708256). {ECO:0000250|UniProtKB:Q8R1H0, ECO:0000269|PubMed:27708256}. |
| Q9BQ89 | FAM110A | S7 | ochoa | Protein FAM110A | None |
| Q9BQC3 | DPH2 | S6 | ochoa | 2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 (Diphthamide biosynthesis protein 2) (Diphtheria toxin resistance protein 2) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 2) | Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (PubMed:32576952). DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit (By similarity). {ECO:0000250|UniProtKB:P32461, ECO:0000269|PubMed:32576952}. |
| Q9BQC3 | DPH2 | S7 | ochoa | 2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 (Diphthamide biosynthesis protein 2) (Diphtheria toxin resistance protein 2) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 2) | Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (PubMed:32576952). DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit (By similarity). {ECO:0000250|UniProtKB:P32461, ECO:0000269|PubMed:32576952}. |
| Q9BQI3 | EIF2AK1 | S6 | ochoa | Eukaryotic translation initiation factor 2-alpha kinase 1 (EC 2.7.11.1) (Heme-controlled repressor) (HCR) (Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase) (Heme-regulated inhibitor) (hHRI) (Hemin-sensitive initiation factor 2-alpha kinase) | Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress conditions (PubMed:32132706, PubMed:32132707, PubMed:37327776, PubMed:37550454, PubMed:38340717). Key activator of the integrated stress response (ISR) required for adaptation to various stress, such as heme deficiency, oxidative stress, osmotic shock, mitochondrial dysfunction and heat shock (PubMed:32132706, PubMed:32132707, PubMed:37327776, PubMed:37550454, PubMed:38340717). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming (PubMed:32132706, PubMed:32132707, PubMed:37327776). Acts as a key sensor of heme-deficiency: in normal conditions, binds hemin via a cysteine thiolate and histidine nitrogenous coordination, leading to inhibit the protein kinase activity (By similarity). This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell: heme depletion relieves inhibition and stimulates kinase activity, activating the ISR (By similarity). Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions (By similarity). In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties (By similarity). It thereby plays an essential protective role for RBC survival in anemias of iron deficiency (By similarity). Iron deficiency also triggers activation by full-length DELE1 (PubMed:37327776). Also activates the ISR in response to mitochondrial dysfunction: HRI/EIF2AK1 protein kinase activity is activated upon binding to the processed form of DELE1 (S-DELE1), thereby promoting the ATF4-mediated reprogramming (PubMed:32132706, PubMed:32132707). Also acts as an activator of mitophagy in response to mitochondrial damage: catalyzes phosphorylation of eIF-2-alpha (EIF2S1) following activation by S-DELE1, thereby promoting mitochondrial localization of EIF2S1, triggering PRKN-independent mitophagy (PubMed:38340717). {ECO:0000250|UniProtKB:Q9Z2R9, ECO:0000269|PubMed:32132706, ECO:0000269|PubMed:32132707, ECO:0000269|PubMed:32197074, ECO:0000269|PubMed:37550454, ECO:0000269|PubMed:38340717}. |
| Q9BQJ4 | TMEM47 | S6 | ochoa | Transmembrane protein 47 (Brain cell membrane protein 1) (Transmembrane 4 superfamily member 10) | Regulates cell junction organization in epithelial cells. May play a role in the transition from adherens junction to tight junction assembly. May regulate F-actin polymerization required for tight junctional localization dynamics and affect the junctional localization of PARD6B. During podocyte differentiation may negatively regulate activity of FYN and subsequently the abundance of nephrin (By similarity). {ECO:0000250|UniProtKB:Q9JJG6, ECO:0000250|UniProtKB:Q9XSV3}. |
| Q9BR77 | CCDC77 | T6 | ochoa | Coiled-coil domain-containing protein 77 | None |
| Q9BRP8 | PYM1 | S6 | ochoa | Partner of Y14 and mago (PYM homolog 1 exon junction complex-associated factor) (Protein wibg homolog) | Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions. May bind RNA; the relevance of RNA-binding remains unclear in vivo, RNA-binding was detected by PubMed:14968132, while PubMed:19410547 did not detect RNA-binding activity independently of the EJC. {ECO:0000269|PubMed:18026120, ECO:0000269|PubMed:19410547}. |
| Q9BRR8 | GPATCH1 | S6 | ochoa | G patch domain-containing protein 1 (Evolutionarily conserved G-patch domain-containing protein) | None |
| Q9BRT8 | ZNG1A | S7 | ochoa | Zinc-regulated GTPase metalloprotein activator 1A (EC 3.6.5.-) (Cobalamin synthase W domain-containing protein 1) (COBW domain-containing protein 1) (NPC-A-6 COBW domain-containing protein 1) (NPC-A-6) | Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1A to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1. {ECO:0000250|UniProtKB:Q8VEH6}. |
| Q9BRZ2 | TRIM56 | S6 | ochoa | E3 ubiquitin-protein ligase TRIM56 (EC 2.3.2.27) (RING finger protein 109) (Tripartite motif-containing protein 56) | E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity by mediating ubiquitination of CGAS and STING1 (PubMed:21289118, PubMed:29426904). In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets STING1 to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for the production of type I interferon IFN-beta (By similarity). Also mediate monoubiquitination of CGAS, thereby promoting CGAS oligomerization and subsequent activation (PubMed:29426904). Promotes also TNFalpha-induced NF-kappa-B signaling by mediating 'Lys-63'-linked ubiquitination TAK1, leading to enhanced interaction between TAK1 and CHUK/IKKalpha (PubMed:35952808). Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling. Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (PubMed:22948160). Promotes establishment of an antiviral state by TLR3 ligand and TLR3-mediated chemokine induction following infection by hepatitis C virus (PubMed:22948160). Acts as a restriction factor of Zika virus through direct interaction with the viral RNA via its C-terminal region (PubMed:31251739). {ECO:0000250|UniProtKB:Q80VI1, ECO:0000269|PubMed:21289118, ECO:0000269|PubMed:22948160, ECO:0000269|PubMed:29426904, ECO:0000269|PubMed:31251739, ECO:0000269|PubMed:35952808}. |
| Q9BRZ2 | TRIM56 | S7 | ochoa | E3 ubiquitin-protein ligase TRIM56 (EC 2.3.2.27) (RING finger protein 109) (Tripartite motif-containing protein 56) | E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity by mediating ubiquitination of CGAS and STING1 (PubMed:21289118, PubMed:29426904). In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets STING1 to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for the production of type I interferon IFN-beta (By similarity). Also mediate monoubiquitination of CGAS, thereby promoting CGAS oligomerization and subsequent activation (PubMed:29426904). Promotes also TNFalpha-induced NF-kappa-B signaling by mediating 'Lys-63'-linked ubiquitination TAK1, leading to enhanced interaction between TAK1 and CHUK/IKKalpha (PubMed:35952808). Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling. Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (PubMed:22948160). Promotes establishment of an antiviral state by TLR3 ligand and TLR3-mediated chemokine induction following infection by hepatitis C virus (PubMed:22948160). Acts as a restriction factor of Zika virus through direct interaction with the viral RNA via its C-terminal region (PubMed:31251739). {ECO:0000250|UniProtKB:Q80VI1, ECO:0000269|PubMed:21289118, ECO:0000269|PubMed:22948160, ECO:0000269|PubMed:29426904, ECO:0000269|PubMed:31251739, ECO:0000269|PubMed:35952808}. |
| Q9BSA9 | TMEM175 | T6 | ochoa | Endosomal/lysosomal proton channel TMEM175 (Potassium channel TMEM175) (Transmembrane protein 175) (hTMEM175) | Proton-activated proton channel that catalyzes proton efflux from endosomes and lysosomes to maintain a steady-state pH (PubMed:35333573, PubMed:35750034, PubMed:37390818). Activated at low pH (under pH 4.6) by luminal side protons: selectively mediates lysosomal proton release from lysosomes, eliciting a proton leak that balances V-ATPase activity to maintain pH homeostasis (PubMed:35750034). Regulation of lumenal pH stability is required for autophagosome-lysosome fusion (PubMed:26317472, PubMed:32267231). Also acts as a potassium channel at higher pH, regulating potassium conductance in endosomes and lysosomes (PubMed:26317472, PubMed:28723891, PubMed:32228865, PubMed:32267231, PubMed:33505021). Constitutes the pore-forming subunit of the lysoK(GF) complex, a complex activated by extracellular growth factors (PubMed:33505021). The lysoK(GF) complex is composed of TMEM175 and AKT (AKT1, AKT2 or AKT3), a major target of growth factor receptors: in the complex, TMEM175 channel is opened by conformational changes by AKT, leading to its activation (PubMed:33505021). The lysoK(GF) complex is required to protect neurons against stress-induced damage (PubMed:33505021). {ECO:0000269|PubMed:26317472, ECO:0000269|PubMed:28723891, ECO:0000269|PubMed:32228865, ECO:0000269|PubMed:32267231, ECO:0000269|PubMed:33505021, ECO:0000269|PubMed:35333573, ECO:0000269|PubMed:35750034, ECO:0000269|PubMed:37390818}. |
| Q9BTV4 | TMEM43 | S7 | ochoa | Transmembrane protein 43 (Protein LUMA) | May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (PubMed:32614325). In addition, functions as a critical signaling component in mediating NF-kappa-B activation by acting downstream of EGFR and upstream of CARD10 (PubMed:27991920). Contributes to passive conductance current in cochlear glia-like supporting cells, mediated by gap junctions and necessary for hearing and speech discrimination (PubMed:34050020). {ECO:0000250|UniProtKB:Q9DBS1, ECO:0000269|PubMed:27991920, ECO:0000269|PubMed:32614325, ECO:0000269|PubMed:34050020}. |
| Q9BVC4 | MLST8 | T7 | ochoa | Target of rapamycin complex subunit LST8 (TORC subunit LST8) (G protein beta subunit-like) (Gable) (Protein GbetaL) (Mammalian lethal with SEC13 protein 8) (mLST8) | Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073, PubMed:28489822). mTORC1 is activated in response to growth factors or amino acids (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). In response to nutrients, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). In the same time, it inhibits catabolic pathways by phosphorylating the autophagy initiation components ULK1 and ATG13, as well as transcription factor TFEB, a master regulators of lysosomal biogenesis and autophagy (PubMed:24403073). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:24403073). Within mTORC1, MLST8 interacts directly with MTOR and enhances its kinase activity (PubMed:12718876). In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity (PubMed:12718876). As part of the mTORC2 complex, transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15467718, PubMed:35926713). mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive (PubMed:15467718, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:15467718, PubMed:35926713). mTORC2 functions upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15467718). mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:15467718). mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657' (PubMed:15467718). Within mTORC2, MLST8 acts as a bridge between MAPKAP1/SIN1 and MTOR (PubMed:31085701). {ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:24403073, ECO:0000269|PubMed:28489822, ECO:0000269|PubMed:31085701, ECO:0000269|PubMed:35926713}. |
| Q9BW19 | KIFC1 | S6 | ochoa|psp | Kinesin-like protein KIFC1 (Kinesin-like protein 2) (Kinesin-related protein HSET) | Minus end-directed microtubule-dependent motor required for bipolar spindle formation (PubMed:15843429). May contribute to movement of early endocytic vesicles (By similarity). Regulates cilium formation and structure (By similarity). {ECO:0000250|UniProtKB:Q9QWT9, ECO:0000269|PubMed:15843429}. |
| Q9BX40 | LSM14B | T7 | ochoa | Protein LSM14 homolog B (RNA-associated protein 55B) (hRAP55B) | mRNA-binding protein essential for female fertility, oocyte meiotic maturation and the assembly of MARDO (mitochondria-associated ribonucleoprotein domain), a membraneless compartment that stores maternal mRNAs in oocytes. Ensures the proper accumulation and clearance of mRNAs essential for oocyte meiotic maturation and the normal progression from Meiosis I to Meiosis II in oocytes. Promotes the translation of some oogenesis-related mRNAs. Regulates the expression and/or localization of some key P-body proteins in oocytes. Essential for the assembly of the primordial follicle in the ovary. {ECO:0000250|UniProtKB:Q8CGC4}. |
| Q9BXP2 | SLC12A9 | S6 | ochoa | Solute carrier family 12 member 9 (Cation-chloride cotransporter 6) (hCCC6) (Cation-chloride cotransporter-interacting protein 1) (CCC-interacting protein 1) (hCIP1) (Potassium-chloride transporter 9) (WO3.3) | May be an inhibitor of SLC12A1. Seems to correspond to a subunit of a multimeric transport system and thus, additional subunits may be required for its function (PubMed:10871601). May play a role in lysosomal ion flux and osmoregulation (PubMed:38334070). {ECO:0000269|PubMed:10871601, ECO:0000269|PubMed:38334070}. |
| Q9C0B1 | FTO | T6 | psp | Alpha-ketoglutarate-dependent dioxygenase FTO (Fat mass and obesity-associated protein) (U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (EC 1.14.11.-) (U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO) (EC 1.14.11.-) (mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (m6A(m)-demethylase FTO) (EC 1.14.11.-) (mRNA N(6)-methyladenosine demethylase FTO) (EC 1.14.11.53) (tRNA N1-methyl adenine demethylase FTO) (EC 1.14.11.-) | RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis (PubMed:22002720, PubMed:25452335, PubMed:26457839, PubMed:26458103, PubMed:28002401, PubMed:30197295). Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:22002720, PubMed:25452335, PubMed:26457839, PubMed:26458103, PubMed:30197295). M6A demethylation by FTO affects mRNA expression and stability (PubMed:30197295). Also able to demethylate m6A in U6 small nuclear RNA (snRNA) (PubMed:30197295). Mediates demethylation of N(6),2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N(6)-methyladenosine at the second transcribed position of mRNAs and U6 snRNA (PubMed:28002401, PubMed:30197295). Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping (PubMed:28002401). Also acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs (PubMed:30197295). Has no activity towards 1-methylguanine (PubMed:20376003). Has no detectable activity towards double-stranded DNA (PubMed:20376003). Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single-stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine (PubMed:18775698, PubMed:20376003). Ability to repair alkylated DNA and RNA is however unsure in vivo (PubMed:18775698, PubMed:20376003). Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation (PubMed:18775698, PubMed:20376003). Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells (PubMed:26287746). Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs (By similarity). Plays an oncogenic role in a number of acute myeloid leukemias by enhancing leukemic oncogene-mediated cell transformation: acts by mediating m6A demethylation of target transcripts such as MYC, CEBPA, ASB2 and RARA, leading to promote their expression (PubMed:28017614, PubMed:29249359). {ECO:0000250|UniProtKB:Q8BGW1, ECO:0000269|PubMed:18775698, ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:22002720, ECO:0000269|PubMed:25452335, ECO:0000269|PubMed:26287746, ECO:0000269|PubMed:26457839, ECO:0000269|PubMed:26458103, ECO:0000269|PubMed:28002401, ECO:0000269|PubMed:28017614, ECO:0000269|PubMed:29249359, ECO:0000269|PubMed:30197295}. |
| Q9C0H5 | ARHGAP39 | Y7 | ochoa | Rho GTPase-activating protein 39 | None |
| Q9C0J8 | WDR33 | S7 | ochoa | pre-mRNA 3' end processing protein WDR33 (WD repeat-containing protein 33) (WD repeat-containing protein of 146 kDa) | Essential for both cleavage and polyadenylation of pre-mRNA 3' ends. {ECO:0000269|PubMed:19217410}. |
| Q9GZQ8 | MAP1LC3B | T6 | psp | Microtubule-associated protein 1 light chain 3 beta (Autophagy-related protein LC3 B) (Autophagy-related ubiquitin-like modifier LC3 B) (MAP1 light chain 3-like protein 2) (Microtubule-associated proteins 1A/1B light chain 3B) (MAP1A/MAP1B LC3 B) (MAP1A/MAP1B light chain 3 B) | Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes) (PubMed:20418806, PubMed:23209295, PubMed:28017329). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (PubMed:23209295, PubMed:28017329). In response to cellular stress and upon mitochondria fission, binds C-18 ceramides and anchors autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria (PubMed:22922758). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20418806, PubMed:23209295, PubMed:28017329). Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway (PubMed:24089205). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006537, PubMed:31006538). Upon nutrient stress, directly recruits cofactor JMY to the phagophore membrane surfaces and promotes JMY's actin nucleation activity and autophagosome biogenesis during autophagy (PubMed:30420355). {ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:22922758, ECO:0000269|PubMed:23209295, ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:30420355, ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}. |
| Q9H098 | FAM107B | Y6 | ochoa | Protein FAM107B | None |
| Q9H0W8 | SMG9 | S7 | ochoa | Nonsense-mediated mRNA decay factor SMG9 | Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (PubMed:19417104). Is recruited by release factors to stalled ribosomes together with SMG1 and SMG8 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required for the efficient association between SMG1 and SMG8 (PubMed:19417104). Plays a role in brain, heart, and eye development (By similarity). {ECO:0000250|UniProtKB:Q9DB90, ECO:0000269|PubMed:19417104}. |
| Q9H190 | SDCBP2 | S7 | ochoa | Syntenin-2 (Similar to TACIP18) (SITAC) (Syndecan-binding protein 2) | Binds phosphatidylinositol 4,5-bisphosphate (PIP2). May play a role in the organization of nuclear PIP2, cell division and cell survival (PubMed:15961997). {ECO:0000269|PubMed:15961997}. |
| Q9H211 | CDT1 | T7 | psp | DNA replication factor Cdt1 (Double parked homolog) (DUP) | Required for both DNA replication and mitosis (PubMed:11125146, PubMed:14993212, PubMed:21856198, PubMed:22581055, PubMed:26842564). DNA replication licensing factor, required for pre-replication complex assembly. Cooperates with CDC6 and the origin recognition complex (ORC) during G1 phase of the cell cycle to promote the loading of the mini-chromosome maintenance (MCM) complex onto DNA to generate pre-replication complexes (pre-RC) (PubMed:14672932). Required also for mitosis by promoting stable kinetochore-microtubule attachments (PubMed:22581055). Potential oncogene (By similarity). {ECO:0000250|UniProtKB:Q8R4E9, ECO:0000269|PubMed:11125146, ECO:0000269|PubMed:14672932, ECO:0000269|PubMed:14993212, ECO:0000269|PubMed:21856198, ECO:0000269|PubMed:22581055, ECO:0000269|PubMed:26842564}. |
| Q9H3P2 | NELFA | S7 | ochoa | Negative elongation factor A (NELF-A) (Wolf-Hirschhorn syndrome candidate 2 protein) | Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:12563561, ECO:0000269|PubMed:12612062}.; FUNCTION: (Microbial infection) The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. {ECO:0000269|PubMed:23884411}. |
| Q9H4A4 | RNPEP | S7 | ochoa | Aminopeptidase B (AP-B) (EC 3.4.11.6) (Arginine aminopeptidase) (Arginyl aminopeptidase) | Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). {ECO:0000250}. |
| Q9H4I2 | ZHX3 | S7 | ochoa | Zinc fingers and homeoboxes protein 3 (Triple homeobox protein 1) (Zinc finger and homeodomain protein 3) | Acts as a transcriptional repressor. Involved in the early stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a regulator of podocyte gene expression during primary glomerula disease. Binds to promoter DNA. {ECO:0000269|PubMed:12659632, ECO:0000269|PubMed:21174497}. |
| Q9H6E5 | TUT1 | S6 | ochoa|psp | Speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) (EC 2.7.7.19) (RNA-binding motif protein 21) (RNA-binding protein 21) (U6 snRNA-specific terminal uridylyltransferase 1) (U6-TUTase) (EC 2.7.7.52) | Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs (PubMed:18288197, PubMed:21102410). Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1 (PubMed:18288197). In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs (PubMed:21102410). In addition to adenylyltransferase activity, also has uridylyltransferase activity (PubMed:16790842, PubMed:18288197, PubMed:28589955). However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase (PubMed:18288197). Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA (PubMed:16790842, PubMed:18288197, PubMed:28589955). Not involved in replication-dependent histone mRNA degradation. {ECO:0000269|PubMed:16790842, ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:21102410, ECO:0000269|PubMed:28589955}. |
| Q9H6S0 | YTHDC2 | S6 | ochoa | 3'-5' RNA helicase YTHDC2 (EC 3.6.4.13) (YTH domain-containing protein 2) (hYTHDC2) | 3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells (PubMed:26318451, PubMed:29033321, PubMed:29970596). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability (PubMed:26318451, PubMed:29033321). Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs (By similarity). Acts by binding and promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both spermatogenesis and oogenesis (By similarity). {ECO:0000250|UniProtKB:B2RR83, ECO:0000269|PubMed:26318451, ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29970596}. |
| Q9H813 | PACC1 | S7 | ochoa | Proton-activated chloride channel (PAC) (hPAC) (Acid-sensitive outwardly-rectifying anion channel) (ASOR) (Proton-activated outwardly rectifying anion channel) (PAORAC) (Transmembrane protein 206) (hTMEM206) | Chloride channel gated by pH that facilitates the entry of chloride ions into cells upon exposure to extracellular acidic pH (PubMed:31023925, PubMed:31318332). Involved in acidosis-induced cell death by mediating chloride influx and subsequent cell swelling (PubMed:31023925, PubMed:31318332). {ECO:0000269|PubMed:31023925, ECO:0000269|PubMed:31318332}. |
| Q9H8S9 | MOB1A | S6 | ochoa | MOB kinase activator 1A (Mob1 alpha) (Mob1A) (Mob1 homolog 1B) (Mps one binder kinase activator-like 1B) | Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38 and STK38L. Acts cooperatively with STK3/MST2 to activate STK38. {ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:18362890, ECO:0000269|PubMed:19739119}. |
| Q9H8S9 | MOB1A | S7 | ochoa | MOB kinase activator 1A (Mob1 alpha) (Mob1A) (Mob1 homolog 1B) (Mps one binder kinase activator-like 1B) | Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38 and STK38L. Acts cooperatively with STK3/MST2 to activate STK38. {ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:18362890, ECO:0000269|PubMed:19739119}. |
| Q9H9E3 | COG4 | S6 | ochoa | Conserved oligomeric Golgi complex subunit 4 (COG complex subunit 4) (Component of oligomeric Golgi complex 4) | Required for normal Golgi function (PubMed:19536132, PubMed:30290151). Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1 (PubMed:19536132). {ECO:0000269|PubMed:19536132, ECO:0000269|PubMed:30290151}. |
| Q9HAJ7 | SAP30L | T6 | ochoa | Histone deacetylase complex subunit SAP30L (HCV non-structural protein 4A-transactivated protein 2) (Sin3 corepressor complex subunit SAP30L) (Sin3-associated protein p30-like) | [Isoform 1]: Functions as a transcription repressor, probably via its interaction with histone deacetylase complexes (PubMed:16820529, PubMed:18070604). Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus (PubMed:16820529). Binds DNA, apparently without sequence-specificity, and bends bound double-stranded DNA (PubMed:19015240). Binds phosphoinositol phosphates (phosphoinositol 3-phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate) via the same basic sequence motif that mediates DNA binding and nuclear import (PubMed:19015240, PubMed:26609676). {ECO:0000269|PubMed:16820529, ECO:0000269|PubMed:18070604, ECO:0000269|PubMed:19015240, ECO:0000269|PubMed:26609676}.; FUNCTION: [Isoform 2]: Functions as a transcription repressor; isoform 2 has lower transcription repressor activity than isoform 1 and isoform 3. {ECO:0000269|PubMed:18070604}.; FUNCTION: [Isoform 3]: Functions as a transcription repressor; its activity is marginally lower than that of isoform 1. {ECO:0000269|PubMed:18070604}. |
| Q9HBI0 | PARVG | Y7 | ochoa | Gamma-parvin | Plays a role with ILK in promoting the cell adhesion and spreading of leukocytes. {ECO:0000269|PubMed:16517730}. |
| Q9HBI1 | PARVB | S7 | ochoa | Beta-parvin (Affixin) | Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. {ECO:0000269|PubMed:11402068, ECO:0000269|PubMed:15005707, ECO:0000269|PubMed:15159419, ECO:0000269|PubMed:15284246, ECO:0000269|PubMed:18325335}. |
| Q9HC35 | EML4 | S7 | ochoa | Echinoderm microtubule-associated protein-like 4 (EMAP-4) (Restrictedly overexpressed proliferation-associated protein) (Ropp 120) | Essential for the formation and stability of microtubules (MTs) (PubMed:16890222, PubMed:31409757). Required for the organization of the mitotic spindle and for the proper attachment of kinetochores to MTs (PubMed:25789526). Promotes the recruitment of NUDC to the mitotic spindle for mitotic progression (PubMed:25789526). {ECO:0000269|PubMed:16890222, ECO:0000269|PubMed:25789526, ECO:0000269|PubMed:31409757}. |
| Q9HCD5 | NCOA5 | S6 | ochoa | Nuclear receptor coactivator 5 (NCoA-5) (Coactivator independent of AF-2) (CIA) | Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2). {ECO:0000269|PubMed:15073177}. |
| Q9HCY8 | S100A14 | S6 | ochoa | Protein S100-A14 (S100 calcium-binding protein A14) (S114) | Modulates P53/TP53 protein levels, and thereby plays a role in the regulation of cell survival and apoptosis. Depending on the context, it can promote cell proliferation or apoptosis. Plays a role in the regulation of cell migration by modulating the levels of MMP2, a matrix protease that is under transcriptional control of P53/TP53. Does not bind calcium. {ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:22032898, ECO:0000269|PubMed:22451655}. |
| Q9NP98 | MYOZ1 | T6 | ochoa | Myozenin-1 (Calsarcin-2) (Filamin-, actinin- and telethonin-binding protein) (Protein FATZ) | Myozenins may serve as intracellular binding proteins involved in linking Z-disk proteins such as alpha-actinin, gamma-filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis. |
| Q9NQC3 | RTN4 | S7 | ochoa | Reticulon-4 (Foocen) (Neurite outgrowth inhibitor) (Nogo protein) (Neuroendocrine-specific protein) (NSP) (Neuroendocrine-specific protein C homolog) (RTN-x) (Reticulon-5) | Required to induce the formation and stabilization of endoplasmic reticulum (ER) tubules (PubMed:24262037, PubMed:25612671, PubMed:27619977). They regulate membrane morphogenesis in the ER by promoting tubular ER production (PubMed:24262037, PubMed:25612671, PubMed:27619977, PubMed:27786289). They influence nuclear envelope expansion, nuclear pore complex formation and proper localization of inner nuclear membrane proteins (PubMed:26906412). However each isoform have specific functions mainly depending on their tissue expression specificities (Probable). {ECO:0000269|PubMed:24262037, ECO:0000269|PubMed:25612671, ECO:0000269|PubMed:26906412, ECO:0000269|PubMed:27619977, ECO:0000269|PubMed:27786289, ECO:0000305}.; FUNCTION: [Isoform A]: Developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Regulates neurite fasciculation, branching and extension in the developing nervous system. Involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS (PubMed:10667797, PubMed:11201742). Regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex (By similarity). Acts as a negative regulator of central nervous system angiogenesis. Inhibits spreading, migration and sprouting of primary brain microvascular endothelial cells (MVECs). Also induces the retraction of MVECs lamellipodia and filopodia in a ROCK pathway-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q99P72, ECO:0000269|PubMed:10667797, ECO:0000269|PubMed:11201742, ECO:0000269|PubMed:19699797}.; FUNCTION: [Isoform B]: Mainly function in endothelial cells and vascular smooth muscle cells, is also involved in immune system regulation (Probable). Modulator of vascular remodeling, promotes the migration of endothelial cells but inhibits the migration of vascular smooth muscle cells. Regulates endothelial sphingolipid biosynthesis with direct effects on vascular function and blood pressure. Inhibits serine palmitoyltransferase, SPTLC1, the rate-limiting enzyme of the novo sphingolipid biosynthetic pathway, thereby controlling production of endothelial sphingosine-1-phosphate (S1P). Required to promote macrophage homing and functions such as cytokine/chemokine gene expression involved in angiogenesis, arteriogenesis and tissue repair. Mediates ICAM1 induced transendothelial migration of leukocytes such as monocytes and neutrophils and acute inflammation. Necessary for immune responses triggered by nucleic acid sensing TLRs, such as TLR9, is required for proper TLR9 location to endolysosomes. Also involved in immune response to LPS. Plays a role in liver regeneration through the modulation of hepatocytes proliferation (By similarity). Reduces the anti-apoptotic activity of Bcl-xl and Bcl-2. This is likely consecutive to their change in subcellular location, from the mitochondria to the endoplasmic reticulum, after binding and sequestration (PubMed:11126360). With isoform C, inhibits BACE1 activity and amyloid precursor protein processing (PubMed:16965550). {ECO:0000250|UniProtKB:Q99P72, ECO:0000269|PubMed:11126360, ECO:0000269|PubMed:16965550, ECO:0000305}.; FUNCTION: [Isoform C]: Regulates cardiomyocyte apoptosis upon hypoxic conditions (By similarity). With isoform B, inhibits BACE1 activity and amyloid precursor protein processing (PubMed:16965550). {ECO:0000250|UniProtKB:Q99P72, ECO:0000269|PubMed:16965550}. |
| Q9NQT5 | EXOSC3 | S6 | ochoa | Exosome complex component RRP40 (Exosome component 3) (Ribosomal RNA-processing protein 40) (p10) | Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC3 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC9 and EXOSC5. {ECO:0000269|PubMed:11782436, ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:19056938, ECO:0000269|PubMed:21255825}. |
| Q9NR28 | DIABLO | S6 | psp | Diablo IAP-binding mitochondrial protein (Diablo homolog, mitochondrial) (Direct IAP-binding protein with low pI) (Second mitochondria-derived activator of caspases) (SMAC) [Cleaved into: Diablo IAP-binding mitochondrial protein, cleaved form] | Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/BRUCE by inhibiting its binding to caspases (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). {ECO:0000269|PubMed:10929711, ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:36758104, ECO:0000269|PubMed:36758105, ECO:0000269|PubMed:36758106}.; FUNCTION: [Isoform 3]: Attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. {ECO:0000269|PubMed:14523016}.; FUNCTION: [Isoform 1]: Defective in the capacity to down-regulate the XIAP/BIRC4 abundance. {ECO:0000269|PubMed:14523016}. |
| Q9NR30 | DDX21 | S7 | ochoa | Nucleolar RNA helicase 2 (EC 3.6.4.13) (DEAD box protein 21) (Gu-alpha) (Nucleolar RNA helicase Gu) (Nucleolar RNA helicase II) (RH II/Gu) | RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (PubMed:25470060, PubMed:28790157). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (PubMed:25470060, PubMed:25477391). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (PubMed:25470060). Functions as a cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) (PubMed:9461305). Together with SIRT7, required to prevent R-loop-associated DNA damage and transcription-associated genomic instability: deacetylation by SIRT7 activates the helicase activity, thereby overcoming R-loop-mediated stalling of RNA polymerases (PubMed:28790157). Involved in rRNA processing (PubMed:14559904, PubMed:18180292). May bind to specific miRNA hairpins (PubMed:28431233). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1 (By similarity). {ECO:0000250|UniProtKB:Q9JIK5, ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:14559904, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:25477391, ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305}. |
| Q9NR56 | MBNL1 | T6 | ochoa | Muscleblind-like protein 1 (Triplet-expansion RNA-binding protein) | Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to expanded CUG repeat RNA, which folds into a hairpin structure containing GC base pairs and bulged, unpaired U residues. Together with RNA binding proteins RBPMS and RBFOX2, activates vascular smooth muscle cells alternative splicing events (PubMed:37548402). Regulates NCOR2 alternative splicing (By similarity). {ECO:0000250|UniProtKB:A0A8I6B1J2, ECO:0000269|PubMed:10970838, ECO:0000269|PubMed:15257297, ECO:0000269|PubMed:16946708, ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:19470458, ECO:0000269|PubMed:37548402}. |
| Q9NS39 | ADARB2 | S7 | ochoa | Double-stranded RNA-specific editase B2 (EC 3.5.-.-) (RNA-dependent adenosine deaminase 3) (RNA-editing deaminase 2) (RNA-editing enzyme 2) (dsRNA adenosine deaminase B2) | Lacks editing activity. It prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. Capable of binding to dsRNA but also to ssRNA. |
| Q9NS91 | RAD18 | S7 | ochoa | E3 ubiquitin-protein ligase RAD18 (EC 2.3.2.27) (Postreplication repair protein RAD18) (hHR18) (hRAD18) (RING finger protein 73) (RING-type E3 ubiquitin transferase RAD18) | E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity. {ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:21659603}. |
| Q9NSI8 | SAMSN1 | S7 | ochoa | SAM domain-containing protein SAMSN-1 (Hematopoietic adaptor containing SH3 and SAM domains 1) (Nash1) (SAM domain, SH3 domain and nuclear localization signals protein 1) (SH3-SAM adaptor protein) | Negative regulator of B-cell activation. Down-regulates cell proliferation (in vitro). Promotes RAC1-dependent membrane ruffle formation and reorganization of the actin cytoskeleton. Regulates cell spreading and cell polarization. Stimulates HDAC1 activity. Regulates LYN activity by modulating its tyrosine phosphorylation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15381729}. |
| Q9NUE0 | ZDHHC18 | Y6 | ochoa | Palmitoyltransferase ZDHHC18 (EC 2.3.1.225) (DHHC domain-containing cysteine-rich protein 18) (DHHC-18) (Zinc finger DHHC domain-containing protein 18) | Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates, such as CGAS, HRAS and LCK (PubMed:23034182, PubMed:27481942, PubMed:35438208). Acts as a negative regulator of the cGAS-STING pathway be mediating palmitoylation and inactivation of CGAS (PubMed:35438208). May also have a palmitoyltransferase activity toward the beta-2 adrenergic receptor/ADRB2 and therefore regulate G protein-coupled receptor signaling (PubMed:27481942). {ECO:0000269|PubMed:23034182, ECO:0000269|PubMed:27481942, ECO:0000269|PubMed:35438208}. |
| Q9NUP7 | TRMT13 | T6 | ochoa | tRNA:m(4)X modification enzyme TRM13 homolog (EC 2.1.1.225) (Coiled-coil domain-containing protein 76) | tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His). {ECO:0000250|UniProtKB:Q12383}. |
| Q9NUP7 | TRMT13 | S7 | ochoa | tRNA:m(4)X modification enzyme TRM13 homolog (EC 2.1.1.225) (Coiled-coil domain-containing protein 76) | tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His). {ECO:0000250|UniProtKB:Q12383}. |
| Q9NUU6 | OTULINL | S6 | ochoa | Inactive ubiquitin thioesterase OTULINL | Lacks deubiquitinase activity. {ECO:0000269|PubMed:31056421}. |
| Q9NVH1 | DNAJC11 | S6 | ochoa | DnaJ homolog subfamily C member 11 | [Isoform 1]: Required for mitochondrial inner membrane organization. Seems to function through its association with the MICOS complex and the mitochondrial outer membrane sorting assembly machinery (SAM) complex. {ECO:0000269|PubMed:25111180, ECO:0000305}. |
| Q9NVT9 | ARMC1 | S6 | ochoa | Armadillo repeat-containing protein 1 | In association with mitochondrial contact site and cristae organizing system (MICOS) complex components and mitochondrial outer membrane sorting assembly machinery (SAM) complex components may regulate mitochondrial dynamics playing a role in determining mitochondrial length, distribution and motility. {ECO:0000269|PubMed:31644573}. |
| Q9NVT9 | ARMC1 | T7 | ochoa | Armadillo repeat-containing protein 1 | In association with mitochondrial contact site and cristae organizing system (MICOS) complex components and mitochondrial outer membrane sorting assembly machinery (SAM) complex components may regulate mitochondrial dynamics playing a role in determining mitochondrial length, distribution and motility. {ECO:0000269|PubMed:31644573}. |
| Q9NW15 | ANO10 | S6 | ochoa | Anoctamin-10 (Transmembrane protein 16K) | Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1. {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}. |
| Q9NWV8 | BABAM1 | S7 | ochoa | BRISC and BRCA1-A complex member 1 (Mediator of RAP80 interactions and targeting subunit of 40 kDa) (New component of the BRCA1-A complex) | Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:24075985, PubMed:26195665). In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (PubMed:24075985). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). {ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749}. |
| Q9NWZ3 | IRAK4 | T6 | psp | Interleukin-1 receptor-associated kinase 4 (IRAK-4) (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-64) | Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways (PubMed:17878374). Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections. {ECO:0000269|PubMed:11960013, ECO:0000269|PubMed:12538665, ECO:0000269|PubMed:15084582, ECO:0000269|PubMed:17217339, ECO:0000269|PubMed:17337443, ECO:0000269|PubMed:17878374, ECO:0000269|PubMed:17997719, ECO:0000269|PubMed:20400509, ECO:0000269|PubMed:24316379}. |
| Q9NX76 | CMTM6 | Y7 | ochoa | CKLF-like MARVEL transmembrane domain-containing protein 6 (Chemokine-like factor superfamily member 6) | Master regulator of recycling and plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Associates with both constitutive and IFNG-induced PD-L1/CD274 at recycling endosomes, where it protects PD-L1/CD274 from being targeted for lysosomal degradation, likely by preventing its STUB1-mediated ubiquitination. May stabilize PD-L1/CD274 expression on antigen presenting cells and potentiates inhibitory signaling by PDCD1/CD279, its receptor on T-cells, ultimately triggering T-cell anergy. {ECO:0000269|PubMed:28813410, ECO:0000269|PubMed:28813417}. |
| Q9NY33 | DPP3 | Y6 | ochoa | Dipeptidyl peptidase 3 (EC 3.4.14.4) (Dipeptidyl aminopeptidase III) (Dipeptidyl arylamidase III) (Dipeptidyl peptidase III) (DPP III) (Enkephalinase B) | Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin (PubMed:1515063, PubMed:3233187). Also cleaves Arg-Arg-beta-naphthylamide (in vitro) (PubMed:11209758, PubMed:3233187, PubMed:9425109). {ECO:0000269|PubMed:11209758, ECO:0000269|PubMed:1515063, ECO:0000269|PubMed:3233187, ECO:0000269|PubMed:9425109}. |
| Q9NYF5 | FAM13B | S6 | ochoa | Protein FAM13B (GAP-like protein N61) | None |
| Q9NYZ1 | TVP23B | S6 | ochoa | Golgi apparatus membrane protein TVP23 homolog B | None |
| Q9NZ45 | CISD1 | S6 | ochoa | CDGSH iron-sulfur domain-containing protein 1 (Cysteine transaminase CISD1) (EC 2.6.1.3) (MitoNEET) | L-cysteine transaminase that catalyzes the reversible transfer of the amino group from L-cysteine to the alpha-keto acid 2-oxoglutarate to respectively form 2-oxo-3-sulfanylpropanoate and L-glutamate (PubMed:36194135). The catalytic cycle occurs in the presence of pyridoxal 5'-phosphate (PLP) cofactor that facilitates transamination by initially forming an internal aldimine with the epsilon-amino group of active site Lys-55 residue on the enzyme (PLP-enzyme aldimine), subsequently displaced by formation of an external aldimine with the substrate amino group (PLP-L-cysteine aldimine). The external aldimine is further deprotonated to form a carbanion intermediate, which in the presence of 2-oxoglutarate regenerates PLP yielding final products 2-oxo-3-sulfanylpropanoate and L-glutamate. The proton transfer in carbanion intermediate is suggested to be controlled by the active site lysine residue, whereas PLP stabilizes carbanion structure through electron delocalization, also known as the electron sink effect (PubMed:36194135). Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in iron-sulfur cluster shuttling and/or in redox reactions. Can transfer the [2Fe-2S] cluster to an apo-acceptor protein only when in the oxidation state, likely serving as a redox sensor that regulates mitochondrial iron-sulfur cluster assembly and iron trafficking upon oxidative stress (PubMed:17584744, PubMed:21788481, PubMed:23758282). {ECO:0000250, ECO:0000250|UniProtKB:Q91WS0, ECO:0000269|PubMed:17584744, ECO:0000269|PubMed:17766440, ECO:0000269|PubMed:21788481, ECO:0000269|PubMed:23758282, ECO:0000269|PubMed:36194135}. |
| Q9NZ45 | CISD1 | S7 | ochoa | CDGSH iron-sulfur domain-containing protein 1 (Cysteine transaminase CISD1) (EC 2.6.1.3) (MitoNEET) | L-cysteine transaminase that catalyzes the reversible transfer of the amino group from L-cysteine to the alpha-keto acid 2-oxoglutarate to respectively form 2-oxo-3-sulfanylpropanoate and L-glutamate (PubMed:36194135). The catalytic cycle occurs in the presence of pyridoxal 5'-phosphate (PLP) cofactor that facilitates transamination by initially forming an internal aldimine with the epsilon-amino group of active site Lys-55 residue on the enzyme (PLP-enzyme aldimine), subsequently displaced by formation of an external aldimine with the substrate amino group (PLP-L-cysteine aldimine). The external aldimine is further deprotonated to form a carbanion intermediate, which in the presence of 2-oxoglutarate regenerates PLP yielding final products 2-oxo-3-sulfanylpropanoate and L-glutamate. The proton transfer in carbanion intermediate is suggested to be controlled by the active site lysine residue, whereas PLP stabilizes carbanion structure through electron delocalization, also known as the electron sink effect (PubMed:36194135). Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in iron-sulfur cluster shuttling and/or in redox reactions. Can transfer the [2Fe-2S] cluster to an apo-acceptor protein only when in the oxidation state, likely serving as a redox sensor that regulates mitochondrial iron-sulfur cluster assembly and iron trafficking upon oxidative stress (PubMed:17584744, PubMed:21788481, PubMed:23758282). {ECO:0000250, ECO:0000250|UniProtKB:Q91WS0, ECO:0000269|PubMed:17584744, ECO:0000269|PubMed:17766440, ECO:0000269|PubMed:21788481, ECO:0000269|PubMed:23758282, ECO:0000269|PubMed:36194135}. |
| Q9NZC7 | WWOX | Y6 | ochoa | WW domain-containing oxidoreductase (EC 1.1.1.-) (Fragile site FRA16D oxidoreductase) (Short chain dehydrogenase/reductase family 41C member 1) | Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. Required for normal bone development (By similarity). May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. May also play a role in tumor necrosis factor (TNF)-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm. {ECO:0000250, ECO:0000269|PubMed:11719429, ECO:0000269|PubMed:15070730, ECO:0000269|PubMed:15548692, ECO:0000269|PubMed:16061658, ECO:0000269|PubMed:16219768, ECO:0000269|PubMed:19366691, ECO:0000269|PubMed:19465938}. |
| Q9NZN3 | EHD3 | T7 | ochoa | EH domain-containing protein 3 (PAST homolog 3) | ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis (PubMed:25686250). In vitro causes tubulation of endocytic membranes (PubMed:24019528). Binding to phosphatidic acid induces its membrane tubulation activity (By similarity). Plays a role in endocytic transport. Involved in early endosome to recycling endosome compartment (ERC), retrograde early endosome to Golgi, and endosome to plasma membrane (rapid recycling) protein transport. Involved in the regulation of Golgi maintenance and morphology (PubMed:16251358, PubMed:17233914, PubMed:19139087, PubMed:23781025). Involved in the recycling of internalized D1 dopamine receptor (PubMed:21791287). Plays a role in cardiac protein trafficking probably implicating ANK2 (PubMed:20489164). Involved in the ventricular membrane targeting of SLC8A1 and CACNA1C and probably the atrial membrane localization of CACNA1GG and CACNA1H implicated in the regulation of atrial myocyte excitability and cardiac conduction (By similarity). In conjunction with EHD4 may be involved in endocytic trafficking of KDR/VEGFR2 implicated in control of glomerular function (By similarity). Involved in the rapid recycling of integrin beta-3 implicated in cell adhesion maintenance (PubMed:23781025). Involved in the unidirectional retrograde dendritic transport of endocytosed BACE1 and in efficient sorting of BACE1 to axons implicating a function in neuronal APP processing (By similarity). Plays a role in the formation of the ciliary vesicle, an early step in cilium biogenesis; possibly sharing redundant functions with EHD1 (PubMed:25686250). {ECO:0000250|UniProtKB:Q9QXY6, ECO:0000269|PubMed:16251358, ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:19139087, ECO:0000269|PubMed:21791287, ECO:0000269|PubMed:23781025, ECO:0000269|PubMed:24019528, ECO:0000269|PubMed:25686250, ECO:0000305|PubMed:20489164}. |
| Q9NZS2 | KLRF1 | Y7 | psp | Killer cell lectin-like receptor subfamily F member 1 (Lectin-like receptor F1) (Activating coreceptor NKp80) (C-type lectin domain family 5 member C) | Functions as an activating receptor involved in immunosurveillance upon binding to various ligands displayed at the surface of myeloid cells. Upon interaction with CLEC2B ligand, stimulates NK-cell cytotoxicity and cytokine production leading to the cytolysis of malignant CLEC2B-expressing myeloid cells. Actviation of the common cytotoxicity pathway involves SRC and SYK kinases (PubMed:21149606). {ECO:0000269|PubMed:17057721, ECO:0000269|PubMed:21149606}. |
| Q9NZT1 | CALML5 | T6 | ochoa | Calmodulin-like protein 5 (Calmodulin-like skin protein) | Binds calcium. May be involved in terminal differentiation of keratinocytes. |
| Q9P0K8 | FOXJ2 | S7 | ochoa | Forkhead box protein J2 (Fork head homologous X) | [Isoform FOXJ2.L]: Transcriptional activator. Able to bind to two different type of DNA binding sites. More effective than isoform FOXJ2.S in transcriptional activation (PubMed:10777590, PubMed:10966786). Plays an important role in spermatogenesis, especially in spermatocyte meiosis (By similarity). {ECO:0000250|UniProtKB:Q9ES18, ECO:0000269|PubMed:10777590, ECO:0000269|PubMed:10966786}.; FUNCTION: [Isoform FOXJ2.S]: Transcriptional activator. {ECO:0000269|PubMed:10966786}. |
| Q9P0U4 | CXXC1 | S6 | ochoa | CXXC-type zinc finger protein 1 (CpG-binding protein) (PHD finger and CXXC domain-containing protein 1) | Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG. {ECO:0000269|PubMed:21407193}. |
| Q9P126 | CLEC1B | Y7 | psp | C-type lectin domain family 1 member B (C-type lectin-like receptor 2) (CLEC-2) | C-type lectin-like receptor that functions as a platelet receptor for the lymphatic endothelial marker, PDPN (PubMed:18215137). After ligand activation, signals via sequential activation of SRC and SYK tyrosine kinases leading to activation of PLCG2 (PubMed:18955485). {ECO:0000269|PubMed:18215137, ECO:0000269|PubMed:18955485}.; FUNCTION: (Microbial infection) Acts as a receptor for the platelet-aggregating snake venom protein rhodocytin. Rhodocytin binding leads to tyrosine phosphorylation and this promotes the binding of spleen tyrosine kinase (SYK) and initiation of downstream tyrosine phosphorylation events and activation of PLCG2 (PubMed:16174766, PubMed:18955485). {ECO:0000269|PubMed:18955485, ECO:0000305|PubMed:16174766}.; FUNCTION: (Microbial infection) Acts as an attachment factor for Human immunodeficiency virus type 1 (HIV-1) and facilitates its capture by platelets (PubMed:16940507). {ECO:0000305|PubMed:16940507}. |
| Q9P1Q0 | VPS54 | S6 | ochoa | Vacuolar protein sorting-associated protein 54 (Hepatocellular carcinoma protein 8) (Tumor antigen HOM-HCC-8) (Tumor antigen SLP-8p) | Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD (PubMed:18367545). Within the GARP complex, required to tether the complex to the TGN. Not involved in endocytic recycling (PubMed:25799061). {ECO:0000269|PubMed:18367545, ECO:0000269|PubMed:25799061}. |
| Q9P1Q0 | VPS54 | S7 | ochoa | Vacuolar protein sorting-associated protein 54 (Hepatocellular carcinoma protein 8) (Tumor antigen HOM-HCC-8) (Tumor antigen SLP-8p) | Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD (PubMed:18367545). Within the GARP complex, required to tether the complex to the TGN. Not involved in endocytic recycling (PubMed:25799061). {ECO:0000269|PubMed:18367545, ECO:0000269|PubMed:25799061}. |
| Q9UBI6 | GNG12 | S7 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12 | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. |
| Q9UBU9 | NXF1 | S7 | ochoa | Nuclear RNA export factor 1 (Tip-associated protein) (Tip-associating protein) (mRNA export factor TAP) | Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway) (PubMed:10924507). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex (PubMed:18364396, PubMed:19165146, PubMed:9660949). ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export (PubMed:18364396, PubMed:19165146, PubMed:9660949). Also involved in nuclear export of m6A-containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:28984244, ECO:0000269|PubMed:9660949}. |
| Q9UBY9 | HSPB7 | S7 | ochoa | Heat shock protein beta-7 (HspB7) (Cardiovascular heat shock protein) (cvHsp) | None |
| Q9UEY8 | ADD3 | S6 | ochoa | Gamma-adducin (Adducin-like protein 70) | Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Plays a role in actin filament capping (PubMed:23836506). Binds to calmodulin (Probable). Involved in myogenic reactivity of the renal afferent arteriole (Af-art), renal interlobular arteries and middle cerebral artery (MCA) to increased perfusion pressure. Involved in regulation of potassium channels in the vascular smooth muscle cells (VSMCs) of the Af-art and MCA ex vivo. Involved in regulation of glomerular capillary pressure, glomerular filtration rate (GFR) and glomerular nephrin expression in response to hypertension. Involved in renal blood flow (RBF) autoregulation. Plays a role in podocyte structure and function. Regulates globular monomer actin (G-actin) and filamentous polymer actin (F-actin) ratios in the primary podocytes affecting actin cytoskeleton organization. Regulates expression of synaptopodin, RhoA, Rac1 and CDC42 in the renal cortex and the primary podocytes. Regulates expression of nephrin in the glomeruli and in the primary podocytes, expression of nephrin and podocinin in the renal cortex, and expression of focal adhesion proteins integrin alpha-3 and integrin beta-1 in the glomeruli. Involved in cell migration and cell adhesion of podocytes, and in podocyte foot process effacement. Regulates expression of profibrotics markers MMP2, MMP9, TGF beta-1, tubular tight junction protein E-cadherin, and mesenchymal markers vimentin and alpha-SMA (By similarity). Promotes the growth of neurites (By similarity). {ECO:0000250|UniProtKB:Q62847, ECO:0000250|UniProtKB:Q9QYB5, ECO:0000269|PubMed:23836506, ECO:0000305}. |
| Q9UH92 | MLX | S7 | ochoa | Max-like protein X (Class D basic helix-loop-helix protein 13) (bHLHd13) (Max-like bHLHZip protein) (Protein BigMax) (Transcription factor-like protein 4) | Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MAD1, MAD4, MNT, WBSCR14 and MLXIP which recognizes the core sequence 5'-CACGTG-3'. The TCFL4-MAD1, TCFL4-MAD4, TCFL4-WBSCR14 complexes are transcriptional repressors. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation. {ECO:0000269|PubMed:10593926, ECO:0000269|PubMed:12446771, ECO:0000269|PubMed:16782875}. |
| Q9UHK0 | NUFIP1 | S6 | ochoa | FMR1-interacting protein NUFIP1 (Nuclear FMR1-interacting protein 1) (Nuclear FMRP-interacting protein 1) | Binds RNA. {ECO:0000269|PubMed:10556305}. |
| Q9UHY1 | NRBP1 | S6 | ochoa | Nuclear receptor-binding protein | Required for embryonic development (By similarity). Plays a role in intestinal epithelial cell fate and proliferation, thereby involved in the architectural development of the intestine potentially via the regulation of Wnt-responsive genes (By similarity). May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases (PubMed:11956649). Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication (PubMed:15084397). {ECO:0000250|UniProtKB:Q99J45, ECO:0000269|PubMed:11956649, ECO:0000269|PubMed:15084397}. |
| Q9UIU6 | SIX4 | T7 | ochoa | Homeobox protein SIX4 (Sine oculis homeobox homolog 4) | Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a DNA sequence on these target genes and is involved in processes like cell differentiation, cell migration and cell survival. Transactivates gene expression by binding a 5'-[CAT]A[CT][CT][CTG]GA[GAT]-3' motif present in the Trex site and a 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 site of the muscle-specific genes enhancer. Acts cooperatively with EYA proteins to transactivate their target genes through interaction and nuclear translocation of EYA protein. Acts synergistically with SIX1 to regulate target genes involved in formation of various organs, including muscle, kidney, gonad, ganglia, olfactory epithelium and cranial skeleton. Plays a role in several important steps of muscle development. Controls the genesis of hypaxial myogenic progenitors in the dermomyotome by transactivating PAX3 and the delamination and migration of the hypaxial precursors from the ventral lip to the limb buds through the transactivation of PAX3, MET and LBX1. Controls myoblast determination by transactivating MYF5, MYOD1 and MYF6. Controls somitic differentiation in myocyte through MYOG transactivation. Plays a role in synaptogenesis and sarcomere organization by participating in myofiber specialization during embryogenesis by activating fast muscle program in the primary myotome resulting in an up-regulation of fast muscle genes, including ATP2A1, MYL1 and TNNT3. Simultaneously, is also able to activate inhibitors of slow muscle genes, such as SOX6, HRASLS, and HDAC4, thereby restricting the activation of the slow muscle genes. During muscle regeneration, negatively regulates differentiation of muscle satellite cells through down-regulation of MYOG expression. During kidney development regulates the early stages of metanephros development and ureteric bud formation through regulation of GDNF, SALL1, PAX8 and PAX2 expression. Plays a role in gonad development by regulating both testis determination and size determination. In gonadal sex determination, transactivates ZFPM2 by binding a MEF3 consensus sequence, resulting in SRY up-regulation. In gonadal size determination, transactivates NR5A1 by binding a MEF3 consensus sequence resulting in gonadal precursor cell formation regulation. During olfactory development mediates the specification and patterning of olfactory placode through fibroblast growth factor and BMP4 signaling pathways and also regulates epithelial cell proliferation during placode formation. Promotes survival of sensory neurons during early trigeminal gangliogenesis. In the developing dorsal root ganglia, up-regulates SLC12A2 transcription. Regulates early thymus/parathyroid organogenesis through regulation of GCM2 and FOXN1 expression. Forms gustatory papillae during development of the tongue. Also plays a role during embryonic cranial skeleton morphogenesis. {ECO:0000250|UniProtKB:Q61321}. |
| Q9UKK9 | NUDT5 | T7 | ochoa | ADP-sugar pyrophosphatase (EC 3.6.1.13) (8-oxo-dGDP phosphatase) (EC 3.6.1.58) (Nuclear ATP-synthesis protein NUDIX5) (EC 2.7.7.96) (Nucleoside diphosphate-linked moiety X motif 5) (Nudix motif 5) (hNUDT5) (YSA1H) | Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate (PubMed:27257257). In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP (PubMed:10567213, PubMed:10722730, PubMed:17052728, PubMed:19699693, PubMed:21389046). Can also hydrolyze other nucleotide sugars with low activity (PubMed:19699693, PubMed:21389046). In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate. Nuclear ATP synthesis takes place when dephosphorylated at Thr-45 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). Does not play a role in U8 snoRNA decapping activity (By similarity). Binds U8 snoRNA (By similarity). {ECO:0000250|UniProtKB:Q9JKX6, ECO:0000269|PubMed:10567213, ECO:0000269|PubMed:10722730, ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:19699693, ECO:0000269|PubMed:21389046, ECO:0000269|PubMed:27257257}. |
| Q9UL45 | BLOC1S6 | S7 | ochoa | Biogenesis of lysosome-related organelles complex 1 subunit 6 (BLOC-1 subunit 6) (Pallid protein homolog) (Pallidin) (Syntaxin 13-interacting protein) | Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. May play a role in intracellular vesicle trafficking, particularly in the vesicle-docking and fusion process. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:21998198}. |
| Q9ULD2 | MTUS1 | S6 | ochoa | Microtubule-associated tumor suppressor 1 (AT2 receptor-binding protein) (Angiotensin-II type 2 receptor-interacting protein) (Mitochondrial tumor suppressor 1) | Cooperates with AGTR2 to inhibit ERK2 activation and cell proliferation. May be required for AGTR2 cell surface expression. Together with PTPN6, induces UBE2V2 expression upon angiotensin-II stimulation. Isoform 1 inhibits breast cancer cell proliferation, delays the progression of mitosis by prolonging metaphase and reduces tumor growth. {ECO:0000269|PubMed:12692079, ECO:0000269|PubMed:19794912}. |
| Q9ULD5 | ZNF777 | S6 | ochoa | Zinc finger protein 777 | May be involved in transcriptional repression (PubMed:31856708). Inhibits cell proliferation through CDKN1A/p21 induction by down-regulation of NIBAN1/FAM129A at low cell density (PubMed:25560148). {ECO:0000269|PubMed:25560148, ECO:0000269|PubMed:31856708}. |
| Q9ULD5 | ZNF777 | S7 | ochoa | Zinc finger protein 777 | May be involved in transcriptional repression (PubMed:31856708). Inhibits cell proliferation through CDKN1A/p21 induction by down-regulation of NIBAN1/FAM129A at low cell density (PubMed:25560148). {ECO:0000269|PubMed:25560148, ECO:0000269|PubMed:31856708}. |
| Q9ULS5 | TMCC3 | T6 | ochoa | Transmembrane and coiled-coil domain protein 3 | None |
| Q9UMX0 | UBQLN1 | S7 | ochoa | Ubiquilin-1 (Protein linking IAP with cytoskeleton 1) (PLIC-1) (hPLIC-1) | Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (PubMed:15147878). Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome (PubMed:18307982, PubMed:19822669). Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:19148225, PubMed:20529957, PubMed:23459205). Negatively regulates the TICAM1/TRIF-dependent toll-like receptor signaling pathway by decreasing the abundance of TICAM1 via the autophagic pathway (PubMed:21695056). Promotes the ubiquitination and lysosomal degradation of ORAI1, consequently down-regulating the ORAI1-mediated Ca2+ mobilization (PubMed:23307288). Suppresses the maturation and proteasomal degradation of amyloid beta A4 protein (A4) by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of A4 by sequestering it in the Golgi apparatus and preventing its transport to the cell surface for subsequent processing (By similarity). Ubiquitinates BCL2L10 and thereby stabilizes protein abundance (PubMed:22233804). {ECO:0000250|UniProtKB:Q9JJP9, ECO:0000269|PubMed:18307982, ECO:0000269|PubMed:19148225, ECO:0000269|PubMed:19822669, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:22233804, ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:23459205, ECO:0000303|PubMed:15147878}.; FUNCTION: [Isoform 1]: Plays a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress (PubMed:18953672). Plays a key role in the regulation of the levels of PSEN1 by targeting its accumulation to aggresomes which may then be removed from cells by autophagocytosis (PubMed:21143716). {ECO:0000269|PubMed:18953672, ECO:0000269|PubMed:21143716}.; FUNCTION: [Isoform 2]: Plays a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress. {ECO:0000269|PubMed:18953672}.; FUNCTION: [Isoform 3]: Plays a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress (PubMed:18953672). Plays a key role in the regulation of the levels of PSEN1 by targeting its accumulation to aggresomes which may then be removed from cells by autophagocytosis (PubMed:21143716). {ECO:0000269|PubMed:18953672, ECO:0000269|PubMed:21143716}. |
| Q9UMX3 | BOK | S7 | ochoa | Bcl-2-related ovarian killer protein (hBOK) (Bcl-2-like protein 9) (Bcl2-L-9) | [Isoform 1]: Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:15102863, PubMed:20673843, PubMed:27076518). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner (PubMed:15102863, PubMed:27076518). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (By similarity). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD-proteasome degradation system, resulting in cytochrome c release (PubMed:27076518). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner (PubMed:15102863). Plays a role in granulosa cell apoptosis by CASP3 activation (PubMed:20673843). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (By similarity). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression (PubMed:19942931). May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (PubMed:24113155). {ECO:0000250|UniProtKB:O35425, ECO:0000269|PubMed:15102863, ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:20673843, ECO:0000269|PubMed:24113155, ECO:0000269|PubMed:27076518}.; FUNCTION: [Isoform 2]: Pro-apoptotic molecule exerting its function through the mitochondrial pathway. {ECO:0000269|PubMed:15775999}. |
| Q9UN30 | SCML1 | S7 | ochoa | Sex comb on midleg-like protein 1 | Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. May be involved in spermatogenesis during sexual maturation (By similarity). {ECO:0000250}. |
| Q9UN86 | G3BP2 | S7 | ochoa | Ras GTPase-activating protein-binding protein 2 (G3BP-2) (GAP SH3 domain-binding protein 2) | Scaffold protein that plays an essential role in cytoplasmic stress granule formation which acts as a platform for antiviral signaling (PubMed:23279204, PubMed:32302570, PubMed:32302571, PubMed:32302572). Plays an essential role in stress granule formation (PubMed:27022092, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:35977029). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed:32302570, PubMed:32302571, PubMed:32302572). Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding: functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (By similarity). {ECO:0000250|UniProtKB:Q13283, ECO:0000269|PubMed:23279204, ECO:0000269|PubMed:27022092, ECO:0000269|PubMed:32302570, ECO:0000269|PubMed:32302571, ECO:0000269|PubMed:32302572, ECO:0000269|PubMed:35977029}. |
| Q9UNL2 | SSR3 | S6 | ochoa | Translocon-associated protein subunit gamma (TRAP-gamma) (Signal sequence receptor subunit gamma) (SSR-gamma) | TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. |
| Q9UNL2 | SSR3 | S7 | ochoa | Translocon-associated protein subunit gamma (TRAP-gamma) (Signal sequence receptor subunit gamma) (SSR-gamma) | TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. |
| Q9UPW6 | SATB2 | S7 | ochoa | DNA-binding protein SATB2 (Special AT-rich sequence-binding protein 2) | Binds to DNA, at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcription factor controlling nuclear gene expression, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Required for the initiation of the upper-layer neurons (UL1) specific genetic program and for the inactivation of deep-layer neurons (DL) and UL2 specific genes, probably by modulating BCL11B expression. Repressor of Ctip2 and regulatory determinant of corticocortical connections in the developing cerebral cortex. May play an important role in palate formation. Acts as a molecular node in a transcriptional network regulating skeletal development and osteoblast differentiation. {ECO:0000269|PubMed:14701874}. |
| Q9Y281 | CFL2 | T6 | ochoa | Cofilin-2 (Cofilin, muscle isoform) | Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3 (PubMed:19752190). It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere (By similarity). {ECO:0000250|UniProtKB:P45591, ECO:0000269|PubMed:19752190}. |
| Q9Y284 | WDR83OS | S7 | ochoa | PAT complex subunit Asterix (Protein associated with the ER translocon of 10kDa) (PAT-10) (PAT10) (WD repeat domain 83 opposite strand) (WDR83 opposite strand) | Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (PubMed:12475939, PubMed:32814900, PubMed:36261522). The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions (PubMed:32814900, PubMed:36261522). Within the MPT complex, the PAT subcomplex sequesters any highly polar regions in the transmembrane domains away from the non-polar membrane environment until they can be buried in the interior of the fully assembled protein (By similarity). Within the PAT subcomplex, WDR83OS/Asterix binds to and redirects the substrate to a location behind the SEC61 complex (By similarity). {ECO:0000250|UniProtKB:A0A8I3NQW8, ECO:0000269|PubMed:12475939, ECO:0000269|PubMed:32814900, ECO:0000269|PubMed:36261522}. |
| Q9Y2I7 | PIKFYVE | T7 | ochoa | 1-phosphatidylinositol 3-phosphate 5-kinase (Phosphatidylinositol 3-phosphate 5-kinase) (EC 2.7.1.150) (FYVE finger-containing phosphoinositide kinase) (PIKfyve) (Phosphatidylinositol 3-phosphate 5-kinase type III) (PIPkin-III) (Type III PIP kinase) (Serine-protein kinase PIKFYVE) (EC 2.7.11.1) | Dual specificity kinase implicated in myriad essential cellular processes such as maintenance of endomembrane homeostasis, and endocytic-vacuolar pathway, lysosomal trafficking, nuclear transport, stress- or hormone-induced signaling and cell cycle progression (PubMed:23086417). The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Sole enzyme to catalyze the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form (PtdIns(3,5)P2) (PubMed:17556371). Also catalyzes the phosphorylation of phosphatidylinositol on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 5-phosphate (PtdIns(5)P) (PubMed:22621786). Has serine-protein kinase activity and is able to autophosphorylate and transphosphorylate. Autophosphorylation inhibits its own phosphatidylinositol 3-phosphate 5-kinase activity, stimulates FIG4 lipid phosphatase activity and down-regulates lipid product formation (PubMed:33098764). Involved in key endosome operations such as fission and fusion in the course of endosomal cargo transport (PubMed:22621786). Required for the maturation of early into late endosomes, phagosomes and lysosomes (PubMed:30612035). Regulates vacuole maturation and nutrient recovery following engulfment of macromolecules, initiates the redistribution of accumulated lysosomal contents back into the endosome network (PubMed:27623384). Critical regulator of the morphology, degradative activity, and protein turnover of the endolysosomal system in macrophages and platelets (By similarity). In neutrophils, critical to perform chemotaxis, generate ROS, and undertake phagosome fusion with lysosomes (PubMed:28779020). Plays a key role in the processing and presentation of antigens by major histocompatibility complex class II (MHC class II) mediated by CTSS (PubMed:30612035). Regulates melanosome biogenesis by controlling the delivery of proteins from the endosomal compartment to the melanosome (PubMed:29584722). Essential for systemic glucose homeostasis, mediates insulin-induced signals for endosome/actin remodeling in the course of GLUT4 translocation/glucose uptake activation (By similarity). Supports microtubule-based endosome-to-trans-Golgi network cargo transport, through association with SPAG9 and RABEPK (By similarity). Mediates EGFR trafficking to the nucleus (PubMed:17909029). {ECO:0000250|UniProtKB:Q9Z1T6, ECO:0000269|PubMed:17556371, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:22621786, ECO:0000269|PubMed:27623384, ECO:0000269|PubMed:28779020, ECO:0000269|PubMed:29584722, ECO:0000269|PubMed:30612035, ECO:0000269|PubMed:33098764, ECO:0000303|PubMed:23086417}.; FUNCTION: (Microbial infection) Required for cell entry of coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus EMC (HCoV-EMC) by endocytosis. {ECO:0000269|PubMed:32221306}. |
| Q9Y2J2 | EPB41L3 | S7 | ochoa | Band 4.1-like protein 3 (4.1B) (Differentially expressed in adenocarcinoma of the lung protein 1) (DAL-1) (Erythrocyte membrane protein band 4.1-like 3) [Cleaved into: Band 4.1-like protein 3, N-terminally processed] | Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N-methyltransferases, including PRMT3 and PRMT5. {ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15737618, ECO:0000269|PubMed:16420693, ECO:0000269|PubMed:9892180}. |
| Q9Y2U8 | LEMD3 | S7 | ochoa | Inner nuclear membrane protein Man1 (LEM domain-containing protein 3) | Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest. {ECO:0000269|PubMed:15601644, ECO:0000269|PubMed:15647271}. |
| Q9Y365 | STARD10 | S7 | ochoa | START domain-containing protein 10 (StARD10) (Antigen NY-CO-28) (PCTP-like protein) (PCTP-L) (Serologically defined colon cancer antigen 28) (StAR-related lipid transfer protein 10) | May play metabolic roles in sperm maturation or fertilization (By similarity). Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes. {ECO:0000250, ECO:0000269|PubMed:15911624}. |
| Q9Y3C5 | RNF11 | S7 | ochoa | RING finger protein 11 | Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome. {ECO:0000269|PubMed:14755250}. |
| Q9Y3Z3 | SAMHD1 | S6 | ochoa | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Dendritic cell-derived IFNG-induced protein) (DCIP) (Monocyte protein 5) (MOP-5) (SAM domain and HD domain-containing protein 1) (hSAMHD1) | Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks (PubMed:19525956, PubMed:21613998, PubMed:21720370, PubMed:22056990, PubMed:23601106, PubMed:23602554, PubMed:24336198, PubMed:26294762, PubMed:26431200, PubMed:28229507, PubMed:28834754, PubMed:29670289). Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses, such as HIV-1: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells (PubMed:19525956, PubMed:21613998, PubMed:21720370, PubMed:22056990, PubMed:23364794, PubMed:23601106, PubMed:23602554, PubMed:24336198, PubMed:25038827, PubMed:26101257, PubMed:26294762, PubMed:26431200, PubMed:28229507). Likewise, suppresses LINE-1 retrotransposon activity (PubMed:24035396, PubMed:24217394, PubMed:29610582). Not able to restrict infection by HIV-2 virus; because restriction activity is counteracted by HIV-2 viral protein Vpx (PubMed:21613998, PubMed:21720370). In addition to virus restriction, dNTPase activity acts as a regulator of DNA precursor pools by regulating dNTP pools (PubMed:23858451). Phosphorylation at Thr-592 acts as a switch to control dNTPase-dependent and -independent functions: it inhibits dNTPase activity and ability to restrict infection by viruses, while it promotes DNA end resection at stalled replication forks (PubMed:23601106, PubMed:23602554, PubMed:29610582, PubMed:29670289). Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of MRE11, activating the ATR-CHK1 pathway and allowing the forks to restart replication (PubMed:29670289). Its ability to promote degradation of nascent DNA at stalled replication forks is required to prevent induction of type I interferons, thereby preventing chronic inflammation (PubMed:27477283, PubMed:29670289). Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity (PubMed:29670289). Enhances immunoglobulin hypermutation in B-lymphocytes by promoting transversion mutation (By similarity). {ECO:0000250|UniProtKB:Q60710, ECO:0000269|PubMed:19525956, ECO:0000269|PubMed:21613998, ECO:0000269|PubMed:21720370, ECO:0000269|PubMed:22056990, ECO:0000269|PubMed:23364794, ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:23602554, ECO:0000269|PubMed:23858451, ECO:0000269|PubMed:24035396, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:24336198, ECO:0000269|PubMed:25038827, ECO:0000269|PubMed:26101257, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200, ECO:0000269|PubMed:27477283, ECO:0000269|PubMed:28229507, ECO:0000269|PubMed:28834754, ECO:0000269|PubMed:29610582, ECO:0000269|PubMed:29670289}. |
| Q9Y4P1 | ATG4B | T7 | ochoa | Cysteine protease ATG4B (EC 3.4.22.-) (AUT-like 1 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 1) (Autophagin-1) (Autophagy-related protein 4 homolog B) (HsAPG4B) (hAPG4B) | Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:22302004, PubMed:26378241, PubMed:27527864, PubMed:28633005, PubMed:28821708, PubMed:29232556, PubMed:30076329, PubMed:30443548, PubMed:30661429). Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy (PubMed:33773106, PubMed:33909989). The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:20818167, PubMed:21177865, PubMed:22302004, PubMed:27527864, PubMed:28287329, PubMed:28633005, PubMed:29458288, PubMed:30661429). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:22302004). Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3 (PubMed:31315929, PubMed:33773106). In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed:15187094, PubMed:19322194, PubMed:28633005, PubMed:29458288, PubMed:32686895, PubMed:33909989). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed:15187094, PubMed:19322194, PubMed:29458288, PubMed:32686895, PubMed:33909989). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989). Compared to other members of the family (ATG4A, ATG4C or ATG4C), constitutes the major protein for proteolytic activation of ATG8 proteins, while it displays weaker delipidation activity than other ATG4 paralogs (PubMed:29458288, PubMed:30661429). Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (PubMed:33773106). {ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:17347651, ECO:0000269|PubMed:19322194, ECO:0000269|PubMed:20818167, ECO:0000269|PubMed:21177865, ECO:0000269|PubMed:22302004, ECO:0000269|PubMed:26378241, ECO:0000269|PubMed:27527864, ECO:0000269|PubMed:28287329, ECO:0000269|PubMed:28633005, ECO:0000269|PubMed:28821708, ECO:0000269|PubMed:29232556, ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:30076329, ECO:0000269|PubMed:30443548, ECO:0000269|PubMed:30661429, ECO:0000269|PubMed:31315929, ECO:0000269|PubMed:32686895, ECO:0000269|PubMed:33773106, ECO:0000269|PubMed:33909989}. |
| Q9Y534 | CSDC2 | T6 | ochoa | Cold shock domain-containing protein C2 (RNA-binding protein PIPPin) | RNA-binding factor which binds specifically to the very 3'-UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain (By similarity). {ECO:0000250}. |
| Q9Y534 | CSDC2 | S7 | ochoa | Cold shock domain-containing protein C2 (RNA-binding protein PIPPin) | RNA-binding factor which binds specifically to the very 3'-UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain (By similarity). {ECO:0000250}. |
| Q9Y576 | ASB1 | S6 | ochoa | Ankyrin repeat and SOCS box protein 1 (ASB-1) | Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:16325183). Mediates Notch-induced ubiquitination and degradation of TCF3/E2A and JAK2 (PubMed:21119685). Functions as a tumor suppressor by enhancing CHCHD3 'Lys-48'-linked ubiquitination, leading to inhibition of the CHCHD3/ROS signaling pathway (PubMed:39113857). Suppresses TAB2-linked 'Lys-48' polyubiquitination and consequently facilitates the initiation of NF-kappa-B and MAPK signaling cascades (PubMed:33431678). May play a role in testis development (By similarity). {ECO:0000250|UniProtKB:Q9WV74, ECO:0000269|PubMed:16325183, ECO:0000269|PubMed:21119685, ECO:0000269|PubMed:33431678, ECO:0000269|PubMed:39113857}. |
| Q9Y5L4 | TIMM13 | S7 | ochoa | Mitochondrial import inner membrane translocase subunit Tim13 | Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}. |
| Q9Y5M8 | SRPRB | S6 | ochoa | Signal recognition particle receptor subunit beta (SR-beta) (Protein APMCF1) | Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity). {ECO:0000250|UniProtKB:P47758}. |
| Q9Y5S1 | TRPV2 | S6 | ochoa | Transient receptor potential cation channel subfamily V member 2 (TrpV2) (Osm-9-like TRP channel 2) (OTRPC2) (Vanilloid receptor-like protein 1) (VRL-1) | Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF1, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH. {ECO:0000269|PubMed:10201375}. |
| Q9Y5S1 | TRPV2 | S7 | ochoa | Transient receptor potential cation channel subfamily V member 2 (TrpV2) (Osm-9-like TRP channel 2) (OTRPC2) (Vanilloid receptor-like protein 1) (VRL-1) | Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF1, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH. {ECO:0000269|PubMed:10201375}. |
| S4R325 | URGCP-MRPS24 | S7 | ochoa | URGCP-MRPS24 readthrough | None |
| S4R3Y5 | MTRNR2L11 | S7 | ochoa | Humanin-like 11 (HN11) (MT-RNR2-like protein 11) | Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}. |
| U3KQ54 | PMF1-BGLAP | S6 | ochoa | HCG2044777 (PMF1-BGLAP readthrough) | None |
| P25789 | PSMA4 | S7 | Sugiyama | Proteasome subunit alpha type-4 (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L) (Proteasome subunit alpha-3) (alpha-3) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
| P62942 | FKBP1A | T7 | Sugiyama | Peptidyl-prolyl cis-trans isomerase FKBP1A (PPIase FKBP1A) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FKBP-12) (Calstabin-1) (FK506-binding protein 1A) (FKBP-1A) (Immunophilin FKBP12) (Rotamase) | Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. {ECO:0000269|PubMed:16720724, ECO:0000269|PubMed:1696686, ECO:0000269|PubMed:1701173, ECO:0000269|PubMed:9233797}. |
| P56537 | EIF6 | S6 | Sugiyama | Eukaryotic translation initiation factor 6 (eIF-6) (B(2)GCN homolog) (B4 integrin interactor) (CAB) (p27(BBP)) | Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm (PubMed:10085284, PubMed:14654845, PubMed:21536732, PubMed:32669547). Behaves as a stimulatory translation initiation factor downstream insulin/growth factors. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by a RACK1 (RACK1)-dependent protein kinase C activity (PubMed:10085284, PubMed:14654845, PubMed:21536732). In tissues responsive to insulin, controls fatty acid synthesis and glycolysis by exerting translational control of adipogenic transcription factors such as CEBPB, CEBPD and ATF4 that have G/C rich or uORF in their 5'UTR. Required for ROS-dependent megakaryocyte maturation and platelets formation, controls the expression of mitochondrial respiratory chain genes involved in reactive oxygen species (ROS) synthesis (By similarity). Involved in miRNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC (PubMed:17507929). Modulates cell cycle progression and global translation of pre-B cells, its activation seems to be rate-limiting in tumorigenesis and tumor growth (By similarity). {ECO:0000255|HAMAP-Rule:MF_03132, ECO:0000269|PubMed:10085284, ECO:0000269|PubMed:14654845, ECO:0000269|PubMed:17507929, ECO:0000269|PubMed:21536732, ECO:0000269|PubMed:32669547}. |
| P25685 | DNAJB1 | Y6 | Sugiyama | DnaJ homolog subfamily B member 1 (DnaJ protein homolog 1) (Heat shock 40 kDa protein 1) (HSP40) (Heat shock protein 40) (Human DnaJ protein 1) (hDj-1) | Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877). {ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:9499401}. |
| P25786 | PSMA1 | Y6 | Sugiyama | Proteasome subunit alpha type-1 (30 kDa prosomal protein) (PROS-30) (Macropain subunit C2) (Multicatalytic endopeptidase complex subunit C2) (Proteasome component C2) (Proteasome nu chain) (Proteasome subunit alpha-6) (alpha-6) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
| A0A2R8Y4L2 | HNRNPA1L3 | S6 | Sugiyama | Heterogeneous nuclear ribonucleoprotein A1-like 3 (Heterogeneous nuclear ribonucleoprotein A1 pseudogene 48) | None |
| P61024 | CKS1B | Y7 | Sugiyama | Cyclin-dependent kinases regulatory subunit 1 (CKS-1) | Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. |
| P61313 | RPL15 | Y6 | Sugiyama | Large ribosomal subunit protein eL15 (60S ribosomal protein L15) | 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}. |
| P28066 | PSMA5 | S6 | Sugiyama | Proteasome subunit alpha type-5 (Macropain zeta chain) (Multicatalytic endopeptidase complex zeta chain) (Proteasome subunit alpha-5) (alpha-5) (Proteasome zeta chain) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
| Q9UDY4 | DNAJB4 | Y6 | Sugiyama | DnaJ homolog subfamily B member 4 (Heat shock 40 kDa protein 1 homolog) (HSP40 homolog) (Heat shock protein 40 homolog) (Human liver DnaJ-like protein) | Probable chaperone. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877). {ECO:0000269|PubMed:24318877}. |
| P62906 | RPL10A | S6 | Sugiyama | Large ribosomal subunit protein uL1 (60S ribosomal protein L10a) (CSA-19) (Neural precursor cell expressed developmentally down-regulated protein 6) (NEDD-6) | Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}. |
| P68431 | H3C1 | T7 | EPSD | Histone H3.1 (Histone H3/a) (Histone H3/b) (Histone H3/c) (Histone H3/d) (Histone H3/f) (Histone H3/h) (Histone H3/i) (Histone H3/j) (Histone H3/k) (Histone H3/l) | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. |
| Q5VWX1 | KHDRBS2 | Y6 | Sugiyama | KH domain-containing, RNA-binding, signal transduction-associated protein 2 (Sam68-like mammalian protein 1) (SLM-1) (hSLM-1) | RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds both poly(A) and poly(U) homopolymers. Phosphorylation by PTK6 inhibits its RNA-binding ability (By similarity). Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer. Can regulate alternative splicing of NRXN1 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. Regulates cell-type specific alternative splicing of NRXN1 at AS4 and acts synergystically with SAM68 in exon skipping. In contrast acts antagonistically with SAM68 in NRXN3 exon skipping at AS4. Its phosphorylation by FYN inhibits its ability to regulate splice site selection. May function as an adapter protein for Src kinases during mitosis. {ECO:0000250|UniProtKB:Q920F3, ECO:0000250|UniProtKB:Q9WU01}. |
| Q9BV57 | ADI1 | Y6 | Sugiyama | Acireductone dioxygenase (Acireductone dioxygenase (Fe(2+)-requiring)) (ARD') (Fe-ARD) (EC 1.13.11.54) (Acireductone dioxygenase (Ni(2+)-requiring)) (ARD) (Ni-ARD) (EC 1.13.11.53) (Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1) (MTCBP-1) (Submergence-induced protein-like factor) (Sip-L) | Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site (By similarity). Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway (PubMed:15938715). Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway (By similarity). Also down-regulates cell migration mediated by MMP14 (PubMed:14718544). Necessary for hepatitis C virus replication in an otherwise non-permissive cell line (PubMed:11602742). {ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|PubMed:11602742, ECO:0000269|PubMed:14718544, ECO:0000269|PubMed:15938715}. |
| P31689 | DNAJA1 | Y7 | Sugiyama | DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (HSDJ) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2) (Human DnaJ protein 2) (hDj-2) | Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as a co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202). {ECO:0000269|PubMed:10816573, ECO:0000269|PubMed:14752510, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24512202, ECO:0000269|PubMed:9192730}. |
| Q15369 | ELOC | T7 | Sugiyama | Elongin-C (EloC) (Elongin 15 kDa subunit) (RNA polymerase II transcription factor SIII subunit C) (SIII p15) (Transcription elongation factor B polypeptide 1) | SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (PubMed:7821821). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity). {ECO:0000250|UniProtKB:P83940, ECO:0000269|PubMed:7821821}.; FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694, PubMed:21199876, PubMed:26138980, PubMed:29775578, PubMed:29779948, PubMed:30166453, PubMed:33268465, PubMed:38326650, PubMed:35512830). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694). Component the von Hippel-Lindau ubiquitination complex CBC(VHL) (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:26138980, PubMed:29775578, PubMed:29779948, PubMed:36805027, PubMed:38177675). The ECS(ASB9) complex mediates ubiquitination and degradation of CKB (PubMed:33268465). As part of a multisubunit ubiquitin ligase complex, polyubiquitinates monoubiquitinated POLR2A (PubMed:19920177). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity). As part of the ECS(RAB40C) complex, mediates ANKRD28 ubiquitination and degradation, thereby inhibiting protein phosphatase 6 (PP6) complex activity and focal adhesion assembly during cell migration (PubMed:35512830). {ECO:0000250|UniProtKB:P83940, ECO:0000269|PubMed:10205047, ECO:0000269|PubMed:12004076, ECO:0000269|PubMed:12050673, ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:19920177, ECO:0000269|PubMed:21199876, ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30166453, ECO:0000269|PubMed:33268465, ECO:0000269|PubMed:35512830, ECO:0000269|PubMed:36805027, ECO:0000269|PubMed:38177675, ECO:0000269|PubMed:38326650}.; FUNCTION: (Microbial infection) Following infection by HIV-1 virus, component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, which catalyzes ubiquitination and degradation of APOBEC3F and APOBEC3G (PubMed:18562529, PubMed:20532212, PubMed:22190037, PubMed:24225024, PubMed:24402281, PubMed:36754086). The complex can also ubiquitinate APOBEC3H to some extent (PubMed:37640699). {ECO:0000269|PubMed:18562529, ECO:0000269|PubMed:20532212, ECO:0000269|PubMed:22190037, ECO:0000269|PubMed:24225024, ECO:0000269|PubMed:24402281, ECO:0000269|PubMed:36754086, ECO:0000269|PubMed:37640699}. |
| P31689 | DNAJA1 | T6 | Sugiyama | DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (HSDJ) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2) (Human DnaJ protein 2) (hDj-2) | Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as a co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202). {ECO:0000269|PubMed:10816573, ECO:0000269|PubMed:14752510, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24512202, ECO:0000269|PubMed:9192730}. |
| P14410 | SI | S7 | ELM|iPTMNet|EPSD | Sucrase-isomaltase, intestinal [Cleaved into: Sucrase (EC 3.2.1.48); Isomaltase (EC 3.2.1.10)] | Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides. {ECO:0000269|PubMed:20356844}. |
| O60829 | PAGE4 | S7 | EPSD|PSP | P antigen family member 4 (PAGE-4) (G antigen family C member 1) (PAGE-1) | Intrinsically disordered protein that potentiates the transcriptional activator activity of JUN (PubMed:24263171, PubMed:28289210). Protects cells from stress-induced apoptosis by inhibiting reactive oxygen species (ROS) production and via regulation of the MAPK signaling pathway (PubMed:21357425, PubMed:25374899, PubMed:30658679). {ECO:0000269|PubMed:21357425, ECO:0000269|PubMed:24263171, ECO:0000269|PubMed:25374899, ECO:0000269|PubMed:28289210, ECO:0000269|PubMed:30658679}. |
| A1L429 | GAGE12B; | S7 | Sugiyama | G antigen 12B/C/D/E (GAGE-12B) (GAGE-12C) (GAGE-12D) (GAGE-12E) | None |
| A6NDE8 | GAGE12H | S7 | Sugiyama | G antigen 12H (GAGE-12H) | None |
| A6NER3 | GAGE12J | S7 | Sugiyama | G antigen 12J (GAGE-12J) | None |
| O76087 | GAGE7 | S7 | Sugiyama | G antigen 7 (GAGE-7) (AL4) (Cancer/testis antigen 4.7) (CT4.7) (GAGE-12I) (GAGE-7B) (GAGE-8) | None |
| P0CL80 | GAGE12F | S7 | Sugiyama | G antigen 12F (GAGE-12F) | None |
| P0DSO3 | GAGE4 | S7 | Sugiyama | G antigen 4 (Cancer/testis antigen 4.4) (CT4.4) | Antigen, recognized on melanoma by autologous cytolytic T-lymphocytes. {ECO:0000269|PubMed:7544395}. |
| Q13069 | GAGE5 | S7 | Sugiyama | G antigen 5 (GAGE-5) (Cancer/testis antigen 4.5) (CT4.5) | None |
| Q13070 | GAGE6 | S7 | Sugiyama | G antigen 6 (GAGE-6) (Cancer/testis antigen 4.6) (CT4.6) | None |
| P52565 | ARHGDIA | T7 | SIGNOR | Rho GDP-dissociation inhibitor 1 (Rho GDI 1) (Rho-GDI alpha) | Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. {ECO:0000269|PubMed:20400958, ECO:0000269|PubMed:23434736}. |
| P37108 | SRP14 | S6 | Sugiyama | Signal recognition particle 14 kDa protein (SRP14) (18 kDa Alu RNA-binding protein) | Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:11089964). SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP (PubMed:11089964). The complex of SRP9 and SRP14 is required for SRP RNA binding (PubMed:11089964). {ECO:0000269|PubMed:11089964}. |
| Q96SI9 | STRBP | S6 | Sugiyama | Spermatid perinuclear RNA-binding protein | Involved in spermatogenesis and sperm function. Plays a role in regulation of cell growth. Binds to double-stranded DNA and RNA. Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA. Binds also to single-stranded poly(G) RNA. Binds non-specifically to the mRNA PRM1 3'-UTR and adenovirus VA RNA (By similarity). {ECO:0000250}. |
| Q8IX01 | SUGP2 | T7 | PSP | SURP and G-patch domain-containing protein 2 (Arginine/serine-rich-splicing factor 14) (Splicing factor, arginine/serine-rich 14) | May play a role in mRNA splicing. {ECO:0000305}. |
| O75874 | IDH1 | S6 | Sugiyama | Isocitrate dehydrogenase [NADP] cytoplasmic (IDH) (IDH1) (EC 1.1.1.42) (Cytosolic NADP-isocitrate dehydrogenase) (IDPc) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) | Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase (PubMed:10521434, PubMed:19935646). Plays a critical role in the generation of NADPH, an important cofactor in many biosynthesis pathways (PubMed:10521434). May act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency (By similarity). {ECO:0000250|UniProtKB:Q9XSG3, ECO:0000269|PubMed:10521434, ECO:0000269|PubMed:19935646, ECO:0000303|PubMed:10521434}. |
| P05787 | KRT8 | T6 | EPSD|PSP | Keratin, type II cytoskeletal 8 (Cytokeratin-8) (CK-8) (Keratin-8) (K8) (Type-II keratin Kb8) | Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}. |
| O14829 | PPEF1 | S6 | Sugiyama | Serine/threonine-protein phosphatase with EF-hands 1 (PPEF-1) (EC 3.1.3.16) (Protein phosphatase with EF calcium-binding domain) (PPEF) (Serine/threonine-protein phosphatase 7) (PP7) | May have a role in the recovery or adaptation response of photoreceptors. May have a role in development. |
Download
| reactome_id | name | p | -log10_p |
|---|---|---|---|
| R-HSA-68867 | Assembly of the pre-replicative complex | 5.213641e-11 | 10.283 |
| R-HSA-69002 | DNA Replication Pre-Initiation | 1.106709e-09 | 8.956 |
| R-HSA-69620 | Cell Cycle Checkpoints | 8.905194e-10 | 9.050 |
| R-HSA-69481 | G2/M Checkpoints | 2.060187e-08 | 7.686 |
| R-HSA-9645723 | Diseases of programmed cell death | 1.000189e-07 | 7.000 |
| R-HSA-69306 | DNA Replication | 1.393369e-07 | 6.856 |
| R-HSA-2559583 | Cellular Senescence | 1.656423e-07 | 6.781 |
| R-HSA-8953897 | Cellular responses to stimuli | 2.492554e-07 | 6.603 |
| R-HSA-2262752 | Cellular responses to stress | 3.255977e-07 | 6.487 |
| R-HSA-2559580 | Oxidative Stress Induced Senescence | 8.811855e-07 | 6.055 |
| R-HSA-8939236 | RUNX1 regulates transcription of genes involved in differentiation of HSCs | 1.167071e-06 | 5.933 |
| R-HSA-68616 | Assembly of the ORC complex at the origin of replication | 4.509731e-06 | 5.346 |
| R-HSA-69052 | Switching of origins to a post-replicative state | 5.747367e-06 | 5.241 |
| R-HSA-9710421 | Defective pyroptosis | 7.664848e-06 | 5.115 |
| R-HSA-212300 | PRC2 methylates histones and DNA | 1.042445e-05 | 4.982 |
| R-HSA-5693571 | Nonhomologous End-Joining (NHEJ) | 1.801793e-05 | 4.744 |
| R-HSA-8853884 | Transcriptional Regulation by VENTX | 2.634613e-05 | 4.579 |
| R-HSA-68949 | Orc1 removal from chromatin | 3.348869e-05 | 4.475 |
| R-HSA-8878159 | Transcriptional regulation by RUNX3 | 3.377503e-05 | 4.471 |
| R-HSA-69473 | G2/M DNA damage checkpoint | 2.975174e-05 | 4.526 |
| R-HSA-5250924 | B-WICH complex positively regulates rRNA expression | 3.879471e-05 | 4.411 |
| R-HSA-110328 | Recognition and association of DNA glycosylase with site containing an affected ... | 4.449741e-05 | 4.352 |
| R-HSA-171306 | Packaging Of Telomere Ends | 5.941178e-05 | 4.226 |
| R-HSA-73728 | RNA Polymerase I Promoter Opening | 5.941178e-05 | 4.226 |
| R-HSA-2559582 | Senescence-Associated Secretory Phenotype (SASP) | 7.537494e-05 | 4.123 |
| R-HSA-9764560 | Regulation of CDH1 Gene Transcription | 7.882776e-05 | 4.103 |
| R-HSA-5334118 | DNA methylation | 8.890110e-05 | 4.051 |
| R-HSA-5250913 | Positive epigenetic regulation of rRNA expression | 8.869983e-05 | 4.052 |
| R-HSA-9909648 | Regulation of PD-L1(CD274) expression | 9.349766e-05 | 4.029 |
| R-HSA-1640170 | Cell Cycle | 1.157828e-04 | 3.936 |
| R-HSA-9670095 | Inhibition of DNA recombination at telomere | 1.239008e-04 | 3.907 |
| R-HSA-427389 | ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression | 1.239008e-04 | 3.907 |
| R-HSA-9821002 | Chromatin modifications during the maternal to zygotic transition (MZT) | 1.447230e-04 | 3.839 |
| R-HSA-110330 | Recognition and association of DNA glycosylase with site containing an affected ... | 1.550911e-04 | 3.809 |
| R-HSA-73772 | RNA Polymerase I Promoter Escape | 1.622422e-04 | 3.790 |
| R-HSA-69278 | Cell Cycle, Mitotic | 1.711662e-04 | 3.767 |
| R-HSA-174178 | APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins ... | 1.849318e-04 | 3.733 |
| R-HSA-383280 | Nuclear Receptor transcription pathway | 1.925149e-04 | 3.716 |
| R-HSA-9948299 | Ribosome-associated quality control | 1.802401e-04 | 3.744 |
| R-HSA-110329 | Cleavage of the damaged pyrimidine | 1.951913e-04 | 3.710 |
| R-HSA-73928 | Depyrimidination | 1.951913e-04 | 3.710 |
| R-HSA-9821993 | Replacement of protamines by nucleosomes in the male pronucleus | 2.149254e-04 | 3.668 |
| R-HSA-9843970 | Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex | 2.573999e-04 | 3.589 |
| R-HSA-9764265 | Regulation of CDH1 Expression and Function | 2.787709e-04 | 3.555 |
| R-HSA-9764274 | Regulation of Expression and Function of Type I Classical Cadherins | 2.787709e-04 | 3.555 |
| R-HSA-2559585 | Oncogene Induced Senescence | 3.017771e-04 | 3.520 |
| R-HSA-174084 | Autodegradation of Cdh1 by Cdh1:APC/C | 3.404680e-04 | 3.468 |
| R-HSA-2299718 | Condensation of Prophase Chromosomes | 3.404680e-04 | 3.468 |
| R-HSA-69239 | Synthesis of DNA | 3.292195e-04 | 3.483 |
| R-HSA-211000 | Gene Silencing by RNA | 3.292195e-04 | 3.483 |
| R-HSA-174154 | APC/C:Cdc20 mediated degradation of Securin | 3.881618e-04 | 3.411 |
| R-HSA-9845323 | Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) | 4.309090e-04 | 3.366 |
| R-HSA-9954709 | Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide | 3.614033e-04 | 3.442 |
| R-HSA-5693565 | Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at... | 3.845430e-04 | 3.415 |
| R-HSA-427359 | SIRT1 negatively regulates rRNA expression | 4.093022e-04 | 3.388 |
| R-HSA-68886 | M Phase | 3.714835e-04 | 3.430 |
| R-HSA-69242 | S Phase | 3.916828e-04 | 3.407 |
| R-HSA-110331 | Cleavage of the damaged purine | 4.093022e-04 | 3.388 |
| R-HSA-446728 | Cell junction organization | 3.981868e-04 | 3.400 |
| R-HSA-9764725 | Negative Regulation of CDH1 Gene Transcription | 4.309090e-04 | 3.366 |
| R-HSA-1500931 | Cell-Cell communication | 4.564493e-04 | 3.341 |
| R-HSA-73927 | Depurination | 4.736955e-04 | 3.325 |
| R-HSA-389948 | Co-inhibition by PD-1 | 5.318259e-04 | 3.274 |
| R-HSA-2559586 | DNA Damage/Telomere Stress Induced Senescence | 5.376408e-04 | 3.270 |
| R-HSA-69541 | Stabilization of p53 | 5.460668e-04 | 3.263 |
| R-HSA-9020702 | Interleukin-1 signaling | 5.997128e-04 | 3.222 |
| R-HSA-912446 | Meiotic recombination | 6.373010e-04 | 3.196 |
| R-HSA-174184 | Cdc20:Phospho-APC/C mediated degradation of Cyclin A | 7.166148e-04 | 3.145 |
| R-HSA-8866654 | E3 ubiquitin ligases ubiquitinate target proteins | 7.166148e-04 | 3.145 |
| R-HSA-5625886 | Activated PKN1 stimulates transcription of AR (androgen receptor) regulated gene... | 7.176350e-04 | 3.144 |
| R-HSA-388841 | Regulation of T cell activation by CD28 family | 7.301261e-04 | 3.137 |
| R-HSA-157118 | Signaling by NOTCH | 7.772020e-04 | 3.109 |
| R-HSA-179419 | APC:Cdc20 mediated degradation of cell cycle proteins prior to satisfation of th... | 8.037993e-04 | 3.095 |
| R-HSA-156842 | Eukaryotic Translation Elongation | 8.557525e-04 | 3.068 |
| R-HSA-5610780 | Degradation of GLI1 by the proteasome | 8.183688e-04 | 3.087 |
| R-HSA-69017 | CDK-mediated phosphorylation and removal of Cdc6 | 8.994260e-04 | 3.046 |
| R-HSA-9909649 | Regulation of PD-L1(CD274) transcription | 8.171970e-04 | 3.088 |
| R-HSA-73929 | Base-Excision Repair, AP Site Formation | 8.994260e-04 | 3.046 |
| R-HSA-5693606 | DNA Double Strand Break Response | 9.031519e-04 | 3.044 |
| R-HSA-5693607 | Processing of DNA double-strand break ends | 9.391473e-04 | 3.027 |
| R-HSA-176409 | APC/C:Cdc20 mediated degradation of mitotic proteins | 1.004091e-03 | 2.998 |
| R-HSA-446353 | Cell-extracellular matrix interactions | 1.012203e-03 | 2.995 |
| R-HSA-74160 | Gene expression (Transcription) | 9.615484e-04 | 3.017 |
| R-HSA-195721 | Signaling by WNT | 9.870827e-04 | 3.006 |
| R-HSA-1799339 | SRP-dependent cotranslational protein targeting to membrane | 1.033563e-03 | 2.986 |
| R-HSA-176814 | Activation of APC/C and APC/C:Cdc20 mediated degradation of mitotic proteins | 1.118413e-03 | 2.951 |
| R-HSA-9734779 | Developmental Cell Lineages of the Integumentary System | 1.112941e-03 | 2.954 |
| R-HSA-2467813 | Separation of Sister Chromatids | 1.063799e-03 | 2.973 |
| R-HSA-9759476 | Regulation of Homotypic Cell-Cell Adhesion | 1.057491e-03 | 2.976 |
| R-HSA-6814122 | Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding | 1.328422e-03 | 2.877 |
| R-HSA-774815 | Nucleosome assembly | 1.340576e-03 | 2.873 |
| R-HSA-606279 | Deposition of new CENPA-containing nucleosomes at the centromere | 1.340576e-03 | 2.873 |
| R-HSA-174143 | APC/C-mediated degradation of cell cycle proteins | 1.324436e-03 | 2.878 |
| R-HSA-453276 | Regulation of mitotic cell cycle | 1.324436e-03 | 2.878 |
| R-HSA-427413 | NoRC negatively regulates rRNA expression | 1.324436e-03 | 2.878 |
| R-HSA-162909 | Host Interactions of HIV factors | 1.347195e-03 | 2.871 |
| R-HSA-73857 | RNA Polymerase II Transcription | 1.257257e-03 | 2.901 |
| R-HSA-349425 | Autodegradation of the E3 ubiquitin ligase COP1 | 1.328422e-03 | 2.877 |
| R-HSA-75815 | Ubiquitin-dependent degradation of Cyclin D | 1.328422e-03 | 2.877 |
| R-HSA-9010553 | Regulation of expression of SLITs and ROBOs | 1.364799e-03 | 2.865 |
| R-HSA-9824446 | Viral Infection Pathways | 1.270230e-03 | 2.896 |
| R-HSA-201681 | TCF dependent signaling in response to WNT | 1.292802e-03 | 2.888 |
| R-HSA-9755511 | KEAP1-NFE2L2 pathway | 1.286292e-03 | 2.891 |
| R-HSA-5693532 | DNA Double-Strand Break Repair | 1.447306e-03 | 2.839 |
| R-HSA-5578749 | Transcriptional regulation by small RNAs | 1.451535e-03 | 2.838 |
| R-HSA-69206 | G1/S Transition | 1.536741e-03 | 2.813 |
| R-HSA-9912633 | Antigen processing: Ub, ATP-independent proteasomal degradation | 1.566854e-03 | 2.805 |
| R-HSA-5693567 | HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA) | 1.703559e-03 | 2.769 |
| R-HSA-180585 | Vif-mediated degradation of APOBEC3G | 1.735452e-03 | 2.761 |
| R-HSA-8852276 | The role of GTSE1 in G2/M progression after G2 checkpoint | 2.044809e-03 | 2.689 |
| R-HSA-73854 | RNA Polymerase I Promoter Clearance | 2.062767e-03 | 2.686 |
| R-HSA-9762114 | GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 | 1.972235e-03 | 2.705 |
| R-HSA-9734009 | Defective Intrinsic Pathway for Apoptosis | 2.125062e-03 | 2.673 |
| R-HSA-69580 | p53-Dependent G1/S DNA damage checkpoint | 2.098522e-03 | 2.678 |
| R-HSA-69563 | p53-Dependent G1 DNA Damage Response | 2.098522e-03 | 2.678 |
| R-HSA-72766 | Translation | 2.093855e-03 | 2.679 |
| R-HSA-176408 | Regulation of APC/C activators between G1/S and early anaphase | 2.044809e-03 | 2.689 |
| R-HSA-8878171 | Transcriptional regulation by RUNX1 | 2.085645e-03 | 2.681 |
| R-HSA-9678108 | SARS-CoV-1 Infection | 2.063650e-03 | 2.685 |
| R-HSA-162906 | HIV Infection | 2.183167e-03 | 2.661 |
| R-HSA-69615 | G1/S DNA Damage Checkpoints | 2.246040e-03 | 2.649 |
| R-HSA-1912408 | Pre-NOTCH Transcription and Translation | 2.318533e-03 | 2.635 |
| R-HSA-212436 | Generic Transcription Pathway | 2.344719e-03 | 2.630 |
| R-HSA-73864 | RNA Polymerase I Transcription | 2.438052e-03 | 2.613 |
| R-HSA-453279 | Mitotic G1 phase and G1/S transition | 2.481692e-03 | 2.605 |
| R-HSA-9929356 | GSK3B-mediated proteasomal degradation of PD-L1(CD274) | 2.520206e-03 | 2.599 |
| R-HSA-5693538 | Homology Directed Repair | 2.532653e-03 | 2.596 |
| R-HSA-6798695 | Neutrophil degranulation | 2.752902e-03 | 2.560 |
| R-HSA-73894 | DNA Repair | 2.615618e-03 | 2.582 |
| R-HSA-9692914 | SARS-CoV-1-host interactions | 2.828317e-03 | 2.548 |
| R-HSA-8941858 | Regulation of RUNX3 expression and activity | 2.834663e-03 | 2.547 |
| R-HSA-9931269 | AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) | 2.861422e-03 | 2.543 |
| R-HSA-5250941 | Negative epigenetic regulation of rRNA expression | 2.866228e-03 | 2.543 |
| R-HSA-1221632 | Meiotic synapsis | 3.158732e-03 | 2.500 |
| R-HSA-9929491 | SPOP-mediated proteasomal degradation of PD-L1(CD274) | 3.178337e-03 | 2.498 |
| R-HSA-5362768 | Hh mutants are degraded by ERAD | 3.178337e-03 | 2.498 |
| R-HSA-5676590 | NIK-->noncanonical NF-kB signaling | 3.178337e-03 | 2.498 |
| R-HSA-418990 | Adherens junctions interactions | 3.232395e-03 | 2.490 |
| R-HSA-211733 | Regulation of activated PAK-2p34 by proteasome mediated degradation | 3.708987e-03 | 2.431 |
| R-HSA-8953854 | Metabolism of RNA | 3.590135e-03 | 2.445 |
| R-HSA-9018519 | Estrogen-dependent gene expression | 3.386971e-03 | 2.470 |
| R-HSA-5610785 | GLI3 is processed to GLI3R by the proteasome | 3.552944e-03 | 2.449 |
| R-HSA-5610783 | Degradation of GLI2 by the proteasome | 3.552944e-03 | 2.449 |
| R-HSA-8939211 | ESR-mediated signaling | 3.388698e-03 | 2.470 |
| R-HSA-3214815 | HDACs deacetylate histones | 3.824967e-03 | 2.417 |
| R-HSA-5357801 | Programmed Cell Death | 4.000987e-03 | 2.398 |
| R-HSA-446388 | Regulation of cytoskeletal remodeling and cell spreading by IPP complex componen... | 4.033416e-03 | 2.394 |
| R-HSA-195253 | Degradation of beta-catenin by the destruction complex | 4.134246e-03 | 2.384 |
| R-HSA-1500620 | Meiosis | 4.202297e-03 | 2.377 |
| R-HSA-350562 | Regulation of ornithine decarboxylase (ODC) | 4.214201e-03 | 2.375 |
| R-HSA-9924644 | Developmental Lineages of the Mammary Gland | 4.854231e-03 | 2.314 |
| R-HSA-5387390 | Hh mutants abrogate ligand secretion | 4.401958e-03 | 2.356 |
| R-HSA-187577 | SCF(Skp2)-mediated degradation of p27/p21 | 4.879916e-03 | 2.312 |
| R-HSA-9909615 | Regulation of PD-L1(CD274) Post-translational modification | 4.520531e-03 | 2.345 |
| R-HSA-450531 | Regulation of mRNA stability by proteins that bind AU-rich elements | 4.854231e-03 | 2.314 |
| R-HSA-5689880 | Ub-specific processing proteases | 4.422270e-03 | 2.354 |
| R-HSA-1912422 | Pre-NOTCH Expression and Processing | 4.437736e-03 | 2.353 |
| R-HSA-5632684 | Hedgehog 'on' state | 4.482991e-03 | 2.348 |
| R-HSA-69618 | Mitotic Spindle Checkpoint | 5.014038e-03 | 2.300 |
| R-HSA-72662 | Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub... | 5.021827e-03 | 2.299 |
| R-HSA-201722 | Formation of the beta-catenin:TCF transactivating complex | 5.021827e-03 | 2.299 |
| R-HSA-166208 | mTORC1-mediated signalling | 5.292813e-03 | 2.276 |
| R-HSA-180534 | Vpu mediated degradation of CD4 | 5.374609e-03 | 2.270 |
| R-HSA-5678895 | Defective CFTR causes cystic fibrosis | 5.395906e-03 | 2.268 |
| R-HSA-9824272 | Somitogenesis | 5.395906e-03 | 2.268 |
| R-HSA-5607761 | Dectin-1 mediated noncanonical NF-kB signaling | 5.395906e-03 | 2.268 |
| R-HSA-69613 | p53-Independent G1/S DNA Damage Checkpoint | 5.395906e-03 | 2.268 |
| R-HSA-69601 | Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A | 5.395906e-03 | 2.268 |
| R-HSA-421270 | Cell-cell junction organization | 5.968613e-03 | 2.224 |
| R-HSA-72737 | Cap-dependent Translation Initiation | 5.983094e-03 | 2.223 |
| R-HSA-72613 | Eukaryotic Translation Initiation | 5.983094e-03 | 2.223 |
| R-HSA-9735869 | SARS-CoV-1 modulates host translation machinery | 6.035243e-03 | 2.219 |
| R-HSA-68882 | Mitotic Anaphase | 6.416809e-03 | 2.193 |
| R-HSA-2555396 | Mitotic Metaphase and Anaphase | 6.685294e-03 | 2.175 |
| R-HSA-8852135 | Protein ubiquitination | 6.112481e-03 | 2.214 |
| R-HSA-8854050 | FBXL7 down-regulates AURKA during mitotic entry and in early mitosis | 6.753117e-03 | 2.170 |
| R-HSA-174113 | SCF-beta-TrCP mediated degradation of Emi1 | 6.753117e-03 | 2.170 |
| R-HSA-5688426 | Deubiquitination | 6.947651e-03 | 2.158 |
| R-HSA-8939902 | Regulation of RUNX2 expression and activity | 6.486151e-03 | 2.188 |
| R-HSA-169911 | Regulation of Apoptosis | 6.753117e-03 | 2.170 |
| R-HSA-418592 | ADP signalling through P2Y purinoceptor 1 | 7.017725e-03 | 2.154 |
| R-HSA-8964315 | G beta:gamma signalling through BTK | 7.029845e-03 | 2.153 |
| R-HSA-9616222 | Transcriptional regulation of granulopoiesis | 7.039753e-03 | 2.152 |
| R-HSA-975956 | Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) | 7.312788e-03 | 2.136 |
| R-HSA-450408 | AUF1 (hnRNP D0) binds and destabilizes mRNA | 7.530927e-03 | 2.123 |
| R-HSA-376176 | Signaling by ROBO receptors | 7.641623e-03 | 2.117 |
| R-HSA-9766229 | Degradation of CDH1 | 7.876555e-03 | 2.104 |
| R-HSA-5663202 | Diseases of signal transduction by growth factor receptors and second messengers | 8.050992e-03 | 2.094 |
| R-HSA-4641258 | Degradation of DVL | 8.371345e-03 | 2.077 |
| R-HSA-4641257 | Degradation of AXIN | 8.371345e-03 | 2.077 |
| R-HSA-5658442 | Regulation of RAS by GAPs | 8.610013e-03 | 2.065 |
| R-HSA-72706 | GTP hydrolysis and joining of the 60S ribosomal subunit | 8.695766e-03 | 2.061 |
| R-HSA-156827 | L13a-mediated translational silencing of Ceruloplasmin expression | 8.695766e-03 | 2.061 |
| R-HSA-9816359 | Maternal to zygotic transition (MZT) | 8.830459e-03 | 2.054 |
| R-HSA-9917777 | Epigenetic regulation by WDR5-containing histone modifying complexes | 9.022305e-03 | 2.045 |
| R-HSA-977225 | Amyloid fiber formation | 9.367798e-03 | 2.028 |
| R-HSA-1234176 | Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha | 9.392428e-03 | 2.027 |
| R-HSA-1169091 | Activation of NF-kappaB in B cells | 9.392428e-03 | 2.027 |
| R-HSA-5358346 | Hedgehog ligand biogenesis | 9.392428e-03 | 2.027 |
| R-HSA-6804754 | Regulation of TP53 Expression | 1.102538e-02 | 1.958 |
| R-HSA-9675132 | Diseases of cellular response to stress | 1.102538e-02 | 1.958 |
| R-HSA-9630747 | Diseases of Cellular Senescence | 1.102538e-02 | 1.958 |
| R-HSA-927802 | Nonsense-Mediated Decay (NMD) | 1.088568e-02 | 1.963 |
| R-HSA-975957 | Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) | 1.088568e-02 | 1.963 |
| R-HSA-8964616 | G beta:gamma signalling through CDC42 | 9.874556e-03 | 2.005 |
| R-HSA-212165 | Epigenetic regulation of gene expression | 9.980472e-03 | 2.001 |
| R-HSA-9612973 | Autophagy | 9.898570e-03 | 2.004 |
| R-HSA-5607764 | CLEC7A (Dectin-1) signaling | 1.063279e-02 | 1.973 |
| R-HSA-1236978 | Cross-presentation of soluble exogenous antigens (endosomes) | 1.025053e-02 | 1.989 |
| R-HSA-9711123 | Cellular response to chemical stress | 1.106867e-02 | 1.956 |
| R-HSA-432722 | Golgi Associated Vesicle Biogenesis | 1.111133e-02 | 1.954 |
| R-HSA-8936459 | RUNX1 regulates genes involved in megakaryocyte differentiation and platelet fun... | 1.114142e-02 | 1.953 |
| R-HSA-9604323 | Negative regulation of NOTCH4 signaling | 1.129446e-02 | 1.947 |
| R-HSA-72649 | Translation initiation complex formation | 1.205138e-02 | 1.919 |
| R-HSA-176974 | Unwinding of DNA | 1.213984e-02 | 1.916 |
| R-HSA-9843940 | Regulation of endogenous retroelements by KRAB-ZFP proteins | 1.283750e-02 | 1.892 |
| R-HSA-1168372 | Downstream signaling events of B Cell Receptor (BCR) | 1.283750e-02 | 1.892 |
| R-HSA-69202 | Cyclin E associated events during G1/S transition | 1.283750e-02 | 1.892 |
| R-HSA-109581 | Apoptosis | 1.293300e-02 | 1.888 |
| R-HSA-9927432 | Developmental Lineage of Mammary Gland Myoepithelial Cells | 1.296970e-02 | 1.887 |
| R-HSA-9613829 | Chaperone Mediated Autophagy | 1.337638e-02 | 1.874 |
| R-HSA-418217 | G beta:gamma signalling through PLC beta | 1.337638e-02 | 1.874 |
| R-HSA-500657 | Presynaptic function of Kainate receptors | 1.337638e-02 | 1.874 |
| R-HSA-9932298 | Degradation of CRY and PER proteins | 1.360351e-02 | 1.866 |
| R-HSA-72702 | Ribosomal scanning and start codon recognition | 1.410140e-02 | 1.851 |
| R-HSA-68962 | Activation of the pre-replicative complex | 1.447267e-02 | 1.839 |
| R-HSA-390450 | Folding of actin by CCT/TriC | 1.500135e-02 | 1.824 |
| R-HSA-72203 | Processing of Capped Intron-Containing Pre-mRNA | 1.591155e-02 | 1.798 |
| R-HSA-390466 | Chaperonin-mediated protein folding | 1.465458e-02 | 1.834 |
| R-HSA-9842860 | Regulation of endogenous retroelements | 1.498943e-02 | 1.824 |
| R-HSA-156902 | Peptide chain elongation | 1.555953e-02 | 1.808 |
| R-HSA-199992 | trans-Golgi Network Vesicle Budding | 1.471542e-02 | 1.832 |
| R-HSA-5423599 | Diseases of Mismatch Repair (MMR) | 1.679141e-02 | 1.775 |
| R-HSA-392851 | Prostacyclin signalling through prostacyclin receptor | 1.538846e-02 | 1.813 |
| R-HSA-165159 | MTOR signalling | 1.487345e-02 | 1.828 |
| R-HSA-9013694 | Signaling by NOTCH4 | 1.678533e-02 | 1.775 |
| R-HSA-1236974 | ER-Phagosome pathway | 1.650488e-02 | 1.782 |
| R-HSA-69656 | Cyclin A:Cdk2-associated events at S phase entry | 1.471542e-02 | 1.832 |
| R-HSA-9764561 | Regulation of CDH1 Function | 1.521478e-02 | 1.818 |
| R-HSA-8878166 | Transcriptional regulation by RUNX2 | 1.733740e-02 | 1.761 |
| R-HSA-73884 | Base Excision Repair | 1.749160e-02 | 1.757 |
| R-HSA-5619507 | Activation of HOX genes during differentiation | 1.761056e-02 | 1.754 |
| R-HSA-5617472 | Activation of anterior HOX genes in hindbrain development during early embryogen... | 1.761056e-02 | 1.754 |
| R-HSA-9907900 | Proteasome assembly | 1.765571e-02 | 1.753 |
| R-HSA-68875 | Mitotic Prophase | 1.819984e-02 | 1.740 |
| R-HSA-446652 | Interleukin-1 family signaling | 1.832807e-02 | 1.737 |
| R-HSA-9759194 | Nuclear events mediated by NFE2L2 | 1.909377e-02 | 1.719 |
| R-HSA-4608870 | Asymmetric localization of PCP proteins | 1.917240e-02 | 1.717 |
| R-HSA-9930044 | Nuclear RNA decay | 1.966947e-02 | 1.706 |
| R-HSA-202040 | G-protein activation | 1.995948e-02 | 1.700 |
| R-HSA-392170 | ADP signalling through P2Y purinoceptor 12 | 1.995948e-02 | 1.700 |
| R-HSA-73856 | RNA Polymerase II Transcription Termination | 2.029577e-02 | 1.693 |
| R-HSA-9793380 | Formation of paraxial mesoderm | 2.029577e-02 | 1.693 |
| R-HSA-391251 | Protein folding | 2.070950e-02 | 1.684 |
| R-HSA-6796648 | TP53 Regulates Transcription of DNA Repair Genes | 2.154038e-02 | 1.667 |
| R-HSA-6811440 | Retrograde transport at the Trans-Golgi-Network | 2.246723e-02 | 1.648 |
| R-HSA-8941333 | RUNX2 regulates genes involved in differentiation of myeloid cells | 2.357003e-02 | 1.628 |
| R-HSA-9022927 | MECP2 regulates transcription of genes involved in GABA signaling | 2.357003e-02 | 1.628 |
| R-HSA-392518 | Signal amplification | 2.373693e-02 | 1.625 |
| R-HSA-9851695 | Epigenetic regulation of adipogenesis genes by MLL3 and MLL4 complexes | 2.405783e-02 | 1.619 |
| R-HSA-9841922 | MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesi... | 2.405783e-02 | 1.619 |
| R-HSA-9818564 | Epigenetic regulation of gene expression by MLL3 and MLL4 complexes | 2.405783e-02 | 1.619 |
| R-HSA-6803529 | FGFR2 alternative splicing | 2.528564e-02 | 1.597 |
| R-HSA-72689 | Formation of a pool of free 40S subunits | 2.563580e-02 | 1.591 |
| R-HSA-8951936 | RUNX3 regulates p14-ARF | 2.568692e-02 | 1.590 |
| R-HSA-1234174 | Cellular response to hypoxia | 2.645396e-02 | 1.578 |
| R-HSA-72202 | Transport of Mature Transcript to Cytoplasm | 2.717740e-02 | 1.566 |
| R-HSA-389957 | Prefoldin mediated transfer of substrate to CCT/TriC | 2.823952e-02 | 1.549 |
| R-HSA-75067 | Processing of Capped Intronless Pre-mRNA | 3.139022e-02 | 1.503 |
| R-HSA-997272 | Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits | 3.473928e-02 | 1.459 |
| R-HSA-1296041 | Activation of G protein gated Potassium channels | 3.473928e-02 | 1.459 |
| R-HSA-1296059 | G protein gated Potassium channels | 3.473928e-02 | 1.459 |
| R-HSA-72187 | mRNA 3'-end processing | 3.231441e-02 | 1.491 |
| R-HSA-112382 | Formation of RNA Pol II elongation complex | 3.231441e-02 | 1.491 |
| R-HSA-75955 | RNA Polymerase II Transcription Elongation | 3.457258e-02 | 1.461 |
| R-HSA-141444 | Amplification of signal from unattached kinetochores via a MAD2 inhibitory si... | 3.376386e-02 | 1.472 |
| R-HSA-141424 | Amplification of signal from the kinetochores | 3.376386e-02 | 1.472 |
| R-HSA-157579 | Telomere Maintenance | 2.838721e-02 | 1.547 |
| R-HSA-428930 | Thromboxane signalling through TP receptor | 3.139022e-02 | 1.503 |
| R-HSA-3214847 | HATs acetylate histones | 3.133957e-02 | 1.504 |
| R-HSA-9818025 | NFE2L2 regulating TCA cycle genes | 3.127531e-02 | 1.505 |
| R-HSA-392451 | G beta:gamma signalling through PI3Kgamma | 2.823952e-02 | 1.549 |
| R-HSA-8862803 | Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's dis... | 3.139022e-02 | 1.503 |
| R-HSA-8863678 | Neurodegenerative Diseases | 3.139022e-02 | 1.503 |
| R-HSA-5218859 | Regulated Necrosis | 3.183264e-02 | 1.497 |
| R-HSA-5668541 | TNFR2 non-canonical NF-kB pathway | 2.873255e-02 | 1.542 |
| R-HSA-5610787 | Hedgehog 'off' state | 3.289303e-02 | 1.483 |
| R-HSA-5687128 | MAPK6/MAPK4 signaling | 3.202487e-02 | 1.495 |
| R-HSA-5674400 | Constitutive Signaling by AKT1 E17K in Cancer | 2.823952e-02 | 1.549 |
| R-HSA-8948751 | Regulation of PTEN stability and activity | 3.457258e-02 | 1.461 |
| R-HSA-199991 | Membrane Trafficking | 3.604697e-02 | 1.443 |
| R-HSA-1280215 | Cytokine Signaling in Immune system | 3.614330e-02 | 1.442 |
| R-HSA-167200 | Formation of HIV-1 elongation complex containing HIV-1 Tat | 3.615506e-02 | 1.442 |
| R-HSA-400042 | Adrenaline,noradrenaline inhibits insulin secretion | 3.828771e-02 | 1.417 |
| R-HSA-9646303 | Evasion of Oncogene Induced Senescence Due to p14ARF Defects | 3.836889e-02 | 1.416 |
| R-HSA-9723905 | Loss of function of TP53 in cancer due to loss of tetramerization ability | 3.836889e-02 | 1.416 |
| R-HSA-9723907 | Loss of Function of TP53 in Cancer | 3.836889e-02 | 1.416 |
| R-HSA-9646304 | Evasion of Oxidative Stress Induced Senescence Due to p14ARF Defects | 3.836889e-02 | 1.416 |
| R-HSA-167169 | HIV Transcription Elongation | 3.903858e-02 | 1.409 |
| R-HSA-159234 | Transport of Mature mRNAs Derived from Intronless Transcripts | 3.903858e-02 | 1.409 |
| R-HSA-167246 | Tat-mediated elongation of the HIV-1 transcript | 3.903858e-02 | 1.409 |
| R-HSA-167152 | Formation of HIV elongation complex in the absence of HIV Tat | 3.903858e-02 | 1.409 |
| R-HSA-9735871 | SARS-CoV-1 targets host intracellular signalling and regulatory pathways | 3.952804e-02 | 1.403 |
| R-HSA-9017802 | Noncanonical activation of NOTCH3 | 3.982638e-02 | 1.400 |
| R-HSA-111457 | Release of apoptotic factors from the mitochondria | 3.982638e-02 | 1.400 |
| R-HSA-8941855 | RUNX3 regulates CDKN1A transcription | 3.982638e-02 | 1.400 |
| R-HSA-3858494 | Beta-catenin independent WNT signaling | 4.125717e-02 | 1.385 |
| R-HSA-5357956 | TNFR1-induced NF-kappa-B signaling pathway | 4.203601e-02 | 1.376 |
| R-HSA-167243 | Tat-mediated HIV elongation arrest and recovery | 4.203601e-02 | 1.376 |
| R-HSA-167238 | Pausing and recovery of Tat-mediated HIV elongation | 4.203601e-02 | 1.376 |
| R-HSA-73886 | Chromosome Maintenance | 4.252782e-02 | 1.371 |
| R-HSA-3371556 | Cellular response to heat stress | 4.252782e-02 | 1.371 |
| R-HSA-202424 | Downstream TCR signaling | 4.342028e-02 | 1.362 |
| R-HSA-72163 | mRNA Splicing - Major Pathway | 4.399400e-02 | 1.357 |
| R-HSA-5358351 | Signaling by Hedgehog | 4.450686e-02 | 1.352 |
| R-HSA-674695 | RNA Polymerase II Pre-transcription Events | 4.467720e-02 | 1.350 |
| R-HSA-176412 | Phosphorylation of the APC/C | 4.482836e-02 | 1.348 |
| R-HSA-9687136 | Aberrant regulation of mitotic exit in cancer due to RB1 defects | 4.482836e-02 | 1.348 |
| R-HSA-9954714 | PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA | 4.554898e-02 | 1.342 |
| R-HSA-167287 | HIV elongation arrest and recovery | 4.598422e-02 | 1.337 |
| R-HSA-167290 | Pausing and recovery of HIV elongation | 4.598422e-02 | 1.337 |
| R-HSA-451326 | Activation of kainate receptors upon glutamate binding | 4.598422e-02 | 1.337 |
| R-HSA-9927418 | Developmental Lineage of Mammary Gland Luminal Epithelial Cells | 4.850993e-02 | 1.314 |
| R-HSA-1236975 | Antigen processing-Cross presentation | 4.931531e-02 | 1.307 |
| R-HSA-5689603 | UCH proteinases | 4.960334e-02 | 1.304 |
| R-HSA-1632852 | Macroautophagy | 4.970377e-02 | 1.304 |
| R-HSA-420092 | Glucagon-type ligand receptors | 5.013187e-02 | 1.300 |
| R-HSA-913531 | Interferon Signaling | 5.019247e-02 | 1.299 |
| R-HSA-77595 | Processing of Intronless Pre-mRNAs | 5.046223e-02 | 1.297 |
| R-HSA-141430 | Inactivation of APC/C via direct inhibition of the APC/C complex | 5.046223e-02 | 1.297 |
| R-HSA-141405 | Inhibition of the proteolytic activity of APC/C required for the onset of anapha... | 5.046223e-02 | 1.297 |
| R-HSA-9006931 | Signaling by Nuclear Receptors | 5.050110e-02 | 1.297 |
| R-HSA-112412 | SOS-mediated signalling | 5.916637e-02 | 1.228 |
| R-HSA-5637810 | Constitutive Signaling by EGFRvIII | 5.642218e-02 | 1.249 |
| R-HSA-5637812 | Signaling by EGFRvIII in Cancer | 5.642218e-02 | 1.249 |
| R-HSA-389958 | Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding | 5.902144e-02 | 1.229 |
| R-HSA-9954716 | ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri... | 5.721257e-02 | 1.243 |
| R-HSA-72172 | mRNA Splicing | 6.122573e-02 | 1.213 |
| R-HSA-9665348 | Signaling by ERBB2 ECD mutants | 6.269983e-02 | 1.203 |
| R-HSA-9648025 | EML4 and NUDC in mitotic spindle formation | 5.142201e-02 | 1.289 |
| R-HSA-8951664 | Neddylation | 5.566565e-02 | 1.254 |
| R-HSA-5654738 | Signaling by FGFR2 | 6.045281e-02 | 1.219 |
| R-HSA-176407 | Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase | 5.642218e-02 | 1.249 |
| R-HSA-72764 | Eukaryotic Translation Termination | 5.975250e-02 | 1.224 |
| R-HSA-111471 | Apoptotic factor-mediated response | 6.269983e-02 | 1.203 |
| R-HSA-2028269 | Signaling by Hippo | 5.642218e-02 | 1.249 |
| R-HSA-1296065 | Inwardly rectifying K+ channels | 6.376027e-02 | 1.195 |
| R-HSA-975871 | MyD88 cascade initiated on plasma membrane | 6.779282e-02 | 1.169 |
| R-HSA-168142 | Toll Like Receptor 10 (TLR10) Cascade | 6.779282e-02 | 1.169 |
| R-HSA-168176 | Toll Like Receptor 5 (TLR5) Cascade | 6.779282e-02 | 1.169 |
| R-HSA-6811442 | Intra-Golgi and retrograde Golgi-to-ER traffic | 5.290644e-02 | 1.276 |
| R-HSA-456926 | Thrombin signalling through proteinase activated receptors (PARs) | 5.447805e-02 | 1.264 |
| R-HSA-72695 | Formation of the ternary complex, and subsequently, the 43S complex | 6.307033e-02 | 1.200 |
| R-HSA-202403 | TCR signaling | 5.358692e-02 | 1.271 |
| R-HSA-1474165 | Reproduction | 6.463923e-02 | 1.190 |
| R-HSA-9856530 | High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR... | 6.045281e-02 | 1.219 |
| R-HSA-168255 | Influenza Infection | 5.125070e-02 | 1.290 |
| R-HSA-5619084 | ABC transporter disorders | 5.486067e-02 | 1.261 |
| R-HSA-4086400 | PCP/CE pathway | 5.486067e-02 | 1.261 |
| R-HSA-351202 | Metabolism of polyamines | 5.321669e-02 | 1.274 |
| R-HSA-5693568 | Resolution of D-loop Structures through Holliday Junction Intermediates | 6.869242e-02 | 1.163 |
| R-HSA-397795 | G-protein beta:gamma signalling | 6.869242e-02 | 1.163 |
| R-HSA-5675482 | Regulation of necroptotic cell death | 6.869242e-02 | 1.163 |
| R-HSA-176187 | Activation of ATR in response to replication stress | 6.869242e-02 | 1.163 |
| R-HSA-168256 | Immune System | 6.889305e-02 | 1.162 |
| R-HSA-174048 | APC/C:Cdc20 mediated degradation of Cyclin B | 6.928599e-02 | 1.159 |
| R-HSA-167242 | Abortive elongation of HIV-1 transcript in the absence of Tat | 6.928599e-02 | 1.159 |
| R-HSA-9909396 | Circadian clock | 6.932708e-02 | 1.159 |
| R-HSA-77588 | SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs | 6.981671e-02 | 1.156 |
| R-HSA-193634 | Axonal growth inhibition (RHOA activation) | 6.981671e-02 | 1.156 |
| R-HSA-8866904 | Negative regulation of activity of TFAP2 (AP-2) family transcription factors | 6.981671e-02 | 1.156 |
| R-HSA-8939246 | RUNX1 regulates transcription of genes involved in differentiation of myeloid ce... | 6.981671e-02 | 1.156 |
| R-HSA-9825895 | Regulation of MITF-M-dependent genes involved in DNA replication, damage repair ... | 6.981671e-02 | 1.156 |
| R-HSA-909733 | Interferon alpha/beta signaling | 7.040052e-02 | 1.152 |
| R-HSA-9679506 | SARS-CoV Infections | 7.214261e-02 | 1.142 |
| R-HSA-159230 | Transport of the SLBP Dependant Mature mRNA | 7.381537e-02 | 1.132 |
| R-HSA-390471 | Association of TriC/CCT with target proteins during biosynthesis | 7.381537e-02 | 1.132 |
| R-HSA-5693537 | Resolution of D-Loop Structures | 7.381537e-02 | 1.132 |
| R-HSA-163359 | Glucagon signaling in metabolic regulation | 7.381537e-02 | 1.132 |
| R-HSA-5632987 | Defective Mismatch Repair Associated With PMS2 | 7.526785e-02 | 1.123 |
| R-HSA-9630791 | Evasion of Oncogene Induced Senescence Due to Defective p16INK4A binding to CDK4 | 7.526785e-02 | 1.123 |
| R-HSA-9632697 | Evasion of Oxidative Stress Induced Senescence Due to Defective p16INK4A binding... | 7.526785e-02 | 1.123 |
| R-HSA-9645722 | Defective Intrinsic Pathway for Apoptosis Due to p14ARF Loss of Function | 7.526785e-02 | 1.123 |
| R-HSA-5545483 | Defective Mismatch Repair Associated With MLH1 | 7.526785e-02 | 1.123 |
| R-HSA-5632968 | Defective Mismatch Repair Associated With MSH6 | 7.526785e-02 | 1.123 |
| R-HSA-169131 | Inhibition of PKR | 7.526785e-02 | 1.123 |
| R-HSA-2408557 | Selenocysteine synthesis | 7.646786e-02 | 1.117 |
| R-HSA-9675108 | Nervous system development | 7.780647e-02 | 1.109 |
| R-HSA-9927426 | Developmental Lineage of Mammary Gland Alveolar Cells | 7.912626e-02 | 1.102 |
| R-HSA-1368108 | BMAL1:CLOCK,NPAS2 activates circadian expression | 7.912626e-02 | 1.102 |
| R-HSA-73887 | Death Receptor Signaling | 7.931444e-02 | 1.101 |
| R-HSA-167172 | Transcription of the HIV genome | 8.078099e-02 | 1.093 |
| R-HSA-193697 | p75NTR regulates axonogenesis | 8.103520e-02 | 1.091 |
| R-HSA-168273 | Influenza Viral RNA Transcription and Replication | 8.177748e-02 | 1.087 |
| R-HSA-192823 | Viral mRNA Translation | 8.260488e-02 | 1.083 |
| R-HSA-6804756 | Regulation of TP53 Activity through Phosphorylation | 8.268647e-02 | 1.083 |
| R-HSA-5637815 | Signaling by Ligand-Responsive EGFR Variants in Cancer | 8.334389e-02 | 1.079 |
| R-HSA-1236382 | Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants | 8.334389e-02 | 1.079 |
| R-HSA-179409 | APC-Cdc20 mediated degradation of Nek2A | 8.334389e-02 | 1.079 |
| R-HSA-450321 | JNK (c-Jun kinases) phosphorylation and activation mediated by activated human ... | 8.334389e-02 | 1.079 |
| R-HSA-9633012 | Response of EIF2AK4 (GCN2) to amino acid deficiency | 8.577938e-02 | 1.067 |
| R-HSA-162587 | HIV Life Cycle | 8.684492e-02 | 1.061 |
| R-HSA-9630750 | Evasion of Oncogene Induced Senescence Due to p16INK4A Defects | 1.107531e-01 | 0.956 |
| R-HSA-9632693 | Evasion of Oxidative Stress Induced Senescence Due to p16INK4A Defects | 1.107531e-01 | 0.956 |
| R-HSA-176034 | Interactions of Tat with host cellular proteins | 1.107531e-01 | 0.956 |
| R-HSA-5083628 | Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3 | 1.107531e-01 | 0.956 |
| R-HSA-5660724 | Defective SLC6A3 causes Parkinsonism-dystonia infantile (PKDYS) | 1.107531e-01 | 0.956 |
| R-HSA-5619081 | Defective SLC6A3 causes Parkinsonism-dystonia infantile (PKDYS) | 1.107531e-01 | 0.956 |
| R-HSA-9632700 | Evasion of Oxidative Stress Induced Senescence Due to Defective p16INK4A binding... | 1.107531e-01 | 0.956 |
| R-HSA-9630794 | Evasion of Oncogene Induced Senescence Due to Defective p16INK4A binding to CDK4... | 1.107531e-01 | 0.956 |
| R-HSA-164843 | 2-LTR circle formation | 9.276275e-02 | 1.033 |
| R-HSA-5467340 | AXIN missense mutants destabilize the destruction complex | 1.049439e-01 | 0.979 |
| R-HSA-5467337 | APC truncation mutants have impaired AXIN binding | 1.049439e-01 | 0.979 |
| R-HSA-5467348 | Truncations of AMER1 destabilize the destruction complex | 1.049439e-01 | 0.979 |
| R-HSA-9623433 | NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis | 1.175267e-01 | 0.930 |
| R-HSA-5339716 | Signaling by GSK3beta mutants | 1.175267e-01 | 0.930 |
| R-HSA-4839743 | Signaling by CTNNB1 phospho-site mutants | 1.304626e-01 | 0.885 |
| R-HSA-5358749 | CTNNB1 S37 mutants aren't phosphorylated | 1.304626e-01 | 0.885 |
| R-HSA-5358751 | CTNNB1 S45 mutants aren't phosphorylated | 1.304626e-01 | 0.885 |
| R-HSA-5358747 | CTNNB1 S33 mutants aren't phosphorylated | 1.304626e-01 | 0.885 |
| R-HSA-5358752 | CTNNB1 T41 mutants aren't phosphorylated | 1.304626e-01 | 0.885 |
| R-HSA-389960 | Formation of tubulin folding intermediates by CCT/TriC | 1.146947e-01 | 0.940 |
| R-HSA-9725554 | Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin | 1.083785e-01 | 0.965 |
| R-HSA-159231 | Transport of Mature mRNA Derived from an Intronless Transcript | 1.083785e-01 | 0.965 |
| R-HSA-159236 | Transport of Mature mRNA derived from an Intron-Containing Transcript | 1.013854e-01 | 0.994 |
| R-HSA-6791226 | Major pathway of rRNA processing in the nucleolus and cytosol | 1.275732e-01 | 0.894 |
| R-HSA-1643713 | Signaling by EGFR in Cancer | 1.318001e-01 | 0.880 |
| R-HSA-162592 | Integration of provirus | 1.175267e-01 | 0.930 |
| R-HSA-9617828 | FOXO-mediated transcription of cell cycle genes | 9.079428e-02 | 1.042 |
| R-HSA-9614399 | Regulation of localization of FOXO transcription factors | 1.049439e-01 | 0.979 |
| R-HSA-9665686 | Signaling by ERBB2 TMD/JMD mutants | 1.146947e-01 | 0.940 |
| R-HSA-9634285 | Constitutive Signaling by Overexpressed ERBB2 | 1.304626e-01 | 0.885 |
| R-HSA-8866427 | VLDLR internalisation and degradation | 1.304626e-01 | 0.885 |
| R-HSA-74749 | Signal attenuation | 9.276275e-02 | 1.033 |
| R-HSA-3371511 | HSF1 activation | 9.029888e-02 | 1.044 |
| R-HSA-3247509 | Chromatin modifying enzymes | 1.292612e-01 | 0.889 |
| R-HSA-9646399 | Aggrephagy | 1.147404e-01 | 0.940 |
| R-HSA-75893 | TNF signaling | 1.089418e-01 | 0.963 |
| R-HSA-450302 | activated TAK1 mediates p38 MAPK activation | 9.079428e-02 | 1.042 |
| R-HSA-5632928 | Defective Mismatch Repair Associated With MSH2 | 1.107531e-01 | 0.956 |
| R-HSA-4839744 | Signaling by APC mutants | 1.049439e-01 | 0.979 |
| R-HSA-4839748 | Signaling by AMER1 mutants | 1.175267e-01 | 0.930 |
| R-HSA-4839735 | Signaling by AXIN mutants | 1.175267e-01 | 0.930 |
| R-HSA-9842663 | Signaling by LTK | 1.304626e-01 | 0.885 |
| R-HSA-9663891 | Selective autophagy | 8.979847e-02 | 1.047 |
| R-HSA-6806003 | Regulation of TP53 Expression and Degradation | 1.083785e-01 | 0.965 |
| R-HSA-975155 | MyD88 dependent cascade initiated on endosome | 1.062988e-01 | 0.973 |
| R-HSA-937061 | TRIF (TICAM1)-mediated TLR4 signaling | 1.099613e-01 | 0.959 |
| R-HSA-166166 | MyD88-independent TLR4 cascade | 1.099613e-01 | 0.959 |
| R-HSA-168164 | Toll Like Receptor 3 (TLR3) Cascade | 9.233970e-02 | 1.035 |
| R-HSA-168181 | Toll Like Receptor 7/8 (TLR7/8) Cascade | 1.213560e-01 | 0.916 |
| R-HSA-9034015 | Signaling by NTRK3 (TRKC) | 9.079428e-02 | 1.042 |
| R-HSA-975138 | TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation | 1.027050e-01 | 0.988 |
| R-HSA-5213460 | RIPK1-mediated regulated necrosis | 1.021813e-01 | 0.991 |
| R-HSA-2122948 | Activated NOTCH1 Transmits Signal to the Nucleus | 1.318001e-01 | 0.880 |
| R-HSA-8953750 | Transcriptional Regulation by E2F6 | 1.083785e-01 | 0.965 |
| R-HSA-109606 | Intrinsic Pathway for Apoptosis | 1.089418e-01 | 0.963 |
| R-HSA-416482 | G alpha (12/13) signalling events | 1.244760e-01 | 0.905 |
| R-HSA-1169408 | ISG15 antiviral mechanism | 1.103311e-01 | 0.957 |
| R-HSA-1280218 | Adaptive Immune System | 1.090671e-01 | 0.962 |
| R-HSA-9764790 | Positive Regulation of CDH1 Gene Transcription | 9.276275e-02 | 1.033 |
| R-HSA-9725370 | Signaling by ALK fusions and activated point mutants | 9.918032e-02 | 1.004 |
| R-HSA-9700206 | Signaling by ALK in cancer | 9.918032e-02 | 1.004 |
| R-HSA-9755088 | Ribavirin ADME | 9.079428e-02 | 1.042 |
| R-HSA-1236394 | Signaling by ERBB4 | 1.058090e-01 | 0.975 |
| R-HSA-422475 | Axon guidance | 8.843003e-02 | 1.053 |
| R-HSA-5601884 | PIWI-interacting RNA (piRNA) biogenesis | 1.231383e-01 | 0.910 |
| R-HSA-1251985 | Nuclear signaling by ERBB4 | 1.147404e-01 | 0.940 |
| R-HSA-198323 | AKT phosphorylates targets in the cytosol | 1.304626e-01 | 0.885 |
| R-HSA-168138 | Toll Like Receptor 9 (TLR9) Cascade | 1.333495e-01 | 0.875 |
| R-HSA-991365 | Activation of GABAB receptors | 1.347665e-01 | 0.870 |
| R-HSA-381676 | Glucagon-like Peptide-1 (GLP1) regulates insulin secretion | 1.347665e-01 | 0.870 |
| R-HSA-977444 | GABA B receptor activation | 1.347665e-01 | 0.870 |
| R-HSA-450294 | MAP kinase activation | 1.366013e-01 | 0.865 |
| R-HSA-190236 | Signaling by FGFR | 1.393084e-01 | 0.856 |
| R-HSA-983168 | Antigen processing: Ubiquitination & Proteasome degradation | 1.404328e-01 | 0.853 |
| R-HSA-9694516 | SARS-CoV-2 Infection | 1.404733e-01 | 0.852 |
| R-HSA-4641262 | Disassembly of the destruction complex and recruitment of AXIN to the membrane | 1.406677e-01 | 0.852 |
| R-HSA-1268020 | Mitochondrial protein import | 1.424754e-01 | 0.846 |
| R-HSA-9707616 | Heme signaling | 1.424754e-01 | 0.846 |
| R-HSA-2559584 | Formation of Senescence-Associated Heterochromatin Foci (SAHF) | 1.437060e-01 | 0.843 |
| R-HSA-9683610 | Maturation of nucleoprotein | 1.437060e-01 | 0.843 |
| R-HSA-9665230 | Drug resistance in ERBB2 KD mutants | 1.448788e-01 | 0.839 |
| R-HSA-9652282 | Drug-mediated inhibition of ERBB2 signaling | 1.448788e-01 | 0.839 |
| R-HSA-3656535 | TGFBR1 LBD Mutants in Cancer | 1.448788e-01 | 0.839 |
| R-HSA-9665247 | Resistance of ERBB2 KD mutants to osimertinib | 1.448788e-01 | 0.839 |
| R-HSA-9665233 | Resistance of ERBB2 KD mutants to trastuzumab | 1.448788e-01 | 0.839 |
| R-HSA-9665246 | Resistance of ERBB2 KD mutants to neratinib | 1.448788e-01 | 0.839 |
| R-HSA-9665737 | Drug resistance in ERBB2 TMD/JMD mutants | 1.448788e-01 | 0.839 |
| R-HSA-9665250 | Resistance of ERBB2 KD mutants to AEE788 | 1.448788e-01 | 0.839 |
| R-HSA-9665244 | Resistance of ERBB2 KD mutants to sapitinib | 1.448788e-01 | 0.839 |
| R-HSA-9665251 | Resistance of ERBB2 KD mutants to lapatinib | 1.448788e-01 | 0.839 |
| R-HSA-3878781 | Glycogen storage disease type IV (GBE1) | 1.448788e-01 | 0.839 |
| R-HSA-9665249 | Resistance of ERBB2 KD mutants to afatinib | 1.448788e-01 | 0.839 |
| R-HSA-9665245 | Resistance of ERBB2 KD mutants to tesevatinib | 1.448788e-01 | 0.839 |
| R-HSA-180897 | Vpr-mediated induction of apoptosis by mitochondrial outer membrane permeabiliza... | 1.448788e-01 | 0.839 |
| R-HSA-382556 | ABC-family proteins mediated transport | 1.486402e-01 | 0.828 |
| R-HSA-167158 | Formation of the HIV-1 Early Elongation Complex | 1.497290e-01 | 0.825 |
| R-HSA-113418 | Formation of the Early Elongation Complex | 1.497290e-01 | 0.825 |
| R-HSA-5205685 | PINK1-PRKN Mediated Mitophagy | 1.497290e-01 | 0.825 |
| R-HSA-5620971 | Pyroptosis | 1.497290e-01 | 0.825 |
| R-HSA-9009391 | Extra-nuclear estrogen signaling | 1.534140e-01 | 0.814 |
| R-HSA-166058 | MyD88:MAL(TIRAP) cascade initiated on plasma membrane | 1.546177e-01 | 0.811 |
| R-HSA-168188 | Toll Like Receptor TLR6:TLR2 Cascade | 1.546177e-01 | 0.811 |
| R-HSA-6783310 | Fanconi Anemia Pathway | 1.560963e-01 | 0.807 |
| R-HSA-9660821 | ADORA2B mediated anti-inflammatory cytokines production | 1.560963e-01 | 0.807 |
| R-HSA-432040 | Vasopressin regulates renal water homeostasis via Aquaporins | 1.560963e-01 | 0.807 |
| R-HSA-5684264 | MAP3K8 (TPL2)-dependent MAPK1/3 activation | 1.572144e-01 | 0.804 |
| R-HSA-9933939 | Formation of the polybromo-BAF (pBAF) complex | 1.572144e-01 | 0.804 |
| R-HSA-5655291 | Signaling by FGFR4 in disease | 1.572144e-01 | 0.804 |
| R-HSA-391160 | Signal regulatory protein family interactions | 1.572144e-01 | 0.804 |
| R-HSA-9664565 | Signaling by ERBB2 KD Mutants | 1.589715e-01 | 0.799 |
| R-HSA-9034793 | Activated NTRK3 signals through PLCG1 | 1.776968e-01 | 0.750 |
| R-HSA-167021 | PLC-gamma1 signalling | 1.776968e-01 | 0.750 |
| R-HSA-8853336 | Signaling by plasma membrane FGFR1 fusions | 1.776968e-01 | 0.750 |
| R-HSA-209563 | Axonal growth stimulation | 1.776968e-01 | 0.750 |
| R-HSA-8865999 | MET activates PTPN11 | 1.776968e-01 | 0.750 |
| R-HSA-4719360 | Defective DPM3 causes DPM3-CDG | 1.776968e-01 | 0.750 |
| R-HSA-4719377 | Defective DPM2 causes DPM2-CDG | 1.776968e-01 | 0.750 |
| R-HSA-5603037 | IRAK4 deficiency (TLR5) | 1.776968e-01 | 0.750 |
| R-HSA-4717374 | Defective DPM1 causes DPM1-CDG | 1.776968e-01 | 0.750 |
| R-HSA-9673240 | Defective gamma-carboxylation of F9 | 1.776968e-01 | 0.750 |
| R-HSA-9026527 | Activated NTRK2 signals through PLCG1 | 2.092573e-01 | 0.679 |
| R-HSA-8952158 | RUNX3 regulates BCL2L11 (BIM) transcription | 2.092573e-01 | 0.679 |
| R-HSA-1251932 | PLCG1 events in ERBB2 signaling | 2.092573e-01 | 0.679 |
| R-HSA-2978092 | Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate | 2.092573e-01 | 0.679 |
| R-HSA-1306955 | GRB7 events in ERBB2 signaling | 2.092573e-01 | 0.679 |
| R-HSA-111463 | SMAC (DIABLO) binds to IAPs | 2.396083e-01 | 0.620 |
| R-HSA-111464 | SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes | 2.396083e-01 | 0.620 |
| R-HSA-74713 | IRS activation | 2.396083e-01 | 0.620 |
| R-HSA-182218 | Nef Mediated CD8 Down-regulation | 2.687961e-01 | 0.571 |
| R-HSA-9645135 | STAT5 Activation | 2.968653e-01 | 0.527 |
| R-HSA-8951671 | RUNX3 regulates YAP1-mediated transcription | 2.968653e-01 | 0.527 |
| R-HSA-177539 | Autointegration results in viral DNA circles | 2.968653e-01 | 0.527 |
| R-HSA-113507 | E2F-enabled inhibition of pre-replication complex formation | 2.968653e-01 | 0.527 |
| R-HSA-3595174 | Defective CHST14 causes EDS, musculocontractural type | 2.968653e-01 | 0.527 |
| R-HSA-1295596 | Spry regulation of FGF signaling | 1.709480e-01 | 0.767 |
| R-HSA-9933946 | Formation of the embryonic stem cell BAF (esBAF) complex | 1.709480e-01 | 0.767 |
| R-HSA-196299 | Beta-catenin phosphorylation cascade | 1.709480e-01 | 0.767 |
| R-HSA-9709603 | Impaired BRCA2 binding to PALB2 | 2.417817e-01 | 0.617 |
| R-HSA-9934037 | Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) | 2.561710e-01 | 0.591 |
| R-HSA-9701193 | Defective homologous recombination repair (HRR) due to PALB2 loss of function | 2.561710e-01 | 0.591 |
| R-HSA-9704646 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 2.561710e-01 | 0.591 |
| R-HSA-9704331 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 2.561710e-01 | 0.591 |
| R-HSA-9701192 | Defective homologous recombination repair (HRR) due to BRCA1 loss of function | 2.561710e-01 | 0.591 |
| R-HSA-159227 | Transport of the SLBP independent Mature mRNA | 1.975117e-01 | 0.704 |
| R-HSA-3371497 | HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig... | 1.798751e-01 | 0.745 |
| R-HSA-6802952 | Signaling by BRAF and RAF1 fusions | 3.204683e-01 | 0.494 |
| R-HSA-6807505 | RNA polymerase II transcribes snRNA genes | 3.158439e-01 | 0.501 |
| R-HSA-111469 | SMAC, XIAP-regulated apoptotic response | 2.687961e-01 | 0.571 |
| R-HSA-9609523 | Insertion of tail-anchored proteins into the endoplasmic reticulum membrane | 2.561710e-01 | 0.591 |
| R-HSA-1227990 | Signaling by ERBB2 in Cancer | 1.683832e-01 | 0.774 |
| R-HSA-5659898 | Intestinal saccharidase deficiencies | 2.687961e-01 | 0.571 |
| R-HSA-5358565 | Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) | 2.131419e-01 | 0.671 |
| R-HSA-3371568 | Attenuation phase | 2.797229e-01 | 0.553 |
| R-HSA-3214841 | PKMTs methylate histone lysines | 2.902706e-01 | 0.537 |
| R-HSA-8856828 | Clathrin-mediated endocytosis | 1.841323e-01 | 0.735 |
| R-HSA-3371571 | HSF1-dependent transactivation | 2.020762e-01 | 0.694 |
| R-HSA-176033 | Interactions of Vpr with host cellular proteins | 2.797229e-01 | 0.553 |
| R-HSA-4839726 | Chromatin organization | 1.749135e-01 | 0.757 |
| R-HSA-162599 | Late Phase of HIV Life Cycle | 1.797301e-01 | 0.745 |
| R-HSA-1660517 | Synthesis of PIPs at the late endosome membrane | 2.131419e-01 | 0.671 |
| R-HSA-5358508 | Mismatch Repair | 2.274300e-01 | 0.643 |
| R-HSA-5626978 | TNFR1-mediated ceramide production | 2.092573e-01 | 0.679 |
| R-HSA-5633007 | Regulation of TP53 Activity | 1.647258e-01 | 0.783 |
| R-HSA-5654743 | Signaling by FGFR4 | 3.220439e-01 | 0.492 |
| R-HSA-9843743 | Transcriptional regulation of brown and beige adipocyte differentiation | 2.797229e-01 | 0.553 |
| R-HSA-9844594 | Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 | 2.797229e-01 | 0.553 |
| R-HSA-5205647 | Mitophagy | 2.175576e-01 | 0.662 |
| R-HSA-69560 | Transcriptional activation of p53 responsive genes | 2.092573e-01 | 0.679 |
| R-HSA-69895 | Transcriptional activation of cell cycle inhibitor p21 | 2.092573e-01 | 0.679 |
| R-HSA-975110 | TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling | 1.989452e-01 | 0.701 |
| R-HSA-164938 | Nef-mediates down modulation of cell surface receptors by recruiting them to cla... | 2.131419e-01 | 0.671 |
| R-HSA-9734767 | Developmental Cell Lineages | 2.237936e-01 | 0.650 |
| R-HSA-5218920 | VEGFR2 mediated vascular permeability | 2.902706e-01 | 0.537 |
| R-HSA-8868773 | rRNA processing in the nucleus and cytosol | 1.927546e-01 | 0.715 |
| R-HSA-8856825 | Cargo recognition for clathrin-mediated endocytosis | 2.966184e-01 | 0.528 |
| R-HSA-2871837 | FCERI mediated NF-kB activation | 1.885821e-01 | 0.724 |
| R-HSA-2454202 | Fc epsilon receptor (FCERI) signaling | 1.661243e-01 | 0.780 |
| R-HSA-8875513 | MET interacts with TNS proteins | 1.776968e-01 | 0.750 |
| R-HSA-888568 | GABA synthesis | 2.092573e-01 | 0.679 |
| R-HSA-3656534 | Loss of Function of TGFBR1 in Cancer | 2.396083e-01 | 0.620 |
| R-HSA-1483101 | Synthesis of PS | 2.687961e-01 | 0.571 |
| R-HSA-162699 | Synthesis of dolichyl-phosphate mannose | 2.687961e-01 | 0.571 |
| R-HSA-68689 | CDC6 association with the ORC:origin complex | 2.687961e-01 | 0.571 |
| R-HSA-389542 | NADPH regeneration | 2.968653e-01 | 0.527 |
| R-HSA-450385 | Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA | 1.709480e-01 | 0.767 |
| R-HSA-450513 | Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA | 1.709480e-01 | 0.767 |
| R-HSA-8851708 | Signaling by FGFR2 IIIa TM | 2.417817e-01 | 0.617 |
| R-HSA-168276 | NS1 Mediated Effects on Host Pathways | 2.692121e-01 | 0.570 |
| R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | 2.832761e-01 | 0.548 |
| R-HSA-5655302 | Signaling by FGFR1 in disease | 3.008459e-01 | 0.522 |
| R-HSA-2426168 | Activation of gene expression by SREBF (SREBP) | 3.030053e-01 | 0.519 |
| R-HSA-1445148 | Translocation of SLC2A4 (GLUT4) to the plasma membrane | 2.135127e-01 | 0.671 |
| R-HSA-164952 | The role of Nef in HIV-1 replication and disease pathogenesis | 3.136515e-01 | 0.504 |
| R-HSA-9682385 | FLT3 signaling in disease | 2.379986e-01 | 0.623 |
| R-HSA-68877 | Mitotic Prometaphase | 2.131352e-01 | 0.671 |
| R-HSA-392517 | Rap1 signalling | 2.417817e-01 | 0.617 |
| R-HSA-983189 | Kinesins | 2.770335e-01 | 0.557 |
| R-HSA-1226099 | Signaling by FGFR in disease | 2.204695e-01 | 0.657 |
| R-HSA-166016 | Toll Like Receptor 4 (TLR4) Cascade | 2.068383e-01 | 0.684 |
| R-HSA-1227986 | Signaling by ERBB2 | 2.770335e-01 | 0.557 |
| R-HSA-168179 | Toll Like Receptor TLR1:TLR2 Cascade | 1.681092e-01 | 0.774 |
| R-HSA-168898 | Toll-like Receptor Cascades | 3.098362e-01 | 0.509 |
| R-HSA-111448 | Activation of NOXA and translocation to mitochondria | 2.092573e-01 | 0.679 |
| R-HSA-9755779 | SARS-CoV-2 targets host intracellular signalling and regulatory pathways | 1.709480e-01 | 0.767 |
| R-HSA-9634597 | GPER1 signaling | 1.785837e-01 | 0.748 |
| R-HSA-6804757 | Regulation of TP53 Degradation | 2.379986e-01 | 0.623 |
| R-HSA-181438 | Toll Like Receptor 2 (TLR2) Cascade | 1.681092e-01 | 0.774 |
| R-HSA-8873719 | RAB geranylgeranylation | 2.770335e-01 | 0.557 |
| R-HSA-186763 | Downstream signal transduction | 1.779517e-01 | 0.750 |
| R-HSA-8853659 | RET signaling | 2.379986e-01 | 0.623 |
| R-HSA-448424 | Interleukin-17 signaling | 1.930872e-01 | 0.714 |
| R-HSA-5653656 | Vesicle-mediated transport | 2.278597e-01 | 0.642 |
| R-HSA-429593 | Inositol transporters | 2.396083e-01 | 0.620 |
| R-HSA-175567 | Integration of viral DNA into host genomic DNA | 2.968653e-01 | 0.527 |
| R-HSA-8876725 | Protein methylation | 1.709480e-01 | 0.767 |
| R-HSA-9687139 | Aberrant regulation of mitotic cell cycle due to RB1 defects | 1.683832e-01 | 0.774 |
| R-HSA-168638 | NOD1/2 Signaling Pathway | 2.175576e-01 | 0.662 |
| R-HSA-8856688 | Golgi-to-ER retrograde transport | 2.269371e-01 | 0.644 |
| R-HSA-983705 | Signaling by the B Cell Receptor (BCR) | 2.553416e-01 | 0.593 |
| R-HSA-5655253 | Signaling by FGFR2 in disease | 1.941433e-01 | 0.712 |
| R-HSA-162594 | Early Phase of HIV Life Cycle | 2.705740e-01 | 0.568 |
| R-HSA-418597 | G alpha (z) signalling events | 2.346945e-01 | 0.629 |
| R-HSA-2500257 | Resolution of Sister Chromatid Cohesion | 1.635533e-01 | 0.786 |
| R-HSA-2132295 | MHC class II antigen presentation | 2.916760e-01 | 0.535 |
| R-HSA-917937 | Iron uptake and transport | 2.274946e-01 | 0.643 |
| R-HSA-69275 | G2/M Transition | 1.848595e-01 | 0.733 |
| R-HSA-445989 | TAK1-dependent IKK and NF-kappa-B activation | 1.709686e-01 | 0.767 |
| R-HSA-2173796 | SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription | 2.483399e-01 | 0.605 |
| R-HSA-453274 | Mitotic G2-G2/M phases | 1.927546e-01 | 0.715 |
| R-HSA-983169 | Class I MHC mediated antigen processing & presentation | 2.394573e-01 | 0.621 |
| R-HSA-210993 | Tie2 Signaling | 2.274300e-01 | 0.643 |
| R-HSA-9609507 | Protein localization | 2.306166e-01 | 0.637 |
| R-HSA-9758274 | Regulation of NF-kappa B signaling | 1.848698e-01 | 0.733 |
| R-HSA-9675135 | Diseases of DNA repair | 1.634709e-01 | 0.787 |
| R-HSA-9927353 | Co-inhibition by BTLA | 2.396083e-01 | 0.620 |
| R-HSA-1181150 | Signaling by NODAL | 2.561710e-01 | 0.591 |
| R-HSA-977443 | GABA receptor activation | 2.770335e-01 | 0.557 |
| R-HSA-9711097 | Cellular response to starvation | 2.553416e-01 | 0.593 |
| R-HSA-9772755 | Formation of WDR5-containing histone-modifying complexes | 2.277342e-01 | 0.643 |
| R-HSA-3134975 | Regulation of innate immune responses to cytosolic DNA | 1.989452e-01 | 0.701 |
| R-HSA-432142 | Platelet sensitization by LDL | 2.274300e-01 | 0.643 |
| R-HSA-5621481 | C-type lectin receptors (CLRs) | 2.149684e-01 | 0.668 |
| R-HSA-5689896 | Ovarian tumor domain proteases | 2.483399e-01 | 0.605 |
| R-HSA-426486 | Small interfering RNA (siRNA) biogenesis | 2.968653e-01 | 0.527 |
| R-HSA-9733458 | Induction of Cell-Cell Fusion | 1.848698e-01 | 0.733 |
| R-HSA-1483148 | Synthesis of PG | 1.989452e-01 | 0.701 |
| R-HSA-9675126 | Diseases of mitotic cell cycle | 1.876652e-01 | 0.727 |
| R-HSA-9013507 | NOTCH3 Activation and Transmission of Signal to the Nucleus | 2.993340e-01 | 0.524 |
| R-HSA-193704 | p75 NTR receptor-mediated signalling | 2.635287e-01 | 0.579 |
| R-HSA-5663205 | Infectious disease | 2.351517e-01 | 0.629 |
| R-HSA-9754678 | SARS-CoV-2 modulates host translation machinery | 2.264185e-01 | 0.645 |
| R-HSA-9705683 | SARS-CoV-2-host interactions | 1.795317e-01 | 0.746 |
| R-HSA-418346 | Platelet homeostasis | 3.168496e-01 | 0.499 |
| R-HSA-6794361 | Neurexins and neuroligins | 2.101036e-01 | 0.678 |
| R-HSA-8982491 | Glycogen metabolism | 2.797229e-01 | 0.553 |
| R-HSA-8849468 | PTK6 Regulates Proteins Involved in RNA Processing | 2.396083e-01 | 0.620 |
| R-HSA-447043 | Neurofascin interactions | 2.968653e-01 | 0.527 |
| R-HSA-3304351 | Signaling by TGF-beta Receptor Complex in Cancer | 2.968653e-01 | 0.527 |
| R-HSA-9694631 | Maturation of nucleoprotein | 2.417817e-01 | 0.617 |
| R-HSA-69205 | G1/S-Specific Transcription | 2.379986e-01 | 0.623 |
| R-HSA-8854214 | TBC/RABGAPs | 3.220439e-01 | 0.492 |
| R-HSA-9860931 | Response of endothelial cells to shear stress | 1.681517e-01 | 0.774 |
| R-HSA-2022377 | Metabolism of Angiotensinogen to Angiotensins | 2.849685e-01 | 0.545 |
| R-HSA-1257604 | PIP3 activates AKT signaling | 1.778821e-01 | 0.750 |
| R-HSA-69190 | DNA strand elongation | 1.876652e-01 | 0.727 |
| R-HSA-449147 | Signaling by Interleukins | 1.929666e-01 | 0.715 |
| R-HSA-2408522 | Selenoamino acid metabolism | 2.860717e-01 | 0.544 |
| R-HSA-445717 | Aquaporin-mediated transport | 2.856542e-01 | 0.544 |
| R-HSA-9855142 | Cellular responses to mechanical stimuli | 2.269768e-01 | 0.644 |
| R-HSA-9006925 | Intracellular signaling by second messengers | 2.564529e-01 | 0.591 |
| R-HSA-9933387 | RORA,B,C and NR1D1 (REV-ERBA) regulate gene expression | 1.683832e-01 | 0.774 |
| R-HSA-6807070 | PTEN Regulation | 1.626131e-01 | 0.789 |
| R-HSA-5210891 | Uptake and function of anthrax toxins | 2.131419e-01 | 0.671 |
| R-HSA-9825892 | Regulation of MITF-M-dependent genes involved in cell cycle and proliferation | 2.849685e-01 | 0.545 |
| R-HSA-9931509 | Expression of BMAL (ARNTL), CLOCK, and NPAS2 | 2.692121e-01 | 0.570 |
| R-HSA-381038 | XBP1(S) activates chaperone genes | 1.717577e-01 | 0.765 |
| R-HSA-381070 | IRE1alpha activates chaperones | 2.068160e-01 | 0.684 |
| R-HSA-8950505 | Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulati... | 3.204683e-01 | 0.494 |
| R-HSA-203641 | NOSTRIN mediated eNOS trafficking | 3.238585e-01 | 0.490 |
| R-HSA-9031525 | NR1H2 & NR1H3 regulate gene expression to limit cholesterol uptake | 3.238585e-01 | 0.490 |
| R-HSA-111367 | SLBP independent Processing of Histone Pre-mRNAs | 3.238585e-01 | 0.490 |
| R-HSA-9031528 | NR1H2 & NR1H3 regulate gene expression linked to triglyceride lipolysis in adipo... | 3.238585e-01 | 0.490 |
| R-HSA-9726840 | SHOC2 M1731 mutant abolishes MRAS complex function | 3.238585e-01 | 0.490 |
| R-HSA-8851907 | MET activates PI3K/AKT signaling | 3.238585e-01 | 0.490 |
| R-HSA-8849473 | PTK6 Expression | 3.238585e-01 | 0.490 |
| R-HSA-167590 | Nef Mediated CD4 Down-regulation | 3.238585e-01 | 0.490 |
| R-HSA-8932506 | DAG1 core M1 glycosylations | 3.238585e-01 | 0.490 |
| R-HSA-1912399 | Pre-NOTCH Processing in the Endoplasmic Reticulum | 3.238585e-01 | 0.490 |
| R-HSA-9603381 | Activated NTRK3 signals through PI3K | 3.238585e-01 | 0.490 |
| R-HSA-139915 | Activation of PUMA and translocation to mitochondria | 3.238585e-01 | 0.490 |
| R-HSA-5336415 | Uptake and function of diphtheria toxin | 3.238585e-01 | 0.490 |
| R-HSA-110357 | Displacement of DNA glycosylase by APEX1 | 3.238585e-01 | 0.490 |
| R-HSA-110314 | Recognition of DNA damage by PCNA-containing replication complex | 3.279036e-01 | 0.484 |
| R-HSA-187037 | Signaling by NTRK1 (TRKA) | 3.286005e-01 | 0.483 |
| R-HSA-9758941 | Gastrulation | 3.317980e-01 | 0.479 |
| R-HSA-3214858 | RMTs methylate histone arginines | 3.326495e-01 | 0.478 |
| R-HSA-9609690 | HCMV Early Events | 3.350471e-01 | 0.475 |
| R-HSA-5685942 | HDR through Homologous Recombination (HRR) | 3.380029e-01 | 0.471 |
| R-HSA-5693554 | Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD... | 3.420743e-01 | 0.466 |
| R-HSA-9932444 | ATP-dependent chromatin remodelers | 3.420743e-01 | 0.466 |
| R-HSA-9932451 | SWI/SNF chromatin remodelers | 3.420743e-01 | 0.466 |
| R-HSA-1660516 | Synthesis of PIPs at the early endosome membrane | 3.420743e-01 | 0.466 |
| R-HSA-203927 | MicroRNA (miRNA) biogenesis | 3.420743e-01 | 0.466 |
| R-HSA-70221 | Glycogen breakdown (glycogenolysis) | 3.420743e-01 | 0.466 |
| R-HSA-1266695 | Interleukin-7 signaling | 3.420743e-01 | 0.466 |
| R-HSA-5654741 | Signaling by FGFR3 | 3.432488e-01 | 0.464 |
| R-HSA-168249 | Innate Immune System | 3.435880e-01 | 0.464 |
| R-HSA-212718 | EGFR interacts with phospholipase C-gamma | 3.498171e-01 | 0.456 |
| R-HSA-111995 | phospho-PLA2 pathway | 3.498171e-01 | 0.456 |
| R-HSA-9828211 | Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation | 3.498171e-01 | 0.456 |
| R-HSA-196025 | Formation of annular gap junctions | 3.498171e-01 | 0.456 |
| R-HSA-9028335 | Activated NTRK2 signals through PI3K | 3.498171e-01 | 0.456 |
| R-HSA-9660537 | Signaling by MRAS-complex mutants | 3.498171e-01 | 0.456 |
| R-HSA-8875656 | MET receptor recycling | 3.498171e-01 | 0.456 |
| R-HSA-9726842 | Gain-of-function MRAS complexes activate RAF signaling | 3.498171e-01 | 0.456 |
| R-HSA-164940 | Nef mediated downregulation of MHC class I complex cell surface expression | 3.498171e-01 | 0.456 |
| R-HSA-3371378 | Regulation by c-FLIP | 3.498171e-01 | 0.456 |
| R-HSA-1253288 | Downregulation of ERBB4 signaling | 3.498171e-01 | 0.456 |
| R-HSA-8932504 | DAG1 core M2 glycosylations | 3.498171e-01 | 0.456 |
| R-HSA-69416 | Dimerization of procaspase-8 | 3.498171e-01 | 0.456 |
| R-HSA-9839383 | TGFBR3 PTM regulation | 3.498171e-01 | 0.456 |
| R-HSA-351906 | Apoptotic cleavage of cell adhesion proteins | 3.498171e-01 | 0.456 |
| R-HSA-983231 | Factors involved in megakaryocyte development and platelet production | 3.500661e-01 | 0.456 |
| R-HSA-72165 | mRNA Splicing - Minor Pathway | 3.538341e-01 | 0.451 |
| R-HSA-5357905 | Regulation of TNFR1 signaling | 3.538341e-01 | 0.451 |
| R-HSA-9703465 | Signaling by FLT3 fusion proteins | 3.561487e-01 | 0.448 |
| R-HSA-1169410 | Antiviral mechanism by IFN-stimulated genes | 3.607875e-01 | 0.443 |
| R-HSA-1834949 | Cytosolic sensors of pathogen-associated DNA | 3.643558e-01 | 0.438 |
| R-HSA-5655332 | Signaling by FGFR3 in disease | 3.701135e-01 | 0.432 |
| R-HSA-9841251 | Mitochondrial unfolded protein response (UPRmt) | 3.701135e-01 | 0.432 |
| R-HSA-9006115 | Signaling by NTRK2 (TRKB) | 3.701135e-01 | 0.432 |
| R-HSA-190873 | Gap junction degradation | 3.747807e-01 | 0.426 |
| R-HSA-5218900 | CASP8 activity is inhibited | 3.747807e-01 | 0.426 |
| R-HSA-9700645 | ALK mutants bind TKIs | 3.747807e-01 | 0.426 |
| R-HSA-2025928 | Calcineurin activates NFAT | 3.747807e-01 | 0.426 |
| R-HSA-428543 | Inactivation of CDC42 and RAC1 | 3.747807e-01 | 0.426 |
| R-HSA-937042 | IRAK2 mediated activation of TAK1 complex | 3.747807e-01 | 0.426 |
| R-HSA-170984 | ARMS-mediated activation | 3.747807e-01 | 0.426 |
| R-HSA-9840373 | Cellular response to mitochondrial stress | 3.747807e-01 | 0.426 |
| R-HSA-1433617 | Regulation of signaling by NODAL | 3.747807e-01 | 0.426 |
| R-HSA-264870 | Caspase-mediated cleavage of cytoskeletal proteins | 3.747807e-01 | 0.426 |
| R-HSA-450520 | HuR (ELAVL1) binds and stabilizes mRNA | 3.747807e-01 | 0.426 |
| R-HSA-198693 | AKT phosphorylates targets in the nucleus | 3.747807e-01 | 0.426 |
| R-HSA-8866907 | Activation of the TFAP2 (AP-2) family of transcription factors | 3.747807e-01 | 0.426 |
| R-HSA-163680 | AMPK inhibits chREBP transcriptional activation activity | 3.747807e-01 | 0.426 |
| R-HSA-9768777 | Regulation of NPAS4 gene transcription | 3.747807e-01 | 0.426 |
| R-HSA-9762293 | Regulation of CDH11 gene transcription | 3.747807e-01 | 0.426 |
| R-HSA-9013700 | NOTCH4 Activation and Transmission of Signal to the Nucleus | 3.747807e-01 | 0.426 |
| R-HSA-9834752 | Respiratory syncytial virus genome replication | 3.747807e-01 | 0.426 |
| R-HSA-9613354 | Lipophagy | 3.747807e-01 | 0.426 |
| R-HSA-193692 | Regulated proteolysis of p75NTR | 3.747807e-01 | 0.426 |
| R-HSA-389356 | Co-stimulation by CD28 | 3.749332e-01 | 0.426 |
| R-HSA-9610379 | HCMV Late Events | 3.783081e-01 | 0.422 |
| R-HSA-5654732 | Negative regulation of FGFR3 signaling | 3.839564e-01 | 0.416 |
| R-HSA-5628897 | TP53 Regulates Metabolic Genes | 3.854059e-01 | 0.414 |
| R-HSA-73893 | DNA Damage Bypass | 3.854331e-01 | 0.414 |
| R-HSA-4086398 | Ca2+ pathway | 3.906619e-01 | 0.408 |
| R-HSA-72086 | mRNA Capping | 3.976662e-01 | 0.400 |
| R-HSA-9615710 | Late endosomal microautophagy | 3.976662e-01 | 0.400 |
| R-HSA-9709570 | Impaired BRCA2 binding to RAD51 | 3.976662e-01 | 0.400 |
| R-HSA-5654733 | Negative regulation of FGFR4 signaling | 3.976662e-01 | 0.400 |
| R-HSA-5654708 | Downstream signaling of activated FGFR3 | 3.976662e-01 | 0.400 |
| R-HSA-9006335 | Signaling by Erythropoietin | 3.976662e-01 | 0.400 |
| R-HSA-9674555 | Signaling by CSF3 (G-CSF) | 3.976662e-01 | 0.400 |
| R-HSA-8875555 | MET activates RAP1 and RAC1 | 3.987872e-01 | 0.399 |
| R-HSA-9027277 | Erythropoietin activates Phospholipase C gamma (PLCG) | 3.987872e-01 | 0.399 |
| R-HSA-198203 | PI3K/AKT activation | 3.987872e-01 | 0.399 |
| R-HSA-9014325 | TICAM1,TRAF6-dependent induction of TAK1 complex | 3.987872e-01 | 0.399 |
| R-HSA-5140745 | WNT5A-dependent internalization of FZD2, FZD5 and ROR2 | 3.987872e-01 | 0.399 |
| R-HSA-6803544 | Ion influx/efflux at host-pathogen interface | 3.987872e-01 | 0.399 |
| R-HSA-2151209 | Activation of PPARGC1A (PGC-1alpha) by phosphorylation | 3.987872e-01 | 0.399 |
| R-HSA-9761174 | Formation of intermediate mesoderm | 3.987872e-01 | 0.399 |
| R-HSA-2179392 | EGFR Transactivation by Gastrin | 3.987872e-01 | 0.399 |
| R-HSA-426048 | Arachidonate production from DAG | 3.987872e-01 | 0.399 |
| R-HSA-8934903 | Receptor Mediated Mitophagy | 3.987872e-01 | 0.399 |
| R-HSA-9668250 | Defective factor IX causes hemophilia B | 3.987872e-01 | 0.399 |
| R-HSA-9820962 | Assembly and release of respiratory syncytial virus (RSV) virions | 3.987872e-01 | 0.399 |
| R-HSA-9664873 | Pexophagy | 3.987872e-01 | 0.399 |
| R-HSA-6799990 | Metal sequestration by antimicrobial proteins | 3.987872e-01 | 0.399 |
| R-HSA-9627069 | Regulation of the apoptosome activity | 3.987872e-01 | 0.399 |
| R-HSA-5689877 | Josephin domain DUBs | 3.987872e-01 | 0.399 |
| R-HSA-2586552 | Signaling by Leptin | 3.987872e-01 | 0.399 |
| R-HSA-111458 | Formation of apoptosome | 3.987872e-01 | 0.399 |
| R-HSA-9693928 | Defective RIPK1-mediated regulated necrosis | 3.987872e-01 | 0.399 |
| R-HSA-72312 | rRNA processing | 3.991875e-01 | 0.399 |
| R-HSA-1592230 | Mitochondrial biogenesis | 4.060734e-01 | 0.391 |
| R-HSA-6807878 | COPI-mediated anterograde transport | 4.076047e-01 | 0.390 |
| R-HSA-6811434 | COPI-dependent Golgi-to-ER retrograde traffic | 4.076047e-01 | 0.390 |
| R-HSA-1296071 | Potassium Channels | 4.076047e-01 | 0.390 |
| R-HSA-381119 | Unfolded Protein Response (UPR) | 4.103499e-01 | 0.387 |
| R-HSA-380972 | Energy dependent regulation of mTOR by LKB1-AMPK | 4.112326e-01 | 0.386 |
| R-HSA-2424491 | DAP12 signaling | 4.112326e-01 | 0.386 |
| R-HSA-5654716 | Downstream signaling of activated FGFR4 | 4.112326e-01 | 0.386 |
| R-HSA-114452 | Activation of BH3-only proteins | 4.112326e-01 | 0.386 |
| R-HSA-2219528 | PI3K/AKT Signaling in Cancer | 4.129529e-01 | 0.384 |
| R-HSA-170834 | Signaling by TGF-beta Receptor Complex | 4.152355e-01 | 0.382 |
| R-HSA-9692916 | SARS-CoV-1 activates/modulates innate immune responses | 4.166581e-01 | 0.380 |
| R-HSA-5339562 | Uptake and actions of bacterial toxins | 4.166581e-01 | 0.380 |
| R-HSA-1980143 | Signaling by NOTCH1 | 4.168086e-01 | 0.380 |
| R-HSA-9020591 | Interleukin-12 signaling | 4.168086e-01 | 0.380 |
| R-HSA-1643685 | Disease | 4.195620e-01 | 0.377 |
| R-HSA-163765 | ChREBP activates metabolic gene expression | 4.218733e-01 | 0.375 |
| R-HSA-1483248 | Synthesis of PIPs at the ER membrane | 4.218733e-01 | 0.375 |
| R-HSA-9034864 | Activated NTRK3 signals through RAS | 4.218733e-01 | 0.375 |
| R-HSA-192905 | vRNP Assembly | 4.218733e-01 | 0.375 |
| R-HSA-9645460 | Alpha-protein kinase 1 signaling pathway | 4.218733e-01 | 0.375 |
| R-HSA-9754560 | SARS-CoV-2 modulates autophagy | 4.218733e-01 | 0.375 |
| R-HSA-9635465 | Suppression of apoptosis | 4.218733e-01 | 0.375 |
| R-HSA-210990 | PECAM1 interactions | 4.218733e-01 | 0.375 |
| R-HSA-182971 | EGFR downregulation | 4.246465e-01 | 0.372 |
| R-HSA-9833109 | Evasion by RSV of host interferon responses | 4.246465e-01 | 0.372 |
| R-HSA-9820960 | Respiratory syncytial virus (RSV) attachment and entry | 4.246465e-01 | 0.372 |
| R-HSA-9614085 | FOXO-mediated transcription | 4.304478e-01 | 0.366 |
| R-HSA-5673001 | RAF/MAP kinase cascade | 4.343139e-01 | 0.362 |
| R-HSA-4791275 | Signaling by WNT in cancer | 4.378997e-01 | 0.359 |
| R-HSA-111465 | Apoptotic cleavage of cellular proteins | 4.378997e-01 | 0.359 |
| R-HSA-3700989 | Transcriptional Regulation by TP53 | 4.406669e-01 | 0.356 |
| R-HSA-1655829 | Regulation of cholesterol biosynthesis by SREBP (SREBF) | 4.426934e-01 | 0.354 |
| R-HSA-159740 | Gamma-carboxylation of protein precursors | 4.440743e-01 | 0.353 |
| R-HSA-9824878 | Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 | 4.440743e-01 | 0.353 |
| R-HSA-9013973 | TICAM1-dependent activation of IRF3/IRF7 | 4.440743e-01 | 0.353 |
| R-HSA-9026519 | Activated NTRK2 signals through RAS | 4.440743e-01 | 0.353 |
| R-HSA-180689 | APOBEC3G mediated resistance to HIV-1 infection | 4.440743e-01 | 0.353 |
| R-HSA-68884 | Mitotic Telophase/Cytokinesis | 4.440743e-01 | 0.353 |
| R-HSA-5358493 | Synthesis of diphthamide-EEF2 | 4.440743e-01 | 0.353 |
| R-HSA-2022923 | DS-GAG biosynthesis | 4.440743e-01 | 0.353 |
| R-HSA-416550 | Sema4D mediated inhibition of cell attachment and migration | 4.440743e-01 | 0.353 |
| R-HSA-111461 | Cytochrome c-mediated apoptotic response | 4.440743e-01 | 0.353 |
| R-HSA-9012852 | Signaling by NOTCH3 | 4.473507e-01 | 0.349 |
| R-HSA-6811436 | COPI-independent Golgi-to-ER retrograde traffic | 4.473507e-01 | 0.349 |
| R-HSA-5654726 | Negative regulation of FGFR1 signaling | 4.509847e-01 | 0.346 |
| R-HSA-5685938 | HDR through Single Strand Annealing (SSA) | 4.509847e-01 | 0.346 |
| R-HSA-1839124 | FGFR1 mutant receptor activation | 4.509847e-01 | 0.346 |
| R-HSA-8939243 | RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not kno... | 4.509847e-01 | 0.346 |
| R-HSA-1855204 | Synthesis of IP3 and IP4 in the cytosol | 4.509847e-01 | 0.346 |
| R-HSA-177929 | Signaling by EGFR | 4.574392e-01 | 0.340 |
| R-HSA-5654736 | Signaling by FGFR1 | 4.574392e-01 | 0.340 |
| R-HSA-2173793 | Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer | 4.574392e-01 | 0.340 |
| R-HSA-2151201 | Transcriptional activation of mitochondrial biogenesis | 4.597584e-01 | 0.337 |
| R-HSA-390522 | Striated Muscle Contraction | 4.638948e-01 | 0.334 |
| R-HSA-9619665 | EGR2 and SOX10-mediated initiation of Schwann cell myelination | 4.638948e-01 | 0.334 |
| R-HSA-2197563 | NOTCH2 intracellular domain regulates transcription | 4.654241e-01 | 0.332 |
| R-HSA-9820865 | Z-decay: degradation of maternal mRNAs by zygotically expressed factors | 4.654241e-01 | 0.332 |
| R-HSA-179812 | GRB2 events in EGFR signaling | 4.654241e-01 | 0.332 |
| R-HSA-3000484 | Scavenging by Class F Receptors | 4.654241e-01 | 0.332 |
| R-HSA-8941856 | RUNX3 regulates NOTCH signaling | 4.654241e-01 | 0.332 |
| R-HSA-418890 | Role of second messengers in netrin-1 signaling | 4.654241e-01 | 0.332 |
| R-HSA-8851805 | MET activates RAS signaling | 4.654241e-01 | 0.332 |
| R-HSA-2428933 | SHC-related events triggered by IGF1R | 4.654241e-01 | 0.332 |
| R-HSA-159854 | Gamma-carboxylation, transport, and amino-terminal cleavage of proteins | 4.654241e-01 | 0.332 |
| R-HSA-9028731 | Activated NTRK2 signals through FRS2 and FRS3 | 4.654241e-01 | 0.332 |
| R-HSA-975144 | IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation | 4.654241e-01 | 0.332 |
| R-HSA-937039 | IRAK1 recruits IKK complex | 4.654241e-01 | 0.332 |
| R-HSA-879415 | Advanced glycosylation endproduct receptor signaling | 4.654241e-01 | 0.332 |
| R-HSA-8983432 | Interleukin-15 signaling | 4.654241e-01 | 0.332 |
| R-HSA-9617629 | Regulation of FOXO transcriptional activity by acetylation | 4.654241e-01 | 0.332 |
| R-HSA-4641265 | Repression of WNT target genes | 4.654241e-01 | 0.332 |
| R-HSA-5661231 | Metallothioneins bind metals | 4.654241e-01 | 0.332 |
| R-HSA-209543 | p75NTR recruits signalling complexes | 4.654241e-01 | 0.332 |
| R-HSA-73943 | Reversal of alkylation damage by DNA dioxygenases | 4.654241e-01 | 0.332 |
| R-HSA-5684996 | MAPK1/MAPK3 signaling | 4.658732e-01 | 0.332 |
| R-HSA-5683057 | MAPK family signaling cascades | 4.679044e-01 | 0.330 |
| R-HSA-111885 | Opioid Signalling | 4.680767e-01 | 0.330 |
| R-HSA-166520 | Signaling by NTRKs | 4.730042e-01 | 0.325 |
| R-HSA-5654727 | Negative regulation of FGFR2 signaling | 4.766243e-01 | 0.322 |
| R-HSA-5673000 | RAF activation | 4.766243e-01 | 0.322 |
| R-HSA-9675136 | Diseases of DNA Double-Strand Break Repair | 4.766243e-01 | 0.322 |
| R-HSA-203615 | eNOS activation | 4.766243e-01 | 0.322 |
| R-HSA-1980145 | Signaling by NOTCH2 | 4.766243e-01 | 0.322 |
| R-HSA-9701190 | Defective homologous recombination repair (HRR) due to BRCA2 loss of function | 4.766243e-01 | 0.322 |
| R-HSA-9680350 | Signaling by CSF1 (M-CSF) in myeloid cells | 4.766243e-01 | 0.322 |
| R-HSA-9707564 | Cytoprotection by HMOX1 | 4.766407e-01 | 0.322 |
| R-HSA-9772572 | Early SARS-CoV-2 Infection Events | 4.773757e-01 | 0.321 |
| R-HSA-76002 | Platelet activation, signaling and aggregation | 4.810077e-01 | 0.318 |
| R-HSA-9679191 | Potential therapeutics for SARS | 4.853601e-01 | 0.314 |
| R-HSA-5685939 | HDR through MMEJ (alt-NHEJ) | 4.859552e-01 | 0.313 |
| R-HSA-9029558 | NR1H2 & NR1H3 regulate gene expression linked to lipogenesis | 4.859552e-01 | 0.313 |
| R-HSA-9933947 | Formation of the non-canonical BAF (ncBAF) complex | 4.859552e-01 | 0.313 |
| R-HSA-6804759 | Regulation of TP53 Activity through Association with Co-factors | 4.859552e-01 | 0.313 |
| R-HSA-389359 | CD28 dependent Vav1 pathway | 4.859552e-01 | 0.313 |
| R-HSA-174490 | Membrane binding and targetting of GAG proteins | 4.859552e-01 | 0.313 |
| R-HSA-170968 | Frs2-mediated activation | 4.859552e-01 | 0.313 |
| R-HSA-5676594 | TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway | 4.859552e-01 | 0.313 |
| R-HSA-6811555 | PI5P Regulates TP53 Acetylation | 4.859552e-01 | 0.313 |
| R-HSA-75035 | Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex | 4.859552e-01 | 0.313 |
| R-HSA-9818030 | NFE2L2 regulating tumorigenic genes | 4.859552e-01 | 0.313 |
| R-HSA-6788467 | IL-6-type cytokine receptor ligand interactions | 4.859552e-01 | 0.313 |
| R-HSA-1482883 | Acyl chain remodeling of DAG and TAG | 4.859552e-01 | 0.313 |
| R-HSA-9682706 | Replication of the SARS-CoV-1 genome | 4.859552e-01 | 0.313 |
| R-HSA-162582 | Signal Transduction | 4.871375e-01 | 0.312 |
| R-HSA-429914 | Deadenylation-dependent mRNA decay | 4.872156e-01 | 0.312 |
| R-HSA-9609646 | HCMV Infection | 4.876539e-01 | 0.312 |
| R-HSA-5654696 | Downstream signaling of activated FGFR2 | 4.891680e-01 | 0.311 |
| R-HSA-5654687 | Downstream signaling of activated FGFR1 | 4.891680e-01 | 0.311 |
| R-HSA-187687 | Signalling to ERKs | 4.891680e-01 | 0.311 |
| R-HSA-5693616 | Presynaptic phase of homologous DNA pairing and strand exchange | 4.891680e-01 | 0.311 |
| R-HSA-9860927 | Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZ... | 4.891680e-01 | 0.311 |
| R-HSA-6802957 | Oncogenic MAPK signaling | 4.933175e-01 | 0.307 |
| R-HSA-6794362 | Protein-protein interactions at synapses | 4.933175e-01 | 0.307 |
| R-HSA-8943724 | Regulation of PTEN gene transcription | 4.969649e-01 | 0.304 |
| R-HSA-163560 | Triglyceride catabolism | 5.015214e-01 | 0.300 |
| R-HSA-1839126 | FGFR2 mutant receptor activation | 5.015214e-01 | 0.300 |
| R-HSA-8876198 | RAB GEFs exchange GTP for GDP on RABs | 5.015722e-01 | 0.300 |
| R-HSA-177504 | Retrograde neurotrophin signalling | 5.056989e-01 | 0.296 |
| R-HSA-5654227 | Phospholipase C-mediated cascade; FGFR3 | 5.056989e-01 | 0.296 |
| R-HSA-6803211 | TP53 Regulates Transcription of Death Receptors and Ligands | 5.056989e-01 | 0.296 |
| R-HSA-9933937 | Formation of the canonical BAF (cBAF) complex | 5.056989e-01 | 0.296 |
| R-HSA-1855191 | Synthesis of IPs in the nucleus | 5.056989e-01 | 0.296 |
| R-HSA-975163 | IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation | 5.056989e-01 | 0.296 |
| R-HSA-174495 | Synthesis And Processing Of GAG, GAGPOL Polyproteins | 5.056989e-01 | 0.296 |
| R-HSA-2032785 | YAP1- and WWTR1 (TAZ)-stimulated gene expression | 5.056989e-01 | 0.296 |
| R-HSA-1483115 | Hydrolysis of LPC | 5.056989e-01 | 0.296 |
| R-HSA-399956 | CRMPs in Sema3A signaling | 5.056989e-01 | 0.296 |
| R-HSA-5578768 | Physiological factors | 5.056989e-01 | 0.296 |
| R-HSA-205043 | NRIF signals cell death from the nucleus | 5.056989e-01 | 0.296 |
| R-HSA-9856872 | Malate-aspartate shuttle | 5.056989e-01 | 0.296 |
| R-HSA-1433559 | Regulation of KIT signaling | 5.056989e-01 | 0.296 |
| R-HSA-1482798 | Acyl chain remodeling of CL | 5.056989e-01 | 0.296 |
| R-HSA-9679514 | SARS-CoV-1 Genome Replication and Transcription | 5.056989e-01 | 0.296 |
| R-HSA-180910 | Vpr-mediated nuclear import of PICs | 5.136806e-01 | 0.289 |
| R-HSA-933541 | TRAF6 mediated IRF7 activation | 5.136806e-01 | 0.289 |
| R-HSA-1989781 | PPARA activates gene expression | 5.158644e-01 | 0.287 |
| R-HSA-6784531 | tRNA processing in the nucleus | 5.161784e-01 | 0.287 |
| R-HSA-186797 | Signaling by PDGF | 5.161784e-01 | 0.287 |
| R-HSA-1266738 | Developmental Biology | 5.178752e-01 | 0.286 |
| R-HSA-447115 | Interleukin-12 family signaling | 5.179019e-01 | 0.286 |
| R-HSA-5654228 | Phospholipase C-mediated cascade; FGFR4 | 5.246855e-01 | 0.280 |
| R-HSA-73780 | RNA Polymerase III Chain Elongation | 5.246855e-01 | 0.280 |
| R-HSA-174430 | Telomere C-strand synthesis initiation | 5.246855e-01 | 0.280 |
| R-HSA-8875360 | InlB-mediated entry of Listeria monocytogenes into host cell | 5.246855e-01 | 0.280 |
| R-HSA-9027284 | Erythropoietin activates RAS | 5.246855e-01 | 0.280 |
| R-HSA-937072 | TRAF6-mediated induction of TAK1 complex within TLR4 complex | 5.246855e-01 | 0.280 |
| R-HSA-180336 | SHC1 events in EGFR signaling | 5.246855e-01 | 0.280 |
| R-HSA-111447 | Activation of BAD and translocation to mitochondria | 5.246855e-01 | 0.280 |
| R-HSA-174362 | Transport and metabolism of PAPS | 5.246855e-01 | 0.280 |
| R-HSA-399954 | Sema3A PAK dependent Axon repulsion | 5.246855e-01 | 0.280 |
| R-HSA-2173791 | TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) | 5.246855e-01 | 0.280 |
| R-HSA-168927 | TICAM1, RIP1-mediated IKK complex recruitment | 5.246855e-01 | 0.280 |
| R-HSA-9673767 | Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants | 5.246855e-01 | 0.280 |
| R-HSA-9673770 | Signaling by PDGFRA extracellular domain mutants | 5.246855e-01 | 0.280 |
| R-HSA-379401 | Dopamine clearance from the synaptic cleft | 5.246855e-01 | 0.280 |
| R-HSA-3270619 | IRF3-mediated induction of type I IFN | 5.246855e-01 | 0.280 |
| R-HSA-196780 | Biotin transport and metabolism | 5.246855e-01 | 0.280 |
| R-HSA-193639 | p75NTR signals via NF-kB | 5.246855e-01 | 0.280 |
| R-HSA-73942 | DNA Damage Reversal | 5.246855e-01 | 0.280 |
| R-HSA-380284 | Loss of proteins required for interphase microtubule organization from the centr... | 5.256363e-01 | 0.279 |
| R-HSA-380259 | Loss of Nlp from mitotic centrosomes | 5.256363e-01 | 0.279 |
| R-HSA-373755 | Semaphorin interactions | 5.256363e-01 | 0.279 |
| R-HSA-202131 | Metabolism of nitric oxide: NOS3 activation and regulation | 5.256423e-01 | 0.279 |
| R-HSA-8875878 | MET promotes cell motility | 5.256423e-01 | 0.279 |
| R-HSA-165054 | Rev-mediated nuclear export of HIV RNA | 5.256423e-01 | 0.279 |
| R-HSA-5693579 | Homologous DNA Pairing and Strand Exchange | 5.256423e-01 | 0.279 |
| R-HSA-400206 | Regulation of lipid metabolism by PPARalpha | 5.278871e-01 | 0.277 |
| R-HSA-168643 | Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali... | 5.349914e-01 | 0.272 |
| R-HSA-8964043 | Plasma lipoprotein clearance | 5.374037e-01 | 0.270 |
| R-HSA-201556 | Signaling by ALK | 5.374037e-01 | 0.270 |
| R-HSA-877300 | Interferon gamma signaling | 5.397942e-01 | 0.268 |
| R-HSA-5620912 | Anchoring of the basal body to the plasma membrane | 5.419140e-01 | 0.266 |
| R-HSA-373080 | Class B/2 (Secretin family receptors) | 5.419140e-01 | 0.266 |
| R-HSA-354194 | GRB2:SOS provides linkage to MAPK signaling for Integrins | 5.429439e-01 | 0.265 |
| R-HSA-6803207 | TP53 Regulates Transcription of Caspase Activators and Caspases | 5.429439e-01 | 0.265 |
| R-HSA-6804116 | TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest | 5.429439e-01 | 0.265 |
| R-HSA-140534 | Caspase activation via Death Receptors in the presence of ligand | 5.429439e-01 | 0.265 |
| R-HSA-169893 | Prolonged ERK activation events | 5.429439e-01 | 0.265 |
| R-HSA-5099900 | WNT5A-dependent internalization of FZD4 | 5.429439e-01 | 0.265 |
| R-HSA-210744 | Regulation of gene expression in late stage (branching morphogenesis) pancreatic... | 5.429439e-01 | 0.265 |
| R-HSA-9634600 | Regulation of glycolysis by fructose 2,6-bisphosphate metabolism | 5.429439e-01 | 0.265 |
| R-HSA-450604 | KSRP (KHSRP) binds and destabilizes mRNA | 5.429439e-01 | 0.265 |
| R-HSA-70350 | Fructose catabolism | 5.429439e-01 | 0.265 |
| R-HSA-399955 | SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion | 5.429439e-01 | 0.265 |
| R-HSA-1362300 | Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL... | 5.429439e-01 | 0.265 |
| R-HSA-9678110 | Attachment and Entry | 5.429439e-01 | 0.265 |
| R-HSA-166187 | Mitochondrial Uncoupling | 5.429439e-01 | 0.265 |
| R-HSA-73779 | RNA Polymerase II Transcription Pre-Initiation And Promoter Opening | 5.489626e-01 | 0.260 |
| R-HSA-177243 | Interactions of Rev with host cellular proteins | 5.489626e-01 | 0.260 |
| R-HSA-451927 | Interleukin-2 family signaling | 5.489626e-01 | 0.260 |
| R-HSA-8986944 | Transcriptional Regulation by MECP2 | 5.497813e-01 | 0.260 |
| R-HSA-163685 | Integration of energy metabolism | 5.528015e-01 | 0.257 |
| R-HSA-8854518 | AURKA Activation by TPX2 | 5.533829e-01 | 0.257 |
| R-HSA-9820952 | Respiratory Syncytial Virus Infection Pathway | 5.591099e-01 | 0.253 |
| R-HSA-9607240 | FLT3 Signaling | 5.603172e-01 | 0.252 |
| R-HSA-9820841 | M-decay: degradation of maternal mRNAs by maternally stored factors | 5.603172e-01 | 0.252 |
| R-HSA-1963640 | GRB2 events in ERBB2 signaling | 5.605020e-01 | 0.251 |
| R-HSA-936964 | Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) | 5.605020e-01 | 0.251 |
| R-HSA-6804114 | TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest | 5.605020e-01 | 0.251 |
| R-HSA-1250347 | SHC1 events in ERBB4 signaling | 5.605020e-01 | 0.251 |
| R-HSA-430039 | mRNA decay by 5' to 3' exoribonuclease | 5.605020e-01 | 0.251 |
| R-HSA-9702518 | STAT5 activation downstream of FLT3 ITD mutants | 5.605020e-01 | 0.251 |
| R-HSA-5660526 | Response to metal ions | 5.605020e-01 | 0.251 |
| R-HSA-9651496 | Defects of contact activation system (CAS) and kallikrein/kinin system (KKS) | 5.605020e-01 | 0.251 |
| R-HSA-392499 | Metabolism of proteins | 5.643604e-01 | 0.248 |
| R-HSA-9772573 | Late SARS-CoV-2 Infection Events | 5.653001e-01 | 0.248 |
| R-HSA-167162 | RNA Polymerase II HIV Promoter Escape | 5.714661e-01 | 0.243 |
| R-HSA-167161 | HIV Transcription Initiation | 5.714661e-01 | 0.243 |
| R-HSA-75953 | RNA Polymerase II Transcription Initiation | 5.714661e-01 | 0.243 |
| R-HSA-9615017 | FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes | 5.714661e-01 | 0.243 |
| R-HSA-6811438 | Intra-Golgi traffic | 5.714661e-01 | 0.243 |
| R-HSA-5675221 | Negative regulation of MAPK pathway | 5.714661e-01 | 0.243 |
| R-HSA-9683701 | Translation of Structural Proteins | 5.714661e-01 | 0.243 |
| R-HSA-174437 | Removal of the Flap Intermediate from the C-strand | 5.773867e-01 | 0.239 |
| R-HSA-5654219 | Phospholipase C-mediated cascade: FGFR1 | 5.773867e-01 | 0.239 |
| R-HSA-5358606 | Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) | 5.773867e-01 | 0.239 |
| R-HSA-1963642 | PI3K events in ERBB2 signaling | 5.773867e-01 | 0.239 |
| R-HSA-2408550 | Metabolism of ingested H2SeO4 and H2SeO3 into H2Se | 5.773867e-01 | 0.239 |
| R-HSA-9768759 | Regulation of NPAS4 gene expression | 5.773867e-01 | 0.239 |
| R-HSA-209905 | Catecholamine biosynthesis | 5.773867e-01 | 0.239 |
| R-HSA-3229121 | Glycogen storage diseases | 5.773867e-01 | 0.239 |
| R-HSA-9694686 | Replication of the SARS-CoV-2 genome | 5.773867e-01 | 0.239 |
| R-HSA-9007101 | Rab regulation of trafficking | 5.819677e-01 | 0.235 |
| R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | 5.831460e-01 | 0.234 |
| R-HSA-168928 | DDX58/IFIH1-mediated induction of interferon-alpha/beta | 5.880151e-01 | 0.231 |
| R-HSA-73776 | RNA Polymerase II Promoter Escape | 5.931435e-01 | 0.227 |
| R-HSA-1433557 | Signaling by SCF-KIT | 5.931435e-01 | 0.227 |
| R-HSA-9637690 | Response of Mtb to phagocytosis | 5.931435e-01 | 0.227 |
| R-HSA-2173789 | TGF-beta receptor signaling activates SMADs | 5.931435e-01 | 0.227 |
| R-HSA-180292 | GAB1 signalosome | 5.936236e-01 | 0.226 |
| R-HSA-73980 | RNA Polymerase III Transcription Termination | 5.936236e-01 | 0.226 |
| R-HSA-9614657 | FOXO-mediated transcription of cell death genes | 5.936236e-01 | 0.226 |
| R-HSA-6804760 | Regulation of TP53 Activity through Methylation | 5.936236e-01 | 0.226 |
| R-HSA-156711 | Polo-like kinase mediated events | 5.936236e-01 | 0.226 |
| R-HSA-1839117 | Signaling by cytosolic FGFR1 fusion mutants | 5.936236e-01 | 0.226 |
| R-HSA-416993 | Trafficking of GluR2-containing AMPA receptors | 5.936236e-01 | 0.226 |
| R-HSA-4419969 | Depolymerization of the Nuclear Lamina | 5.936236e-01 | 0.226 |
| R-HSA-428643 | Organic anion transport by SLC5/17/25 transporters | 5.936236e-01 | 0.226 |
| R-HSA-9679504 | Translation of Replicase and Assembly of the Replication Transcription Complex | 5.936236e-01 | 0.226 |
| R-HSA-3928664 | Ephrin signaling | 5.936236e-01 | 0.226 |
| R-HSA-9705671 | SARS-CoV-2 activates/modulates innate and adaptive immune responses | 5.960468e-01 | 0.225 |
| R-HSA-381340 | Transcriptional regulation of white adipocyte differentiation | 6.027672e-01 | 0.220 |
| R-HSA-2172127 | DAP12 interactions | 6.036711e-01 | 0.219 |
| R-HSA-69236 | G1 Phase | 6.036711e-01 | 0.219 |
| R-HSA-69231 | Cyclin D associated events in G1 | 6.036711e-01 | 0.219 |
| R-HSA-373752 | Netrin-1 signaling | 6.036711e-01 | 0.219 |
| R-HSA-8864260 | Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors | 6.036711e-01 | 0.219 |
| R-HSA-5654710 | PI-3K cascade:FGFR3 | 6.092377e-01 | 0.215 |
| R-HSA-912631 | Regulation of signaling by CBL | 6.092377e-01 | 0.215 |
| R-HSA-937041 | IKK complex recruitment mediated by RIP1 | 6.092377e-01 | 0.215 |
| R-HSA-429958 | mRNA decay by 3' to 5' exoribonuclease | 6.092377e-01 | 0.215 |
| R-HSA-110320 | Translesion Synthesis by POLH | 6.092377e-01 | 0.215 |
| R-HSA-113510 | E2F mediated regulation of DNA replication | 6.092377e-01 | 0.215 |
| R-HSA-881907 | Gastrin-CREB signalling pathway via PKC and MAPK | 6.092377e-01 | 0.215 |
| R-HSA-9913635 | Strand-asynchronous mitochondrial DNA replication | 6.092377e-01 | 0.215 |
| R-HSA-1237112 | Methionine salvage pathway | 6.092377e-01 | 0.215 |
| R-HSA-1834941 | STING mediated induction of host immune responses | 6.092377e-01 | 0.215 |
| R-HSA-9671793 | Diseases of hemostasis | 6.092377e-01 | 0.215 |
| R-HSA-9694682 | SARS-CoV-2 Genome Replication and Transcription | 6.092377e-01 | 0.215 |
| R-HSA-76042 | RNA Polymerase II Transcription Initiation And Promoter Clearance | 6.139914e-01 | 0.212 |
| R-HSA-9824585 | Regulation of MITF-M-dependent genes involved in pigmentation | 6.139914e-01 | 0.212 |
| R-HSA-380270 | Recruitment of mitotic centrosome proteins and complexes | 6.142059e-01 | 0.212 |
| R-HSA-204998 | Cell death signalling via NRAGE, NRIF and NADE | 6.142059e-01 | 0.212 |
| R-HSA-422356 | Regulation of insulin secretion | 6.171955e-01 | 0.210 |
| R-HSA-6781823 | Formation of TC-NER Pre-Incision Complex | 6.241047e-01 | 0.205 |
| R-HSA-9839373 | Signaling by TGFBR3 | 6.241047e-01 | 0.205 |
| R-HSA-2514859 | Inactivation, recovery and regulation of the phototransduction cascade | 6.241047e-01 | 0.205 |
| R-HSA-75153 | Apoptotic execution phase | 6.241047e-01 | 0.205 |
| R-HSA-1362277 | Transcription of E2F targets under negative control by DREAM complex | 6.242528e-01 | 0.205 |
| R-HSA-5654720 | PI-3K cascade:FGFR4 | 6.242528e-01 | 0.205 |
| R-HSA-5654221 | Phospholipase C-mediated cascade; FGFR2 | 6.242528e-01 | 0.205 |
| R-HSA-389513 | Co-inhibition by CTLA4 | 6.242528e-01 | 0.205 |
| R-HSA-6807004 | Negative regulation of MET activity | 6.242528e-01 | 0.205 |
| R-HSA-5620916 | VxPx cargo-targeting to cilium | 6.242528e-01 | 0.205 |
| R-HSA-5620922 | BBSome-mediated cargo-targeting to cilium | 6.242528e-01 | 0.205 |
| R-HSA-1482922 | Acyl chain remodelling of PI | 6.242528e-01 | 0.205 |
| R-HSA-71288 | Creatine metabolism | 6.242528e-01 | 0.205 |
| R-HSA-3322077 | Glycogen synthesis | 6.242528e-01 | 0.205 |
| R-HSA-9629569 | Protein hydroxylation | 6.242528e-01 | 0.205 |
| R-HSA-373753 | Nephrin family interactions | 6.242528e-01 | 0.205 |
| R-HSA-6809371 | Formation of the cornified envelope | 6.274923e-01 | 0.202 |
| R-HSA-380287 | Centrosome maturation | 6.305246e-01 | 0.200 |
| R-HSA-70171 | Glycolysis | 6.312926e-01 | 0.200 |
| R-HSA-437239 | Recycling pathway of L1 | 6.340117e-01 | 0.198 |
| R-HSA-1483191 | Synthesis of PC | 6.340117e-01 | 0.198 |
| R-HSA-3928665 | EPH-ephrin mediated repulsion of cells | 6.340117e-01 | 0.198 |
| R-HSA-5357786 | TNFR1-induced proapoptotic signaling | 6.386918e-01 | 0.195 |
| R-HSA-9013695 | NOTCH4 Intracellular Domain Regulates Transcription | 6.386918e-01 | 0.195 |
| R-HSA-5654704 | SHC-mediated cascade:FGFR3 | 6.386918e-01 | 0.195 |
| R-HSA-167044 | Signalling to RAS | 6.386918e-01 | 0.195 |
| R-HSA-2979096 | NOTCH2 Activation and Transmission of Signal to the Nucleus | 6.386918e-01 | 0.195 |
| R-HSA-2161541 | Abacavir metabolism | 6.386918e-01 | 0.195 |
| R-HSA-9819196 | Zygotic genome activation (ZGA) | 6.386918e-01 | 0.195 |
| R-HSA-210991 | Basigin interactions | 6.386918e-01 | 0.195 |
| R-HSA-1482925 | Acyl chain remodelling of PG | 6.386918e-01 | 0.195 |
| R-HSA-9939291 | Matriglycan biosynthesis on DAG1 | 6.386918e-01 | 0.195 |
| R-HSA-9636383 | Prevention of phagosomal-lysosomal fusion | 6.386918e-01 | 0.195 |
| R-HSA-1483206 | Glycerophospholipid biosynthesis | 6.394527e-01 | 0.194 |
| R-HSA-9856651 | MITF-M-dependent gene expression | 6.426159e-01 | 0.192 |
| R-HSA-9031628 | NGF-stimulated transcription | 6.437133e-01 | 0.191 |
| R-HSA-5603041 | IRAK4 deficiency (TLR2/4) | 6.525767e-01 | 0.185 |
| R-HSA-76066 | RNA Polymerase III Transcription Initiation From Type 2 Promoter | 6.525767e-01 | 0.185 |
| R-HSA-5654719 | SHC-mediated cascade:FGFR4 | 6.525767e-01 | 0.185 |
| R-HSA-8876384 | Listeria monocytogenes entry into host cells | 6.525767e-01 | 0.185 |
| R-HSA-189085 | Digestion of dietary carbohydrate | 6.525767e-01 | 0.185 |
| R-HSA-5654706 | FRS-mediated FGFR3 signaling | 6.525767e-01 | 0.185 |
| R-HSA-9705462 | Inactivation of CSF3 (G-CSF) signaling | 6.525767e-01 | 0.185 |
| R-HSA-9671555 | Signaling by PDGFR in disease | 6.525767e-01 | 0.185 |
| R-HSA-2995383 | Initiation of Nuclear Envelope (NE) Reformation | 6.525767e-01 | 0.185 |
| R-HSA-175474 | Assembly Of The HIV Virion | 6.525767e-01 | 0.185 |
| R-HSA-9694614 | Attachment and Entry | 6.525767e-01 | 0.185 |
| R-HSA-109704 | PI3K Cascade | 6.625052e-01 | 0.179 |
| R-HSA-9748787 | Azathioprine ADME | 6.625052e-01 | 0.179 |
| R-HSA-5654689 | PI-3K cascade:FGFR1 | 6.659289e-01 | 0.177 |
| R-HSA-350054 | Notch-HLH transcription pathway | 6.659289e-01 | 0.177 |
| R-HSA-9938206 | Developmental Lineage of Mammary Stem Cells | 6.659289e-01 | 0.177 |
| R-HSA-6803205 | TP53 regulates transcription of several additional cell death genes whose specif... | 6.659289e-01 | 0.177 |
| R-HSA-6804115 | TP53 regulates transcription of additional cell cycle genes whose exact role in ... | 6.659289e-01 | 0.177 |
| R-HSA-76071 | RNA Polymerase III Transcription Initiation From Type 3 Promoter | 6.659289e-01 | 0.177 |
| R-HSA-76061 | RNA Polymerase III Transcription Initiation From Type 1 Promoter | 6.659289e-01 | 0.177 |
| R-HSA-3238698 | WNT ligand biogenesis and trafficking | 6.659289e-01 | 0.177 |
| R-HSA-5654712 | FRS-mediated FGFR4 signaling | 6.659289e-01 | 0.177 |
| R-HSA-9670439 | Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT m... | 6.659289e-01 | 0.177 |
| R-HSA-8964038 | LDL clearance | 6.659289e-01 | 0.177 |
| R-HSA-5652084 | Fructose metabolism | 6.659289e-01 | 0.177 |
| R-HSA-71384 | Ethanol oxidation | 6.659289e-01 | 0.177 |
| R-HSA-9669938 | Signaling by KIT in disease | 6.659289e-01 | 0.177 |
| R-HSA-9694676 | Translation of Replicase and Assembly of the Replication Transcription Complex | 6.659289e-01 | 0.177 |
| R-HSA-9833482 | PKR-mediated signaling | 6.691994e-01 | 0.174 |
| R-HSA-2514856 | The phototransduction cascade | 6.715984e-01 | 0.173 |
| R-HSA-9006934 | Signaling by Receptor Tyrosine Kinases | 6.726102e-01 | 0.172 |
| R-HSA-77075 | RNA Pol II CTD phosphorylation and interaction with CE | 6.787688e-01 | 0.168 |
| R-HSA-167160 | RNA Pol II CTD phosphorylation and interaction with CE during HIV infection | 6.787688e-01 | 0.168 |
| R-HSA-912526 | Interleukin receptor SHC signaling | 6.787688e-01 | 0.168 |
| R-HSA-9634638 | Estrogen-dependent nuclear events downstream of ESR-membrane signaling | 6.787688e-01 | 0.168 |
| R-HSA-9648895 | Response of EIF2AK1 (HRI) to heme deficiency | 6.787688e-01 | 0.168 |
| R-HSA-9830674 | Formation of the ureteric bud | 6.787688e-01 | 0.168 |
| R-HSA-3000170 | Syndecan interactions | 6.787688e-01 | 0.168 |
| R-HSA-982772 | Growth hormone receptor signaling | 6.787688e-01 | 0.168 |
| R-HSA-1852241 | Organelle biogenesis and maintenance | 6.791166e-01 | 0.168 |
| R-HSA-9843745 | Adipogenesis | 6.814122e-01 | 0.167 |
| R-HSA-1483257 | Phospholipid metabolism | 6.880521e-01 | 0.162 |
| R-HSA-429947 | Deadenylation of mRNA | 6.911159e-01 | 0.160 |
| R-HSA-9703648 | Signaling by FLT3 ITD and TKD mutants | 6.911159e-01 | 0.160 |
| R-HSA-5654688 | SHC-mediated cascade:FGFR1 | 6.911159e-01 | 0.160 |
| R-HSA-933542 | TRAF6 mediated NF-kB activation | 6.911159e-01 | 0.160 |
| R-HSA-6783589 | Interleukin-6 family signaling | 6.911159e-01 | 0.160 |
| R-HSA-9730414 | MITF-M-regulated melanocyte development | 6.912374e-01 | 0.160 |
| R-HSA-9006936 | Signaling by TGFB family members | 6.960687e-01 | 0.157 |
| R-HSA-2565942 | Regulation of PLK1 Activity at G2/M Transition | 6.979458e-01 | 0.156 |
| R-HSA-5654695 | PI-3K cascade:FGFR2 | 7.029891e-01 | 0.153 |
| R-HSA-3214842 | HDMs demethylate histones | 7.029891e-01 | 0.153 |
| R-HSA-174411 | Polymerase switching on the C-strand of the telomere | 7.029891e-01 | 0.153 |
| R-HSA-5218921 | VEGFR2 mediated cell proliferation | 7.029891e-01 | 0.153 |
| R-HSA-420029 | Tight junction interactions | 7.029891e-01 | 0.153 |
| R-HSA-1482801 | Acyl chain remodelling of PS | 7.029891e-01 | 0.153 |
| R-HSA-9839394 | TGFBR3 expression | 7.029891e-01 | 0.153 |
| R-HSA-5654693 | FRS-mediated FGFR1 signaling | 7.029891e-01 | 0.153 |
| R-HSA-2160916 | Hyaluronan degradation | 7.029891e-01 | 0.153 |
| R-HSA-400685 | Sema4D in semaphorin signaling | 7.029891e-01 | 0.153 |
| R-HSA-6782210 | Gap-filling DNA repair synthesis and ligation in TC-NER | 7.141110e-01 | 0.146 |
| R-HSA-209776 | Metabolism of amine-derived hormones | 7.141110e-01 | 0.146 |
| R-HSA-193648 | NRAGE signals death through JNK | 7.141110e-01 | 0.146 |
| R-HSA-9615933 | Postmitotic nuclear pore complex (NPC) reformation | 7.144066e-01 | 0.146 |
| R-HSA-525793 | Myogenesis | 7.144066e-01 | 0.146 |
| R-HSA-5689901 | Metalloprotease DUBs | 7.144066e-01 | 0.146 |
| R-HSA-5357769 | Caspase activation via extrinsic apoptotic signalling pathway | 7.144066e-01 | 0.146 |
| R-HSA-1660514 | Synthesis of PIPs at the Golgi membrane | 7.144066e-01 | 0.146 |
| R-HSA-3295583 | TRP channels | 7.144066e-01 | 0.146 |
| R-HSA-2161522 | Abacavir ADME | 7.144066e-01 | 0.146 |
| R-HSA-9637687 | Suppression of phagosomal maturation | 7.144066e-01 | 0.146 |
| R-HSA-1483249 | Inositol phosphate metabolism | 7.145370e-01 | 0.146 |
| R-HSA-5619115 | Disorders of transmembrane transporters | 7.171819e-01 | 0.144 |
| R-HSA-163841 | Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation | 7.182347e-01 | 0.144 |
| R-HSA-112399 | IRS-mediated signalling | 7.220380e-01 | 0.141 |
| R-HSA-2980766 | Nuclear Envelope Breakdown | 7.220380e-01 | 0.141 |
| R-HSA-1483166 | Synthesis of PA | 7.220380e-01 | 0.141 |
| R-HSA-174414 | Processive synthesis on the C-strand of the telomere | 7.253859e-01 | 0.139 |
| R-HSA-6803204 | TP53 Regulates Transcription of Genes Involved in Cytochrome C Release | 7.253859e-01 | 0.139 |
| R-HSA-73863 | RNA Polymerase I Transcription Termination | 7.253859e-01 | 0.139 |
| R-HSA-445095 | Interaction between L1 and Ankyrins | 7.253859e-01 | 0.139 |
| R-HSA-5654699 | SHC-mediated cascade:FGFR2 | 7.253859e-01 | 0.139 |
| R-HSA-8949613 | Cristae formation | 7.253859e-01 | 0.139 |
| R-HSA-83936 | Transport of nucleosides and free purine and pyrimidine bases across the plasma ... | 7.253859e-01 | 0.139 |
| R-HSA-389357 | CD28 dependent PI3K/Akt signaling | 7.253859e-01 | 0.139 |
| R-HSA-193807 | Synthesis of bile acids and bile salts via 27-hydroxycholesterol | 7.253859e-01 | 0.139 |
| R-HSA-8866652 | Synthesis of active ubiquitin: roles of E1 and E2 enzymes | 7.253859e-01 | 0.139 |
| R-HSA-264876 | Insulin processing | 7.253859e-01 | 0.139 |
| R-HSA-6782135 | Dual incision in TC-NER | 7.297788e-01 | 0.137 |
| R-HSA-9029569 | NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflu... | 7.297788e-01 | 0.137 |
| R-HSA-380320 | Recruitment of NuMA to mitotic centrosomes | 7.311635e-01 | 0.136 |
| R-HSA-9619483 | Activation of AMPK downstream of NMDARs | 7.359438e-01 | 0.133 |
| R-HSA-171319 | Telomere Extension By Telomerase | 7.359438e-01 | 0.133 |
| R-HSA-5654700 | FRS-mediated FGFR2 signaling | 7.359438e-01 | 0.133 |
| R-HSA-380994 | ATF4 activates genes in response to endoplasmic reticulum stress | 7.359438e-01 | 0.133 |
| R-HSA-73614 | Pyrimidine salvage | 7.359438e-01 | 0.133 |
| R-HSA-8940973 | RUNX2 regulates osteoblast differentiation | 7.359438e-01 | 0.133 |
| R-HSA-194441 | Metabolism of non-coding RNA | 7.373360e-01 | 0.132 |
| R-HSA-191859 | snRNP Assembly | 7.373360e-01 | 0.132 |
| R-HSA-9033241 | Peroxisomal protein import | 7.373360e-01 | 0.132 |
| R-HSA-8979227 | Triglyceride metabolism | 7.373360e-01 | 0.132 |
| R-HSA-4420097 | VEGFA-VEGFR2 Pathway | 7.426275e-01 | 0.129 |
| R-HSA-2644602 | Signaling by NOTCH1 PEST Domain Mutants in Cancer | 7.447123e-01 | 0.128 |
| R-HSA-2894862 | Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants | 7.447123e-01 | 0.128 |
| R-HSA-2644606 | Constitutive Signaling by NOTCH1 PEST Domain Mutants | 7.447123e-01 | 0.128 |
| R-HSA-2894858 | Signaling by NOTCH1 HD+PEST Domain Mutants in Cancer | 7.447123e-01 | 0.128 |
| R-HSA-2644603 | Signaling by NOTCH1 in Cancer | 7.447123e-01 | 0.128 |
| R-HSA-1660661 | Sphingolipid de novo biosynthesis | 7.447123e-01 | 0.128 |
| R-HSA-209968 | Thyroxine biosynthesis | 7.460963e-01 | 0.127 |
| R-HSA-917729 | Endosomal Sorting Complex Required For Transport (ESCRT) | 7.460963e-01 | 0.127 |
| R-HSA-9759475 | Regulation of CDH11 Expression and Function | 7.460963e-01 | 0.127 |
| R-HSA-373760 | L1CAM interactions | 7.479861e-01 | 0.126 |
| R-HSA-2428928 | IRS-related events triggered by IGF1R | 7.519103e-01 | 0.124 |
| R-HSA-168325 | Viral Messenger RNA Synthesis | 7.519103e-01 | 0.124 |
| R-HSA-70326 | Glucose metabolism | 7.532591e-01 | 0.123 |
| R-HSA-5619107 | Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC... | 7.558591e-01 | 0.122 |
| R-HSA-9013508 | NOTCH3 Intracellular Domain Regulates Transcription | 7.558591e-01 | 0.122 |
| R-HSA-76046 | RNA Polymerase III Transcription Initiation | 7.558591e-01 | 0.122 |
| R-HSA-1250196 | SHC1 events in ERBB2 signaling | 7.558591e-01 | 0.122 |
| R-HSA-888590 | GABA synthesis, release, reuptake and degradation | 7.558591e-01 | 0.122 |
| R-HSA-8863795 | Downregulation of ERBB2 signaling | 7.558591e-01 | 0.122 |
| R-HSA-1474151 | Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation | 7.558591e-01 | 0.122 |
| R-HSA-112311 | Neurotransmitter clearance | 7.558591e-01 | 0.122 |
| R-HSA-375165 | NCAM signaling for neurite out-growth | 7.589330e-01 | 0.120 |
| R-HSA-1660499 | Synthesis of PIPs at the plasma membrane | 7.589330e-01 | 0.120 |
| R-HSA-2682334 | EPH-Ephrin signaling | 7.614409e-01 | 0.118 |
| R-HSA-1855196 | IP3 and IP4 transport between cytosol and nucleus | 7.652471e-01 | 0.116 |
| R-HSA-1855229 | IP6 and IP7 transport between cytosol and nucleus | 7.652471e-01 | 0.116 |
| R-HSA-162588 | Budding and maturation of HIV virion | 7.652471e-01 | 0.116 |
| R-HSA-399719 | Trafficking of AMPA receptors | 7.652471e-01 | 0.116 |
| R-HSA-936440 | Negative regulators of DDX58/IFIH1 signaling | 7.652471e-01 | 0.116 |
| R-HSA-6790901 | rRNA modification in the nucleus and cytosol | 7.657830e-01 | 0.116 |
| R-HSA-8848021 | Signaling by PTK6 | 7.657830e-01 | 0.116 |
| R-HSA-9006927 | Signaling by Non-Receptor Tyrosine Kinases | 7.657830e-01 | 0.116 |
| R-HSA-74751 | Insulin receptor signalling cascade | 7.724633e-01 | 0.112 |
| R-HSA-2428924 | IGF1R signaling cascade | 7.724633e-01 | 0.112 |
| R-HSA-936837 | Ion transport by P-type ATPases | 7.724633e-01 | 0.112 |
| R-HSA-199977 | ER to Golgi Anterograde Transport | 7.727262e-01 | 0.112 |
| R-HSA-1538133 | G0 and Early G1 | 7.742747e-01 | 0.111 |
| R-HSA-8931838 | DAG1 glycosylations | 7.742747e-01 | 0.111 |
| R-HSA-2404192 | Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) | 7.789768e-01 | 0.108 |
| R-HSA-1855170 | IPs transport between nucleus and cytosol | 7.829556e-01 | 0.106 |
| R-HSA-6804758 | Regulation of TP53 Activity through Acetylation | 7.829556e-01 | 0.106 |
| R-HSA-5609975 | Diseases associated with glycosylation precursor biosynthesis | 7.829556e-01 | 0.106 |
| R-HSA-159418 | Recycling of bile acids and salts | 7.829556e-01 | 0.106 |
| R-HSA-399721 | Glutamate binding, activation of AMPA receptors and synaptic plasticity | 7.829556e-01 | 0.106 |
| R-HSA-9764260 | Regulation of Expression and Function of Type II Classical Cadherins | 7.829556e-01 | 0.106 |
| R-HSA-354192 | Integrin signaling | 7.829556e-01 | 0.106 |
| R-HSA-9022692 | Regulation of MECP2 expression and activity | 7.829556e-01 | 0.106 |
| R-HSA-6811558 | PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling | 7.831253e-01 | 0.106 |
| R-HSA-6782315 | tRNA modification in the nucleus and cytosol | 7.853265e-01 | 0.105 |
| R-HSA-170822 | Regulation of Glucokinase by Glucokinase Regulatory Protein | 7.913032e-01 | 0.102 |
| R-HSA-1482788 | Acyl chain remodelling of PC | 7.913032e-01 | 0.102 |
| R-HSA-114508 | Effects of PIP2 hydrolysis | 7.913032e-01 | 0.102 |
| R-HSA-199220 | Vitamin B5 (pantothenate) metabolism | 7.913032e-01 | 0.102 |
| R-HSA-5223345 | Miscellaneous transport and binding events | 7.913032e-01 | 0.102 |
| R-HSA-189483 | Heme degradation | 7.913032e-01 | 0.102 |
| R-HSA-194138 | Signaling by VEGF | 7.969455e-01 | 0.099 |
| R-HSA-180746 | Nuclear import of Rev protein | 7.993302e-01 | 0.097 |
| R-HSA-2142845 | Hyaluronan metabolism | 7.993302e-01 | 0.097 |
| R-HSA-5365859 | RA biosynthesis pathway | 7.993302e-01 | 0.097 |
| R-HSA-5686938 | Regulation of TLR by endogenous ligand | 7.993302e-01 | 0.097 |
| R-HSA-2393930 | Phosphate bond hydrolysis by NUDT proteins | 7.993302e-01 | 0.097 |
| R-HSA-114608 | Platelet degranulation | 8.057588e-01 | 0.094 |
| R-HSA-3301854 | Nuclear Pore Complex (NPC) Disassembly | 8.070489e-01 | 0.093 |
| R-HSA-917977 | Transferrin endocytosis and recycling | 8.070489e-01 | 0.093 |
| R-HSA-1482839 | Acyl chain remodelling of PE | 8.070489e-01 | 0.093 |
| R-HSA-381042 | PERK regulates gene expression | 8.070489e-01 | 0.093 |
| R-HSA-8956319 | Nucleotide catabolism | 8.142590e-01 | 0.089 |
| R-HSA-749476 | RNA Polymerase III Abortive And Retractive Initiation | 8.144712e-01 | 0.089 |
| R-HSA-74158 | RNA Polymerase III Transcription | 8.144712e-01 | 0.089 |
| R-HSA-432720 | Lysosome Vesicle Biogenesis | 8.144712e-01 | 0.089 |
| R-HSA-114604 | GPVI-mediated activation cascade | 8.144712e-01 | 0.089 |
| R-HSA-8941326 | RUNX2 regulates bone development | 8.144712e-01 | 0.089 |
| R-HSA-8978934 | Metabolism of cofactors | 8.147212e-01 | 0.089 |
| R-HSA-5620920 | Cargo trafficking to the periciliary membrane | 8.147212e-01 | 0.089 |
| R-HSA-9856649 | Transcriptional and post-translational regulation of MITF-M expression and activ... | 8.147212e-01 | 0.089 |
| R-HSA-1483255 | PI Metabolism | 8.183297e-01 | 0.087 |
| R-HSA-199418 | Negative regulation of the PI3K/AKT network | 8.183935e-01 | 0.087 |
| R-HSA-198725 | Nuclear Events (kinase and transcription factor activation) | 8.201503e-01 | 0.086 |
| R-HSA-499943 | Interconversion of nucleotide di- and triphosphates | 8.201503e-01 | 0.086 |
| R-HSA-74259 | Purine catabolism | 8.201503e-01 | 0.086 |
| R-HSA-1296072 | Voltage gated Potassium channels | 8.216085e-01 | 0.085 |
| R-HSA-6802948 | Signaling by high-kinase activity BRAF mutants | 8.216085e-01 | 0.085 |
| R-HSA-549127 | SLC-mediated transport of organic cations | 8.216085e-01 | 0.085 |
| R-HSA-3769402 | Deactivation of the beta-catenin transactivating complex | 8.216085e-01 | 0.085 |
| R-HSA-196757 | Metabolism of folate and pterines | 8.216085e-01 | 0.085 |
| R-HSA-5663084 | Diseases of carbohydrate metabolism | 8.254364e-01 | 0.083 |
| R-HSA-5617833 | Cilium Assembly | 8.261966e-01 | 0.083 |
| R-HSA-597592 | Post-translational protein modification | 8.264617e-01 | 0.083 |
| R-HSA-1474228 | Degradation of the extracellular matrix | 8.303449e-01 | 0.081 |
| R-HSA-425397 | Transport of vitamins, nucleosides, and related molecules | 8.305824e-01 | 0.081 |
| R-HSA-9833110 | RSV-host interactions | 8.316915e-01 | 0.080 |
| R-HSA-76005 | Response to elevated platelet cytosolic Ca2+ | 8.341806e-01 | 0.079 |
| R-HSA-9648002 | RAS processing | 8.350710e-01 | 0.078 |
| R-HSA-9820965 | Respiratory syncytial virus (RSV) genome replication, transcription and translat... | 8.350710e-01 | 0.078 |
| R-HSA-6781827 | Transcription-Coupled Nucleotide Excision Repair (TC-NER) | 8.355914e-01 | 0.078 |
| R-HSA-202433 | Generation of second messenger molecules | 8.414169e-01 | 0.075 |
| R-HSA-5602358 | Diseases associated with the TLR signaling cascade | 8.414169e-01 | 0.075 |
| R-HSA-5260271 | Diseases of Immune System | 8.414169e-01 | 0.075 |
| R-HSA-9024446 | NR1H2 and NR1H3-mediated signaling | 8.452096e-01 | 0.073 |
| R-HSA-9694635 | Translation of Structural Proteins | 8.452096e-01 | 0.073 |
| R-HSA-168271 | Transport of Ribonucleoproteins into the Host Nucleus | 8.475190e-01 | 0.072 |
| R-HSA-110313 | Translesion synthesis by Y family DNA polymerases bypasses lesions on DNA templa... | 8.475190e-01 | 0.072 |
| R-HSA-73817 | Purine ribonucleoside monophosphate biosynthesis | 8.475190e-01 | 0.072 |
| R-HSA-73933 | Resolution of Abasic Sites (AP sites) | 8.475190e-01 | 0.072 |
| R-HSA-2672351 | Stimuli-sensing channels | 8.481880e-01 | 0.072 |
| R-HSA-9656223 | Signaling by RAF1 mutants | 8.533867e-01 | 0.069 |
| R-HSA-174417 | Telomere C-strand (Lagging Strand) Synthesis | 8.533867e-01 | 0.069 |
| R-HSA-5674135 | MAP2K and MAPK activation | 8.533867e-01 | 0.069 |
| R-HSA-442660 | SLC-mediated transport of neurotransmitters | 8.533867e-01 | 0.069 |
| R-HSA-6806834 | Signaling by MET | 8.586811e-01 | 0.066 |
| R-HSA-2995410 | Nuclear Envelope (NE) Reassembly | 8.586811e-01 | 0.066 |
| R-HSA-73762 | RNA Polymerase I Transcription Initiation | 8.590289e-01 | 0.066 |
| R-HSA-512988 | Interleukin-3, Interleukin-5 and GM-CSF signaling | 8.590289e-01 | 0.066 |
| R-HSA-111996 | Ca-dependent events | 8.590289e-01 | 0.066 |
| R-HSA-379716 | Cytosolic tRNA aminoacylation | 8.590289e-01 | 0.066 |
| R-HSA-72306 | tRNA processing | 8.615673e-01 | 0.065 |
| R-HSA-2871796 | FCERI mediated MAPK activation | 8.632614e-01 | 0.064 |
| R-HSA-73621 | Pyrimidine catabolism | 8.644543e-01 | 0.063 |
| R-HSA-190828 | Gap junction trafficking | 8.696713e-01 | 0.061 |
| R-HSA-9662851 | Anti-inflammatory response favouring Leishmania parasite infection | 8.703081e-01 | 0.060 |
| R-HSA-9664433 | Leishmania parasite growth and survival | 8.703081e-01 | 0.060 |
| R-HSA-15869 | Metabolism of nucleotides | 8.728439e-01 | 0.059 |
| R-HSA-2029480 | Fcgamma receptor (FCGR) dependent phagocytosis | 8.731162e-01 | 0.059 |
| R-HSA-168333 | NEP/NS2 Interacts with the Cellular Export Machinery | 8.746877e-01 | 0.058 |
| R-HSA-76009 | Platelet Aggregation (Plug Formation) | 8.746877e-01 | 0.058 |
| R-HSA-3560782 | Diseases associated with glycosaminoglycan metabolism | 8.746877e-01 | 0.058 |
| R-HSA-1489509 | DAG and IP3 signaling | 8.746877e-01 | 0.058 |
| R-HSA-9649948 | Signaling downstream of RAS mutants | 8.795114e-01 | 0.056 |
| R-HSA-6802955 | Paradoxical activation of RAF signaling by kinase inactive BRAF | 8.795114e-01 | 0.056 |
| R-HSA-6802946 | Signaling by moderate kinase activity BRAF mutants | 8.795114e-01 | 0.056 |
| R-HSA-6802949 | Signaling by RAS mutants | 8.795114e-01 | 0.056 |
| R-HSA-168274 | Export of Viral Ribonucleoproteins from Nucleus | 8.795114e-01 | 0.056 |
| R-HSA-9861718 | Regulation of pyruvate metabolism | 8.795114e-01 | 0.056 |
| R-HSA-2029485 | Role of phospholipids in phagocytosis | 8.802428e-01 | 0.055 |
| R-HSA-2980736 | Peptide hormone metabolism | 8.864934e-01 | 0.052 |
| R-HSA-9725371 | Nuclear events stimulated by ALK signaling in cancer | 8.886096e-01 | 0.051 |
| R-HSA-70268 | Pyruvate metabolism | 8.895251e-01 | 0.051 |
| R-HSA-112314 | Neurotransmitter receptors and postsynaptic signal transmission | 8.906099e-01 | 0.050 |
| R-HSA-2122947 | NOTCH1 Intracellular Domain Regulates Transcription | 8.928982e-01 | 0.049 |
| R-HSA-157858 | Gap junction trafficking and regulation | 8.928982e-01 | 0.049 |
| R-HSA-532668 | N-glycan trimming in the ER and Calnexin/Calreticulin cycle | 8.928982e-01 | 0.049 |
| R-HSA-9864848 | Complex IV assembly | 9.009870e-01 | 0.045 |
| R-HSA-109582 | Hemostasis | 9.031109e-01 | 0.044 |
| R-HSA-9634815 | Transcriptional Regulation by NPAS4 | 9.047998e-01 | 0.043 |
| R-HSA-74752 | Signaling by Insulin receptor | 9.084271e-01 | 0.042 |
| R-HSA-174824 | Plasma lipoprotein assembly, remodeling, and clearance | 9.084271e-01 | 0.042 |
| R-HSA-445355 | Smooth Muscle Contraction | 9.084659e-01 | 0.042 |
| R-HSA-9639288 | Amino acids regulate mTORC1 | 9.084659e-01 | 0.042 |
| R-HSA-8956320 | Nucleotide biosynthesis | 9.084659e-01 | 0.042 |
| R-HSA-983712 | Ion channel transport | 9.094102e-01 | 0.041 |
| R-HSA-71291 | Metabolism of amino acids and derivatives | 9.123716e-01 | 0.040 |
| R-HSA-2219530 | Constitutive Signaling by Aberrant PI3K in Cancer | 9.140245e-01 | 0.039 |
| R-HSA-1793185 | Chondroitin sulfate/dermatan sulfate metabolism | 9.153806e-01 | 0.038 |
| R-HSA-8935690 | Digestion | 9.186399e-01 | 0.037 |
| R-HSA-9662361 | Sensory processing of sound by outer hair cells of the cochlea | 9.186399e-01 | 0.037 |
| R-HSA-6791312 | TP53 Regulates Transcription of Cell Cycle Genes | 9.217738e-01 | 0.035 |
| R-HSA-180786 | Extension of Telomeres | 9.276847e-01 | 0.033 |
| R-HSA-352230 | Amino acid transport across the plasma membrane | 9.276847e-01 | 0.033 |
| R-HSA-186712 | Regulation of beta-cell development | 9.276847e-01 | 0.033 |
| R-HSA-5362517 | Signaling by Retinoic Acid | 9.304707e-01 | 0.031 |
| R-HSA-379724 | tRNA Aminoacylation | 9.304707e-01 | 0.031 |
| R-HSA-1442490 | Collagen degradation | 9.331495e-01 | 0.030 |
| R-HSA-211976 | Endogenous sterols | 9.331495e-01 | 0.030 |
| R-HSA-112043 | PLC beta mediated events | 9.331495e-01 | 0.030 |
| R-HSA-8956321 | Nucleotide salvage | 9.331495e-01 | 0.030 |
| R-HSA-948021 | Transport to the Golgi and subsequent modification | 9.331677e-01 | 0.030 |
| R-HSA-8963743 | Digestion and absorption | 9.382020e-01 | 0.028 |
| R-HSA-418555 | G alpha (s) signalling events | 9.392709e-01 | 0.027 |
| R-HSA-6805567 | Keratinization | 9.407111e-01 | 0.027 |
| R-HSA-5696398 | Nucleotide Excision Repair | 9.432673e-01 | 0.025 |
| R-HSA-112316 | Neuronal System | 9.454275e-01 | 0.024 |
| R-HSA-9958863 | SLC-mediated transport of amino acids | 9.471919e-01 | 0.024 |
| R-HSA-112040 | G-protein mediated events | 9.471919e-01 | 0.024 |
| R-HSA-193368 | Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol | 9.471919e-01 | 0.024 |
| R-HSA-9830369 | Kidney development | 9.471919e-01 | 0.024 |
| R-HSA-9662360 | Sensory processing of sound by inner hair cells of the cochlea | 9.492274e-01 | 0.023 |
| R-HSA-382551 | Transport of small molecules | 9.498853e-01 | 0.022 |
| R-HSA-6803157 | Antimicrobial peptides | 9.533143e-01 | 0.021 |
| R-HSA-3906995 | Diseases associated with O-glycosylation of proteins | 9.548757e-01 | 0.020 |
| R-HSA-189445 | Metabolism of porphyrins | 9.548757e-01 | 0.020 |
| R-HSA-112315 | Transmission across Chemical Synapses | 9.582635e-01 | 0.019 |
| R-HSA-5633008 | TP53 Regulates Transcription of Cell Death Genes | 9.614430e-01 | 0.017 |
| R-HSA-71403 | Citric acid cycle (TCA cycle) | 9.614430e-01 | 0.017 |
| R-HSA-3000171 | Non-integrin membrane-ECM interactions | 9.614430e-01 | 0.017 |
| R-HSA-2871809 | FCERI mediated Ca+2 mobilization | 9.616480e-01 | 0.017 |
| R-HSA-9955298 | SLC-mediated transport of organic anions | 9.657342e-01 | 0.015 |
| R-HSA-191273 | Cholesterol biosynthesis | 9.657342e-01 | 0.015 |
| R-HSA-416476 | G alpha (q) signalling events | 9.660273e-01 | 0.015 |
| R-HSA-9925561 | Developmental Lineage of Pancreatic Acinar Cells | 9.670558e-01 | 0.015 |
| R-HSA-9659379 | Sensory processing of sound | 9.670558e-01 | 0.015 |
| R-HSA-9635486 | Infection with Mycobacterium tuberculosis | 9.685443e-01 | 0.014 |
| R-HSA-1614635 | Sulfur amino acid metabolism | 9.759520e-01 | 0.011 |
| R-HSA-438064 | Post NMDA receptor activation events | 9.768801e-01 | 0.010 |
| R-HSA-9658195 | Leishmania infection | 9.775258e-01 | 0.010 |
| R-HSA-9824443 | Parasitic Infection Pathways | 9.775258e-01 | 0.010 |
| R-HSA-71387 | Metabolism of carbohydrates and carbohydrate derivatives | 9.791959e-01 | 0.009 |
| R-HSA-112310 | Neurotransmitter release cycle | 9.794552e-01 | 0.009 |
| R-HSA-983695 | Antigen activates B Cell Receptor (BCR) leading to generation of second messenge... | 9.824487e-01 | 0.008 |
| R-HSA-9837999 | Mitochondrial protein degradation | 9.831264e-01 | 0.007 |
| R-HSA-77289 | Mitochondrial Fatty Acid Beta-Oxidation | 9.837779e-01 | 0.007 |
| R-HSA-2730905 | Role of LAT2/NTAL/LAB on calcium mobilization | 9.850066e-01 | 0.007 |
| R-HSA-2029482 | Regulation of actin dynamics for phagocytic cup formation | 9.854765e-01 | 0.006 |
| R-HSA-3781865 | Diseases of glycosylation | 9.860273e-01 | 0.006 |
| R-HSA-192105 | Synthesis of bile acids and bile salts | 9.866776e-01 | 0.006 |
| R-HSA-442755 | Activation of NMDA receptors and postsynaptic events | 9.881627e-01 | 0.005 |
| R-HSA-2187338 | Visual phototransduction | 9.885615e-01 | 0.005 |
| R-HSA-1630316 | Glycosaminoglycan metabolism | 9.894319e-01 | 0.005 |
| R-HSA-163125 | Post-translational modification: synthesis of GPI-anchored proteins | 9.894824e-01 | 0.005 |
| R-HSA-202733 | Cell surface interactions at the vascular wall | 9.904760e-01 | 0.004 |
| R-HSA-194068 | Bile acid and bile salt metabolism | 9.916975e-01 | 0.004 |
| R-HSA-5619102 | SLC transporter disorders | 9.942628e-01 | 0.002 |
| R-HSA-397014 | Muscle contraction | 9.943769e-01 | 0.002 |
| R-HSA-1428517 | Aerobic respiration and respiratory electron transport | 9.952560e-01 | 0.002 |
| R-HSA-9748784 | Drug ADME | 9.953586e-01 | 0.002 |
| R-HSA-9664323 | FCGR3A-mediated IL10 synthesis | 9.960760e-01 | 0.002 |
| R-HSA-611105 | Respiratory electron transport | 9.962264e-01 | 0.002 |
| R-HSA-5576891 | Cardiac conduction | 9.969036e-01 | 0.001 |
| R-HSA-446219 | Synthesis of substrates in N-glycan biosythesis | 9.969036e-01 | 0.001 |
| R-HSA-425407 | SLC-mediated transmembrane transport | 9.971004e-01 | 0.001 |
| R-HSA-8957322 | Metabolism of steroids | 9.975088e-01 | 0.001 |
| R-HSA-5173105 | O-linked glycosylation | 9.976515e-01 | 0.001 |
| R-HSA-9664407 | Parasite infection | 9.979139e-01 | 0.001 |
| R-HSA-9664417 | Leishmania phagocytosis | 9.979139e-01 | 0.001 |
| R-HSA-9664422 | FCGR3A-mediated phagocytosis | 9.979139e-01 | 0.001 |
| R-HSA-1474244 | Extracellular matrix organization | 9.979690e-01 | 0.001 |
| R-HSA-428157 | Sphingolipid metabolism | 9.983244e-01 | 0.001 |
| R-HSA-446203 | Asparagine N-linked glycosylation | 9.985204e-01 | 0.001 |
| R-HSA-2173782 | Binding and Uptake of Ligands by Scavenger Receptors | 9.986494e-01 | 0.001 |
| R-HSA-9820448 | Developmental Cell Lineages of the Exocrine Pancreas | 9.987521e-01 | 0.001 |
| R-HSA-2142753 | Arachidonate metabolism | 9.987521e-01 | 0.001 |
| R-HSA-9824439 | Bacterial Infection Pathways | 9.988199e-01 | 0.001 |
| R-HSA-446193 | Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, L... | 9.989760e-01 | 0.000 |
| R-HSA-211897 | Cytochrome P450 - arranged by substrate type | 9.993106e-01 | 0.000 |
| R-HSA-211945 | Phase I - Functionalization of compounds | 9.993544e-01 | 0.000 |
| R-HSA-198933 | Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell | 9.994065e-01 | 0.000 |
| R-HSA-196849 | Metabolism of water-soluble vitamins and cofactors | 9.994275e-01 | 0.000 |
| R-HSA-5668914 | Diseases of metabolism | 9.995971e-01 | 0.000 |
| R-HSA-418594 | G alpha (i) signalling events | 9.998030e-01 | 0.000 |
| R-HSA-196854 | Metabolism of vitamins and cofactors | 9.998158e-01 | 0.000 |
| R-HSA-8978868 | Fatty acid metabolism | 9.999992e-01 | 0.000 |
| R-HSA-388396 | GPCR downstream signalling | 9.999994e-01 | 0.000 |
| R-HSA-211859 | Biological oxidations | 9.999999e-01 | 0.000 |
| R-HSA-500792 | GPCR ligand binding | 9.999999e-01 | 0.000 |
| R-HSA-372790 | Signaling by GPCR | 1.000000e+00 | 0.000 |
| R-HSA-556833 | Metabolism of lipids | 1.000000e+00 | 0.000 |
| R-HSA-1430728 | Metabolism | 1.000000e+00 | 0.000 |
| R-HSA-9709957 | Sensory Perception | 1.000000e+00 | -0.000 |
Download
| kinase | JSD_mean | pearson_surrounding | kinase_max_IC_position | max_position_JSD |
|---|---|---|---|---|
CLK3 |
0.878 | 0.286 | 1 | 0.910 |
MOS |
0.870 | 0.141 | 1 | 0.873 |
COT |
0.869 | 0.078 | 2 | 0.868 |
SRPK1 |
0.863 | 0.238 | -3 | 0.822 |
CDC7 |
0.863 | 0.093 | 1 | 0.841 |
JNK2 |
0.862 | 0.292 | 1 | 0.809 |
HIPK4 |
0.862 | 0.246 | 1 | 0.882 |
NLK |
0.862 | 0.175 | 1 | 0.923 |
CDKL1 |
0.862 | 0.148 | -3 | 0.854 |
DYRK2 |
0.862 | 0.287 | 1 | 0.865 |
PRPK |
0.861 | -0.025 | -1 | 0.867 |
SKMLCK |
0.861 | 0.126 | -2 | 0.889 |
ICK |
0.861 | 0.195 | -3 | 0.882 |
JNK3 |
0.860 | 0.272 | 1 | 0.837 |
CAMK1B |
0.860 | 0.084 | -3 | 0.890 |
ERK5 |
0.859 | 0.153 | 1 | 0.900 |
MTOR |
0.857 | 0.060 | 1 | 0.827 |
PIM3 |
0.857 | 0.076 | -3 | 0.889 |
CLK2 |
0.857 | 0.280 | -3 | 0.825 |
ATR |
0.856 | 0.013 | 1 | 0.817 |
BMPR1B |
0.856 | 0.144 | 1 | 0.800 |
BMPR2 |
0.856 | -0.090 | -2 | 0.893 |
HIPK2 |
0.856 | 0.302 | 1 | 0.803 |
CDKL5 |
0.855 | 0.158 | -3 | 0.847 |
CDK1 |
0.855 | 0.250 | 1 | 0.823 |
DAPK2 |
0.855 | 0.078 | -3 | 0.889 |
KIS |
0.855 | 0.273 | 1 | 0.857 |
P38B |
0.854 | 0.269 | 1 | 0.828 |
HIPK1 |
0.854 | 0.273 | 1 | 0.873 |
RAF1 |
0.854 | -0.072 | 1 | 0.810 |
CAMLCK |
0.854 | 0.065 | -2 | 0.867 |
P38A |
0.853 | 0.255 | 1 | 0.872 |
NIK |
0.853 | 0.012 | -3 | 0.894 |
CAMK2G |
0.853 | -0.017 | 2 | 0.836 |
P38G |
0.852 | 0.265 | 1 | 0.756 |
PDHK4 |
0.851 | -0.105 | 1 | 0.843 |
CDK8 |
0.851 | 0.228 | 1 | 0.838 |
LATS1 |
0.851 | 0.092 | -3 | 0.884 |
CLK4 |
0.851 | 0.207 | -3 | 0.827 |
GRK1 |
0.851 | 0.081 | -2 | 0.811 |
GRK7 |
0.850 | 0.096 | 1 | 0.783 |
TGFBR1 |
0.850 | 0.091 | -2 | 0.830 |
CDK18 |
0.849 | 0.265 | 1 | 0.800 |
PRKD1 |
0.849 | 0.121 | -3 | 0.869 |
PIM1 |
0.849 | 0.096 | -3 | 0.845 |
DYRK4 |
0.849 | 0.284 | 1 | 0.817 |
ALK4 |
0.849 | 0.048 | -2 | 0.856 |
CHAK2 |
0.849 | 0.022 | -1 | 0.864 |
P38D |
0.848 | 0.284 | 1 | 0.764 |
ERK1 |
0.848 | 0.246 | 1 | 0.817 |
NDR2 |
0.848 | 0.051 | -3 | 0.880 |
DSTYK |
0.848 | -0.057 | 2 | 0.873 |
SRPK3 |
0.848 | 0.165 | -3 | 0.794 |
GRK5 |
0.848 | -0.070 | -3 | 0.852 |
GRK6 |
0.848 | 0.014 | 1 | 0.826 |
RSK2 |
0.848 | 0.105 | -3 | 0.832 |
CDK19 |
0.847 | 0.245 | 1 | 0.810 |
CDK5 |
0.847 | 0.226 | 1 | 0.861 |
IKKB |
0.847 | -0.056 | -2 | 0.747 |
PKN3 |
0.847 | 0.038 | -3 | 0.866 |
AMPKA1 |
0.847 | 0.095 | -3 | 0.883 |
NUAK2 |
0.847 | 0.069 | -3 | 0.882 |
CLK1 |
0.846 | 0.226 | -3 | 0.805 |
CAMK2D |
0.846 | 0.064 | -3 | 0.863 |
CDK7 |
0.846 | 0.224 | 1 | 0.850 |
DYRK1A |
0.845 | 0.241 | 1 | 0.880 |
CDK13 |
0.845 | 0.225 | 1 | 0.830 |
MARK4 |
0.845 | 0.047 | 4 | 0.858 |
TSSK2 |
0.845 | 0.064 | -5 | 0.601 |
SRPK2 |
0.844 | 0.180 | -3 | 0.754 |
WNK1 |
0.844 | 0.004 | -2 | 0.900 |
CAMK2B |
0.843 | 0.093 | 2 | 0.812 |
PRP4 |
0.843 | 0.152 | -3 | 0.777 |
TBK1 |
0.843 | -0.104 | 1 | 0.705 |
ALK2 |
0.843 | 0.061 | -2 | 0.834 |
CAMK2A |
0.843 | 0.108 | 2 | 0.828 |
P90RSK |
0.842 | 0.076 | -3 | 0.838 |
CDK17 |
0.842 | 0.243 | 1 | 0.759 |
HIPK3 |
0.842 | 0.247 | 1 | 0.864 |
PDHK1 |
0.842 | -0.160 | 1 | 0.816 |
MAPKAPK2 |
0.842 | 0.123 | -3 | 0.799 |
DLK |
0.842 | -0.136 | 1 | 0.811 |
PKR |
0.842 | -0.024 | 1 | 0.810 |
ACVR2B |
0.842 | 0.050 | -2 | 0.817 |
MAK |
0.841 | 0.266 | -2 | 0.778 |
PASK |
0.841 | 0.105 | -3 | 0.894 |
MST4 |
0.841 | 0.003 | 2 | 0.836 |
NEK6 |
0.841 | -0.047 | -2 | 0.873 |
VRK2 |
0.841 | -0.095 | 1 | 0.869 |
CDK12 |
0.841 | 0.232 | 1 | 0.809 |
MAPKAPK3 |
0.841 | 0.074 | -3 | 0.827 |
CDK3 |
0.841 | 0.224 | 1 | 0.776 |
IKKA |
0.841 | -0.015 | -2 | 0.741 |
DYRK1B |
0.841 | 0.238 | 1 | 0.833 |
TSSK1 |
0.841 | 0.072 | -3 | 0.900 |
RIPK3 |
0.841 | -0.060 | 3 | 0.751 |
MLK1 |
0.841 | -0.114 | 2 | 0.786 |
MASTL |
0.840 | -0.152 | -2 | 0.822 |
JNK1 |
0.840 | 0.234 | 1 | 0.805 |
ANKRD3 |
0.840 | -0.126 | 1 | 0.827 |
AMPKA2 |
0.840 | 0.091 | -3 | 0.860 |
IKKE |
0.839 | -0.105 | 1 | 0.699 |
PRKD2 |
0.839 | 0.098 | -3 | 0.829 |
MEK1 |
0.839 | -0.108 | 2 | 0.841 |
ACVR2A |
0.839 | 0.029 | -2 | 0.805 |
HUNK |
0.839 | -0.085 | 2 | 0.813 |
ERK2 |
0.839 | 0.192 | 1 | 0.846 |
TGFBR2 |
0.839 | -0.041 | -2 | 0.818 |
NDR1 |
0.839 | -0.016 | -3 | 0.872 |
ATM |
0.839 | 0.003 | 1 | 0.752 |
ULK2 |
0.838 | -0.172 | 2 | 0.772 |
GCN2 |
0.838 | -0.137 | 2 | 0.798 |
CDK14 |
0.838 | 0.242 | 1 | 0.829 |
DYRK3 |
0.838 | 0.222 | 1 | 0.865 |
RSK3 |
0.838 | 0.067 | -3 | 0.830 |
P70S6KB |
0.838 | 0.015 | -3 | 0.842 |
PKCD |
0.838 | 0.007 | 2 | 0.761 |
CHK1 |
0.838 | 0.107 | -3 | 0.856 |
LATS2 |
0.837 | 0.001 | -5 | 0.472 |
TLK2 |
0.837 | -0.027 | 1 | 0.759 |
BMPR1A |
0.837 | 0.090 | 1 | 0.775 |
AURC |
0.837 | 0.093 | -2 | 0.682 |
MLK2 |
0.836 | -0.117 | 2 | 0.799 |
PLK1 |
0.836 | -0.053 | -2 | 0.805 |
PKN2 |
0.836 | -0.013 | -3 | 0.864 |
NEK7 |
0.836 | -0.165 | -3 | 0.822 |
PKACG |
0.836 | 0.041 | -2 | 0.759 |
CDK9 |
0.835 | 0.201 | 1 | 0.835 |
PAK1 |
0.835 | 0.020 | -2 | 0.801 |
GAK |
0.835 | 0.064 | 1 | 0.847 |
GRK4 |
0.834 | -0.081 | -2 | 0.844 |
MSK1 |
0.834 | 0.095 | -3 | 0.809 |
RSK4 |
0.834 | 0.083 | -3 | 0.812 |
DCAMKL1 |
0.834 | 0.066 | -3 | 0.841 |
RIPK1 |
0.833 | -0.111 | 1 | 0.781 |
NEK9 |
0.833 | -0.154 | 2 | 0.813 |
GSK3A |
0.833 | 0.120 | 4 | 0.513 |
BRAF |
0.833 | -0.070 | -4 | 0.823 |
AKT2 |
0.833 | 0.107 | -3 | 0.762 |
PKACB |
0.833 | 0.104 | -2 | 0.693 |
QSK |
0.833 | 0.074 | 4 | 0.834 |
YSK4 |
0.833 | -0.114 | 1 | 0.744 |
MSK2 |
0.832 | 0.056 | -3 | 0.809 |
CDK2 |
0.832 | 0.128 | 1 | 0.874 |
DNAPK |
0.832 | 0.025 | 1 | 0.691 |
CDK16 |
0.831 | 0.226 | 1 | 0.774 |
MYLK4 |
0.830 | 0.052 | -2 | 0.788 |
GRK2 |
0.830 | -0.016 | -2 | 0.734 |
FAM20C |
0.830 | 0.052 | 2 | 0.625 |
MPSK1 |
0.830 | 0.068 | 1 | 0.783 |
CDK10 |
0.830 | 0.226 | 1 | 0.819 |
MLK3 |
0.829 | -0.082 | 2 | 0.714 |
NIM1 |
0.829 | -0.027 | 3 | 0.782 |
TAO3 |
0.829 | -0.040 | 1 | 0.779 |
SGK3 |
0.829 | 0.064 | -3 | 0.812 |
PLK3 |
0.829 | -0.043 | 2 | 0.798 |
NEK5 |
0.828 | -0.083 | 1 | 0.797 |
CAMK4 |
0.828 | -0.028 | -3 | 0.851 |
MEKK2 |
0.828 | -0.090 | 2 | 0.783 |
SMG1 |
0.828 | -0.040 | 1 | 0.765 |
BCKDK |
0.828 | -0.129 | -1 | 0.800 |
MST3 |
0.828 | -0.030 | 2 | 0.819 |
PRKD3 |
0.827 | 0.047 | -3 | 0.805 |
PAK3 |
0.827 | -0.024 | -2 | 0.795 |
MEKK3 |
0.827 | -0.123 | 1 | 0.780 |
MEK5 |
0.827 | -0.196 | 2 | 0.812 |
PIM2 |
0.827 | 0.047 | -3 | 0.805 |
MOK |
0.827 | 0.215 | 1 | 0.870 |
PRKX |
0.827 | 0.128 | -3 | 0.752 |
PKCB |
0.827 | 0.002 | 2 | 0.701 |
TTBK2 |
0.826 | -0.152 | 2 | 0.711 |
WNK3 |
0.826 | -0.226 | 1 | 0.784 |
MELK |
0.826 | 0.014 | -3 | 0.842 |
AURB |
0.826 | 0.041 | -2 | 0.676 |
DAPK3 |
0.826 | 0.067 | -3 | 0.852 |
MARK3 |
0.826 | 0.046 | 4 | 0.792 |
ULK1 |
0.826 | -0.185 | -3 | 0.796 |
IRE1 |
0.825 | -0.090 | 1 | 0.759 |
DRAK1 |
0.825 | -0.046 | 1 | 0.764 |
AURA |
0.825 | 0.040 | -2 | 0.652 |
MLK4 |
0.825 | -0.103 | 2 | 0.693 |
SMMLCK |
0.825 | 0.019 | -3 | 0.852 |
BRSK1 |
0.825 | 0.060 | -3 | 0.841 |
MNK2 |
0.825 | 0.025 | -2 | 0.811 |
PKCZ |
0.825 | -0.032 | 2 | 0.754 |
MARK2 |
0.825 | 0.026 | 4 | 0.759 |
LKB1 |
0.825 | -0.044 | -3 | 0.822 |
PKCA |
0.824 | -0.015 | 2 | 0.695 |
GCK |
0.824 | -0.013 | 1 | 0.776 |
GSK3B |
0.824 | 0.053 | 4 | 0.505 |
NEK2 |
0.824 | -0.114 | 2 | 0.793 |
PINK1 |
0.824 | -0.068 | 1 | 0.856 |
QIK |
0.824 | -0.037 | -3 | 0.852 |
PKCG |
0.824 | -0.027 | 2 | 0.712 |
SIK |
0.824 | 0.049 | -3 | 0.812 |
NUAK1 |
0.824 | 0.033 | -3 | 0.836 |
PDK1 |
0.823 | -0.034 | 1 | 0.780 |
MEKK1 |
0.823 | -0.166 | 1 | 0.777 |
PAK2 |
0.823 | -0.047 | -2 | 0.783 |
MNK1 |
0.823 | 0.023 | -2 | 0.818 |
PERK |
0.823 | -0.131 | -2 | 0.845 |
DCAMKL2 |
0.822 | 0.022 | -3 | 0.854 |
PKG2 |
0.822 | 0.041 | -2 | 0.694 |
TLK1 |
0.821 | -0.090 | -2 | 0.848 |
DAPK1 |
0.821 | 0.070 | -3 | 0.837 |
CHAK1 |
0.821 | -0.143 | 2 | 0.772 |
WNK4 |
0.821 | -0.076 | -2 | 0.895 |
ZAK |
0.820 | -0.167 | 1 | 0.749 |
CAMK1G |
0.820 | 0.027 | -3 | 0.812 |
CK1E |
0.820 | 0.029 | -3 | 0.583 |
ERK7 |
0.820 | 0.061 | 2 | 0.522 |
CK1D |
0.819 | 0.042 | -3 | 0.529 |
NEK11 |
0.819 | -0.115 | 1 | 0.767 |
PKCH |
0.819 | -0.047 | 2 | 0.687 |
CDK6 |
0.819 | 0.188 | 1 | 0.812 |
CDK4 |
0.819 | 0.201 | 1 | 0.799 |
TNIK |
0.819 | -0.014 | 3 | 0.865 |
CK2A2 |
0.818 | 0.091 | 1 | 0.725 |
MARK1 |
0.818 | 0.003 | 4 | 0.808 |
CAMKK2 |
0.818 | -0.117 | -2 | 0.746 |
EEF2K |
0.818 | -0.034 | 3 | 0.835 |
CAMK1D |
0.817 | 0.063 | -3 | 0.755 |
PKACA |
0.817 | 0.086 | -2 | 0.644 |
MST2 |
0.817 | -0.104 | 1 | 0.778 |
CAMKK1 |
0.817 | -0.160 | -2 | 0.746 |
GRK3 |
0.817 | -0.005 | -2 | 0.696 |
LRRK2 |
0.817 | -0.078 | 2 | 0.836 |
AKT1 |
0.817 | 0.073 | -3 | 0.774 |
NEK8 |
0.817 | -0.172 | 2 | 0.798 |
HPK1 |
0.816 | -0.019 | 1 | 0.758 |
TAO2 |
0.816 | -0.117 | 2 | 0.825 |
IRE2 |
0.816 | -0.121 | 2 | 0.720 |
HRI |
0.816 | -0.184 | -2 | 0.857 |
BRSK2 |
0.816 | -0.016 | -3 | 0.846 |
MINK |
0.815 | -0.065 | 1 | 0.753 |
SGK1 |
0.815 | 0.098 | -3 | 0.692 |
MAPKAPK5 |
0.815 | -0.005 | -3 | 0.772 |
PLK4 |
0.815 | -0.104 | 2 | 0.642 |
TAK1 |
0.815 | -0.110 | 1 | 0.785 |
PHKG1 |
0.815 | -0.052 | -3 | 0.864 |
MAP3K15 |
0.815 | -0.087 | 1 | 0.741 |
PAK6 |
0.814 | 0.034 | -2 | 0.715 |
PLK2 |
0.814 | 0.021 | -3 | 0.817 |
SBK |
0.814 | 0.128 | -3 | 0.657 |
CK1A2 |
0.814 | 0.032 | -3 | 0.533 |
HGK |
0.814 | -0.065 | 3 | 0.858 |
PBK |
0.813 | 0.026 | 1 | 0.775 |
KHS1 |
0.813 | -0.008 | 1 | 0.746 |
SSTK |
0.813 | -0.011 | 4 | 0.818 |
KHS2 |
0.812 | 0.012 | 1 | 0.762 |
MEKK6 |
0.812 | -0.101 | 1 | 0.775 |
BUB1 |
0.811 | 0.069 | -5 | 0.546 |
ROCK2 |
0.811 | 0.036 | -3 | 0.834 |
IRAK4 |
0.811 | -0.143 | 1 | 0.759 |
NEK1 |
0.811 | -0.100 | 1 | 0.766 |
VRK1 |
0.810 | -0.157 | 2 | 0.819 |
NEK4 |
0.810 | -0.148 | 1 | 0.750 |
CK2A1 |
0.809 | 0.079 | 1 | 0.705 |
CHK2 |
0.808 | 0.073 | -3 | 0.711 |
DMPK1 |
0.807 | 0.067 | -3 | 0.813 |
SNRK |
0.807 | -0.138 | 2 | 0.687 |
PKCT |
0.806 | -0.041 | 2 | 0.695 |
PKCE |
0.806 | 0.011 | 2 | 0.693 |
MST1 |
0.806 | -0.156 | 1 | 0.756 |
AKT3 |
0.805 | 0.085 | -3 | 0.711 |
MRCKB |
0.805 | 0.032 | -3 | 0.790 |
P70S6K |
0.805 | -0.024 | -3 | 0.762 |
PKCI |
0.804 | -0.035 | 2 | 0.716 |
LOK |
0.804 | -0.103 | -2 | 0.773 |
MRCKA |
0.804 | 0.008 | -3 | 0.803 |
SLK |
0.803 | -0.097 | -2 | 0.720 |
OSR1 |
0.803 | -0.090 | 2 | 0.785 |
TTK |
0.803 | -0.051 | -2 | 0.831 |
CK1G1 |
0.802 | -0.010 | -3 | 0.574 |
PDHK3_TYR |
0.801 | 0.173 | 4 | 0.923 |
CAMK1A |
0.801 | 0.054 | -3 | 0.729 |
YSK1 |
0.801 | -0.107 | 2 | 0.781 |
MEK2 |
0.799 | -0.235 | 2 | 0.801 |
ALPHAK3 |
0.799 | -0.050 | -1 | 0.786 |
PAK5 |
0.798 | -0.001 | -2 | 0.655 |
BIKE |
0.797 | 0.017 | 1 | 0.738 |
CRIK |
0.797 | 0.041 | -3 | 0.773 |
IRAK1 |
0.797 | -0.253 | -1 | 0.756 |
HASPIN |
0.796 | 0.004 | -1 | 0.743 |
PKN1 |
0.795 | 0.006 | -3 | 0.777 |
ROCK1 |
0.795 | 0.015 | -3 | 0.803 |
ASK1 |
0.795 | -0.141 | 1 | 0.728 |
STK33 |
0.794 | -0.144 | 2 | 0.640 |
TTBK1 |
0.794 | -0.189 | 2 | 0.640 |
PAK4 |
0.794 | 0.006 | -2 | 0.663 |
MAP2K4_TYR |
0.794 | 0.083 | -1 | 0.887 |
PDHK4_TYR |
0.794 | 0.067 | 2 | 0.893 |
MAP2K6_TYR |
0.793 | 0.072 | -1 | 0.892 |
MYO3B |
0.793 | -0.068 | 2 | 0.803 |
PHKG2 |
0.793 | -0.074 | -3 | 0.831 |
NEK3 |
0.790 | -0.122 | 1 | 0.732 |
BMPR2_TYR |
0.790 | 0.054 | -1 | 0.889 |
PDHK1_TYR |
0.789 | 0.023 | -1 | 0.897 |
YANK3 |
0.789 | -0.028 | 2 | 0.447 |
TESK1_TYR |
0.789 | -0.036 | 3 | 0.885 |
PKMYT1_TYR |
0.788 | 0.035 | 3 | 0.855 |
MYO3A |
0.788 | -0.121 | 1 | 0.742 |
AAK1 |
0.787 | 0.068 | 1 | 0.649 |
RIPK2 |
0.785 | -0.247 | 1 | 0.701 |
MAP2K7_TYR |
0.785 | -0.128 | 2 | 0.863 |
TAO1 |
0.784 | -0.128 | 1 | 0.695 |
LIMK2_TYR |
0.783 | 0.007 | -3 | 0.886 |
PINK1_TYR |
0.780 | -0.147 | 1 | 0.836 |
EPHA6 |
0.780 | 0.028 | -1 | 0.861 |
STLK3 |
0.778 | -0.210 | 1 | 0.713 |
PKG1 |
0.777 | 0.010 | -2 | 0.614 |
EPHB4 |
0.777 | -0.005 | -1 | 0.828 |
CK1A |
0.776 | 0.016 | -3 | 0.442 |
TXK |
0.775 | 0.043 | 1 | 0.835 |
RET |
0.774 | -0.129 | 1 | 0.788 |
ABL2 |
0.773 | -0.008 | -1 | 0.794 |
LIMK1_TYR |
0.772 | -0.153 | 2 | 0.842 |
FGR |
0.772 | -0.053 | 1 | 0.841 |
CSF1R |
0.771 | -0.076 | 3 | 0.785 |
EPHA4 |
0.771 | -0.010 | 2 | 0.805 |
MST1R |
0.770 | -0.130 | 3 | 0.807 |
YES1 |
0.770 | -0.061 | -1 | 0.829 |
BLK |
0.770 | 0.037 | -1 | 0.825 |
ABL1 |
0.769 | -0.021 | -1 | 0.784 |
FER |
0.769 | -0.090 | 1 | 0.856 |
TYRO3 |
0.769 | -0.140 | 3 | 0.785 |
DDR1 |
0.768 | -0.147 | 4 | 0.835 |
LCK |
0.768 | 0.007 | -1 | 0.819 |
ROS1 |
0.768 | -0.125 | 3 | 0.755 |
JAK2 |
0.768 | -0.133 | 1 | 0.782 |
SRMS |
0.768 | -0.049 | 1 | 0.834 |
JAK3 |
0.767 | -0.097 | 1 | 0.772 |
TNK2 |
0.767 | -0.050 | 3 | 0.752 |
HCK |
0.767 | -0.041 | -1 | 0.813 |
TYK2 |
0.767 | -0.209 | 1 | 0.779 |
INSRR |
0.766 | -0.089 | 3 | 0.734 |
ITK |
0.765 | -0.055 | -1 | 0.782 |
FYN |
0.764 | 0.027 | -1 | 0.801 |
CK1G3 |
0.764 | -0.010 | -3 | 0.397 |
FGFR2 |
0.764 | -0.114 | 3 | 0.791 |
EPHB2 |
0.763 | -0.047 | -1 | 0.803 |
KIT |
0.763 | -0.107 | 3 | 0.787 |
MET |
0.762 | -0.077 | 3 | 0.779 |
EPHB1 |
0.762 | -0.093 | 1 | 0.825 |
EPHB3 |
0.762 | -0.073 | -1 | 0.807 |
KDR |
0.761 | -0.103 | 3 | 0.751 |
MERTK |
0.760 | -0.073 | 3 | 0.775 |
BMX |
0.758 | -0.053 | -1 | 0.702 |
FLT1 |
0.758 | -0.086 | -1 | 0.839 |
PTK2 |
0.758 | 0.058 | -1 | 0.808 |
NEK10_TYR |
0.758 | -0.115 | 1 | 0.667 |
YANK2 |
0.758 | -0.062 | 2 | 0.458 |
TNK1 |
0.757 | -0.097 | 3 | 0.774 |
FGFR1 |
0.757 | -0.134 | 3 | 0.754 |
PDGFRB |
0.756 | -0.206 | 3 | 0.791 |
JAK1 |
0.756 | -0.089 | 1 | 0.721 |
TNNI3K_TYR |
0.756 | -0.084 | 1 | 0.788 |
FGFR3 |
0.755 | -0.106 | 3 | 0.762 |
EPHA7 |
0.755 | -0.066 | 2 | 0.799 |
AXL |
0.754 | -0.144 | 3 | 0.767 |
FLT3 |
0.754 | -0.187 | 3 | 0.785 |
PTK2B |
0.754 | -0.033 | -1 | 0.748 |
SYK |
0.753 | 0.031 | -1 | 0.786 |
TEK |
0.753 | -0.163 | 3 | 0.720 |
TEC |
0.753 | -0.101 | -1 | 0.708 |
EPHA3 |
0.753 | -0.114 | 2 | 0.775 |
FRK |
0.752 | -0.072 | -1 | 0.819 |
ERBB2 |
0.752 | -0.134 | 1 | 0.754 |
LYN |
0.752 | -0.068 | 3 | 0.714 |
SRC |
0.751 | -0.051 | -1 | 0.792 |
NTRK1 |
0.751 | -0.179 | -1 | 0.805 |
EPHA8 |
0.751 | -0.044 | -1 | 0.798 |
EPHA5 |
0.750 | -0.057 | 2 | 0.787 |
DDR2 |
0.750 | -0.066 | 3 | 0.721 |
BTK |
0.750 | -0.180 | -1 | 0.736 |
EGFR |
0.750 | -0.058 | 1 | 0.673 |
PTK6 |
0.750 | -0.188 | -1 | 0.709 |
WEE1_TYR |
0.749 | -0.125 | -1 | 0.742 |
EPHA1 |
0.748 | -0.121 | 3 | 0.759 |
MATK |
0.748 | -0.106 | -1 | 0.729 |
LTK |
0.748 | -0.163 | 3 | 0.730 |
ALK |
0.748 | -0.168 | 3 | 0.698 |
NTRK3 |
0.748 | -0.120 | -1 | 0.757 |
INSR |
0.748 | -0.148 | 3 | 0.716 |
CSK |
0.747 | -0.099 | 2 | 0.800 |
PDGFRA |
0.747 | -0.235 | 3 | 0.789 |
FGFR4 |
0.747 | -0.076 | -1 | 0.762 |
CK1G2 |
0.747 | -0.014 | -3 | 0.491 |
FLT4 |
0.746 | -0.171 | 3 | 0.750 |
NTRK2 |
0.743 | -0.223 | 3 | 0.741 |
ERBB4 |
0.741 | -0.030 | 1 | 0.694 |
EPHA2 |
0.740 | -0.060 | -1 | 0.765 |
ZAP70 |
0.735 | -0.000 | -1 | 0.711 |
IGF1R |
0.734 | -0.134 | 3 | 0.655 |
MUSK |
0.727 | -0.153 | 1 | 0.663 |
FES |
0.720 | -0.128 | -1 | 0.679 |