Motif 1209 (n=380)
Position-wise Probabilities
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| uniprot | genes | site | source | protein | function |
|---|---|---|---|---|---|
| A0A0A6YYH1 | C15orf38-AP3S2 | Y5 | ochoa | Arpin | Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. {ECO:0000256|ARBA:ARBA00025605}. |
| A0A0B4J1R7 | BORCS7-ASMT | T6 | ochoa | BLOC-1-related complex subunit 7 | None |
| 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}. |
| 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}. |
| C9JAW5 | None | T5 | ochoa | HIG1 domain-containing protein | None |
| C9JQL5 | None | T7 | ochoa | Putative dispanin subfamily A member 2d (DSPA2d) | None |
| K7EJ46 | SMIM22 | T5 | ochoa | Small integral membrane protein 22 (Cancer-associated small integral membrane open reading frame 1) | May modulate lipid droplet formation throught interaction with SQLE. {ECO:0000269|PubMed:29765154}. |
| O00631 | SLN | T5 | psp | Sarcolipin | Reversibly inhibits the activity of ATP2A1/SERCA1 and ATP2A2/SERCA2 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+) (PubMed:11781085, PubMed:9575189). Also inhibits the activity of ATP2A3/SERCA3 (By similarity). Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. Required for muscle-based, non-shivering thermogenesis (By similarity). {ECO:0000250|UniProtKB:Q9CQD6, ECO:0000269|PubMed:11781085, ECO:0000269|PubMed:9575189}. |
| O15042 | U2SURP | T5 | ochoa | U2 snRNP-associated SURP motif-containing protein (140 kDa Ser/Arg-rich domain protein) (U2-associated protein SR140) | None |
| 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}. |
| 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}. |
| O60256 | PRPSAP2 | T5 | ochoa | Phosphoribosyl pyrophosphate synthase-associated protein 2 (PRPP synthase-associated protein 2) (41 kDa phosphoribosypyrophosphate synthetase-associated protein) (PAP41) | Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis. |
| 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}. |
| O60671 | RAD1 | T5 | ochoa | Cell cycle checkpoint protein RAD1 (hRAD1) (Rad1-like DNA damage checkpoint protein) | Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:10846170, PubMed:10884395). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:12578958). Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER) (PubMed:15871698). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates (PubMed:15314187, PubMed:15556996, PubMed:15871698). The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (PubMed:21659603). {ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:10884395, ECO:0000269|PubMed:12578958, ECO:0000269|PubMed:15314187, ECO:0000269|PubMed:15556996, ECO:0000269|PubMed:15871698, ECO:0000269|PubMed:21659603}. |
| O75179 | ANKRD17 | T5 | ochoa | Ankyrin repeat domain-containing protein 17 (Gene trap ankyrin repeat protein) (Serologically defined breast cancer antigen NY-BR-16) | Could play pivotal roles in cell cycle and DNA regulation (PubMed:19150984). Involved in innate immune defense against viruse by positively regulating the viral dsRNA receptors DDX58 and IFIH1 signaling pathways (PubMed:22328336). Involves in NOD2- and NOD1-mediated responses to bacteria suggesting a role in innate antibacterial immune pathways too (PubMed:23711367). Target of enterovirus 71 which is the major etiological agent of HFMD (hand, foot and mouth disease) (PubMed:17276651). Could play a central role for the formation and/or maintenance of the blood vessels of the circulation system (By similarity). {ECO:0000250|UniProtKB:Q99NH0, ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984, ECO:0000269|PubMed:22328336, ECO:0000269|PubMed:23711367}. |
| 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}. |
| O75607 | NPM3 | T5 | ochoa | Nucleoplasmin-3 | Plays a role in the regulation of diverse cellular processes such as ribosome biogenesis, chromatin remodeling or protein chaperoning (PubMed:20073534, PubMed:22362753). Modulates the histone chaperone function and the RNA-binding activity of nucleolar phosphoprotein B23/NPM (PubMed:22362753). Efficiently mediates chromatin remodeling when included in a pentamer containing NPM3 and NPM (PubMed:15596447). {ECO:0000269|PubMed:15596447, ECO:0000269|PubMed:20073534, ECO:0000269|PubMed:22362753}. |
| O95139 | NDUFB6 | T5 | psp | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 (Complex I-B17) (CI-B17) (NADH-ubiquinone oxidoreductase B17 subunit) | Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}. |
| O95817 | BAG3 | T5 | 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}. |
| O96018 | APBA3 | T5 | 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}. |
| P02042 | HBD | T5 | ochoa | Hemoglobin subunit delta (Delta-globin) (Hemoglobin delta chain) | Involved in oxygen transport from the lung to the various peripheral tissues. |
| P05783 | KRT18 | T5 | 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}. |
| P06400 | RB1 | T5 | psp | Retinoblastoma-associated protein (p105-Rb) (p110-RB1) (pRb) (Rb) (pp110) | Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle (PubMed:10499802). The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes (PubMed:10499802). Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription (PubMed:10499802). Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase (PubMed:10499802). RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C (PubMed:15084261). Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). {ECO:0000250|UniProtKB:P13405, ECO:0000250|UniProtKB:P33568, ECO:0000269|PubMed:10499802, ECO:0000269|PubMed:15084261}.; FUNCTION: (Microbial infection) In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity. {ECO:0000269|PubMed:1316611, ECO:0000269|PubMed:17974914, ECO:0000269|PubMed:18701596, ECO:0000269|PubMed:2839300, ECO:0000269|PubMed:8892909}. |
| 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 | T5 | 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}. |
| 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}. |
| P09234 | SNRPC | Y5 | ochoa | U1 small nuclear ribonucleoprotein C (U1 snRNP C) (U1-C) (U1C) | Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRPC/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. {ECO:0000255|HAMAP-Rule:MF_03153, ECO:0000269|PubMed:1826349, ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:2136774, ECO:0000269|PubMed:8798632}. |
| 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}. |
| 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. |
| 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}. |
| 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}. |
| 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}. |
| P20700 | LMNB1 | T5 | ochoa | Lamin-B1 | Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:28716252, PubMed:32910914). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:28716252, PubMed:32910914). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:28716252, PubMed:32910914). {ECO:0000269|PubMed:28716252, ECO:0000269|PubMed:32910914}. |
| 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}. |
| 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}. |
| 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}. |
| 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}. |
| P35520 | CBS | T5 | ochoa | Cystathionine beta-synthase (EC 4.2.1.22) (Beta-thionase) (Serine sulfhydrase) | Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine (PubMed:20506325, PubMed:23974653, PubMed:23981774). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (By similarity). {ECO:0000250|UniProtKB:P32232, ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653, ECO:0000269|PubMed:23981774}. |
| 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}. |
| 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}. |
| 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}. |
| 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}. |
| 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}. |
| 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}. |
| 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}. |
| 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}. |
| P55055 | NR1H2 | T5 | 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 | 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}. |
| P57088 | TMEM33 | T5 | ochoa | Transmembrane protein 33 (Protein DB83) (SHINC-3) | Acts as a regulator of the tubular endoplasmic reticulum (ER) network by modulating intracellular calcium homeostasis. Mechanistically, stimulates PKD2 calcium-dependent activity (By similarity). Suppresses the RTN3/4-induced formation of the ER tubules (PubMed:25612671). Positively regulates PERK-mediated and IRE1-mediated unfolded protein response signaling (PubMed:26268696). Plays an essential role in VEGF-mediated release of Ca(2+) from ER stores during angiogenesis (PubMed:30760708). Also plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (PubMed:32614325). Participates in lipid metabolism by acting as a downstream effector of the pyruvate kinase/PKM. Forms a complex with RNF5 to facilitate polyubiquitination and subsequent degradation of SCAP on the ER membrane (PubMed:34487377). {ECO:0000250|UniProtKB:Q9CR67, ECO:0000269|PubMed:25612671, ECO:0000269|PubMed:26268696, ECO:0000269|PubMed:30760708, ECO:0000269|PubMed:32614325, ECO:0000269|PubMed:34487377}. |
| 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 | T5 | 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}. |
| 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}. |
| 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 | T5 | 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}. |
| P63215 | GNG3 | T5 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. |
| P63244 | RACK1 | 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}. |
| P63316 | TNNC1 | Y5 | ochoa | Troponin C, slow skeletal and cardiac muscles (TN-C) | Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. |
| 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}. |
| 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}. |
| P68871 | HBB | T5 | ochoa | Hemoglobin subunit beta (Beta-globin) (Hemoglobin beta chain) [Cleaved into: LVV-hemorphin-7; Spinorphin] | Involved in oxygen transport from the lung to the various peripheral tissues. {ECO:0000269|PubMed:28066926}.; FUNCTION: LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure.; FUNCTION: [Spinorphin]: Functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation. |
| 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}. |
| Q00872 | MYBPC1 | T5 | ochoa | Myosin-binding protein C, slow-type (Slow MyBP-C) (C-protein, skeletal muscle slow isoform) | Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. Slow skeletal protein that binds to both myosin and actin (PubMed:31025394, PubMed:31264822). In vitro, binds to native thin filaments and modifies the activity of actin-activated myosin ATPase. May modulate muscle contraction or may play a more structural role. {ECO:0000269|PubMed:31025394, ECO:0000269|PubMed:31264822}. |
| 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}. |
| 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}. |
| 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}. |
| 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}. |
| 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. |
| 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}. |
| 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}. |
| Q13615 | MTMR3 | T5 | ochoa | Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 (EC 3.1.3.95) (FYVE domain-containing dual specificity protein phosphatase 1) (FYVE-DSP1) (Myotubularin-related protein 3) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (Phosphatidylinositol-3-phosphate phosphatase) (Zinc finger FYVE domain-containing protein 10) | Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate (PubMed:10733931, PubMed:11302699, PubMed:11676921, PubMed:12646134). Decreases the levels of phosphatidylinositol 3-phosphate, a phospholipid found in cell membranes where it acts as key regulator of both cell signaling and intracellular membrane traffic (PubMed:11302699, PubMed:11676921, PubMed:12646134). Could also have a molecular sequestering/adapter activity and regulate biological processes independently of its phosphatase activity. It includes the regulation of midbody abscission during mitotic cytokinesis (PubMed:25659891). {ECO:0000269|PubMed:10733931, ECO:0000269|PubMed:11302699, ECO:0000269|PubMed:11676921, ECO:0000269|PubMed:12646134, ECO:0000269|PubMed:25659891}. |
| 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}. |
| Q14123 | PDE1C | T5 | ochoa | Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C (Cam-PDE 1C) (EC 3.1.4.17) (Hcam3) | Calmodulin-dependent cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes (PubMed:29860631, PubMed:8557689). Has a high affinity for both cAMP and cGMP (PubMed:8557689). Modulates the amplitude and duration of the cAMP signal in sensory cilia in response to odorant stimulation, hence contributing to the generation of action potentials. Regulates smooth muscle cell proliferation. Regulates the stability of growth factor receptors, including PDGFRB (Probable). {ECO:0000269|PubMed:29860631, ECO:0000269|PubMed:8557689, ECO:0000305|PubMed:29860631}. |
| 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}. |
| 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}. |
| 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 | 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}. |
| Q15555 | MAPRE2 | T5 | ochoa | Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2) (End-binding protein 2) (EB2) | Adapter protein that is involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. Therefore, ensures mitotic progression and genome stability (PubMed:27030108). Acts as a central regulator of microtubule reorganization in apico-basal epithelial differentiation (By similarity). Plays a role during oocyte meiosis by regulating microtubule dynamics (By similarity). Participates in neurite growth by interacting with plexin B3/PLXNB3 and microtubule reorganization during apico-basal epithelial differentiation (PubMed:22373814). Also plays an essential role for cell migration and focal adhesion dynamics. Mechanistically, recruits HAX1 to microtubules in order to regulate focal adhesion dynamics (PubMed:26527684). {ECO:0000250|UniProtKB:Q8R001, ECO:0000269|PubMed:22373814, ECO:0000269|PubMed:23844040, ECO:0000269|PubMed:26527684, ECO:0000269|PubMed:27030108}. |
| Q15555 | MAPRE2 | 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}. |
| 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}. |
| 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. |
| Q16644 | MAPKAPK3 | T5 | psp | MAP kinase-activated protein kinase 3 (MAPK-activated protein kinase 3) (MAPKAP kinase 3) (MAPKAP-K3) (MAPKAPK-3) (MK-3) (EC 2.7.11.1) (Chromosome 3p kinase) (3pK) | Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins, such as TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression. {ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:15563468, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:20599781, ECO:0000269|PubMed:8626550, ECO:0000269|PubMed:8774846}. |
| Q53QZ3 | ARHGAP15 | T5 | 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}. |
| Q56A73 | SPIN4 | T5 | ochoa | Spindlin-4 | Binds to acetylated and methylated histones, including H3K4me3 and H4K20me3, probably acting as a histone reader that recognizes chromatin marks and mediates downstream cellular effects (PubMed:29061846, PubMed:36927955). Promotes canonical WNT signaling, and is involved in the down-regulation of cell proliferation (PubMed:36927955). {ECO:0000269|PubMed:29061846, ECO:0000269|PubMed:36927955}. |
| Q5HY92 | FIGN | T5 | ochoa | Fidgetin | ATP-dependent microtubule severing protein. Severs microtubules along their length and depolymerizes their ends, primarily the minus-end, that may lead to the suppression of microtubule growth from and attachment to centrosomes. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. {ECO:0000269|PubMed:22672901}. |
| 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}. |
| Q5SGD2 | PPM1L | T5 | 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}. |
| 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 | T5 | 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 | T5 | ochoa | Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 2 (Rhodanese domain-containing protein 2) | None |
| 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}. |
| Q641Q2 | WASHC2A | T5 | 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}. |
| 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}. |
| Q6I9Y2 | THOC7 | T5 | ochoa | THO complex subunit 7 (Functional spliceosome-associated protein 24) (fSAP24) (Ngg1-interacting factor 3-like protein 1-binding protein 1) (NIF3L1-binding protein 1) (hTREX30) | Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA (PubMed:23222130). 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). {ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:23222130, ECO:0000269|PubMed:33191911}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269|PubMed:18974867}. |
| 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}. |
| 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}. |
| 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}. |
| Q7L099 | RUFY3 | T5 | ochoa | Protein RUFY3 (RUN and FYVE domain-containing protein 3) (Rap2-interacting protein x) (RIPx) (Single axon-regulated protein) (Singar) | ARL8 effector that promotes the coupling of endolysosomes to dynein-dynactin for retrograde transport along microtubules. Acts by binding both GTP-bound ARL8 and dynein-dynactin. In nonneuronal cells, promotes concentration of endolysosomes in the juxtanuclear area. In hippocampal neurons, drives retrograde transport of endolysosomes from the axon to the soma (PubMed:35314674). Plays a role in the generation of neuronal polarity formation and axon growth (By similarity). Implicated in the formation of a single axon by developing neurons (By similarity). May inhibit the formation of additional axons by inhibition of PI3K in minor neuronal processes (By similarity). Plays a role in the formation of F-actin-enriched protrusive structures at the cell periphery (PubMed:25766321). Plays a role in cytoskeletal organization by regulating the subcellular localization of FSCN1 and DBN1 at axonal growth cones (By similarity). {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q9D394, ECO:0000269|PubMed:25766321, ECO:0000269|PubMed:35314674}. |
| Q7L4I2 | RSRC2 | T6 | ochoa | Arginine/serine-rich coiled-coil protein 2 | None |
| Q7Z6K5 | ARPIN | Y5 | ochoa | Arpin (Arp2/3 inhibition protein) | Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence. {ECO:0000269|PubMed:24132237}. |
| 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}. |
| 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}. |
| 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}. |
| Q8ND56 | LSM14A | T5 | ochoa | Protein LSM14 homolog A (Protein FAM61A) (Protein SCD6 homolog) (Putative alpha-synuclein-binding protein) (AlphaSNBP) (RNA-associated protein 55A) (hRAP55) (hRAP55A) | Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for translationally inactive mRNAs and protect them from degradation (PubMed:16484376, PubMed:17074753, PubMed:29510985). Acts as a repressor of mRNA translation (PubMed:29510985). May play a role in mitotic spindle assembly (PubMed:26339800). {ECO:0000269|PubMed:16484376, ECO:0000269|PubMed:17074753, ECO:0000269|PubMed:26339800, ECO:0000269|PubMed:29510985}. |
| 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}. |
| 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 |
| 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}. |
| Q8TE77 | SSH3 | T5 | 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}. |
| 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}. |
| Q92610 | ZNF592 | T6 | ochoa | Zinc finger protein 592 | May be involved in transcriptional regulation. {ECO:0000269|PubMed:20531441}. |
| 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}. |
| Q96A57 | TMEM230 | T6 | ochoa | Transmembrane protein 230 | Involved in trafficking and recycling of synaptic vesicles. {ECO:0000269|PubMed:27270108}. |
| 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}. |
| Q96B49 | TOMM6 | T5 | ochoa | Mitochondrial import receptor subunit TOM6 homolog (Overexpressed breast tumor protein) (Translocase of outer membrane 6 kDa subunit homolog) | None |
| 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}. |
| Q96CN4 | EVI5L | T5 | ochoa | EVI5-like protein (Ecotropic viral integration site 5-like protein) | Functions as a GTPase-activating protein (GAP) with a broad specificity. {ECO:0000269|PubMed:16923123}. |
| Q96CP6 | GRAMD1A | T5 | ochoa | Protein Aster-A (GRAM domain-containing protein 1A) | Cholesterol transporter that mediates non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) (By similarity). Contains unique domains for binding cholesterol and the PM, thereby serving as a molecular bridge for the transfer of cholesterol from the PM to the ER (By similarity). Plays a crucial role in cholesterol homeostasis and has the unique ability to localize to the PM based on the level of membrane cholesterol (By similarity). In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which is mediated by the GRAM domain (By similarity). At the EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and facilitates its transfer from the PM to ER (By similarity). May play a role in tumor progression (By similarity). Plays a role in autophagy regulation and is required for biogenesis of the autophagosome (PubMed:31222192). This function in autophagy requires its cholesterol-transfer activity (PubMed:31222192). {ECO:0000250|UniProtKB:Q8VEF1, ECO:0000269|PubMed:31222192}. |
| 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}. |
| 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}. |
| 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 | 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}. |
| Q9BPY8 | HOPX | T5 | 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}. |
| Q9BQA1 | WDR77 | T5 | ochoa|psp | Methylosome protein WDR77 (Androgen receptor cofactor p44) (Methylosome protein 50) (MEP-50) (WD repeat-containing protein 77) (p44/Mep50) | Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones (PubMed:11756452). This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed:23071334). {ECO:0000269|PubMed:11756452, ECO:0000269|PubMed:23071334}. |
| Q9BR77 | CCDC77 | T6 | ochoa | Coiled-coil domain-containing protein 77 | None |
| 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}. |
| 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}. |
| Q9BW30 | TPPP3 | T5 | ochoa | Tubulin polymerization-promoting protein family member 3 (TPPP/p20) | Regulator of microtubule dynamic that has microtubule bundling activity (PubMed:17105200, PubMed:19633818). Required for embryo implantation; possibly by regulating beta-catenin (By similarity). Also required for decidualization via regulation of beta-catenin (PubMed:30667362). {ECO:0000250|UniProtKB:Q9CRB6, ECO:0000269|PubMed:17105200, ECO:0000269|PubMed:19633818, ECO:0000269|PubMed:30667362}. |
| 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}. |
| Q9BY44 | EIF2A | T5 | ochoa | Eukaryotic translation initiation factor 2A (eIF-2A) (65 kDa eukaryotic translation initiation factor 2A) [Cleaved into: Eukaryotic translation initiation factor 2A, N-terminally processed] | Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner. {ECO:0000269|PubMed:12133843}. |
| 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}. |
| 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}. |
| Q9H190 | SDCBP2 | Y5 | 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}. |
| 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}. |
| Q9HBH5 | RDH14 | T5 | ochoa | Retinol dehydrogenase 14 (EC 1.1.1.300) (Alcohol dehydrogenase PAN2) (Short chain dehydrogenase/reductase family 7C member 4) | Retinol dehydrogenase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinol. Shows a very weak activity towards 13-cis-retinol. Has no activity towards steroid. {ECO:0000269|PubMed:12435598}. |
| 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. |
| 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}. |
| 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}. |
| Q9NVT9 | ARMC1 | T5 | 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}. |
| 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}. |
| 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}. |
| Q9NZT1 | CALML5 | T6 | ochoa | Calmodulin-like protein 5 (Calmodulin-like skin protein) | Binds calcium. May be involved in terminal differentiation of keratinocytes. |
| Q9UBI6 | GNG12 | T5 | 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. |
| Q9UHK0 | NUFIP1 | T5 | ochoa | FMR1-interacting protein NUFIP1 (Nuclear FMR1-interacting protein 1) (Nuclear FMRP-interacting protein 1) | Binds RNA. {ECO:0000269|PubMed:10556305}. |
| 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}. |
| Q9UK76 | JPT1 | T5 | ochoa | Jupiter microtubule associated homolog 1 (Androgen-regulated protein 2) (Hematological and neurological expressed 1 protein) [Cleaved into: Jupiter microtubule associated homolog 1, N-terminally processed] | Modulates negatively AKT-mediated GSK3B signaling (PubMed:21323578, PubMed:22155408). Induces CTNNB1 'Ser-33' phosphorylation and degradation through the suppression of the inhibitory 'Ser-9' phosphorylation of GSK3B, which represses the function of the APC:CTNNB1:GSK3B complex and the interaction with CDH1/E-cadherin in adherent junctions (PubMed:25169422). Plays a role in the regulation of cell cycle and cell adhesion (PubMed:25169422, PubMed:25450365). Has an inhibitory role on AR-signaling pathway through the induction of receptor proteasomal degradation (PubMed:22155408). {ECO:0000269|PubMed:21323578, ECO:0000269|PubMed:22155408, ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:25450365}. |
| 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}. |
| Q9ULS5 | TMCC3 | T6 | ochoa | Transmembrane and coiled-coil domain protein 3 | None |
| Q9UM01 | SLC7A7 | T5 | ochoa | Y+L amino acid transporter 1 (Monocyte amino acid permease 2) (MOP-2) (Solute carrier family 7 member 7) (y(+)L-type amino acid transporter 1) (Y+LAT1) (y+LAT-1) | Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux route by exporting cationic amino acids from inside the cells in exchange with neutral amino acids plus sodium ions and may participate in nitric oxide synthesis via the transport of L-arginine (PubMed:10080182, PubMed:10655553, PubMed:14603368, PubMed:15756301, PubMed:15776427, PubMed:17329401, PubMed:9829974, PubMed:9878049). Also mediates arginine transport in non-polarized cells, such as monocytes, and is essential for the correct function of these cells (PubMed:15280038, PubMed:31705628). The transport mechanism is electroneutral and operates with a stoichiometry of 1:1 (By similarity). In vitro, Na(+) and Li(+), but also H(+), are cotransported with the neutral amino acids (By similarity). {ECO:0000250|UniProtKB:Q9R0S5, ECO:0000269|PubMed:10080182, ECO:0000269|PubMed:10655553, ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15280038, ECO:0000269|PubMed:15756301, ECO:0000269|PubMed:15776427, ECO:0000269|PubMed:17329401, ECO:0000269|PubMed:31705628, ECO:0000269|PubMed:9829974, ECO:0000269|PubMed:9878049}. |
| Q9Y241 | HIGD1A | T5 | ochoa | HIG1 domain family member 1A, mitochondrial (Hypoxia-inducible gene 1 protein) (RCF1 homolog A) (RCF1a) | Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May play a role in the assembly of respiratory supercomplexes. {ECO:0000269|PubMed:22342701}. |
| 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}. |
| 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}. |
| Q9Y3A5 | SBDS | T5 | ochoa | Ribosome maturation protein SBDS (Shwachman-Bodian-Diamond syndrome protein) | Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation. {ECO:0000269|PubMed:17643419, ECO:0000269|PubMed:19602484, ECO:0000269|PubMed:19759903, ECO:0000269|PubMed:21536732}. |
| Q9Y483 | MTF2 | T5 | ochoa | Metal-response element-binding transcription factor 2 (Metal regulatory transcription factor 2) (Metal-response element DNA-binding protein M96) (Polycomb-like protein 2) (hPCl2) | Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity (PubMed:23142980, PubMed:23228662, PubMed:31959557). Regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation (By similarity). Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells (By similarity). Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex (By similarity). In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally (By similarity). Binds to the metal-regulating-element (MRE) of MT1A gene promoter (By similarity). {ECO:0000250|UniProtKB:Q02395, ECO:0000269|PubMed:23142980, ECO:0000269|PubMed:23228662, ECO:0000269|PubMed:31959557}. |
| Q9Y4P1 | ATG4B | 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}. |
| P13639 | EEF2 | T5 | Sugiyama | Elongation factor 2 (EF-2) (EC 3.6.5.-) | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:26593721). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (PubMed:26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:26593721). {ECO:0000269|PubMed:26593721}. |
| 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}. |
| 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. |
| Q9Y3U8 | RPL36 | Y5 | Sugiyama | Large ribosomal subunit protein eL36 (60S ribosomal protein L36) | Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:25901680, PubMed:25957688, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:25901680, PubMed:25957688, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680, ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}. |
| 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}. |
| 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}. |
| 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}. |
| 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}. |
| A0A087WTJ2 | GIMAP1-GIMAP5 | T8 | ochoa | GIMAP1-GIMAP5 readthrough | None |
| A0A0A6YYG9 | ARPC4-TTLL3 | T4 | ochoa | Protein ARPC4-TTLL3 | None |
| A6NKN8 | PCP4L1 | T8 | ochoa | Purkinje cell protein 4-like protein 1 (PCP4-like protein 1) | None |
| A6NMY6 | ANXA2P2 | T3 | ochoa | Putative annexin A2-like protein (Annexin A2 pseudogene 2) (Lipocortin II pseudogene) | Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. {ECO:0000250}. |
| C9JAW5 | None | T3 | ochoa | HIG1 domain-containing protein | None |
| O14613 | CDC42EP2 | T3 | ochoa | Cdc42 effector protein 2 (Binder of Rho GTPases 1) | Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016}. |
| O15020 | SPTBN2 | T4 | ochoa | Spectrin beta chain, non-erythrocytic 2 (Beta-III spectrin) (Spinocerebellar ataxia 5 protein) | Probably plays an important role in neuronal membrane skeleton. |
| O15020 | SPTBN2 | T8 | ochoa | Spectrin beta chain, non-erythrocytic 2 (Beta-III spectrin) (Spinocerebellar ataxia 5 protein) | Probably plays an important role in neuronal membrane skeleton. |
| O15037 | KHNYN | T3 | ochoa | Protein KHNYN (KH and NYN domain-containing protein) | None |
| O15372 | EIF3H | T8 | ochoa | Eukaryotic translation initiation factor 3 subunit H (eIF3h) (Eukaryotic translation initiation factor 3 subunit 3) (eIF-3-gamma) (eIF3 p40 subunit) | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03007, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. |
| O15400 | STX7 | T4 | ochoa | Syntaxin-7 | May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes. |
| O43167 | ZBTB24 | T4 | ochoa | Zinc finger and BTB domain-containing protein 24 (Zinc finger protein 450) | May be involved in BMP2-induced transcription. {ECO:0000250}. |
| O43491 | EPB41L2 | T3 | 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}. |
| O43719 | HTATSF1 | T4 | ochoa | 17S U2 SnRNP complex component HTATSF1 (HIV Tat-specific factor 1) (Tat-SF1) | Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:30567737, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:30567737, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, HTATSF1 is required to stabilize the branchpoint-interacting stem loop (PubMed:34822310). HTATSF1 is displaced from the 17S U2 SnRNP complex before the stable addition of the 17S U2 SnRNP complex to the spliceosome, destabilizing the branchpoint-interacting stem loop and allowing to probe intron branch site sequences (PubMed:32494006, PubMed:34822310). Also acts as a regulator of transcriptional elongation, possibly by mediating the reciprocal stimulatory effect of splicing on transcriptional elongation (PubMed:10454543, PubMed:10913173, PubMed:11780068). Involved in double-strand break (DSB) repair via homologous recombination in S-phase by promoting the recruitment of TOPBP1 to DNA damage sites (PubMed:35597237). Mechanistically, HTATSF1 is (1) recruited to DNA damage sites in S-phase via interaction with poly-ADP-ribosylated RPA1 and (2) phosphorylated by CK2, promoting recruitment of TOPBP1, thereby facilitating RAD51 nucleofilaments formation and RPA displacement, followed by homologous recombination (PubMed:35597237). {ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10913173, ECO:0000269|PubMed:11780068, ECO:0000269|PubMed:30567737, ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:34822310, ECO:0000269|PubMed:35597237}.; FUNCTION: (Microbial infection) In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus. {ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:11420046, ECO:0000269|PubMed:15905670, ECO:0000269|PubMed:8849451, ECO:0000269|PubMed:9765201}. |
| O60684 | KPNA6 | T3 | 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}. |
| O60739 | EIF1B | T3 | ochoa | Eukaryotic translation initiation factor 1b (eIF1b) (Protein translation factor SUI1 homolog GC20) | Probably involved in translation. |
| O75530 | EED | T8 | ochoa | Polycomb protein EED (hEED) (Embryonic ectoderm development protein) (WD protein associating with integrin cytoplasmic tails 1) (WAIT-1) | Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A. {ECO:0000269|PubMed:10581039, ECO:0000269|PubMed:14532106, ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:20974918, ECO:0000269|PubMed:28229514, ECO:0000269|PubMed:9584199}. |
| O75531 | BANF1 | T3 | ochoa|psp | Barrier-to-autointegration factor (Breakpoint cluster region protein 1) [Cleaved into: Barrier-to-autointegration factor, N-terminally processed] | Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA (PubMed:10908652, PubMed:11792822, PubMed:12163470, PubMed:18005698, PubMed:25991860, PubMed:28841419, PubMed:31796734, PubMed:32792394). Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging (PubMed:9465049). Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner (PubMed:28841419). Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface (PubMed:28841419). Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity (PubMed:32792394). Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses (PubMed:32792394). Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1 (PubMed:31796734). Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy (PubMed:25991860). In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication (PubMed:18005698). {ECO:0000269|PubMed:10908652, ECO:0000269|PubMed:11792822, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:25991860, ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32792394, ECO:0000269|PubMed:9465049}.; FUNCTION: (Microbial infection) Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome (PubMed:11005805, PubMed:16680152, PubMed:9465049). EMD and BAF are cooperative cofactors of HIV-1 infection (PubMed:16680152). Association of EMD with the viral DNA requires the presence of BAF and viral integrase (PubMed:16680152). The association of viral DNA with chromatin requires the presence of BAF and EMD (PubMed:16680152). {ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:9465049}. |
| O75821 | EIF3G | T3 | ochoa | Eukaryotic translation initiation factor 3 subunit G (eIF3g) (Eukaryotic translation initiation factor 3 RNA-binding subunit) (eIF-3 RNA-binding subunit) (Eukaryotic translation initiation factor 3 subunit 4) (eIF-3-delta) (eIF3 p42) (eIF3 p44) | RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). This subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.; FUNCTION: (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}. |
| O76080 | ZFAND5 | T8 | ochoa | AN1-type zinc finger protein 5 (Zinc finger A20 domain-containing protein 2) (Zinc finger protein 216) | Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Also inhibits tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation. {ECO:0000269|PubMed:14754897}. |
| O94763 | URI1 | T8 | ochoa | Unconventional prefoldin RPB5 interactor 1 (Protein NNX3) (Protein phosphatase 1 regulatory subunit 19) (RNA polymerase II subunit 5-mediating protein) (RPB5-mediating protein) | Involved in gene transcription regulation. Acts as a transcriptional repressor in concert with the corepressor UXT to regulate androgen receptor (AR) transcription. May act as a tumor suppressor to repress AR-mediated gene transcription and to inhibit anchorage-independent growth in prostate cancer cells. Required for cell survival in ovarian cancer cells. Together with UXT, associates with chromatin to the NKX3-1 promoter region. Antagonizes transcriptional modulation via hepatitis B virus X protein.; FUNCTION: Plays a central role in maintaining S6K1 signaling and BAD phosphorylation under normal growth conditions thereby protecting cells from potential deleterious effects of sustained S6K1 signaling. The URI1-PPP1CC complex acts as a central component of a negative feedback mechanism that counteracts excessive S6K1 survival signaling to BAD in response to growth factors. Mediates inhibition of PPP1CC phosphatase activity in mitochondria. Coordinates the regulation of nutrient-sensitive gene expression availability in a mTOR-dependent manner. Seems to be a scaffolding protein able to assemble a prefoldin-like complex that contains PFDs and proteins with roles in transcription and ubiquitination. |
| O95197 | RTN3 | T8 | ochoa | Reticulon-3 (Homolog of ASY protein) (HAP) (Neuroendocrine-specific protein-like 2) (NSP-like protein 2) (Neuroendocrine-specific protein-like II) (NSP-like protein II) (NSPLII) | May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. Induces the formation of endoplasmic reticulum tubules (PubMed:25612671). Also acts as an inflammation-resolving regulator by interacting with both TRIM25 and RIGI, subsequently impairing RIGI 'Lys-63'-linked polyubiquitination leading to IRF3 and NF-kappa-B inhibition. {ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17191123, ECO:0000269|PubMed:25612671}.; FUNCTION: (Microbial infection) Plays a positive role in viral replication and pathogenesis of enteroviruses. {ECO:0000269|PubMed:17182608}. |
| O95456 | PSMG1 | T4 | ochoa | Proteasome assembly chaperone 1 (PAC-1) (Chromosome 21 leucine-rich protein) (C21-LRP) (Down syndrome critical region protein 2) (Proteasome chaperone homolog 1) (Pba1) | Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization. {ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:17707236}. |
| P00338 | LDHA | T3 | psp | L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (Cell proliferation-inducing gene 19 protein) (LDH muscle subunit) (LDH-M) (Renal carcinoma antigen NY-REN-59) | Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). {ECO:0000269|PubMed:11276087}. |
| P00492 | HPRT1 | T3 | ochoa | Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (HGPRTase) (EC 2.4.2.8) | Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway. |
| P04150 | NR3C1 | T8 | ochoa | Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1) | Receptor for glucocorticoids (GC) (PubMed:27120390, PubMed:37478846). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors (PubMed:28139699). Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:9590696). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (PubMed:25775514). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:25775514, ECO:0000269|PubMed:27120390, ECO:0000269|PubMed:28139699, ECO:0000269|PubMed:37478846, ECO:0000269|PubMed:9590696}.; FUNCTION: [Isoform Alpha]: Has transcriptional activation and repression activity (PubMed:11435610, PubMed:15769988, PubMed:15866175, PubMed:17635946, PubMed:19141540, PubMed:19248771, PubMed:20484466, PubMed:21664385, PubMed:23820903). Mediates glucocorticoid-induced apoptosis (PubMed:23303127). Promotes accurate chromosome segregation during mitosis (PubMed:25847991). May act as a tumor suppressor (PubMed:25847991). May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (By similarity). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:20484466, ECO:0000269|PubMed:21664385, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903, ECO:0000269|PubMed:25847991}.; FUNCTION: [Isoform Beta]: Acts as a dominant negative inhibitor of isoform Alpha (PubMed:20484466, PubMed:7769088, PubMed:8621628). Has intrinsic transcriptional activity independent of isoform Alpha when both isoforms are coexpressed (PubMed:19248771, PubMed:26711253). Loses this transcription modulator function on its own (PubMed:20484466). Has no hormone-binding activity (PubMed:8621628). May play a role in controlling glucose metabolism by maintaining insulin sensitivity (By similarity). Reduces hepatic gluconeogenesis through down-regulation of PEPCK in an isoform Alpha-dependent manner (PubMed:26711253). Directly regulates STAT1 expression in isoform Alpha-independent manner (PubMed:26711253). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:20484466, ECO:0000269|PubMed:26711253, ECO:0000269|PubMed:7769088, ECO:0000269|PubMed:8621628}.; FUNCTION: [Isoform Alpha-2]: Has lower transcriptional activation activity than isoform Alpha. Exerts a dominant negative effect on isoform Alpha trans-repression mechanism (PubMed:20484466).; FUNCTION: [Isoform GR-P]: Increases activity of isoform Alpha. {ECO:0000269|PubMed:11358809}.; FUNCTION: [Isoform Alpha-B]: More effective than isoform Alpha in transcriptional activation, but not repression activity. {ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform 10]: Has transcriptional activation activity. {ECO:0000269|PubMed:20484466}.; FUNCTION: [Isoform Alpha-C1]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-C2]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-C3]: Has highest transcriptional activation activity of all isoforms created by alternative initiation (PubMed:15866175, PubMed:23820903). Has transcriptional repression activity (PubMed:23303127). Mediates glucocorticoid-induced apoptosis (PubMed:23303127, PubMed:23820903). {ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903}.; FUNCTION: [Isoform Alpha-D1]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-D2]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-D3]: Has lowest transcriptional activation activity of all isoforms created by alternative initiation (PubMed:15866175, PubMed:23820903). Has transcriptional repression activity (PubMed:23303127). {ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903}. |
| P05412 | JUN | T8 | psp | Transcription factor Jun (Activator protein 1) (AP1) (Proto-oncogene c-Jun) (Transcription factor AP-1 subunit Jun) (V-jun avian sarcoma virus 17 oncogene homolog) (p39) | Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:10995748, PubMed:22083952). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (By similarity). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (PubMed:12618758). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (PubMed:17210646). Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells (PubMed:24623306). Binds to the USP28 promoter in colorectal cancer (CRC) cells (PubMed:24623306). {ECO:0000250|UniProtKB:P05627, ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:12618758, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:22083952, ECO:0000269|PubMed:24623306}.; FUNCTION: (Microbial infection) Upon Epstein-Barr virus (EBV) infection, binds to viral BZLF1 Z promoter and activates viral BZLF1 expression. {ECO:0000269|PubMed:31341047}. |
| P05783 | KRT18 | T4 | ochoa | Keratin, type I cytoskeletal 18 (Cell proliferation-inducing gene 46 protein) (Cytokeratin-18) (CK-18) (Keratin-18) (K18) | Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}. |
| P05783 | KRT18 | T8 | ochoa | Keratin, type I cytoskeletal 18 (Cell proliferation-inducing gene 46 protein) (Cytokeratin-18) (CK-18) (Keratin-18) (K18) | Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}. |
| P06454 | PTMA | T8 | ochoa | Prothymosin alpha [Cleaved into: Prothymosin alpha, N-terminally processed; Thymosin alpha-1] | Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections. |
| P06730 | EIF4E | T3 | ochoa | Eukaryotic translation initiation factor 4E (eIF-4E) (eIF4E) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) | Acts in the cytoplasm to initiate and regulate protein synthesis and is required in the nucleus for export of a subset of mRNAs from the nucleus to the cytoplasm which promotes processes such as RNA capping, processing and splicing (PubMed:11606200, PubMed:22578813, PubMed:22684010, PubMed:24335285, PubMed:29987188). Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). This protein recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed:16271312, PubMed:22578813). Together with EIF4G1, antagonizes the scanning promoted by EIF1-EIF4G1 and is required for TISU translation, a process where the TISU element recognition makes scanning unnecessary (PubMed:29987188). In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (PubMed:24335285). Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap (By similarity). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (PubMed:24335285). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (By similarity). As well as its roles in translation, also involved in mRNA nucleocytoplasmic transport (By similarity). Its role in mRNA export from the nucleus to the cytoplasm relies on its ability to bind the m7G cap of RNAs and on the presence of the 50-nucleotide EIF4E sensitivity element (4ESE) in the 3'UTR of sensitive transcripts (By similarity). Interaction with the 4ESE is mediated by LRPPRC which binds simultaneously to both EIF4E and the 4ESE, thereby acting as a platform for assembly for the RNA export complex (By similarity). EIF4E-dependent mRNA export is independent of ongoing protein or RNA synthesis and is also NFX1-independent but is XPO1-dependent with LRPPRC interacting with XPO1 to form an EIF4E-dependent mRNA export complex (By similarity). Alters the composition of the cytoplasmic face of the nuclear pore to promote RNA export by reducing RANBP2 expression, relocalizing nucleoporin NUP214 and increasing expression of RANBP1 and RNA export factors DDX19 and GLE1 (By similarity). Promotes the nuclear export of cyclin CCND1 mRNA (By similarity). Promotes the nuclear export of NOS2/iNOS mRNA (PubMed:23471078). Promotes the nuclear export of MDM2 mRNA (PubMed:22684010). Promotes the export of additional mRNAs, including others involved in the cell cycle (By similarity). In the nucleus, binds to capped splice factor-encoding mRNAs and stimulates their nuclear export to enhance splice factor production by increasing their cytoplasmic availability to the translation machinery (By similarity). May also regulate splicing through interaction with the spliceosome in an RNA and m7G cap-dependent manner (By similarity). Also binds to some pre-mRNAs and may play a role in their recruitment to the spliceosome (By similarity). Promotes steady-state capping of a subset of coding and non-coding RNAs by mediating nuclear export of capping machinery mRNAs including RNMT, RNGTT and RAMAC to enhance their translation (By similarity). Stimulates mRNA 3'-end processing by promoting the expression of several core cleavage complex factors required for mRNA cleavage and polyadenylation, and may also have a direct effect through its interaction with the CPSF3 cleavage enzyme (By similarity). Rescues cells from apoptosis by promoting activation of serine/threonine-protein kinase AKT1 through mRNA export of NBS1 which potentiates AKT1 phosphorylation and also through mRNA export of AKT1 effectors, allowing for increased production of these proteins (By similarity). {ECO:0000250|UniProtKB:P63073, ECO:0000250|UniProtKB:P63074, ECO:0000269|PubMed:11606200, ECO:0000269|PubMed:16271312, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22684010, ECO:0000269|PubMed:23471078, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:29987188}. |
| P06730 | EIF4E | T8 | ochoa | Eukaryotic translation initiation factor 4E (eIF-4E) (eIF4E) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) | Acts in the cytoplasm to initiate and regulate protein synthesis and is required in the nucleus for export of a subset of mRNAs from the nucleus to the cytoplasm which promotes processes such as RNA capping, processing and splicing (PubMed:11606200, PubMed:22578813, PubMed:22684010, PubMed:24335285, PubMed:29987188). Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). This protein recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed:16271312, PubMed:22578813). Together with EIF4G1, antagonizes the scanning promoted by EIF1-EIF4G1 and is required for TISU translation, a process where the TISU element recognition makes scanning unnecessary (PubMed:29987188). In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (PubMed:24335285). Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap (By similarity). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (PubMed:24335285). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (By similarity). As well as its roles in translation, also involved in mRNA nucleocytoplasmic transport (By similarity). Its role in mRNA export from the nucleus to the cytoplasm relies on its ability to bind the m7G cap of RNAs and on the presence of the 50-nucleotide EIF4E sensitivity element (4ESE) in the 3'UTR of sensitive transcripts (By similarity). Interaction with the 4ESE is mediated by LRPPRC which binds simultaneously to both EIF4E and the 4ESE, thereby acting as a platform for assembly for the RNA export complex (By similarity). EIF4E-dependent mRNA export is independent of ongoing protein or RNA synthesis and is also NFX1-independent but is XPO1-dependent with LRPPRC interacting with XPO1 to form an EIF4E-dependent mRNA export complex (By similarity). Alters the composition of the cytoplasmic face of the nuclear pore to promote RNA export by reducing RANBP2 expression, relocalizing nucleoporin NUP214 and increasing expression of RANBP1 and RNA export factors DDX19 and GLE1 (By similarity). Promotes the nuclear export of cyclin CCND1 mRNA (By similarity). Promotes the nuclear export of NOS2/iNOS mRNA (PubMed:23471078). Promotes the nuclear export of MDM2 mRNA (PubMed:22684010). Promotes the export of additional mRNAs, including others involved in the cell cycle (By similarity). In the nucleus, binds to capped splice factor-encoding mRNAs and stimulates their nuclear export to enhance splice factor production by increasing their cytoplasmic availability to the translation machinery (By similarity). May also regulate splicing through interaction with the spliceosome in an RNA and m7G cap-dependent manner (By similarity). Also binds to some pre-mRNAs and may play a role in their recruitment to the spliceosome (By similarity). Promotes steady-state capping of a subset of coding and non-coding RNAs by mediating nuclear export of capping machinery mRNAs including RNMT, RNGTT and RAMAC to enhance their translation (By similarity). Stimulates mRNA 3'-end processing by promoting the expression of several core cleavage complex factors required for mRNA cleavage and polyadenylation, and may also have a direct effect through its interaction with the CPSF3 cleavage enzyme (By similarity). Rescues cells from apoptosis by promoting activation of serine/threonine-protein kinase AKT1 through mRNA export of NBS1 which potentiates AKT1 phosphorylation and also through mRNA export of AKT1 effectors, allowing for increased production of these proteins (By similarity). {ECO:0000250|UniProtKB:P63073, ECO:0000250|UniProtKB:P63074, ECO:0000269|PubMed:11606200, ECO:0000269|PubMed:16271312, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22684010, ECO:0000269|PubMed:23471078, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:29987188}. |
| P07355 | ANXA2 | T3 | ochoa | Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36) | Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:22848640, PubMed:24808179). Binds to endosomes damaged by phagocytosis of particulate wear debris and participates in endosomal membrane stabilization, thereby limiting NLRP3 inflammasome activation (By similarity). Required for endothelial cell surface plasmin generation and may support fibrinolytic surveillance and neoangiogenesis (By similarity). {ECO:0000250|UniProtKB:P07356, ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:22848640, ECO:0000269|PubMed:24808179}.; FUNCTION: (Microbial infection) Binds M.pneumoniae CARDS toxin, probably serves as one receptor for this pathogen. When ANXA2 is down-regulated by siRNA, less toxin binds to human cells and less vacuolization (a symptom of M.pneumoniae infection) is seen. {ECO:0000269|PubMed:25139904}. |
| P08670 | VIM | T3 | ochoa | Vimentin | Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). {ECO:0000250|UniProtKB:A0A8C0N8E3, ECO:0000250|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269|PubMed:21746880}. |
| P09914 | IFIT1 | T3 | ochoa | Antiviral innate immune response effector IFIT1 (IFIT-1) (Interferon-induced 56 kDa protein) (IFI-56K) (P56) (Interferon-induced protein with tetratricopeptide repeats 1) | Plays a key role in the innate immune response as part of an interferon-dependent multiprotein complex, recognizing and sequestering viral RNAs that lack host-specific 2'-O-methylation at their 5' cap. By distinguishing these RNAs from host mRNAs, inhibits their translation by competing with the translation initiation factor eIF4E (PubMed:21642987, PubMed:27240734, PubMed:39009378, PubMed:23334420, PubMed:28251928, PubMed:36285486). Could also prevent viral replication through its interaction with DNA replication origin-binding protein E1 of several viruses. Causes the translocation of E1 from the nucleus to the cytoplasm and can also inhibit its helicase activity in vitro (PubMed:19008854, PubMed:21976647). Exhibits antiviral activity against many viruses from the Flaviviridae (West Nile virus, Dengue virus, hepatitis C virus), Coronaviridae (human 229E coronavirus, SARS-CoV-2 and SARS-CoV), Poxviridae (vaccinia virus) and Togaviridae (Sindbis virus) families (PubMed:19008854, PubMed:21976647, PubMed:28251928, PubMed:36285486). {ECO:0000269|PubMed:19008854, ECO:0000269|PubMed:21642987, ECO:0000269|PubMed:21976647, ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:28251928, ECO:0000269|PubMed:36285486, ECO:0000269|PubMed:39009378}. |
| P0C264 | SBK3 | T8 | ochoa | Uncharacterized serine/threonine-protein kinase SBK3 (EC 2.7.11.1) (SH3 domain-binding kinase family member 3) (Sugen kinase 110) | None |
| P10412 | H1-4 | T4 | ochoa | Histone H1.4 (Histone H1b) (Histone H1s-4) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P11836 | MS4A1 | T3 | 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}. |
| P14621 | ACYP2 | T3 | ochoa | Acylphosphatase-2 (EC 3.6.1.7) (Acylphosphatase, muscle type isozyme) (Acylphosphate phosphohydrolase 2) | Its physiological role is not yet clear. |
| P16401 | H1-5 | T4 | ochoa | Histone H1.5 (Histone H1a) (Histone H1b) (Histone H1s-3) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P16402 | H1-3 | T4 | ochoa | Histone H1.3 (Histone H1c) (Histone H1s-2) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P16403 | H1-2 | T4 | ochoa | Histone H1.2 (Histone H1c) (Histone H1d) (Histone H1s-1) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P16885 | PLCG2 | T3 | ochoa | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-gamma-2) (Phospholipase C-IV) (PLC-IV) (Phospholipase C-gamma-2) (PLC-gamma-2) | The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling. {ECO:0000269|PubMed:23000145}. |
| P16989 | YBX3 | T8 | ochoa | Y-box-binding protein 3 (Cold shock domain-containing protein A) (DNA-binding protein A) (Single-strand DNA-binding protein NF-GMB) | Binds to the GM-CSF promoter. Seems to act as a repressor. Also binds to full-length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity). {ECO:0000250}. |
| P20338 | RAB4A | T4 | ochoa | Ras-related protein Rab-4A (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 (PubMed:15907487, PubMed:16034420). RAB4A is involved in protein transport (PubMed:29425100). Also plays a role in vesicular traffic. Mediates VEGFR2 endosomal trafficking to enhance VEGFR2 signaling (PubMed:29425100). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (By similarity). {ECO:0000250|UniProtKB:P56371, ECO:0000269|PubMed:15907487, ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:29425100}. |
| P20340 | RAB6A | T3 | ochoa | Ras-related protein Rab-6A (Rab-6) (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:25962623). 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:25962623). RAB6A acts as a regulator of COPI-independent retrograde transport from the Golgi apparatus towards the endoplasmic reticulum (ER) (PubMed:25962623). Has a low GTPase activity (PubMed:25962623). Recruits VPS13B to the Golgi membrane (PubMed:25492866). Plays a role in neuron projection development (Probable). {ECO:0000269|PubMed:25492866, ECO:0000269|PubMed:25962623, ECO:0000305|PubMed:25492866}. |
| P20472 | PVALB | T4 | ochoa | Parvalbumin alpha (Alpha-parvalbumin) (Alpha-PV) | In muscle, parvalbumin is thought to be involved in relaxation after contraction (By similarity). It binds two calcium ions (PubMed:15122922, PubMed:39584689). {ECO:0000250|UniProtKB:P02624, ECO:0000269|PubMed:15122922, ECO:0000269|PubMed:39584689}. |
| P22234 | PAICS | T3 | ochoa | Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS) [Includes: Phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) (AIR carboxylase) (AIRC); Phosphoribosylaminoimidazole succinocarboxamide synthetase (EC 6.3.2.6) (SAICAR synthetase)] | Bifunctional phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazole succinocarboxamide synthetase catalyzing two reactions of the de novo purine biosynthetic pathway. {ECO:0000269|PubMed:17224163, ECO:0000269|PubMed:2183217, ECO:0000269|PubMed:31600779}. |
| P22626 | HNRNPA2B1 | T4 | ochoa | Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1) | Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Also plays a role in the activation of the innate immune response (PubMed:31320558). Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10567417, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24356509, ECO:0000269|PubMed:26321680, ECO:0000303|PubMed:19099192}.; FUNCTION: (Microbial infection) Involved in the transport of HIV-1 genomic RNA out of the nucleus, to the microtubule organizing center (MTOC), and then from the MTOC to the cytoplasm: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) sequence motifs present on HIV-1 genomic RNA, and promotes its transport. {ECO:0000269|PubMed:15294897, ECO:0000269|PubMed:17004321}. |
| P25205 | MCM3 | T4 | ochoa | DNA replication licensing factor MCM3 (EC 3.6.4.12) (DNA polymerase alpha holoenzyme-associated protein P1) (P1-MCM3) (RLF subunit beta) (p102) | 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 (Probable). {ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232, ECO:0000305|PubMed:35585232}. |
| P27707 | DCK | T3 | ochoa|psp | Deoxycytidine kinase (dCK) (EC 2.7.1.74) (Deoxyadenosine kinase) (EC 2.7.1.76) (Deoxyguanosine kinase) (EC 2.7.1.113) | Phosphorylates the deoxyribonucleosides deoxycytidine, deoxyguanosine and deoxyadenosine (PubMed:12808445, PubMed:18377927, PubMed:19159229, PubMed:1996353, PubMed:20614893, PubMed:20637175). Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents (PubMed:12808445). {ECO:0000269|PubMed:12808445, ECO:0000269|PubMed:18377927, ECO:0000269|PubMed:19159229, ECO:0000269|PubMed:1996353, ECO:0000269|PubMed:20614893, ECO:0000269|PubMed:20637175}. |
| P35222 | CTNNB1 | T3 | ochoa | Catenin beta-1 (Beta-catenin) | Key downstream component of the canonical Wnt signaling pathway (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). Also acts as a coactivator for other transcription factors, such as NR5A2 (PubMed:22187462). Promotes epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via driving transcription of CTNNB1/TCF-target genes (PubMed:29910125). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (By similarity). Acts as a negative regulator of centrosome cohesion (PubMed:18086858). Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization (PubMed:21262353). Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2 (PubMed:18957423). Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity). Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (By similarity). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, via promoting the transcription of differentiation factors such as LEF1, BMP2 and BMP4 (By similarity). Activity is repressed in a MSX1-mediated manner at the bell stage of mesenchymal tooth germ formation which prevents premature differentiation of odontoblasts (By similarity). {ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18957423, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22187462, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:29910125}. |
| P40121 | CAPG | T3 | ochoa | Macrophage-capping protein (Actin regulatory protein CAP-G) | Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA. |
| P41212 | ETV6 | T4 | ochoa | Transcription factor ETV6 (ETS translocation variant 6) (ETS-related protein Tel1) (Tel) | Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'. Plays a role in hematopoiesis and malignant transformation. {ECO:0000269|PubMed:25581430}. |
| P41743 | PRKCI | T3 | 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}. |
| P42858 | HTT | T3 | psp | Huntingtin (Huntington disease protein) (HD protein) [Cleaved into: Huntingtin, myristoylated N-terminal fragment] | [Huntingtin]: May play a role in microtubule-mediated transport or vesicle function.; FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the formation of autophagic vesicles. {ECO:0000269|PubMed:24459296}. |
| P45973 | CBX5 | T8 | ochoa | Chromobox protein homolog 5 (Antigen p25) (Heterochromatin protein 1 homolog alpha) (HP1 alpha) | Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph) (PubMed:19783980). May contribute to the association of heterochromatin with the inner nuclear membrane by interactions with the lamin-B receptor (LBR) (PubMed:19783980). Involved in the formation of kinetochore through interaction with the MIS12 complex subunit NSL1 (PubMed:19783980, PubMed:20231385). Required for the formation of the inner centromere (PubMed:20231385). {ECO:0000269|PubMed:19783980, ECO:0000269|PubMed:20231385}. |
| P46821 | MAP1B | T3 | ochoa | Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1] | Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269|PubMed:18195017, ECO:0000269|PubMed:33268592}. |
| P47974 | ZFP36L2 | T3 | ochoa | mRNA decay activator protein ZFP36L2 (Butyrate response factor 2) (EGF-response factor 2) (ERF-2) (TPA-induced sequence 11d) (Zinc finger protein 36, C3H1 type-like 2) (ZFP36-like 2) | Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:14981510, PubMed:25106868, PubMed:34611029). Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (PubMed:25106868). Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (PubMed:25106868). Binds to 3'-UTR ARE of numerous mRNAs (PubMed:14981510, PubMed:20506496, PubMed:25106868). Promotes ARE-containing mRNA decay of the low-density lipoprotein (LDL) receptor (LDLR) mRNA in response to phorbol 12-myristate 13-acetate (PMA) treatment in a p38 MAPK-dependent manner (PubMed:25106868). Positively regulates early adipogenesis by promoting ARE-mediated mRNA decay of immediate early genes (IEGs). Plays a role in mature peripheral neuron integrity by promoting ARE-containing mRNA decay of the transcriptional repressor REST mRNA. Plays a role in ovulation and oocyte meiotic maturation by promoting ARE-mediated mRNA decay of the luteinizing hormone receptor LHCGR mRNA. Acts as a negative regulator of erythroid cell differentiation: promotes glucocorticoid-induced self-renewal of erythroid cells by binding mRNAs that are induced or highly expressed during terminal erythroid differentiation and promotes their degradation, preventing erythroid cell differentiation. In association with ZFP36L1 maintains quiescence on developing B lymphocytes by promoting ARE-mediated decay of several mRNAs encoding cell cycle regulators that help B cells progress through the cell cycle, and hence ensuring accurate variable-diversity-joining (VDJ) recombination process and functional immune cell formation. Together with ZFP36L1 is also necessary for thymocyte development and prevention of T-cell acute lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated mRNA decay of the oncogenic transcription factor NOTCH1 mRNA. {ECO:0000250|UniProtKB:P23949, ECO:0000269|PubMed:14981510, ECO:0000269|PubMed:20506496, ECO:0000269|PubMed:25106868, ECO:0000269|PubMed:34611029}. |
| P47974 | ZFP36L2 | T4 | ochoa | mRNA decay activator protein ZFP36L2 (Butyrate response factor 2) (EGF-response factor 2) (ERF-2) (TPA-induced sequence 11d) (Zinc finger protein 36, C3H1 type-like 2) (ZFP36-like 2) | Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:14981510, PubMed:25106868, PubMed:34611029). Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (PubMed:25106868). Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (PubMed:25106868). Binds to 3'-UTR ARE of numerous mRNAs (PubMed:14981510, PubMed:20506496, PubMed:25106868). Promotes ARE-containing mRNA decay of the low-density lipoprotein (LDL) receptor (LDLR) mRNA in response to phorbol 12-myristate 13-acetate (PMA) treatment in a p38 MAPK-dependent manner (PubMed:25106868). Positively regulates early adipogenesis by promoting ARE-mediated mRNA decay of immediate early genes (IEGs). Plays a role in mature peripheral neuron integrity by promoting ARE-containing mRNA decay of the transcriptional repressor REST mRNA. Plays a role in ovulation and oocyte meiotic maturation by promoting ARE-mediated mRNA decay of the luteinizing hormone receptor LHCGR mRNA. Acts as a negative regulator of erythroid cell differentiation: promotes glucocorticoid-induced self-renewal of erythroid cells by binding mRNAs that are induced or highly expressed during terminal erythroid differentiation and promotes their degradation, preventing erythroid cell differentiation. In association with ZFP36L1 maintains quiescence on developing B lymphocytes by promoting ARE-mediated decay of several mRNAs encoding cell cycle regulators that help B cells progress through the cell cycle, and hence ensuring accurate variable-diversity-joining (VDJ) recombination process and functional immune cell formation. Together with ZFP36L1 is also necessary for thymocyte development and prevention of T-cell acute lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated mRNA decay of the oncogenic transcription factor NOTCH1 mRNA. {ECO:0000250|UniProtKB:P23949, ECO:0000269|PubMed:14981510, ECO:0000269|PubMed:20506496, ECO:0000269|PubMed:25106868, ECO:0000269|PubMed:34611029}. |
| P48426 | PIP4K2A | T3 | ochoa | Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha) (Diphosphoinositide kinase 2-alpha) (PIP5KIII) (Phosphatidylinositol 5-Phosphate 4-Kinase) (PI5P4Kalpha) (Phosphatidylinositol 5-phosphate 4-kinase type II alpha) (PI(5)P 4-kinase type II alpha) (PIP4KII-alpha) (PtdIns(4)P-5-kinase B isoform) (PtdIns(4)P-5-kinase C isoform) (PtdIns(5)P-4-kinase isoform 2-alpha) | Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (PubMed:23326584, PubMed:9367159). Has both ATP- and GTP-dependent kinase activities (PubMed:26774281). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2 (PubMed:18364242). May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation (By similarity). Required for lysosome-peroxisome membrane contacts and intracellular cholesterol transport through modulating peroxisomal PtdIns(4,5)P2 level (PubMed:29353240). In collaboration with PIP4K2B, has a role in mediating autophagy in times of nutrient stress (By similarity). Required for autophagosome-lysosome fusion and the regulation of cellular lipid metabolism (PubMed:31091439). May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size (By similarity). Negatively regulates insulin signaling through a catalytic-independent mechanism (PubMed:31091439). PIP4Ks interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (PubMed:31091439). {ECO:0000250|UniProtKB:O70172, ECO:0000250|UniProtKB:Q9R0I8, ECO:0000269|PubMed:18364242, ECO:0000269|PubMed:23326584, ECO:0000269|PubMed:26774281, ECO:0000269|PubMed:29353240, ECO:0000269|PubMed:31091439, ECO:0000269|PubMed:9367159}. |
| P49189 | ALDH9A1 | T3 | ochoa | 4-trimethylaminobutyraldehyde dehydrogenase (TMABA-DH) (TMABALDH) (EC 1.2.1.47) (Aldehyde dehydrogenase E3 isozyme) (Aldehyde dehydrogenase family 9 member A1) (EC 1.2.1.3) (Formaldehyde dehydrogenase) (EC 1.2.1.46) (Gamma-aminobutyraldehyde dehydrogenase) (EC 1.2.1.19) (R-aminobutyraldehyde dehydrogenase) [Cleaved into: 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed] | Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine with high efficiency (in vitro). Can catalyze the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction, but with low efficiency. Catalyzes the oxidation of aldehydes arising from biogenic amines and polyamines. {ECO:0000269|PubMed:10702312, ECO:0000269|PubMed:1799975, ECO:0000269|PubMed:30914451, ECO:0000269|PubMed:8645224}. |
| P49321 | NASP | T8 | ochoa | Nuclear autoantigenic sperm protein (NASP) | Component of the histone chaperone network (PubMed:22195965). Binds and stabilizes histone H3-H4 not bound to chromatin to maintain a soluble reservoir and modulate degradation by chaperone-mediated autophagy (PubMed:22195965). Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA. {ECO:0000250|UniProtKB:Q99MD9, ECO:0000269|PubMed:22195965}.; FUNCTION: [Isoform 1]: Stabilizes soluble histone H3-H4. {ECO:0000269|PubMed:22195965}.; FUNCTION: [Isoform 2]: Stabilizes soluble histone H3-H4. {ECO:0000269|PubMed:22195965}. |
| P49356 | FNTB | T8 | ochoa | Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Ras proteins prenyltransferase subunit beta) | Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8494894}. |
| P49841 | GSK3B | T8 | ochoa | Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1) | Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1 (PubMed:11430833, PubMed:12554650, PubMed:14690523, PubMed:16484495, PubMed:1846781, PubMed:20937854, PubMed:9072970). Requires primed phosphorylation of the majority of its substrates (PubMed:11430833, PubMed:16484495). In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (PubMed:8397507). May also mediate the development of insulin resistance by regulating activation of transcription factors (PubMed:8397507). Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase (PubMed:8397507). In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes (PubMed:12554650). Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA (PubMed:1846781). Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin (PubMed:9072970). Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules (PubMed:14690523). MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease (PubMed:14690523). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair (By similarity). Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA) (By similarity). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin (PubMed:9819408). Is necessary for the establishment of neuronal polarity and axon outgrowth (PubMed:20067585). Phosphorylates MARK2, leading to inhibition of its activity (By similarity). Phosphorylates SIK1 at 'Thr-182', leading to sustainment of its activity (PubMed:18348280). Phosphorylates ZC3HAV1 which enhances its antiviral activity (PubMed:22514281). Phosphorylates SNAI1, leading to its ubiquitination and proteasomal degradation (PubMed:15448698, PubMed:15647282, PubMed:25827072, PubMed:29059170). Phosphorylates SFPQ at 'Thr-687' upon T-cell activation (PubMed:20932480). Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including BMAL1, CLOCK and PER2 (PubMed:19946213, PubMed:28903391). Phosphorylates FBXL2 at 'Thr-404' and primes it for ubiquitination by the SCF(FBXO3) complex and proteasomal degradation (By similarity). Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation (PubMed:19946213). Phosphorylates BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation (PubMed:28903391). Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation (PubMed:24391509). Regulates the circadian rhythmicity of hippocampal long-term potentiation and BMAL1 and PER2 expression (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, activating KAT5/TIP60 acetyltransferase activity and promoting acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (PubMed:18846110). Phosphorylates E2F1, promoting the interaction between E2F1 and USP11, stabilizing E2F1 and promoting its activity (PubMed:17050006, PubMed:28992046). Phosphorylates mTORC2 complex component RICTOR at 'Ser-1235' in response to endoplasmic stress, inhibiting mTORC2 (PubMed:21343617). Phosphorylates mTORC2 complex component RICTOR at 'Thr-1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR (PubMed:25897075). Phosphorylates FXR1, promoting FXR1 ubiquitination by the SCF(FBXO4) complex and FXR1 degradation by the proteasome (By similarity). Phosphorylates interleukin-22 receptor subunit IL22RA1, preventing its proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P18266, ECO:0000250|UniProtKB:Q9WV60, ECO:0000269|PubMed:11430833, ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15448698, ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:17050006, ECO:0000269|PubMed:18348280, ECO:0000269|PubMed:1846781, ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20067585, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:21343617, ECO:0000269|PubMed:22514281, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:25827072, ECO:0000269|PubMed:25897075, ECO:0000269|PubMed:28903391, ECO:0000269|PubMed:28992046, ECO:0000269|PubMed:29059170, ECO:0000269|PubMed:30704899, ECO:0000269|PubMed:8397507, ECO:0000269|PubMed:9072970, ECO:0000269|PubMed:9819408}. |
| P49902 | NT5C2 | T3 | 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}. |
| P49959 | MRE11 | T3 | ochoa | Double-strand break repair protein MRE11 (EC 3.1.-.-) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A) | Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:11741547, PubMed:14657032, PubMed:22078559, PubMed:23080121, PubMed:24316220, PubMed:26240375, PubMed:27889449, PubMed:28867292, PubMed:29670289, PubMed:30464262, PubMed:30612738, PubMed:31353207, PubMed:37696958, PubMed:38128537, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:24316220, PubMed:28867292, PubMed:31353207, PubMed:38128537). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:24316220, PubMed:27889449, PubMed:28867292, PubMed:36050397, PubMed:38128537). Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity (PubMed:11741547, PubMed:22078559, PubMed:24316220, PubMed:26240375, PubMed:27889449, PubMed:29670289, PubMed:31353207, PubMed:36563124, PubMed:9590181, PubMed:9651580, PubMed:9705271). After DSBs, MRE11 is loaded onto DSBs sites and cleaves DNA by cooperating with RBBP8/CtIP to initiate end resection (PubMed:27814491, PubMed:27889449, PubMed:30787182). MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR (PubMed:24316220). It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation to create entry sites for EXO1- and DNA2-mediated 5' to 3' long-range resection, which is required for single-strand invasion and recombination (PubMed:24316220, PubMed:28867292). RBBP8/CtIP specifically promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182). MRE11 endonuclease activity is also enhanced by AGER/RAGE (By similarity). The MRN complex is also required for DNA damage signaling via activation of the ATM and ATR kinases: the nuclease activity of MRE11 is not required to activate ATM and ATR (PubMed:14657032, PubMed:15064416, PubMed:15790808, PubMed:16622404). The MRN complex is also required for the processing of R-loops (PubMed:31537797). The MRN complex is involved in the activation of the cGAS-STING pathway induced by DNA damage during tumorigenesis: the MRN complex acts by displacing CGAS from nucleosome sequestration, thereby activating it (By similarity). In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888). {ECO:0000250|UniProtKB:Q61216, ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:11741547, ECO:0000269|PubMed:14657032, ECO:0000269|PubMed:15064416, ECO:0000269|PubMed:15790808, ECO:0000269|PubMed:16622404, ECO:0000269|PubMed:22078559, ECO:0000269|PubMed:23080121, ECO:0000269|PubMed:24316220, ECO:0000269|PubMed:26240375, ECO:0000269|PubMed:27814491, ECO:0000269|PubMed:27889449, ECO:0000269|PubMed:28867292, ECO:0000269|PubMed:29670289, ECO:0000269|PubMed:30464262, ECO:0000269|PubMed:30612738, ECO:0000269|PubMed:30787182, ECO:0000269|PubMed:31353207, ECO:0000269|PubMed:31537797, ECO:0000269|PubMed:36050397, ECO:0000269|PubMed:36563124, ECO:0000269|PubMed:37696958, ECO:0000269|PubMed:38128537, ECO:0000269|PubMed:9590181, ECO:0000269|PubMed:9651580, ECO:0000269|PubMed:9705271}.; FUNCTION: MRE11 contains two DNA-binding domains (DBDs), enabling it to bind both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). {ECO:0000305}. |
| P50548 | ERF | T3 | 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}. |
| P51532 | SMARCA4 | T3 | ochoa | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4 (SMARCA4) (EC 3.6.4.-) (BRG1-associated factor 190A) (BAF190A) (Mitotic growth and transcription activator) (Protein BRG-1) (Protein brahma homolog 1) (SNF2-beta) (Transcription activator BRG1) | ATPase 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 (PubMed:15075294, PubMed:29374058, PubMed:30339381, PubMed:32459350). Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating the calcium-dependent release of a repressor complex and the recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by SMARCA4-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves the release of HDAC1 and recruitment of CREBBP (By similarity). 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. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues (By similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1 (PubMed:20418909). Binds via DLX1 to enhancers located in the intergenic region between DLX5 and DLX6 and this binding is stabilized by the long non-coding RNA (lncRNA) Evf2 (By similarity). Binds to RNA in a promiscuous manner (By similarity). In brown adipose tissue, involved in the regulation of thermogenic genes expression (By similarity). {ECO:0000250|UniProtKB:Q3TKT4, ECO:0000250|UniProtKB:Q8K1P7, ECO:0000269|PubMed:15075294, ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:20418909, ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:30339381, ECO:0000269|PubMed:32459350, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
| P52292 | KPNA2 | T3 | ochoa | Importin subunit alpha-1 (Karyopherin subunit alpha-2) (RAG cohort protein 1) (SRP1-alpha) | Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1 (PubMed:28991411, PubMed:32130408, PubMed:7604027, PubMed:7754385). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (PubMed:28991411, PubMed:32130408, PubMed:7604027, PubMed:7754385). Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:7604027, PubMed:7754385). At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediator of PR-DUB complex component BAP1 nuclear import; acts redundantly with KPNA1 and Transportin-1/TNPO1 (PubMed:35446349). {ECO:0000269|PubMed:28991411, ECO:0000269|PubMed:32130408, ECO:0000269|PubMed:35446349, ECO:0000269|PubMed:7604027, ECO:0000269|PubMed:7754385}. |
| P52294 | KPNA1 | T3 | ochoa | Importin subunit alpha-5 (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta) [Cleaved into: Importin subunit alpha-5, N-terminally processed] | Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1 (PubMed:27713473, PubMed:7892216, PubMed:8692858). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (PubMed:27713473, PubMed:7892216, PubMed:8692858). Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:27713473, PubMed:7892216). At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin (PubMed:7892216). The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:7892216). Mediator of PR-DUB complex component BAP1 nuclear import; acts redundantly with KPNA2 and Transportin-1/TNPO1 (PubMed:35446349). {ECO:0000269|PubMed:27713473, ECO:0000269|PubMed:35446349, ECO:0000269|PubMed:7892216, ECO:0000269|PubMed:8692858}.; FUNCTION: (Microbial infection) In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. {ECO:0000269|PubMed:12610148}. |
| P53611 | RABGGTB | T3 | ochoa | Geranylgeranyl transferase type-2 subunit beta (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit beta) (GGTase-II-beta) (Rab geranyl-geranyltransferase subunit beta) (Rab GG transferase beta) (Rab GGTase beta) (Rab geranylgeranyltransferase subunit beta) (Type II protein geranyl-geranyltransferase subunit beta) | Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. {ECO:0000269|PubMed:7991565}. |
| P55160 | NCKAP1L | T4 | ochoa | Nck-associated protein 1-like (Hematopoietic protein 1) (Membrane-associated protein HEM-1) | Essential hematopoietic-specific regulator of the actin cytoskeleton (Probable). Controls lymphocyte development, activation, proliferation and homeostasis, erythrocyte membrane stability, as well as phagocytosis and migration by neutrophils and macrophages (PubMed:16417406, PubMed:17696648). Component of the WAVE2 complex which signals downstream of RAC to stimulate F-actin polymerization. Required for stabilization and/or translation of the WAVE2 complex proteins in hematopoietic cells (By similarity). Within the WAVE2 complex, enables the cortical actin network to restrain excessive degranulation and granule release by T-cells (PubMed:32647003). Required for efficient T-lymphocyte and neutrophil migration (PubMed:32647003). Exhibits complex cycles of activation and inhibition to generate waves of propagating the assembly with actin (PubMed:16417406). Also involved in mechanisms WAVE-independent to regulate myosin and actin polymerization during neutrophil chemotaxis (PubMed:17696648). In T-cells, required for proper mechanistic target of rapamycin complex 2 (mTORC2)-dependent AKT phosphorylation, cell proliferation and cytokine secretion, including that of IL2 and TNF (PubMed:32647003). {ECO:0000250|UniProtKB:Q8K1X4, ECO:0000269|PubMed:16417406, ECO:0000269|PubMed:17696648, ECO:0000269|PubMed:32647003, ECO:0000303|PubMed:20969869}. |
| P57088 | TMEM33 | T4 | ochoa | Transmembrane protein 33 (Protein DB83) (SHINC-3) | Acts as a regulator of the tubular endoplasmic reticulum (ER) network by modulating intracellular calcium homeostasis. Mechanistically, stimulates PKD2 calcium-dependent activity (By similarity). Suppresses the RTN3/4-induced formation of the ER tubules (PubMed:25612671). Positively regulates PERK-mediated and IRE1-mediated unfolded protein response signaling (PubMed:26268696). Plays an essential role in VEGF-mediated release of Ca(2+) from ER stores during angiogenesis (PubMed:30760708). Also plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (PubMed:32614325). Participates in lipid metabolism by acting as a downstream effector of the pyruvate kinase/PKM. Forms a complex with RNF5 to facilitate polyubiquitination and subsequent degradation of SCAP on the ER membrane (PubMed:34487377). {ECO:0000250|UniProtKB:Q9CR67, ECO:0000269|PubMed:25612671, ECO:0000269|PubMed:26268696, ECO:0000269|PubMed:30760708, ECO:0000269|PubMed:32614325, ECO:0000269|PubMed:34487377}. |
| P59998 | ARPC4 | T4 | ochoa | Actin-related protein 2/3 complex subunit 4 (Arp2/3 complex 20 kDa subunit) (p20-ARC) | Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). {ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:9230079}. |
| P61978 | HNRNPK | T3 | ochoa | Heterogeneous nuclear ribonucleoprotein K (hnRNP K) (Transformation up-regulated nuclear protein) (TUNP) | One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPL and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). {ECO:0000250, ECO:0000269|PubMed:16360036, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:22825850, ECO:0000269|PubMed:33174841}. |
| P63010 | AP2B1 | T8 | ochoa | AP-2 complex subunit beta (AP105B) (Adaptor protein complex AP-2 subunit beta) (Adaptor-related protein complex 2 subunit beta) (Beta-2-adaptin) (Beta-adaptin) (Clathrin assembly protein complex 2 beta large chain) (Plasma membrane adaptor HA2/AP2 adaptin beta subunit) | Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly. {ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:14985334, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23676497}. |
| P78347 | GTF2I | T8 | ochoa | General transcription factor II-I (GTFII-I) (TFII-I) (Bruton tyrosine kinase-associated protein 135) (BAP-135) (BTK-associated protein 135) (SRF-Phox1-interacting protein) (SPIN) (Williams-Beuren syndrome chromosomal region 6 protein) | Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. {ECO:0000269|PubMed:10373551, ECO:0000269|PubMed:11373296, ECO:0000269|PubMed:16738337}. |
| P84022 | SMAD3 | T8 | ochoa|psp | Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3) | Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:15588252, ECO:0000269|PubMed:16156666, ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16862174, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:19218245, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:9732876, ECO:0000269|PubMed:9892009}. |
| Q00341 | HDLBP | T8 | ochoa | Vigilin (High density lipoprotein-binding protein) (HDL-binding protein) | Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol. |
| Q02539 | H1-1 | T4 | ochoa | Histone H1.1 (Histone H1a) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| Q02978 | SLC25A11 | T4 | 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}. |
| Q04609 | FOLH1 | T8 | ochoa | Glutamate carboxypeptidase 2 (EC 3.4.17.21) (Cell growth-inhibiting gene 27 protein) (Folate hydrolase 1) (Folylpoly-gamma-glutamate carboxypeptidase) (FGCP) (Glutamate carboxypeptidase II) (GCPII) (Membrane glutamate carboxypeptidase) (mGCP) (N-acetylated-alpha-linked acidic dipeptidase I) (NAALADase I) (Prostate-specific membrane antigen) (PSM) (PSMA) (Pteroylpoly-gamma-glutamate carboxypeptidase) | Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Involved in prostate tumor progression.; FUNCTION: Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC. |
| Q06265 | EXOSC9 | T4 | ochoa | Exosome complex component RRP45 (Autoantigen PM/Scl 1) (Exosome component 9) (P75 polymyositis-scleroderma overlap syndrome-associated autoantigen) (Polymyositis/scleroderma autoantigen 1) (Polymyositis/scleroderma autoantigen 75 kDa) (PM/Scl-75) | 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. EXOSC9 binds to ARE-containing RNAs. {ECO:0000269|PubMed:11782436, ECO:0000269|PubMed:16455498, ECO:0000269|PubMed:16912217, ECO:0000269|PubMed:17545563}. |
| Q06330 | RBPJ | T4 | 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}. |
| Q08945 | SSRP1 | T4 | ochoa | FACT complex subunit SSRP1 (Chromatin-specific transcription elongation factor 80 kDa subunit) (Facilitates chromatin transcription complex 80 kDa subunit) (FACT 80 kDa subunit) (FACTp80) (Facilitates chromatin transcription complex subunit SSRP1) (Recombination signal sequence recognition protein 1) (Structure-specific recognition protein 1) (hSSRP1) (T160) | Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63. {ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12374749, ECO:0000269|PubMed:12934006, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704, ECO:0000269|PubMed:9566881, ECO:0000269|PubMed:9836642}. |
| Q12891 | HYAL2 | T8 | ochoa | Hyaluronidase-2 (Hyal-2) (EC 3.2.1.35) (Hyaluronoglucosaminidase-2) (Lung carcinoma protein 2) (LuCa-2) | Catalyzes hyaluronan degradation into small fragments that are endocytosed and degraded in lysosomes by HYAL1 and exoglycosidases (PubMed:9712871). Essential for the breakdown of extracellular matrix hyaluronan (PubMed:28081210). {ECO:0000269|PubMed:28081210, ECO:0000269|PubMed:9712871}. |
| Q13206 | DDX10 | T4 | 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}. |
| Q13451 | FKBP5 | T3 | ochoa | Peptidyl-prolyl cis-trans isomerase FKBP5 (PPIase FKBP5) (EC 5.2.1.8) (51 kDa FK506-binding protein) (51 kDa FKBP) (FKBP-51) (54 kDa progesterone receptor-associated immunophilin) (Androgen-regulated protein 6) (FF1 antigen) (FK506-binding protein 5) (FKBP-5) (FKBP54) (p54) (HSP90-binding immunophilin) (Rotamase) | Immunophilin protein with PPIase and co-chaperone activities (PubMed:11350175). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded (PubMed:12538866). Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1 (PubMed:28147277, PubMed:28363942). Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappa-B activation, and IFN production (PubMed:26101251, PubMed:31434731). {ECO:0000269|PubMed:11350175, ECO:0000269|PubMed:12538866, ECO:0000269|PubMed:26101251, ECO:0000269|PubMed:28147277, ECO:0000269|PubMed:28363942, ECO:0000269|PubMed:31434731}. |
| Q13464 | ROCK1 | T3 | ochoa | Rho-associated protein kinase 1 (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-35) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK) | Protein kinase which is a key regulator of the actin cytoskeleton and cell polarity (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:8617235, PubMed:9722579). Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:23093407, PubMed:23355470, PubMed:8617235, PubMed:9722579). Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing (PubMed:18694941). Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress (PubMed:19036714). Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability (By similarity). Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation (PubMed:19181962). Required for centrosome positioning and centrosome-dependent exit from mitosis (By similarity). Plays a role in terminal erythroid differentiation (PubMed:21072057). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Promotes keratinocyte terminal differentiation (PubMed:19997641). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles (By similarity). {ECO:0000250|UniProtKB:P70335, ECO:0000250|UniProtKB:Q8MIT6, ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:10652353, ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:11283607, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:18694941, ECO:0000269|PubMed:19036714, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19181962, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21072057, ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:8617235, ECO:0000269|PubMed:9722579}. |
| Q13573 | SNW1 | T4 | ochoa | SNW domain-containing protein 1 (Nuclear protein SkiP) (Nuclear receptor coactivator NCoA-62) (Ski-interacting protein) | Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346, PubMed:28502770). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Required for the specific splicing of CDKN1A pre-mRNA; the function probably involves the recruitment of U2AF2 to the mRNA. May recruit PPIL1 to the spliceosome. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in transcriptional regulation. Modulates TGF-beta-mediated transcription via association with SMAD proteins, MYOD1-mediated transcription via association with PABPN1, RB1-mediated transcriptional repression, and retinoid-X receptor (RXR)- and vitamin D receptor (VDR)-dependent gene transcription in a cell line-specific manner probably involving coactivators NCOA1 and GRIP1. Is involved in NOTCH1-mediated transcriptional activation. Binds to multimerized forms of Notch intracellular domain (NICD) and is proposed to recruit transcriptional coactivators such as MAML1 to form an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ to form a transcriptional activation complex by releasing SNW1 and redundant NOTCH1 NICD. {ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:11278756, ECO:0000269|PubMed:11371506, ECO:0000269|PubMed:11514567, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12840015, ECO:0000269|PubMed:14985122, ECO:0000269|PubMed:15194481, ECO:0000269|PubMed:15905409, ECO:0000269|PubMed:18794151, ECO:0000269|PubMed:19818711, ECO:0000269|PubMed:21245387, ECO:0000269|PubMed:21460037, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:9632709, ECO:0000305|PubMed:33509932}.; FUNCTION: (Microbial infection) Is recruited by HIV-1 Tat to Tat:P-TEFb:TAR RNA complexes and is involved in Tat transcription by recruitment of MYC, MEN1 and TRRAP to the HIV promoter. {ECO:0000269|PubMed:15905409, ECO:0000269|PubMed:19818711}.; FUNCTION: (Microbial infection) Proposed to be involved in transcriptional activation by EBV EBNA2 of CBF-1/RBPJ-repressed promoters. {ECO:0000269|PubMed:10644367}. |
| Q14151 | SAFB2 | T4 | ochoa | Scaffold attachment factor B2 (SAF-B2) | Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation. |
| Q14676 | MDC1 | T4 | ochoa|psp | Mediator of DNA damage checkpoint protein 1 (Nuclear factor with BRCT domains 1) | Histone reader protein required for checkpoint-mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle (PubMed:12475977, PubMed:12499369, PubMed:12551934, PubMed:12607003, PubMed:12607004, PubMed:12607005, PubMed:12611903, PubMed:14695167, PubMed:15201865, PubMed:15377652, PubMed:16049003, PubMed:16377563, PubMed:30898438). Specifically recognizes and binds histone H2AX phosphorylated at 'Ser-139', a marker of DNA damage, serving as a scaffold for the recruitment of DNA repair and signal transduction proteins to discrete foci of DNA damage sites (PubMed:12607005, PubMed:15201865, PubMed:16049003, PubMed:16377563, PubMed:30898438). Also required for downstream events subsequent to the recruitment of these proteins (PubMed:12607005, PubMed:15201865, PubMed:16049003, PubMed:16377563, PubMed:18582474). These include phosphorylation and activation of the ATM, CHEK1 and CHEK2 kinases, and stabilization of TP53/p53 and apoptosis (PubMed:12499369, PubMed:12551934, PubMed:12607004). ATM and CHEK2 may also be activated independently by a parallel pathway mediated by TP53BP1 (PubMed:12499369, PubMed:12551934, PubMed:12607004). Required for chromosomal stability during mitosis by promoting recruitment of TOPBP1 to DNA double strand breaks (DSBs): TOPBP1 forms filamentous assemblies that bridge MDC1 and tether broken chromosomes during mitosis (PubMed:30898438). Required for the repair of DSBs via homologous recombination by promoting recruitment of NBN component of the MRN complex to DSBs (PubMed:18411307, PubMed:18582474, PubMed:18583988, PubMed:18678890). {ECO:0000269|PubMed:12475977, ECO:0000269|PubMed:12499369, ECO:0000269|PubMed:12551934, ECO:0000269|PubMed:12607003, ECO:0000269|PubMed:12607004, ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:12611903, ECO:0000269|PubMed:14695167, ECO:0000269|PubMed:15201865, ECO:0000269|PubMed:15377652, ECO:0000269|PubMed:16049003, ECO:0000269|PubMed:16377563, ECO:0000269|PubMed:18411307, ECO:0000269|PubMed:18582474, ECO:0000269|PubMed:18583988, ECO:0000269|PubMed:18678890, ECO:0000269|PubMed:30898438}. |
| Q14749 | GNMT | T8 | psp | Glycine N-methyltransferase (EC 2.1.1.20) | Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy), a reaction regulated by the binding of 5-methyltetrahydrofolate. Plays an important role in the regulation of methyl group metabolism by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. {ECO:0000269|PubMed:14651980, ECO:0000269|PubMed:14739680, ECO:0000269|PubMed:17660255, ECO:0000269|PubMed:8281755}. |
| Q15020 | SART3 | T3 | 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}. |
| Q15637 | SF1 | T3 | ochoa | Splicing factor 1 (Mammalian branch point-binding protein) (BBP) (mBBP) (Transcription factor ZFM1) (Zinc finger gene in MEN1 locus) (Zinc finger protein 162) | Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor. {ECO:0000269|PubMed:10449420, ECO:0000269|PubMed:8752089, ECO:0000269|PubMed:9660765}. |
| Q15637 | SF1 | T8 | ochoa | Splicing factor 1 (Mammalian branch point-binding protein) (BBP) (mBBP) (Transcription factor ZFM1) (Zinc finger gene in MEN1 locus) (Zinc finger protein 162) | Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor. {ECO:0000269|PubMed:10449420, ECO:0000269|PubMed:8752089, ECO:0000269|PubMed:9660765}. |
| Q15691 | MAPRE1 | T8 | ochoa | Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1) (End-binding protein 1) (EB1) | Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:23001180, PubMed:28726242, PubMed:28814570, PubMed:34608293). Recruits other +TIP proteins to microtubules by binding to a conserved Ser-X-Leu-Pro (SXLP) motif in their polypeptide chains (PubMed:19632184, PubMed:36592928). Promotes cytoplasmic microtubule nucleation and elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). Involved in mitotic spindle positioning by stabilizing microtubules and promoting dynamic connection between astral microtubules and the cortex during mitotic chromosome segregation (PubMed:12388762, PubMed:34608293). Assists chromosome alignment in metaphase by recruiting the SKA complex to the spindle and stabilizing its interactions with microtubule bundles (K-fibers) (PubMed:27225956, PubMed:36592928). Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:28814570). Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (PubMed:28814570). Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (PubMed:28726242). Functions downstream of Rho GTPases and DIAPH1 in stable microtubule formation (By similarity). May play a role in cell migration (By similarity). {ECO:0000250|UniProtKB:Q61166, ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:16109370, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:23001180, ECO:0000269|PubMed:27225956, ECO:0000269|PubMed:28726242, ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:34608293, ECO:0000269|PubMed:36592928}. |
| Q15742 | NAB2 | T8 | ochoa | NGFI-A-binding protein 2 (EGR-1-binding protein 2) (Melanoma-associated delayed early response protein) (Protein MADER) | Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability (By similarity). {ECO:0000250}. |
| Q15796 | SMAD2 | T8 | ochoa|psp | Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2) | Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. Promotes TGFB1-mediated transcription of odontoblastic differentiation genes in dental papilla cells (By similarity). Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. May act as a tumor suppressor in colorectal carcinoma (PubMed:8752209). {ECO:0000250|UniProtKB:Q62432, ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16862174, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:8752209, ECO:0000269|PubMed:9892009}. |
| Q15836 | VAMP3 | T3 | 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}. |
| Q16186 | ADRM1 | T3 | ochoa | Proteasomal ubiquitin receptor ADRM1 (110 kDa cell membrane glycoprotein) (Gp110) (Adhesion-regulating molecule 1) (ARM-1) (Proteasome regulatory particle non-ATPase 13) (hRpn13) (Rpn13 homolog) | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). Within the complex, functions as a proteasomal ubiquitin receptor (PubMed:18497817). Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation (PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:24752541). UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex (PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:24752541). {ECO:0000269|PubMed:16815440, ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18497817, ECO:0000269|PubMed:24752541, ECO:0000269|PubMed:25702870, ECO:0000269|PubMed:25702872}. |
| Q5SSJ5 | HP1BP3 | T3 | 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}. |
| Q5T0W9 | FAM83B | T3 | ochoa | Protein FAM83B | Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269|PubMed:22886302, ECO:0000269|PubMed:23676467, ECO:0000269|PubMed:23912460}. |
| Q5T4S7 | UBR4 | T3 | ochoa | E3 ubiquitin-protein ligase UBR4 (EC 2.3.2.27) (600 kDa retinoblastoma protein-associated factor) (p600) (N-recognin-4) (Retinoblastoma-associated factor of 600 kDa) (RBAF600) | E3 ubiquitin-protein ligase involved in different protein quality control pathways in the cytoplasm (PubMed:25582440, PubMed:29033132, PubMed:34893540, PubMed:37891180, PubMed:38030679, PubMed:38182926, PubMed:38297121). Component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation (PubMed:34893540, PubMed:37891180, PubMed:38030679). Recognizes both type-1 and type-2 N-degrons, containing positively charged amino acids (Arg, Lys and His) and bulky and hydrophobic amino acids, respectively (PubMed:38030679). Does not ubiquitinate proteins that are acetylated at the N-terminus (PubMed:37891180). Together with UBR5, part of a cytoplasm protein quality control pathway that prevents protein aggregation by catalyzing assembly of heterotypic 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on aggregated proteins, leading to substrate recognition by the segregase p97/VCP and degradation by the proteasome: UBR4 probably synthesizes mixed chains containing multiple linkages, while UBR5 is likely branching multiple 'Lys-48'-linked chains of substrates initially modified (PubMed:29033132). Together with KCMF1, part of a protein quality control pathway that catalyzes ubiquitination and degradation of proteins that have been oxidized in response to reactive oxygen species (ROS): recognizes proteins with an Arg-CysO3(H) degron at the N-terminus, and mediates assembly of heterotypic 'Lys-63'-/'Lys-27'-linked branched ubiquitin chains on oxidized proteins, leading to their degradation by autophagy (PubMed:34893540). Catalytic component of the SIFI complex, a multiprotein complex required to inhibit the mitochondrial stress response after a specific stress event has been resolved: ubiquitinates and degrades (1) components of the HRI-mediated signaling of the integrated stress response, such as DELE1 and EIF2AK1/HRI, as well as (2) unimported mitochondrial precursors (PubMed:38297121). Within the SIFI complex, UBR4 initiates ubiquitin chain that are further elongated or branched by KCMF1 (PubMed:38297121). Mediates ubiquitination of ACLY, leading to its subsequent degradation (PubMed:23932781). Together with clathrin, forms meshwork structures involved in membrane morphogenesis and cytoskeletal organization (PubMed:16214886). {ECO:0000269|PubMed:16214886, ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:25582440, ECO:0000269|PubMed:29033132, ECO:0000269|PubMed:34893540, ECO:0000269|PubMed:37891180, ECO:0000269|PubMed:38030679, ECO:0000269|PubMed:38182926, ECO:0000269|PubMed:38297121}. |
| Q6NSJ2 | PHLDB3 | T3 | ochoa | Pleckstrin homology-like domain family B member 3 | None |
| Q6PKG0 | LARP1 | T3 | ochoa | La-related protein 1 (La ribonucleoprotein domain family member 1) | RNA-binding protein that regulates the translation of specific target mRNA species downstream of the mTORC1 complex, in function of growth signals and nutrient availability (PubMed:20430826, PubMed:23711370, PubMed:24532714, PubMed:25940091, PubMed:28650797, PubMed:28673543, PubMed:29244122). Interacts on the one hand with the 3' poly-A tails that are present in all mRNA molecules, and on the other hand with the 7-methylguanosine cap structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding ribosomal proteins and several components of the translation machinery (PubMed:23711370, PubMed:25940091, PubMed:26206669, PubMed:28379136, PubMed:28650797, PubMed:29244122). The interaction with the 5' end of mRNAs containing a 5'TOP motif leads to translational repression by preventing the binding of EIF4G1 (PubMed:25940091, PubMed:28379136, PubMed:28650797, PubMed:29244122). When mTORC1 is activated, LARP1 is phosphorylated and dissociates from the 5' untranslated region (UTR) of mRNA (PubMed:25940091, PubMed:28650797). Does not prevent binding of EIF4G1 to mRNAs that lack a 5'TOP motif (PubMed:28379136). Interacts with the free 40S ribosome subunit and with ribosomes, both monosomes and polysomes (PubMed:20430826, PubMed:24532714, PubMed:25940091, PubMed:28673543). Under normal nutrient availability, interacts primarily with the 3' untranslated region (UTR) of mRNAs encoding ribosomal proteins and increases protein synthesis (PubMed:23711370, PubMed:28650797). Associates with actively translating ribosomes and stimulates translation of mRNAs containing a 5'TOP motif, thereby regulating protein synthesis, and as a consequence, cell growth and proliferation (PubMed:20430826, PubMed:24532714). Stabilizes mRNAs species with a 5'TOP motif, which is required to prevent apoptosis (PubMed:20430826, PubMed:23711370, PubMed:25940091, PubMed:28673543). {ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:23711370, ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:25940091, ECO:0000269|PubMed:26206669, ECO:0000269|PubMed:28379136, ECO:0000269|PubMed:28650797, ECO:0000269|PubMed:28673543, ECO:0000269|PubMed:29244122}.; FUNCTION: (Microbial infection) Positively regulates the replication of dengue virus (DENV). {ECO:0000269|PubMed:26735137}. |
| Q6SZW1 | SARM1 | T4 | ochoa | NAD(+) hydrolase SARM1 (NADase SARM1) (hSARM1) (EC 3.2.2.6) (NADP(+) hydrolase SARM1) (EC 3.2.2.-) (Sterile alpha and Armadillo repeat protein) (Sterile alpha and TIR motif-containing protein 1) (Sterile alpha motif domain-containing protein 2) (MyD88-5) (SAM domain-containing protein 2) (Tir-1 homolog) (HsTIR) | NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism (PubMed:25908823, PubMed:27671644, PubMed:28334607). Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site (PubMed:15123841, PubMed:16964262, PubMed:20306472, PubMed:25908823). Wallerian degeneration is triggered by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide; NAD(+) cleavage promoting cytoskeletal degradation and axon destruction (PubMed:25908823, PubMed:28334607, PubMed:30333228, PubMed:31128467, PubMed:31439792, PubMed:31439793, PubMed:32049506, PubMed:32828421, PubMed:33053563). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (PubMed:29395922). Can activate neuronal cell death in response to stress (PubMed:20306472). Regulates dendritic arborization through the MAPK4-JNK pathway (By similarity). Involved in innate immune response: inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38 (PubMed:16964262). {ECO:0000250|UniProtKB:Q6PDS3, ECO:0000269|PubMed:15123841, ECO:0000269|PubMed:16964262, ECO:0000269|PubMed:20306472, ECO:0000269|PubMed:25908823, ECO:0000269|PubMed:27671644, ECO:0000269|PubMed:28334607, ECO:0000269|PubMed:29395922, ECO:0000269|PubMed:30333228, ECO:0000269|PubMed:31128467, ECO:0000269|PubMed:31439792, ECO:0000269|PubMed:31439793, ECO:0000269|PubMed:32049506, ECO:0000269|PubMed:32828421, ECO:0000269|PubMed:33053563}. |
| Q75N03 | CBLL1 | T4 | ochoa | E3 ubiquitin-protein ligase Hakai (EC 2.3.2.27) (Casitas B-lineage lymphoma-transforming sequence-like protein 1) (c-Cbl-like protein 1) (RING finger protein 188) (RING-type E3 ubiquitin transferase Hakai) | E3 ubiquitin-protein ligase that mediates ubiquitination of several tyrosine-phosphorylated Src substrates, including CDH1, CTTN and DOK1 (By similarity). Targets CDH1 for endocytosis and degradation (By similarity). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Its function in the WMM complex is unknown (PubMed:29507755). {ECO:0000250|UniProtKB:Q9JIY2, ECO:0000269|PubMed:29507755}. |
| Q7Z3U7 | MON2 | T4 | 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}. |
| Q86TI2 | DPP9 | T3 | 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}. |
| Q86TI2 | DPP9 | T4 | 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}. |
| Q86TI2 | DPP9 | T8 | ochoa | Dipeptidyl peptidase 9 (DP9) (EC 3.4.14.5) (Dipeptidyl peptidase IV-related protein 2) (DPRP-2) (Dipeptidyl peptidase IX) (DPP IX) (Dipeptidyl peptidase-like protein 9) (DPLP9) | Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:12662155, PubMed:16475979, PubMed:19667070, PubMed:29382749, PubMed:30291141, PubMed:33731929, PubMed:36112693). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed:27820798, PubMed:29967349, PubMed:30291141, PubMed:31525884, PubMed:32796818, PubMed:36112693, PubMed:36357533). Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation (PubMed:33731929, PubMed:33731932, PubMed:34019797). The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP9, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (PubMed:33731929). {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:16475979, ECO:0000269|PubMed:19667070, ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29382749, ECO:0000269|PubMed:29967349, ECO:0000269|PubMed:30291141, ECO:0000269|PubMed:31525884, ECO:0000269|PubMed:32796818, ECO:0000269|PubMed:33731929, ECO:0000269|PubMed:33731932, ECO:0000269|PubMed:34019797, ECO:0000269|PubMed:36112693, ECO:0000269|PubMed:36357533}. |
| Q8IWZ3 | ANKHD1 | T3 | ochoa | Ankyrin repeat and KH domain-containing protein 1 (HIV-1 Vpr-binding ankyrin repeat protein) (Multiple ankyrin repeats single KH domain) (hMASK) | May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases. {ECO:0000269|PubMed:16098192}. |
| Q8IY67 | RAVER1 | T8 | ochoa | Ribonucleoprotein PTB-binding 1 (Protein raver-1) | Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA (By similarity). {ECO:0000250}. |
| Q8IYE0 | CCDC146 | T8 | ochoa | Coiled-coil domain-containing protein 146 | Essential for sperm flagellum biogenesis and male fertility. {ECO:0000250|UniProtKB:E9Q9F7}. |
| Q8N3J5 | PPM1K | T3 | ochoa | Protein phosphatase Mn(2+)-dependent 1K (EC 3.1.3.16) (Branched-chain alpha-ketoacid dehydrogenase phosphatase) (BCKDH) (BDP) (EC 3.1.3.52) (PP2C domain-containing protein phosphatase 1K) (PP2C-like mitochondrial protein) (PP2C-type mitochondrial phosphoprotein phosphatase) (PTMP) (Protein phosphatase 2C family member) (Protein phosphatase 2C isoform kappa) (PP2C-kappa) ([3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase, mitochondrial) | Serine/threonine-protein phosphatase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with BCKDK, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). At high levels of branched-chain ketoacids, dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Tightly associates with the E2 component of BCKDH complex and dephosphorylates BCKDHA on Ser-337 (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). Regulates the reversible phosphorylation of ACLY in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. At fasting state, appears to dephosphorylate ACLY on Ser-455 and inactivate it. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and gluconeogenesis, respectively (PubMed:29779826). Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity (PubMed:29779826). Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death (PubMed:17374715). {ECO:0000269|PubMed:17336929, ECO:0000269|PubMed:17374715, ECO:0000269|PubMed:19411760, ECO:0000269|PubMed:22291014, ECO:0000269|PubMed:22589535, ECO:0000269|PubMed:23086801, ECO:0000269|PubMed:29779826}. |
| Q8N3J5 | PPM1K | T8 | ochoa | Protein phosphatase Mn(2+)-dependent 1K (EC 3.1.3.16) (Branched-chain alpha-ketoacid dehydrogenase phosphatase) (BCKDH) (BDP) (EC 3.1.3.52) (PP2C domain-containing protein phosphatase 1K) (PP2C-like mitochondrial protein) (PP2C-type mitochondrial phosphoprotein phosphatase) (PTMP) (Protein phosphatase 2C family member) (Protein phosphatase 2C isoform kappa) (PP2C-kappa) ([3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase, mitochondrial) | Serine/threonine-protein phosphatase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with BCKDK, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). At high levels of branched-chain ketoacids, dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Tightly associates with the E2 component of BCKDH complex and dephosphorylates BCKDHA on Ser-337 (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). Regulates the reversible phosphorylation of ACLY in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. At fasting state, appears to dephosphorylate ACLY on Ser-455 and inactivate it. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and gluconeogenesis, respectively (PubMed:29779826). Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity (PubMed:29779826). Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death (PubMed:17374715). {ECO:0000269|PubMed:17336929, ECO:0000269|PubMed:17374715, ECO:0000269|PubMed:19411760, ECO:0000269|PubMed:22291014, ECO:0000269|PubMed:22589535, ECO:0000269|PubMed:23086801, ECO:0000269|PubMed:29779826}. |
| Q8N726 | CDKN2A | T8 | psp | Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p14ARF) | Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Plays a role in inhibiting ribosome biogenesis, perhaps by binding to the nucleolar localization sequence of transcription termination factor TTF1, and thereby preventing nucleolar localization of TTF1 (By similarity). Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development. {ECO:0000250|UniProtKB:Q64364, ECO:0000269|PubMed:11314011, ECO:0000269|PubMed:11314038, ECO:0000269|PubMed:12660818, ECO:0000269|PubMed:14636574, ECO:0000269|PubMed:15361825, ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:15876874, ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:16713577, ECO:0000269|PubMed:18305112, ECO:0000269|PubMed:22094112, ECO:0000269|PubMed:9724636}.; FUNCTION: [Isoform smARF]: May be involved in regulation of autophagy and caspase-independent cell death; the short-lived mitochondrial isoform is stabilized by C1QBP. {ECO:0000269|PubMed:16713577}. |
| Q8N8F7 | LSMEM1 | T8 | ochoa | Leucine-rich single-pass membrane protein 1 | None |
| Q8NI77 | KIF18A | T4 | ochoa | Kinesin-like protein KIF18A (Marrow stromal KIF18A) (MS-KIF18A) | Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression. {ECO:0000269|PubMed:17346968, ECO:0000269|PubMed:18267093, ECO:0000269|PubMed:18513970, ECO:0000269|PubMed:19625775}. |
| Q8TBE7 | SLC35G2 | T3 | ochoa | Solute carrier family 35 member G2 (Transmembrane protein 22) | None |
| Q8TDH9 | BLOC1S5 | T8 | ochoa | Biogenesis of lysosome-related organelles complex 1 subunit 5 (BLOC-1 subunit 5) (Protein Muted homolog) | Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes (PubMed:32565547). In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:32565547}. |
| Q8WTW3 | COG1 | T3 | ochoa | Conserved oligomeric Golgi complex subunit 1 (COG complex subunit 1) (Component of oligomeric Golgi complex 1) | Required for normal Golgi function. {ECO:0000250}. |
| Q8WWP7 | GIMAP1 | T8 | ochoa | GTPase IMAP family member 1 (Immunity-associated protein 1) (hIMAP1) | May regulate lymphocyte survival. Required for normal levels of mature T-lymphocytes and mature B-cells (By similarity). {ECO:0000250}. |
| Q92599 | SEPTIN8 | T4 | ochoa | Septin-8 | Filament-forming cytoskeletal GTPase (By similarity). May play a role in platelet secretion (PubMed:15116257). Seems to participate in the process of SNARE complex formation in synaptic vesicles (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:B0BNF1, ECO:0000269|PubMed:15116257}.; FUNCTION: [Isoform 4]: Stabilizes BACE1 protein levels and promotes the sorting and accumulation of BACE1 to the recycling or endosomal compartments, modulating the beta-amyloidogenic processing of APP. {ECO:0000269|PubMed:27084579}. |
| Q92609 | TBC1D5 | T8 | ochoa | TBC1 domain family member 5 | May act as a GTPase-activating protein (GAP) for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity (PubMed:19531583, PubMed:20923837). Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy (PubMed:22354992). May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes (PubMed:24603492). {ECO:0000269|PubMed:19531583, ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:24603492, ECO:0000305|PubMed:19531583, ECO:0000305|PubMed:22354992, ECO:0000305|PubMed:24603492}. |
| Q92621 | NUP205 | T3 | ochoa | Nuclear pore complex protein Nup205 (205 kDa nucleoporin) (Nucleoporin Nup205) | Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:9348540). May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC (PubMed:15229283). In association with TMEM209, may be involved in nuclear transport of various nuclear proteins in addition to MYC (PubMed:22719065). {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:22719065, ECO:0000269|PubMed:9348540}. |
| Q92826 | HOXB13 | T8 | psp | Homeobox protein Hox-B13 | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds preferentially to methylated DNA (PubMed:28473536). {ECO:0000269|PubMed:28473536}. |
| Q96C00 | ZBTB9 | T3 | ochoa | Zinc finger and BTB domain-containing protein 9 | May be involved in transcriptional regulation. |
| Q96C19 | EFHD2 | T3 | ochoa | EF-hand domain-containing protein D2 (Swiprosin-1) | May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis. Plays a role as negative regulator of the canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis through the regulation of BCL2L1 abundance. {ECO:0000250}. |
| Q96C19 | EFHD2 | T8 | ochoa | EF-hand domain-containing protein D2 (Swiprosin-1) | May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis. Plays a role as negative regulator of the canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis through the regulation of BCL2L1 abundance. {ECO:0000250}. |
| Q96C55 | ZNF524 | T3 | ochoa | Zinc finger protein 524 | May be involved in transcriptional regulation. |
| Q96D46 | NMD3 | T8 | ochoa | 60S ribosomal export protein NMD3 (hNMD3) | Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit. {ECO:0000269|PubMed:12724356, ECO:0000269|PubMed:12773398}. |
| Q96DF8 | ESS2 | T3 | 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}. |
| Q96EW2 | HSPBAP1 | T8 | ochoa | HSPB1-associated protein 1 (27 kDa heat shock protein-associated protein 1) (Protein associated with small stress protein 1) | May play a role in cellular stress response. {ECO:0000250}. |
| Q96FV9 | THOC1 | T4 | ochoa | THO complex subunit 1 (Nuclear matrix protein p84) (p84N5) (hTREX84) | Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA (PubMed:23222130). The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B/UAP56 (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). Regulates transcriptional elongation of a subset of genes (PubMed:22144908). Involved in genome stability by preventing co-transcriptional R-loop formation (By similarity). May play a role in hair cell formation, hence may be involved in hearing (By similarity). {ECO:0000250|UniProtKB:Q7SYB2, ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:22144908, ECO:0000269|PubMed:23222130, ECO:0000269|PubMed:33191911}.; FUNCTION: Participates in an apoptotic pathway which is characterized by activation of caspase-6, increases in the expression of BAK1 and BCL2L1 and activation of NF-kappa-B. This pathway does not require p53/TP53, nor does the presence of p53/TP53 affect the efficiency of cell killing. Activates a G2/M cell cycle checkpoint prior to the onset of apoptosis. Apoptosis is inhibited by association with RB1.; 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}. |
| Q96HR3 | MED30 | T3 | ochoa | Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (TRAP/Mediator complex component TRAP25) (Thyroid hormone receptor-associated protein 6) (Thyroid hormone receptor-associated protein complex 25 kDa component) (Trap25) | Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:11909976, ECO:0000269|PubMed:16595664}. |
| Q96IZ0 | PAWR | T8 | ochoa | PRKC apoptosis WT1 regulator protein (Prostate apoptosis response 4 protein) (Par-4) | Pro-apoptotic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Also seems to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1. {ECO:0000269|PubMed:11585763}. |
| Q96LT7 | C9orf72 | T3 | ochoa | Guanine nucleotide exchange factor C9orf72 | Acts as a guanine-nucleotide releasing factor (GEF) for Rab GTPases by promoting the conversion of inactive RAB-GDP to the active form RAB-GTP (PubMed:27103069, PubMed:27193190, PubMed:27617292, PubMed:28195531, PubMed:37821429). Acts as a GEF for RAB39A which enables HOPS-mediated autophagosome-lysosome membrane tethering and fusion in mammalian autophagy (PubMed:37821429). Component of the C9orf72-SMCR8 complex where both subunits display GEF activity and that regulates autophagy (PubMed:27103069, PubMed:27193190, PubMed:27617292, PubMed:28195531). As part of the C9orf72-SMCR8-WDR41 (CSW) complex, functions as GEF for RAB8A and RAB39B, thereby promoting autophagosome maturation (PubMed:27103069). As part of the C9orf72-SMCR8 complex, also functions as GTPase activating protein (GAP) for RAB8A and RAB11A in vitro (PubMed:32303654). The C9orf72-SMCR8 complex also acts as a regulator of autophagy initiation by interacting with the ULK1/ATG1 kinase complex and modulating its protein kinase activity (PubMed:27617292). Promotes initiation of autophagy by regulating the RAB1A-dependent trafficking of the ULK1/ATG1 kinase complex to the phagophore which leads to autophagosome formation (PubMed:27334615). Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates (PubMed:27559131). Plays a role in endosomal trafficking (PubMed:24549040). May be involved in regulating the maturation of phagosomes to lysosomes (By similarity). Promotes the lysosomal localization and lysosome-mediated degradation of CARM1 which leads to inhibition of starvation-induced lipid metabolism (By similarity). Regulates actin dynamics in motor neurons by inhibiting the GTP-binding activity of ARF6, leading to ARF6 inactivation (PubMed:27723745). This reduces the activity of the LIMK1 and LIMK2 kinases which are responsible for phosphorylation and inactivation of cofilin, leading to CFL1/cofilin activation (PubMed:27723745). Positively regulates axon extension and axon growth cone size in spinal motor neurons (PubMed:27723745). Required for SMCR8 protein expression and localization at pre- and post-synaptic compartments in the forebrain, also regulates protein abundance of RAB3A and GRIA1/GLUR1 in post-synaptic compartments in the forebrain and hippocampus (By similarity). Plays a role within the hematopoietic system in restricting inflammation and the development of autoimmunity (By similarity). {ECO:0000250|UniProtKB:Q6DFW0, ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:27103069, ECO:0000269|PubMed:27193190, ECO:0000269|PubMed:27334615, ECO:0000269|PubMed:27559131, ECO:0000269|PubMed:27617292, ECO:0000269|PubMed:27723745, ECO:0000269|PubMed:28195531, ECO:0000269|PubMed:32303654, ECO:0000269|PubMed:37821429}.; FUNCTION: [Isoform 1]: Regulates stress granule assembly in response to cellular stress. {ECO:0000269|PubMed:27037575}.; FUNCTION: [Isoform 2]: Does not play a role in regulation of stress granule assembly in response to cellular stress. {ECO:0000269|PubMed:27037575}. |
| Q96MH2 | HEXIM2 | T4 | ochoa | Protein HEXIM2 (Hexamethylene bis-acetamide-inducible protein 2) | Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor (PubMed:15713661, PubMed:15713662). Core component of the 7SK RNP complex: in cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (PubMed:15713661, PubMed:15713662). {ECO:0000269|PubMed:15713661, ECO:0000269|PubMed:15713662}. |
| Q96QK1 | VPS35 | T4 | 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}. |
| Q96S44 | TP53RK | T8 | ochoa | EKC/KEOPS complex subunit TP53RK (EC 3.6.-.-) (Atypical serine/threonine protein kinase TP53RK) (Nori-2) (TP53-regulating kinase) (EC 2.7.11.1) (p53-related protein kinase) | Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine (PubMed:22912744, PubMed:27903914). The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37 (PubMed:22912744, PubMed:27903914). TP53RK has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit OSGEP (By similarity). Atypical protein kinase that phosphorylates 'Ser-15' of p53/TP53 protein and may therefore participate in its activation (PubMed:11546806). {ECO:0000250|UniProtKB:P53323, ECO:0000250|UniProtKB:Q9UYB9, ECO:0000269|PubMed:11546806, ECO:0000305|PubMed:22912744, ECO:0000305|PubMed:27903914}. |
| Q96S97 | MYADM | T8 | ochoa | Myeloid-associated differentiation marker (Protein SB135) | None |
| Q99439 | CNN2 | T4 | ochoa | Calponin-2 (Calponin H2, smooth muscle) (Neutral calponin) | Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity. |
| Q99471 | PFDN5 | T8 | ochoa | Prefoldin subunit 5 (Myc modulator 1) (c-Myc-binding protein Mm-1) | Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC. {ECO:0000269|PubMed:9630229}. |
| Q99848 | EBNA1BP2 | T3 | ochoa | Probable rRNA-processing protein EBP2 (EBNA1-binding protein 2) (Nucleolar protein p40) | Required for the processing of the 27S pre-rRNA. {ECO:0000250}. |
| Q99865 | SPIN2A | T3 | ochoa | Spindlin-2A (Protein DXF34) (Spindlin-like protein 2A) (SPIN-2) (SPIN-2A) | May be involved in the regulation of cell cycle progression (By similarity). Exhibits H3K4me3-binding activity (PubMed:29061846). {ECO:0000250|UniProtKB:Q9BPZ2, ECO:0000269|PubMed:29061846}. |
| Q9BPY3 | FAM118B | T4 | ochoa | Protein FAM118B | May play a role in Cajal bodies formation. {ECO:0000269|PubMed:24569877}. |
| Q9BPZ2 | SPIN2B | T3 | ochoa | Spindlin-2B (Spindlin-like protein 2B) (SPIN-2) (SPIN-2B) | Involved in the regulation of cell cycle progression, this activity is related to the inhibition of apoptosis following the removal of essential growth factors (PubMed:12145692). Exhibits H3K4me3-binding activity (PubMed:29061846). {ECO:0000269|PubMed:12145692, ECO:0000269|PubMed:29061846}. |
| Q9BR01 | SULT4A1 | T8 | psp | Sulfotransferase 4A1 (ST4A1) (EC 2.8.2.-) (Brain sulfotransferase-like protein) (hBR-STL) (hBR-STL-1) (Nervous system sulfotransferase) (NST) | Atypical sulfotransferase family member with very low affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in the metabolism of drugs and neurotransmitters in the CNS. {ECO:0000269|PubMed:17425406}. |
| Q9BR77 | CCDC77 | T4 | ochoa | Coiled-coil domain-containing protein 77 | None |
| Q9BR77 | CCDC77 | T8 | ochoa | Coiled-coil domain-containing protein 77 | None |
| Q9BTU6 | PI4K2A | T4 | ochoa | Phosphatidylinositol 4-kinase type 2-alpha (EC 2.7.1.67) (Phosphatidylinositol 4-kinase type II-alpha) | Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). {ECO:0000269|PubMed:11279162, ECO:0000269|PubMed:16443754, ECO:0000269|PubMed:20388919, ECO:0000269|PubMed:23146885, ECO:0000269|PubMed:24675427, ECO:0000269|PubMed:25168678, ECO:0000305}. |
| Q9BTV4 | TMEM43 | T8 | ochoa | Transmembrane protein 43 (Protein LUMA) | May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (PubMed:32614325). In addition, functions as a critical signaling component in mediating NF-kappa-B activation by acting downstream of EGFR and upstream of CARD10 (PubMed:27991920). Contributes to passive conductance current in cochlear glia-like supporting cells, mediated by gap junctions and necessary for hearing and speech discrimination (PubMed:34050020). {ECO:0000250|UniProtKB:Q9DBS1, ECO:0000269|PubMed:27991920, ECO:0000269|PubMed:32614325, ECO:0000269|PubMed:34050020}. |
| Q9BVC4 | MLST8 | T3 | 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}. |
| Q9BWQ6 | YIPF2 | T8 | ochoa | Protein YIPF2 (YIP1 family member 2) | None |
| Q9BZX2 | UCK2 | T8 | ochoa | Uridine-cytidine kinase 2 (UCK 2) (EC 2.7.1.48) (Cytidine monophosphokinase 2) (Testis-specific protein TSA903) (Uridine monophosphokinase 2) | Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate (PubMed:11306702, PubMed:11494055). Does not phosphorylate deoxyribonucleosides or purine ribonucleosides (PubMed:11306702). Can use ATP or GTP as a phosphate donor (PubMed:11306702). Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine (PubMed:11306702). {ECO:0000269|PubMed:11306702, ECO:0000269|PubMed:11494055}. |
| Q9C0B1 | FTO | T4 | ochoa|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}. |
| Q9H3U1 | UNC45A | T8 | ochoa | Protein unc-45 homolog A (Unc-45A) (GCUNC-45) (Smooth muscle cell-associated protein 1) (SMAP-1) | Acts as a co-chaperone for HSP90. Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell. May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity). {ECO:0000250, ECO:0000269|PubMed:12119110, ECO:0000269|PubMed:16478993, ECO:0000305}. |
| Q9H4I2 | ZHX3 | T8 | ochoa | Zinc fingers and homeoboxes protein 3 (Triple homeobox protein 1) (Zinc finger and homeodomain protein 3) | Acts as a transcriptional repressor. Involved in the early stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a regulator of podocyte gene expression during primary glomerula disease. Binds to promoter DNA. {ECO:0000269|PubMed:12659632, ECO:0000269|PubMed:21174497}. |
| Q9H813 | PACC1 | T8 | ochoa | Proton-activated chloride channel (PAC) (hPAC) (Acid-sensitive outwardly-rectifying anion channel) (ASOR) (Proton-activated outwardly rectifying anion channel) (PAORAC) (Transmembrane protein 206) (hTMEM206) | Chloride channel gated by pH that facilitates the entry of chloride ions into cells upon exposure to extracellular acidic pH (PubMed:31023925, PubMed:31318332). Involved in acidosis-induced cell death by mediating chloride influx and subsequent cell swelling (PubMed:31023925, PubMed:31318332). {ECO:0000269|PubMed:31023925, ECO:0000269|PubMed:31318332}. |
| Q9H840 | GEMIN7 | T3 | ochoa | Gem-associated protein 7 (Gemin-7) (SIP3) | The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. {ECO:0000269|PubMed:12065586, ECO:0000269|PubMed:18984161}. |
| Q9HCD5 | NCOA5 | T3 | 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}. |
| Q9NUP7 | TRMT13 | T3 | 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}. |
| Q9NVD7 | PARVA | T3 | ochoa | Alpha-parvin (Actopaxin) (CH-ILKBP) (Calponin-like integrin-linked kinase-binding protein) (Matrix-remodeling-associated protein 2) | Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishment of cell polarity, cell adhesion, cell spreading, and directed cell migration. Within the IPP (ILK-PINCH-PARVIN) complex, binds to F-actin, promoting F-actin bundling, a process required to generate force for actin cytoskeleton reorganization and subsequent dynamic cell adhesion events such as cell spreading and migration (PubMed:30367047). {ECO:0000250, ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:11331308, ECO:0000269|PubMed:15284246, ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:30367047}. |
| Q9NVH1 | DNAJC11 | T3 | 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}. |
| Q9NW15 | ANO10 | T4 | 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}. |
| Q9NXW9 | ALKBH4 | T8 | ochoa | Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4 (Alkylated DNA repair protein alkB homolog 4) (DNA N6-methyl adenine demethylase ALKBH4) (EC 1.14.11.51) (Lysine-specific demethylase ALKBH4) (EC 1.14.11.-) | Dioxygenase that mediates demethylation of actin monomethylated at 'Lys-84' (K84me1), thereby acting as a regulator of actomyosin-processes (PubMed:23673617). Demethylation of actin K84me1 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (PubMed:23673617). In addition to proteins, also demethylates DNA: specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA, thereby regulating Polycomb silencing (By similarity). {ECO:0000250|UniProtKB:Q9D8F1, ECO:0000269|PubMed:23673617}. |
| Q9NYD6 | HOXC10 | T8 | ochoa | Homeobox protein Hox-C10 (Homeobox protein Hox-3I) | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
| Q9NYJ1 | COA4 | T3 | ochoa | Cytochrome c oxidase assembly factor 4 homolog, mitochondrial (Coiled-coil-helix-coiled-coil-helix domain-containing protein 8) (E2-induced gene 2 protein) | Putative COX assembly factor. {ECO:0000250}. |
| Q9UBI6 | GNG12 | T8 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12 | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. |
| Q9UHD2 | TBK1 | T4 | ochoa | Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (NF-kappa-B-activating kinase) (T2K) (TANK-binding kinase 1) | Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents (PubMed:10581243, PubMed:11839743, PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:15485837, PubMed:18583960, PubMed:21138416, PubMed:23453971, PubMed:23453972, PubMed:23746807, PubMed:25636800, PubMed:26611359, PubMed:32404352, PubMed:34363755, PubMed:32298923). Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X (PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:18583960, PubMed:25636800). This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB (PubMed:12702806, PubMed:15367631, PubMed:25636800, PubMed:32972995). In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli (PubMed:23453971, PubMed:23453972, PubMed:23746807). Plays a key role in IRF3 activation: acts by first phosphorylating innate adapter proteins MAVS, STING1 and TICAM1 on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1 (PubMed:25636800, PubMed:30842653, PubMed:37926288). Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce expression of interferons (PubMed:25636800). Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes (PubMed:21931631). Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus (PubMed:10783893, PubMed:15489227). Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy (PubMed:21617041). Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation (PubMed:27103069). Phosphorylates ATG8 proteins MAP1LC3C and GABARAPL2, thereby preventing their delipidation and premature removal from nascent autophagosomes (PubMed:31709703). Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, which leads to a negative impact on insulin sensitivity (By similarity). Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C (PubMed:21270402). Phosphorylates Borna disease virus (BDV) P protein (PubMed:16155125). Plays an essential role in the TLR3- and IFN-dependent control of herpes virus HSV-1 and HSV-2 infections in the central nervous system (PubMed:22851595). Acts both as a positive and negative regulator of the mTORC1 complex, depending on the context: activates mTORC1 in response to growth factors by catalyzing phosphorylation of MTOR, while it limits the mTORC1 complex by promoting phosphorylation of RPTOR (PubMed:29150432, PubMed:31530866). Acts as a positive regulator of the mTORC2 complex by mediating phosphorylation of MTOR, leading to increased phosphorylation and activation of AKT1 (By similarity). Phosphorylates and activates AKT1 (PubMed:21464307). Involved in the regulation of TNF-induced RIPK1-mediated cell death, probably acting via CYLD phosphorylation that in turn controls RIPK1 ubiquitination status (PubMed:34363755). Also participates in the differentiation of T follicular regulatory cells together with the receptor ICOS (PubMed:27135603). {ECO:0000250|UniProtKB:Q9WUN2, ECO:0000269|PubMed:10581243, ECO:0000269|PubMed:10783893, ECO:0000269|PubMed:11839743, ECO:0000269|PubMed:12692549, ECO:0000269|PubMed:12702806, ECO:0000269|PubMed:14703513, ECO:0000269|PubMed:15367631, ECO:0000269|PubMed:15485837, ECO:0000269|PubMed:15489227, ECO:0000269|PubMed:16155125, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:21138416, ECO:0000269|PubMed:21270402, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:21617041, ECO:0000269|PubMed:21931631, ECO:0000269|PubMed:22851595, ECO:0000269|PubMed:23453971, ECO:0000269|PubMed:23453972, ECO:0000269|PubMed:23746807, ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:26611359, ECO:0000269|PubMed:27103069, ECO:0000269|PubMed:27135603, ECO:0000269|PubMed:29150432, ECO:0000269|PubMed:30842653, ECO:0000269|PubMed:31530866, ECO:0000269|PubMed:31709703, ECO:0000269|PubMed:32298923, ECO:0000269|PubMed:32972995, ECO:0000269|PubMed:34363755, ECO:0000269|PubMed:37926288}. |
| Q9UHY1 | NRBP1 | T8 | ochoa | Nuclear receptor-binding protein | Required for embryonic development (By similarity). Plays a role in intestinal epithelial cell fate and proliferation, thereby involved in the architectural development of the intestine potentially via the regulation of Wnt-responsive genes (By similarity). May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases (PubMed:11956649). Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication (PubMed:15084397). {ECO:0000250|UniProtKB:Q99J45, ECO:0000269|PubMed:11956649, ECO:0000269|PubMed:15084397}. |
| Q9UIM3 | FKBPL | T3 | ochoa | FK506-binding protein-like (WAF-1/CIP1 stabilizing protein 39) (WISp39) | May be involved in response to X-ray. Regulates p21 protein stability by binding to Hsp90 and p21. {ECO:0000269|PubMed:15664193}. |
| Q9UK41 | VPS28 | T8 | ochoa | Vacuolar protein sorting-associated protein 28 homolog (H-Vps28) (ESCRT-I complex subunit VPS28) | Component of the ESCRT-I complex, a regulator of vesicular trafficking process. {ECO:0000269|PubMed:11916981}. |
| Q9UK76 | JPT1 | T3 | ochoa | Jupiter microtubule associated homolog 1 (Androgen-regulated protein 2) (Hematological and neurological expressed 1 protein) [Cleaved into: Jupiter microtubule associated homolog 1, N-terminally processed] | Modulates negatively AKT-mediated GSK3B signaling (PubMed:21323578, PubMed:22155408). Induces CTNNB1 'Ser-33' phosphorylation and degradation through the suppression of the inhibitory 'Ser-9' phosphorylation of GSK3B, which represses the function of the APC:CTNNB1:GSK3B complex and the interaction with CDH1/E-cadherin in adherent junctions (PubMed:25169422). Plays a role in the regulation of cell cycle and cell adhesion (PubMed:25169422, PubMed:25450365). Has an inhibitory role on AR-signaling pathway through the induction of receptor proteasomal degradation (PubMed:22155408). {ECO:0000269|PubMed:21323578, ECO:0000269|PubMed:22155408, ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:25450365}. |
| Q9UKY7 | CDV3 | T4 | ochoa | Protein CDV3 homolog | None |
| Q9UM13 | ANAPC10 | T3 | ochoa | Anaphase-promoting complex subunit 10 (APC10) (Cyclosome subunit 10) | Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:29033132}. |
| Q9UNF1 | MAGED2 | T4 | ochoa | Melanoma-associated antigen D2 (11B6) (Breast cancer-associated gene 1 protein) (BCG-1) (Hepatocellular carcinoma-associated protein JCL-1) (MAGE-D2 antigen) | Regulates the expression, localization to the plasma membrane and function of the sodium chloride cotransporters SLC12A1 and SLC12A3, two key components of salt reabsorption in the distal renal tubule. {ECO:0000269|PubMed:27120771}. |
| Q9Y241 | HIGD1A | T3 | ochoa | HIG1 domain family member 1A, mitochondrial (Hypoxia-inducible gene 1 protein) (RCF1 homolog A) (RCF1a) | Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May play a role in the assembly of respiratory supercomplexes. {ECO:0000269|PubMed:22342701}. |
| Q9Y277 | VDAC3 | T4 | ochoa | Non-selective voltage-gated ion channel VDAC3 (VDAC-3) (hVDAC3) (Outer mitochondrial membrane protein porin 3) | Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:31935282). Forms a high-conducting channel with a stable open state and a voltage-induced closure with a mild preference for anions over cations (PubMed:31935282). Involved in male fertility and sperm mitochondrial sheath formation (By similarity). {ECO:0000250|UniProtKB:Q60931, ECO:0000269|PubMed:31935282}. |
| Q9Y284 | WDR83OS | T3 | 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}. |
| Q9Y2J2 | EPB41L3 | T3 | 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}. |
| Q9Y2Z0 | SUGT1 | T8 | ochoa | Protein SGT1 homolog (Protein 40-6-3) (Sgt1) (Suppressor of G2 allele of SKP1 homolog) | May play a role in ubiquitination and subsequent proteasomal degradation of target proteins. |
| Q9Y365 | STARD10 | T8 | ochoa | START domain-containing protein 10 (StARD10) (Antigen NY-CO-28) (PCTP-like protein) (PCTP-L) (Serologically defined colon cancer antigen 28) (StAR-related lipid transfer protein 10) | May play metabolic roles in sperm maturation or fertilization (By similarity). Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes. {ECO:0000250, ECO:0000269|PubMed:15911624}. |
| Q9Y6D9 | MAD1L1 | T8 | psp | Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1) (Mitotic checkpoint MAD1 protein homolog) (HsMAD1) (hMAD1) (Tax-binding protein 181) | Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (PubMed:10049595, PubMed:20133940, PubMed:29162720). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (PubMed:29162720). {ECO:0000269|PubMed:10049595, ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:36322655}.; FUNCTION: [Isoform 3]: Sequesters MAD2L1 in the cytoplasm preventing its function as an activator of the mitotic spindle assembly checkpoint (SAC) resulting in SAC impairment and chromosomal instability in hepatocellular carcinomas. {ECO:0000269|PubMed:19010891}. |
| S4R3Y5 | MTRNR2L11 | T3 | ochoa | Humanin-like 11 (HN11) (MT-RNR2-like protein 11) | Plays a role as a neuroprotective and antiapoptotic factor. {ECO:0000250|UniProtKB:Q8IVG9}. |
| P08758 | ANXA5 | T8 | Sugiyama | Annexin A5 (Anchorin CII) (Annexin V) (Annexin-5) (Calphobindin I) (CPB-I) (Endonexin II) (Lipocortin V) (Placental anticoagulant protein 4) (PP4) (Placental anticoagulant protein I) (PAP-I) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. |
| Q7LDG7 | RASGRP2 | T4 | Sugiyama | RAS guanyl-releasing protein 2 (Calcium and DAG-regulated guanine nucleotide exchange factor I) (CalDAG-GEFI) (Cdc25-like protein) (hCDC25L) (F25B3.3 kinase-like protein) | Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. {ECO:0000269|PubMed:10918068, ECO:0000269|PubMed:14702343, ECO:0000269|PubMed:17576779, ECO:0000269|PubMed:17702895, ECO:0000269|PubMed:24958846, ECO:0000269|PubMed:27235135}. |
| P61254 | RPL26 | T8 | Sugiyama | Large ribosomal subunit protein uL24 (60S ribosomal protein L26) | Component of the large ribosomal subunit (PubMed:23636399, PubMed:26100019, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:26100019, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:26100019}. |
| Q9UNX3 | RPL26L1 | T8 | Sugiyama | Ribosomal protein uL24-like (60S ribosomal protein L26-like 1) (Large ribosomal subunit protein uL24-like 1) | None |
| Q13148 | TARDBP | T8 | SIGNOR | TAR DNA-binding protein 43 (TDP-43) | RNA-binding protein that is involved in various steps of RNA biogenesis and processing (PubMed:23519609). Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs (PubMed:23519609, PubMed:24240615, PubMed:24464995). In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases (PubMed:21358640, PubMed:29438978). Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts (PubMed:28794432). Also regulates mRNA stability by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail deadenylation and thus shortening (PubMed:30520513). In response to oxidative insult, associates with stalled ribosomes localized to stress granules (SGs) and contributes to cell survival (PubMed:19765185, PubMed:23398327). Also participates in the normal skeletal muscle formation and regeneration, forming cytoplasmic myo-granules and binding mRNAs that encode sarcomeric proteins (PubMed:30464263). Plays a role in the maintenance of the circadian clock periodicity via stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner (PubMed:27123980). Negatively regulates the expression of CDK6 (PubMed:19760257). Regulates the expression of HDAC6, ATG7 and VCP in a PPIA/CYPA-dependent manner (PubMed:25678563). {ECO:0000269|PubMed:11285240, ECO:0000269|PubMed:17481916, ECO:0000269|PubMed:19760257, ECO:0000269|PubMed:19765185, ECO:0000269|PubMed:21358640, ECO:0000269|PubMed:23398327, ECO:0000269|PubMed:23519609, ECO:0000269|PubMed:24240615, ECO:0000269|PubMed:24464995, ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:27123980, ECO:0000269|PubMed:28794432, ECO:0000269|PubMed:29438978, ECO:0000269|PubMed:30464263, ECO:0000269|PubMed:30520513}. |
| Q6P2M8 | PNCK | T8 | Sugiyama | Calcium/calmodulin-dependent protein kinase type 1B (EC 2.7.11.17) (CaM kinase I beta) (CaM kinase IB) (CaM-KI beta) (CaMKI-beta) (Pregnancy up-regulated non-ubiquitously-expressed CaM kinase) | Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates CREB1 and SYN1/synapsin I. Phosphorylates and activates CAMK1 (By similarity). {ECO:0000250}. |
| P68431 | H3C1 | T4 | GPS6|SIGNOR|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. |
| P84243 | H3-3A | T4 | GPS6|EPSD | Histone H3.3 | Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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. {ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15776021, ECO:0000269|PubMed:16258499}. |
| Q16695 | H3-4 | T4 | GPS6 | Histone H3.1t (H3/t) (H3t) (H3/g) (Histone H3.4) | 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. |
| Q71DI3 | H3C15 | T4 | GPS6|EPSD | Histone H3.2 (H3-clustered histone 13) (H3-clustered histone 14) (H3-clustered histone 15) (Histone H3/m) (Histone H3/o) | 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. |
| O14818 | PSMA7 | T8 | Sugiyama | Proteasome subunit alpha type-7 (Proteasome subunit RC6-1) (Proteasome subunit XAPC7) (Proteasome subunit alpha-4) (alpha-4) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response. {ECO:0000269|PubMed:11389899, ECO:0000269|PubMed:11713272, ECO:0000269|PubMed:12119296, ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:19442227, ECO:0000269|PubMed:19734229, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
Download
| reactome_id | name | p | -log10_p |
|---|---|---|---|
| R-HSA-2559583 | Cellular Senescence | 5.038758e-11 | 10.298 |
| R-HSA-2559584 | Formation of Senescence-Associated Heterochromatin Foci (SAHF) | 2.740892e-07 | 6.562 |
| R-HSA-140342 | Apoptosis induced DNA fragmentation | 1.028474e-06 | 5.988 |
| R-HSA-75153 | Apoptotic execution phase | 1.185158e-06 | 5.926 |
| R-HSA-383280 | Nuclear Receptor transcription pathway | 1.930661e-06 | 5.714 |
| R-HSA-68867 | Assembly of the pre-replicative complex | 2.157168e-06 | 5.666 |
| R-HSA-8953897 | Cellular responses to stimuli | 2.273502e-06 | 5.643 |
| R-HSA-2262752 | Cellular responses to stress | 4.028278e-06 | 5.395 |
| R-HSA-2559580 | Oxidative Stress Induced Senescence | 5.792386e-06 | 5.237 |
| R-HSA-9645723 | Diseases of programmed cell death | 6.453496e-06 | 5.190 |
| R-HSA-69002 | DNA Replication Pre-Initiation | 1.185179e-05 | 4.926 |
| R-HSA-2559586 | DNA Damage/Telomere Stress Induced Senescence | 1.127951e-05 | 4.948 |
| R-HSA-5357801 | Programmed Cell Death | 5.106912e-05 | 4.292 |
| R-HSA-109581 | Apoptosis | 4.800923e-05 | 4.319 |
| R-HSA-2559585 | Oncogene Induced Senescence | 9.169679e-05 | 4.038 |
| R-HSA-212300 | PRC2 methylates histones and DNA | 1.059061e-04 | 3.975 |
| R-HSA-212436 | Generic Transcription Pathway | 1.149893e-04 | 3.939 |
| R-HSA-9612973 | Autophagy | 1.222445e-04 | 3.913 |
| R-HSA-8853884 | Transcriptional Regulation by VENTX | 2.063192e-04 | 3.685 |
| R-HSA-73857 | RNA Polymerase II Transcription | 2.315587e-04 | 3.635 |
| R-HSA-9613829 | Chaperone Mediated Autophagy | 2.827628e-04 | 3.549 |
| R-HSA-9710421 | Defective pyroptosis | 2.964867e-04 | 3.528 |
| R-HSA-69306 | DNA Replication | 3.610911e-04 | 3.442 |
| R-HSA-8878159 | Transcriptional regulation by RUNX3 | 3.841326e-04 | 3.416 |
| R-HSA-68616 | Assembly of the ORC complex at the origin of replication | 4.419036e-04 | 3.355 |
| R-HSA-8950505 | Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulati... | 4.950069e-04 | 3.305 |
| R-HSA-69620 | Cell Cycle Checkpoints | 5.862750e-04 | 3.232 |
| R-HSA-3656534 | Loss of Function of TGFBR1 in Cancer | 7.212677e-04 | 3.142 |
| R-HSA-72706 | GTP hydrolysis and joining of the 60S ribosomal subunit | 8.545504e-04 | 3.068 |
| R-HSA-156827 | L13a-mediated translational silencing of Ceruloplasmin expression | 8.545504e-04 | 3.068 |
| R-HSA-72649 | Translation initiation complex formation | 9.281136e-04 | 3.032 |
| R-HSA-74160 | Gene expression (Transcription) | 1.037097e-03 | 2.984 |
| R-HSA-72702 | Ribosomal scanning and start codon recognition | 1.112540e-03 | 2.954 |
| R-HSA-9020591 | Interleukin-12 signaling | 1.210594e-03 | 2.917 |
| R-HSA-201722 | Formation of the beta-catenin:TCF transactivating complex | 1.324565e-03 | 2.878 |
| R-HSA-72662 | Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub... | 1.324565e-03 | 2.878 |
| R-HSA-6796648 | TP53 Regulates Transcription of DNA Repair Genes | 1.401974e-03 | 2.853 |
| R-HSA-72737 | Cap-dependent Translation Initiation | 1.540440e-03 | 2.812 |
| R-HSA-72613 | Eukaryotic Translation Initiation | 1.540440e-03 | 2.812 |
| R-HSA-3304351 | Signaling by TGF-beta Receptor Complex in Cancer | 1.478909e-03 | 2.830 |
| R-HSA-2559582 | Senescence-Associated Secretory Phenotype (SASP) | 1.856534e-03 | 2.731 |
| R-HSA-1640170 | Cell Cycle | 2.146961e-03 | 2.668 |
| R-HSA-3304347 | Loss of Function of SMAD4 in Cancer | 2.534473e-03 | 2.596 |
| R-HSA-3311021 | SMAD4 MH2 Domain Mutants in Cancer | 2.534473e-03 | 2.596 |
| R-HSA-3315487 | SMAD2/3 MH2 Domain Mutants in Cancer | 2.534473e-03 | 2.596 |
| R-HSA-2299718 | Condensation of Prophase Chromosomes | 2.301720e-03 | 2.638 |
| R-HSA-9909649 | Regulation of PD-L1(CD274) transcription | 2.505327e-03 | 2.601 |
| R-HSA-195721 | Signaling by WNT | 2.417299e-03 | 2.617 |
| R-HSA-69278 | Cell Cycle, Mitotic | 2.827611e-03 | 2.549 |
| R-HSA-447115 | Interleukin-12 family signaling | 2.748115e-03 | 2.561 |
| R-HSA-9764265 | Regulation of CDH1 Expression and Function | 3.042864e-03 | 2.517 |
| R-HSA-9764274 | Regulation of Expression and Function of Type I Classical Cadherins | 3.042864e-03 | 2.517 |
| R-HSA-9734779 | Developmental Cell Lineages of the Integumentary System | 3.072405e-03 | 2.513 |
| R-HSA-6814122 | Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding | 3.572336e-03 | 2.447 |
| R-HSA-5250913 | Positive epigenetic regulation of rRNA expression | 3.575659e-03 | 2.447 |
| R-HSA-912446 | Meiotic recombination | 3.542112e-03 | 2.451 |
| R-HSA-1912408 | Pre-NOTCH Transcription and Translation | 3.507457e-03 | 2.455 |
| R-HSA-9764560 | Regulation of CDH1 Gene Transcription | 3.337926e-03 | 2.477 |
| R-HSA-73772 | RNA Polymerase I Promoter Escape | 3.840279e-03 | 2.416 |
| R-HSA-9924644 | Developmental Lineages of the Mammary Gland | 3.826062e-03 | 2.417 |
| R-HSA-156842 | Eukaryotic Translation Elongation | 3.943441e-03 | 2.404 |
| R-HSA-69052 | Switching of origins to a post-replicative state | 4.089558e-03 | 2.388 |
| R-HSA-1912422 | Pre-NOTCH Expression and Processing | 3.997347e-03 | 2.398 |
| R-HSA-5250924 | B-WICH complex positively regulates rRNA expression | 4.156652e-03 | 2.381 |
| R-HSA-9675132 | Diseases of cellular response to stress | 4.434062e-03 | 2.353 |
| R-HSA-9630747 | Diseases of Cellular Senescence | 4.434062e-03 | 2.353 |
| R-HSA-201681 | TCF dependent signaling in response to WNT | 4.524006e-03 | 2.344 |
| R-HSA-8939211 | ESR-mediated signaling | 4.807336e-03 | 2.318 |
| R-HSA-9018519 | Estrogen-dependent gene expression | 4.841559e-03 | 2.315 |
| R-HSA-68886 | M Phase | 5.331192e-03 | 2.273 |
| R-HSA-5339716 | Signaling by GSK3beta mutants | 6.151077e-03 | 2.211 |
| R-HSA-427389 | ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression | 6.290104e-03 | 2.201 |
| R-HSA-68875 | Mitotic Prophase | 6.197430e-03 | 2.208 |
| R-HSA-1632852 | Macroautophagy | 6.013333e-03 | 2.221 |
| R-HSA-4839743 | Signaling by CTNNB1 phospho-site mutants | 7.333563e-03 | 2.135 |
| R-HSA-5358747 | CTNNB1 S33 mutants aren't phosphorylated | 7.333563e-03 | 2.135 |
| R-HSA-5358752 | CTNNB1 T41 mutants aren't phosphorylated | 7.333563e-03 | 2.135 |
| R-HSA-5358751 | CTNNB1 S45 mutants aren't phosphorylated | 7.333563e-03 | 2.135 |
| R-HSA-5358749 | CTNNB1 S37 mutants aren't phosphorylated | 7.333563e-03 | 2.135 |
| R-HSA-8873719 | RAB geranylgeranylation | 6.935995e-03 | 2.159 |
| R-HSA-9821002 | Chromatin modifications during the maternal to zygotic transition (MZT) | 6.853568e-03 | 2.164 |
| R-HSA-8951936 | RUNX3 regulates p14-ARF | 7.333563e-03 | 2.135 |
| R-HSA-9816359 | Maternal to zygotic transition (MZT) | 7.107181e-03 | 2.148 |
| R-HSA-9759476 | Regulation of Homotypic Cell-Cell Adhesion | 7.257077e-03 | 2.139 |
| R-HSA-9764725 | Negative Regulation of CDH1 Gene Transcription | 6.935995e-03 | 2.159 |
| R-HSA-1280215 | Cytokine Signaling in Immune system | 7.282101e-03 | 2.138 |
| R-HSA-1266695 | Interleukin-7 signaling | 7.374685e-03 | 2.132 |
| R-HSA-72203 | Processing of Capped Intron-Containing Pre-mRNA | 7.416783e-03 | 2.130 |
| R-HSA-9927418 | Developmental Lineage of Mammary Gland Luminal Epithelial Cells | 8.084656e-03 | 2.092 |
| R-HSA-1660499 | Synthesis of PIPs at the plasma membrane | 7.931194e-03 | 2.101 |
| R-HSA-9796292 | Formation of axial mesoderm | 8.641504e-03 | 2.063 |
| R-HSA-1500620 | Meiosis | 8.430613e-03 | 2.074 |
| R-HSA-73728 | RNA Polymerase I Promoter Opening | 9.121018e-03 | 2.040 |
| R-HSA-69481 | G2/M Checkpoints | 8.846440e-03 | 2.053 |
| R-HSA-8854214 | TBC/RABGAPs | 8.754299e-03 | 2.058 |
| R-HSA-9734009 | Defective Intrinsic Pathway for Apoptosis | 9.121018e-03 | 2.040 |
| R-HSA-983231 | Factors involved in megakaryocyte development and platelet production | 8.897188e-03 | 2.051 |
| R-HSA-9824446 | Viral Infection Pathways | 9.483005e-03 | 2.023 |
| R-HSA-3656532 | TGFBR1 KD Mutants in Cancer | 9.662722e-03 | 2.015 |
| R-HSA-5205685 | PINK1-PRKN Mediated Mitophagy | 1.008694e-02 | 1.996 |
| R-HSA-72695 | Formation of the ternary complex, and subsequently, the 43S complex | 1.099134e-02 | 1.959 |
| R-HSA-5334118 | DNA methylation | 1.111680e-02 | 1.954 |
| R-HSA-196299 | Beta-catenin phosphorylation cascade | 1.164415e-02 | 1.934 |
| R-HSA-8964315 | G beta:gamma signalling through BTK | 1.164415e-02 | 1.934 |
| R-HSA-157118 | Signaling by NOTCH | 1.249232e-02 | 1.903 |
| R-HSA-3304356 | SMAD2/3 Phosphorylation Motif Mutants in Cancer | 1.294410e-02 | 1.888 |
| R-HSA-9687136 | Aberrant regulation of mitotic exit in cancer due to RB1 defects | 1.334301e-02 | 1.875 |
| R-HSA-9766229 | Degradation of CDH1 | 1.358999e-02 | 1.867 |
| R-HSA-427413 | NoRC negatively regulates rRNA expression | 1.370470e-02 | 1.863 |
| R-HSA-9006931 | Signaling by Nuclear Receptors | 1.401612e-02 | 1.853 |
| R-HSA-5578749 | Transcriptional regulation by small RNAs | 1.448917e-02 | 1.839 |
| R-HSA-418990 | Adherens junctions interactions | 1.510897e-02 | 1.821 |
| R-HSA-909733 | Interferon alpha/beta signaling | 1.482957e-02 | 1.829 |
| R-HSA-111465 | Apoptotic cleavage of cellular proteins | 1.460419e-02 | 1.836 |
| R-HSA-8964616 | G beta:gamma signalling through CDC42 | 1.517570e-02 | 1.819 |
| R-HSA-936964 | Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) | 1.517570e-02 | 1.819 |
| R-HSA-446728 | Cell junction organization | 1.590565e-02 | 1.798 |
| R-HSA-72689 | Formation of a pool of free 40S subunits | 1.620398e-02 | 1.790 |
| R-HSA-68949 | Orc1 removal from chromatin | 1.657360e-02 | 1.781 |
| R-HSA-3304349 | Loss of Function of SMAD2/3 in Cancer | 1.663982e-02 | 1.779 |
| R-HSA-390522 | Striated Muscle Contraction | 1.727338e-02 | 1.763 |
| R-HSA-9927426 | Developmental Lineage of Mammary Gland Alveolar Cells | 1.871463e-02 | 1.728 |
| R-HSA-174178 | APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins ... | 1.765741e-02 | 1.753 |
| R-HSA-9843970 | Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex | 1.871463e-02 | 1.728 |
| R-HSA-5205647 | Mitophagy | 1.871463e-02 | 1.728 |
| R-HSA-73854 | RNA Polymerase I Promoter Clearance | 1.793962e-02 | 1.746 |
| R-HSA-421270 | Cell-cell junction organization | 1.695486e-02 | 1.771 |
| R-HSA-418217 | G beta:gamma signalling through PLC beta | 1.924679e-02 | 1.716 |
| R-HSA-500657 | Presynaptic function of Kainate receptors | 1.924679e-02 | 1.716 |
| R-HSA-1500931 | Cell-Cell communication | 1.933489e-02 | 1.714 |
| R-HSA-9754189 | Germ layer formation at gastrulation | 2.148649e-02 | 1.668 |
| R-HSA-5250941 | Negative epigenetic regulation of rRNA expression | 2.191521e-02 | 1.659 |
| R-HSA-73864 | RNA Polymerase I Transcription | 1.985978e-02 | 1.702 |
| R-HSA-392851 | Prostacyclin signalling through prostacyclin receptor | 2.148649e-02 | 1.668 |
| R-HSA-162909 | Host Interactions of HIV factors | 2.117198e-02 | 1.674 |
| R-HSA-9909648 | Regulation of PD-L1(CD274) expression | 2.013392e-02 | 1.696 |
| R-HSA-69242 | S Phase | 2.197652e-02 | 1.658 |
| R-HSA-1483255 | PI Metabolism | 2.202553e-02 | 1.657 |
| R-HSA-9764561 | Regulation of CDH1 Function | 2.245808e-02 | 1.649 |
| R-HSA-212165 | Epigenetic regulation of gene expression | 2.268988e-02 | 1.644 |
| R-HSA-9646304 | Evasion of Oxidative Stress Induced Senescence Due to p14ARF Defects | 2.405012e-02 | 1.619 |
| R-HSA-9646303 | Evasion of Oncogene Induced Senescence Due to p14ARF Defects | 2.405012e-02 | 1.619 |
| R-HSA-9661070 | Defective translocation of RB1 mutants to the nucleus | 2.405012e-02 | 1.619 |
| R-HSA-9013695 | NOTCH4 Intracellular Domain Regulates Transcription | 2.637522e-02 | 1.579 |
| R-HSA-9845323 | Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) | 2.656501e-02 | 1.576 |
| R-HSA-9823730 | Formation of definitive endoderm | 2.386266e-02 | 1.622 |
| R-HSA-202040 | G-protein activation | 2.637522e-02 | 1.579 |
| R-HSA-392170 | ADP signalling through P2Y purinoceptor 12 | 2.637522e-02 | 1.579 |
| R-HSA-5617472 | Activation of anterior HOX genes in hindbrain development during early embryogen... | 2.491485e-02 | 1.604 |
| R-HSA-5619507 | Activation of HOX genes during differentiation | 2.491485e-02 | 1.604 |
| R-HSA-427359 | SIRT1 negatively regulates rRNA expression | 2.347616e-02 | 1.629 |
| R-HSA-5336415 | Uptake and function of diphtheria toxin | 2.518820e-02 | 1.599 |
| R-HSA-8939236 | RUNX1 regulates transcription of genes involved in differentiation of HSCs | 2.644647e-02 | 1.578 |
| R-HSA-9679191 | Potential therapeutics for SARS | 2.349175e-02 | 1.629 |
| R-HSA-8953750 | Transcriptional Regulation by E2F6 | 2.702297e-02 | 1.568 |
| R-HSA-9793380 | Formation of paraxial mesoderm | 2.803343e-02 | 1.552 |
| R-HSA-69239 | Synthesis of DNA | 2.805394e-02 | 1.552 |
| R-HSA-211000 | Gene Silencing by RNA | 2.805394e-02 | 1.552 |
| R-HSA-449147 | Signaling by Interleukins | 2.834525e-02 | 1.548 |
| R-HSA-9670095 | Inhibition of DNA recombination at telomere | 2.890996e-02 | 1.539 |
| R-HSA-9825892 | Regulation of MITF-M-dependent genes involved in cell cycle and proliferation | 2.902382e-02 | 1.537 |
| R-HSA-9755088 | Ribavirin ADME | 2.902382e-02 | 1.537 |
| R-HSA-72766 | Translation | 2.916847e-02 | 1.535 |
| R-HSA-9828211 | Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation | 2.999978e-02 | 1.523 |
| R-HSA-156902 | Peptide chain elongation | 3.293241e-02 | 1.482 |
| R-HSA-390466 | Chaperonin-mediated protein folding | 3.156021e-02 | 1.501 |
| R-HSA-3214841 | PKMTs methylate histone lysines | 3.087330e-02 | 1.510 |
| R-HSA-5625886 | Activated PKN1 stimulates transcription of AR (androgen receptor) regulated gene... | 3.087330e-02 | 1.510 |
| R-HSA-9820841 | M-decay: degradation of maternal mRNAs by maternally stored factors | 3.087330e-02 | 1.510 |
| R-HSA-166208 | mTORC1-mediated signalling | 3.180790e-02 | 1.497 |
| R-HSA-1234174 | Cellular response to hypoxia | 3.441665e-02 | 1.463 |
| R-HSA-8852276 | The role of GTSE1 in G2/M progression after G2 checkpoint | 2.955238e-02 | 1.529 |
| R-HSA-9663891 | Selective autophagy | 3.293241e-02 | 1.482 |
| R-HSA-68882 | Mitotic Anaphase | 3.188643e-02 | 1.496 |
| R-HSA-2555396 | Mitotic Metaphase and Anaphase | 3.271640e-02 | 1.485 |
| R-HSA-389957 | Prefoldin mediated transfer of substrate to CCT/TriC | 3.472664e-02 | 1.459 |
| R-HSA-392451 | G beta:gamma signalling through PI3Kgamma | 3.472664e-02 | 1.459 |
| R-HSA-176974 | Unwinding of DNA | 3.514352e-02 | 1.454 |
| R-HSA-428930 | Thromboxane signalling through TP receptor | 3.777902e-02 | 1.423 |
| R-HSA-418592 | ADP signalling through P2Y purinoceptor 1 | 3.777902e-02 | 1.423 |
| R-HSA-8863678 | Neurodegenerative Diseases | 3.777902e-02 | 1.423 |
| R-HSA-8862803 | Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's dis... | 3.777902e-02 | 1.423 |
| R-HSA-5693606 | DNA Double Strand Break Response | 3.791925e-02 | 1.421 |
| R-HSA-72163 | mRNA Splicing - Major Pathway | 3.799183e-02 | 1.420 |
| R-HSA-390450 | Folding of actin by CCT/TriC | 4.060073e-02 | 1.391 |
| R-HSA-8876493 | InlA-mediated entry of Listeria monocytogenes into host cells | 4.635345e-02 | 1.334 |
| R-HSA-5467340 | AXIN missense mutants destabilize the destruction complex | 4.635345e-02 | 1.334 |
| R-HSA-5467348 | Truncations of AMER1 destabilize the destruction complex | 4.635345e-02 | 1.334 |
| R-HSA-5467337 | APC truncation mutants have impaired AXIN binding | 4.635345e-02 | 1.334 |
| R-HSA-1296059 | G protein gated Potassium channels | 4.096382e-02 | 1.388 |
| R-HSA-997272 | Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits | 4.096382e-02 | 1.388 |
| R-HSA-1296041 | Activation of G protein gated Potassium channels | 4.096382e-02 | 1.388 |
| R-HSA-174084 | Autodegradation of Cdh1 by Cdh1:APC/C | 4.427209e-02 | 1.354 |
| R-HSA-9843940 | Regulation of endogenous retroelements by KRAB-ZFP proteins | 4.356851e-02 | 1.361 |
| R-HSA-174143 | APC/C-mediated degradation of cell cycle proteins | 4.555786e-02 | 1.341 |
| R-HSA-453276 | Regulation of mitotic cell cycle | 4.555786e-02 | 1.341 |
| R-HSA-400042 | Adrenaline,noradrenaline inhibits insulin secretion | 4.427964e-02 | 1.354 |
| R-HSA-391251 | Protein folding | 4.037152e-02 | 1.394 |
| R-HSA-3214858 | RMTs methylate histone arginines | 3.949642e-02 | 1.403 |
| R-HSA-195253 | Degradation of beta-catenin by the destruction complex | 4.356851e-02 | 1.361 |
| R-HSA-4839744 | Signaling by APC mutants | 4.635345e-02 | 1.334 |
| R-HSA-162906 | HIV Infection | 4.187363e-02 | 1.378 |
| R-HSA-9824272 | Somitogenesis | 4.184554e-02 | 1.378 |
| R-HSA-388841 | Regulation of T cell activation by CD28 family | 4.024464e-02 | 1.395 |
| R-HSA-389948 | Co-inhibition by PD-1 | 4.432595e-02 | 1.353 |
| R-HSA-174154 | APC/C:Cdc20 mediated degradation of Securin | 4.677598e-02 | 1.330 |
| R-HSA-9734767 | Developmental Cell Lineages | 4.696384e-02 | 1.328 |
| R-HSA-9954709 | Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide | 4.703145e-02 | 1.328 |
| R-HSA-9632697 | Evasion of Oxidative Stress Induced Senescence Due to Defective p16INK4A binding... | 4.752327e-02 | 1.323 |
| R-HSA-9630791 | Evasion of Oncogene Induced Senescence Due to Defective p16INK4A binding to CDK4 | 4.752327e-02 | 1.323 |
| R-HSA-5632968 | Defective Mismatch Repair Associated With MSH6 | 4.752327e-02 | 1.323 |
| R-HSA-9645722 | Defective Intrinsic Pathway for Apoptosis Due to p14ARF Loss of Function | 4.752327e-02 | 1.323 |
| R-HSA-9824878 | Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 | 5.238439e-02 | 1.281 |
| R-HSA-4641262 | Disassembly of the destruction complex and recruitment of AXIN to the membrane | 4.772492e-02 | 1.321 |
| R-HSA-167243 | Tat-mediated HIV elongation arrest and recovery | 4.772492e-02 | 1.321 |
| R-HSA-167238 | Pausing and recovery of Tat-mediated HIV elongation | 4.772492e-02 | 1.321 |
| R-HSA-167287 | HIV elongation arrest and recovery | 5.129793e-02 | 1.290 |
| R-HSA-167290 | Pausing and recovery of HIV elongation | 5.129793e-02 | 1.290 |
| R-HSA-9615710 | Late endosomal microautophagy | 5.499680e-02 | 1.260 |
| R-HSA-9927432 | Developmental Lineage of Mammary Gland Myoepithelial Cells | 5.499680e-02 | 1.260 |
| R-HSA-68962 | Activation of the pre-replicative complex | 5.881953e-02 | 1.230 |
| R-HSA-9687139 | Aberrant regulation of mitotic cell cycle due to RB1 defects | 5.881953e-02 | 1.230 |
| R-HSA-72172 | mRNA Splicing | 5.012433e-02 | 1.300 |
| R-HSA-6798695 | Neutrophil degranulation | 4.744117e-02 | 1.324 |
| R-HSA-5693548 | Sensing of DNA Double Strand Breaks | 5.238439e-02 | 1.281 |
| R-HSA-8866427 | VLDLR internalisation and degradation | 5.867690e-02 | 1.232 |
| R-HSA-9013973 | TICAM1-dependent activation of IRF3/IRF7 | 5.238439e-02 | 1.281 |
| R-HSA-162592 | Integration of provirus | 5.238439e-02 | 1.281 |
| R-HSA-8941856 | RUNX3 regulates NOTCH signaling | 5.867690e-02 | 1.232 |
| R-HSA-69618 | Mitotic Spindle Checkpoint | 5.626136e-02 | 1.250 |
| R-HSA-4839748 | Signaling by AMER1 mutants | 5.238439e-02 | 1.281 |
| R-HSA-4839735 | Signaling by AXIN mutants | 5.238439e-02 | 1.281 |
| R-HSA-9013694 | Signaling by NOTCH4 | 5.184659e-02 | 1.285 |
| R-HSA-456926 | Thrombin signalling through proteinase activated receptors (PARs) | 5.881953e-02 | 1.230 |
| R-HSA-5693571 | Nonhomologous End-Joining (NHEJ) | 4.935709e-02 | 1.307 |
| R-HSA-166016 | Toll Like Receptor 4 (TLR4) Cascade | 5.267190e-02 | 1.278 |
| R-HSA-73614 | Pyrimidine salvage | 5.129793e-02 | 1.290 |
| R-HSA-69206 | G1/S Transition | 5.761736e-02 | 1.239 |
| R-HSA-69473 | G2/M DNA damage checkpoint | 5.184659e-02 | 1.285 |
| R-HSA-1169408 | ISG15 antiviral mechanism | 5.404997e-02 | 1.267 |
| R-HSA-168255 | Influenza Infection | 5.582860e-02 | 1.253 |
| R-HSA-453279 | Mitotic G1 phase and G1/S transition | 4.976664e-02 | 1.303 |
| R-HSA-5663205 | Infectious disease | 5.708990e-02 | 1.243 |
| R-HSA-451326 | Activation of kainate receptors upon glutamate binding | 5.129793e-02 | 1.290 |
| R-HSA-1234158 | Regulation of gene expression by Hypoxia-inducible Factor | 5.238439e-02 | 1.281 |
| R-HSA-420092 | Glucagon-type ligand receptors | 5.499680e-02 | 1.260 |
| R-HSA-9678108 | SARS-CoV-1 Infection | 5.039790e-02 | 1.298 |
| R-HSA-9842860 | Regulation of endogenous retroelements | 6.023774e-02 | 1.220 |
| R-HSA-174184 | Cdc20:Phospho-APC/C mediated degradation of Cyclin A | 6.044832e-02 | 1.219 |
| R-HSA-389958 | Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding | 6.276399e-02 | 1.202 |
| R-HSA-179419 | APC:Cdc20 mediated degradation of cell cycle proteins prior to satisfation of th... | 6.341097e-02 | 1.198 |
| R-HSA-9860931 | Response of endothelial cells to shear stress | 6.437728e-02 | 1.191 |
| R-HSA-9856530 | High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR... | 6.586987e-02 | 1.181 |
| R-HSA-69017 | CDK-mediated phosphorylation and removal of Cdc6 | 6.644861e-02 | 1.178 |
| R-HSA-2173795 | Downregulation of SMAD2/3:SMAD4 transcriptional activity | 6.682794e-02 | 1.175 |
| R-HSA-9675126 | Diseases of mitotic cell cycle | 6.682794e-02 | 1.175 |
| R-HSA-4791275 | Signaling by WNT in cancer | 6.682794e-02 | 1.175 |
| R-HSA-1296065 | Inwardly rectifying K+ channels | 6.682794e-02 | 1.175 |
| R-HSA-162587 | HIV Life Cycle | 6.707917e-02 | 1.173 |
| R-HSA-5693607 | Processing of DNA double-strand break ends | 6.839385e-02 | 1.165 |
| R-HSA-977225 | Amyloid fiber formation | 6.839385e-02 | 1.165 |
| R-HSA-1474165 | Reproduction | 6.864939e-02 | 1.163 |
| R-HSA-168164 | Toll Like Receptor 3 (TLR3) Cascade | 6.868004e-02 | 1.163 |
| R-HSA-176409 | APC/C:Cdc20 mediated degradation of mitotic proteins | 6.956065e-02 | 1.158 |
| R-HSA-3214815 | HDACs deacetylate histones | 6.956065e-02 | 1.158 |
| R-HSA-9630750 | Evasion of Oncogene Induced Senescence Due to p16INK4A Defects | 7.043326e-02 | 1.152 |
| R-HSA-9632693 | Evasion of Oxidative Stress Induced Senescence Due to p16INK4A Defects | 7.043326e-02 | 1.152 |
| R-HSA-9630794 | Evasion of Oncogene Induced Senescence Due to Defective p16INK4A binding to CDK4... | 7.043326e-02 | 1.152 |
| R-HSA-9632700 | Evasion of Oxidative Stress Induced Senescence Due to Defective p16INK4A binding... | 7.043326e-02 | 1.152 |
| R-HSA-9665230 | Drug resistance in ERBB2 KD mutants | 9.279357e-02 | 1.032 |
| R-HSA-9652282 | Drug-mediated inhibition of ERBB2 signaling | 9.279357e-02 | 1.032 |
| R-HSA-9665244 | Resistance of ERBB2 KD mutants to sapitinib | 9.279357e-02 | 1.032 |
| R-HSA-9665251 | Resistance of ERBB2 KD mutants to lapatinib | 9.279357e-02 | 1.032 |
| R-HSA-3656535 | TGFBR1 LBD Mutants in Cancer | 9.279357e-02 | 1.032 |
| R-HSA-9665250 | Resistance of ERBB2 KD mutants to AEE788 | 9.279357e-02 | 1.032 |
| R-HSA-9665245 | Resistance of ERBB2 KD mutants to tesevatinib | 9.279357e-02 | 1.032 |
| R-HSA-9665249 | Resistance of ERBB2 KD mutants to afatinib | 9.279357e-02 | 1.032 |
| R-HSA-3878781 | Glycogen storage disease type IV (GBE1) | 9.279357e-02 | 1.032 |
| R-HSA-9665233 | Resistance of ERBB2 KD mutants to trastuzumab | 9.279357e-02 | 1.032 |
| R-HSA-9665247 | Resistance of ERBB2 KD mutants to osimertinib | 9.279357e-02 | 1.032 |
| R-HSA-9665246 | Resistance of ERBB2 KD mutants to neratinib | 9.279357e-02 | 1.032 |
| R-HSA-9665737 | Drug resistance in ERBB2 TMD/JMD mutants | 9.279357e-02 | 1.032 |
| R-HSA-176412 | Phosphorylation of the APC/C | 8.615186e-02 | 1.065 |
| R-HSA-176814 | Activation of APC/C and APC/C:Cdc20 mediated degradation of mitotic proteins | 7.274646e-02 | 1.138 |
| R-HSA-9948299 | Ribosome-associated quality control | 8.741297e-02 | 1.058 |
| R-HSA-2173793 | Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer | 7.274646e-02 | 1.138 |
| R-HSA-397795 | G-protein beta:gamma signalling | 7.100905e-02 | 1.149 |
| R-HSA-5693565 | Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at... | 8.273951e-02 | 1.082 |
| R-HSA-180585 | Vif-mediated degradation of APOBEC3G | 8.885522e-02 | 1.051 |
| R-HSA-5693567 | HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA) | 9.004956e-02 | 1.046 |
| R-HSA-5685938 | HDR through Single Strand Annealing (SSA) | 7.100905e-02 | 1.149 |
| R-HSA-392518 | Signal amplification | 7.971292e-02 | 1.098 |
| R-HSA-2467813 | Separation of Sister Chromatids | 7.981465e-02 | 1.098 |
| R-HSA-3270619 | IRF3-mediated induction of type I IFN | 7.896697e-02 | 1.103 |
| R-HSA-5632928 | Defective Mismatch Repair Associated With MSH2 | 7.043326e-02 | 1.152 |
| R-HSA-446343 | Localization of the PINCH-ILK-PARVIN complex to focal adhesions | 9.279357e-02 | 1.032 |
| R-HSA-1502540 | Signaling by Activin | 7.896697e-02 | 1.103 |
| R-HSA-75815 | Ubiquitin-dependent degradation of Cyclin D | 7.971292e-02 | 1.098 |
| R-HSA-352238 | Breakdown of the nuclear lamina | 7.043326e-02 | 1.152 |
| R-HSA-8876725 | Protein methylation | 7.896697e-02 | 1.103 |
| R-HSA-176187 | Activation of ATR in response to replication stress | 7.100905e-02 | 1.149 |
| R-HSA-168898 | Toll-like Receptor Cascades | 7.433690e-02 | 1.129 |
| R-HSA-9855142 | Cellular responses to mechanical stimuli | 9.004956e-02 | 1.046 |
| R-HSA-166166 | MyD88-independent TLR4 cascade | 8.014878e-02 | 1.096 |
| R-HSA-937061 | TRIF (TICAM1)-mediated TLR4 signaling | 8.014878e-02 | 1.096 |
| R-HSA-210744 | Regulation of gene expression in late stage (branching morphogenesis) pancreatic... | 8.615186e-02 | 1.065 |
| R-HSA-8939902 | Regulation of RUNX2 expression and activity | 8.975663e-02 | 1.047 |
| R-HSA-3858494 | Beta-catenin independent WNT signaling | 8.301406e-02 | 1.081 |
| R-HSA-8956321 | Nucleotide salvage | 8.975663e-02 | 1.047 |
| R-HSA-163359 | Glucagon signaling in metabolic regulation | 7.530488e-02 | 1.123 |
| R-HSA-9692914 | SARS-CoV-1-host interactions | 7.089256e-02 | 1.149 |
| R-HSA-168256 | Immune System | 8.238582e-02 | 1.084 |
| R-HSA-110328 | Recognition and association of DNA glycosylase with site containing an affected ... | 7.971292e-02 | 1.098 |
| R-HSA-9679506 | SARS-CoV Infections | 7.368034e-02 | 1.133 |
| R-HSA-176408 | Regulation of APC/C activators between G1/S and early anaphase | 9.336913e-02 | 1.030 |
| R-HSA-9616222 | Transcriptional regulation of granulopoiesis | 9.336913e-02 | 1.030 |
| R-HSA-141430 | Inactivation of APC/C via direct inhibition of the APC/C complex | 9.352428e-02 | 1.029 |
| R-HSA-141405 | Inhibition of the proteolytic activity of APC/C required for the onset of anapha... | 9.352428e-02 | 1.029 |
| R-HSA-180910 | Vpr-mediated nuclear import of PICs | 9.358409e-02 | 1.029 |
| R-HSA-2173796 | SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription | 9.358409e-02 | 1.029 |
| R-HSA-933541 | TRAF6 mediated IRF7 activation | 9.358409e-02 | 1.029 |
| R-HSA-9762114 | GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 | 9.358409e-02 | 1.029 |
| R-HSA-69615 | G1/S DNA Damage Checkpoints | 9.704965e-02 | 1.013 |
| R-HSA-4420097 | VEGFA-VEGFR2 Pathway | 9.789208e-02 | 1.009 |
| R-HSA-8986944 | Transcriptional Regulation by MECP2 | 9.959644e-02 | 1.002 |
| R-HSA-5689880 | Ub-specific processing proteases | 1.003381e-01 | 0.999 |
| R-HSA-209563 | Axonal growth stimulation | 1.146173e-01 | 0.941 |
| R-HSA-5603037 | IRAK4 deficiency (TLR5) | 1.146173e-01 | 0.941 |
| R-HSA-5660862 | Defective SLC7A7 causes lysinuric protein intolerance (LPI) | 1.146173e-01 | 0.941 |
| R-HSA-9734281 | Defective HPRT1 disrupts guanine and hypoxanthine salvage | 1.146173e-01 | 0.941 |
| R-HSA-8952158 | RUNX3 regulates BCL2L11 (BIM) transcription | 1.359174e-01 | 0.867 |
| R-HSA-69200 | Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 ... | 1.359174e-01 | 0.867 |
| R-HSA-174048 | APC/C:Cdc20 mediated degradation of Cyclin B | 1.166381e-01 | 0.933 |
| R-HSA-179409 | APC-Cdc20 mediated degradation of Nek2A | 1.327580e-01 | 0.877 |
| R-HSA-5357786 | TNFR1-induced proapoptotic signaling | 1.327580e-01 | 0.877 |
| R-HSA-6803529 | FGFR2 alternative splicing | 1.493434e-01 | 0.826 |
| R-HSA-350054 | Notch-HLH transcription pathway | 1.493434e-01 | 0.826 |
| R-HSA-167152 | Formation of HIV elongation complex in the absence of HIV Tat | 1.083684e-01 | 0.965 |
| R-HSA-3371497 | HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig... | 1.164370e-01 | 0.934 |
| R-HSA-167169 | HIV Transcription Elongation | 1.083684e-01 | 0.965 |
| R-HSA-9851695 | Epigenetic regulation of adipogenesis genes by MLL3 and MLL4 complexes | 1.295945e-01 | 0.887 |
| R-HSA-9841922 | MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesi... | 1.295945e-01 | 0.887 |
| R-HSA-167246 | Tat-mediated elongation of the HIV-1 transcript | 1.083684e-01 | 0.965 |
| R-HSA-9609523 | Insertion of tail-anchored proteins into the endoplasmic reticulum membrane | 1.246346e-01 | 0.904 |
| R-HSA-9818564 | Epigenetic regulation of gene expression by MLL3 and MLL4 complexes | 1.295945e-01 | 0.887 |
| R-HSA-167200 | Formation of HIV-1 elongation complex containing HIV-1 Tat | 1.033435e-01 | 0.986 |
| R-HSA-5693538 | Homology Directed Repair | 1.060856e-01 | 0.974 |
| R-HSA-5693532 | DNA Double-Strand Break Repair | 1.272007e-01 | 0.896 |
| R-HSA-5626978 | TNFR1-mediated ceramide production | 1.359174e-01 | 0.867 |
| R-HSA-176407 | Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase | 1.010711e-01 | 0.995 |
| R-HSA-9907900 | Proteasome assembly | 1.348283e-01 | 0.870 |
| R-HSA-8936459 | RUNX1 regulates genes involved in megakaryocyte differentiation and platelet fun... | 1.164370e-01 | 0.934 |
| R-HSA-9636249 | Inhibition of nitric oxide production | 1.146173e-01 | 0.941 |
| R-HSA-5357905 | Regulation of TNFR1 signaling | 1.459807e-01 | 0.836 |
| R-HSA-1660517 | Synthesis of PIPs at the late endosome membrane | 1.010711e-01 | 0.995 |
| R-HSA-170834 | Signaling by TGF-beta Receptor Complex | 1.260566e-01 | 0.899 |
| R-HSA-5218920 | VEGFR2 mediated vascular permeability | 1.134862e-01 | 0.945 |
| R-HSA-3249367 | STAT6-mediated induction of chemokines | 1.146173e-01 | 0.941 |
| R-HSA-176033 | Interactions of Vpr with host cellular proteins | 1.083684e-01 | 0.965 |
| R-HSA-168273 | Influenza Viral RNA Transcription and Replication | 1.327288e-01 | 0.877 |
| R-HSA-1181150 | Signaling by NODAL | 1.246346e-01 | 0.904 |
| R-HSA-165159 | MTOR signalling | 1.239889e-01 | 0.907 |
| R-HSA-9758941 | Gastrulation | 1.165047e-01 | 0.934 |
| R-HSA-5610785 | GLI3 is processed to GLI3R by the proteasome | 1.186940e-01 | 0.926 |
| R-HSA-5610783 | Degradation of GLI2 by the proteasome | 1.186940e-01 | 0.926 |
| R-HSA-1834949 | Cytosolic sensors of pathogen-associated DNA | 1.246310e-01 | 0.904 |
| R-HSA-8876384 | Listeria monocytogenes entry into host cells | 1.409977e-01 | 0.851 |
| R-HSA-991365 | Activation of GABAB receptors | 1.239889e-01 | 0.907 |
| R-HSA-9633012 | Response of EIF2AK4 (GCN2) to amino acid deficiency | 1.515711e-01 | 0.819 |
| R-HSA-8953854 | Metabolism of RNA | 1.042253e-01 | 0.982 |
| R-HSA-2173788 | Downregulation of TGF-beta receptor signaling | 1.493434e-01 | 0.826 |
| R-HSA-3371556 | Cellular response to heat stress | 1.146232e-01 | 0.941 |
| R-HSA-2173789 | TGF-beta receptor signaling activates SMADs | 1.293680e-01 | 0.888 |
| R-HSA-5423599 | Diseases of Mismatch Repair (MMR) | 1.146173e-01 | 0.941 |
| R-HSA-168276 | NS1 Mediated Effects on Host Pathways | 1.033435e-01 | 0.986 |
| R-HSA-381676 | Glucagon-like Peptide-1 (GLP1) regulates insulin secretion | 1.239889e-01 | 0.907 |
| R-HSA-977444 | GABA B receptor activation | 1.239889e-01 | 0.907 |
| R-HSA-1834941 | STING mediated induction of host immune responses | 1.166381e-01 | 0.933 |
| R-HSA-4086398 | Ca2+ pathway | 1.373632e-01 | 0.862 |
| R-HSA-2995383 | Initiation of Nuclear Envelope (NE) Reformation | 1.409977e-01 | 0.851 |
| R-HSA-9929356 | GSK3B-mediated proteasomal degradation of PD-L1(CD274) | 1.033435e-01 | 0.986 |
| R-HSA-5218859 | Regulated Necrosis | 1.164370e-01 | 0.934 |
| R-HSA-9617828 | FOXO-mediated transcription of cell cycle genes | 1.409977e-01 | 0.851 |
| R-HSA-194138 | Signaling by VEGF | 1.295945e-01 | 0.887 |
| R-HSA-162594 | Early Phase of HIV Life Cycle | 1.327580e-01 | 0.877 |
| R-HSA-9660821 | ADORA2B mediated anti-inflammatory cytokines production | 1.403669e-01 | 0.853 |
| R-HSA-9010553 | Regulation of expression of SLITs and ROBOs | 1.244813e-01 | 0.905 |
| R-HSA-8941858 | Regulation of RUNX3 expression and activity | 1.083684e-01 | 0.965 |
| R-HSA-9675135 | Diseases of DNA repair | 1.459807e-01 | 0.836 |
| R-HSA-432040 | Vasopressin regulates renal water homeostasis via Aquaporins | 1.403669e-01 | 0.853 |
| R-HSA-9007101 | Rab regulation of trafficking | 1.033159e-01 | 0.986 |
| R-HSA-8964043 | Plasma lipoprotein clearance | 1.033435e-01 | 0.986 |
| R-HSA-69601 | Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A | 1.403669e-01 | 0.853 |
| R-HSA-69613 | p53-Independent G1/S DNA Damage Checkpoint | 1.403669e-01 | 0.853 |
| R-HSA-111885 | Opioid Signalling | 1.515711e-01 | 0.819 |
| R-HSA-110329 | Cleavage of the damaged pyrimidine | 1.239889e-01 | 0.907 |
| R-HSA-73928 | Depyrimidination | 1.239889e-01 | 0.907 |
| R-HSA-69541 | Stabilization of p53 | 1.033435e-01 | 0.986 |
| R-HSA-913531 | Interferon Signaling | 1.209927e-01 | 0.917 |
| R-HSA-5633007 | Regulation of TP53 Activity | 1.470583e-01 | 0.833 |
| R-HSA-111471 | Apoptotic factor-mediated response | 1.087798e-01 | 0.963 |
| R-HSA-9615017 | FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes | 1.186940e-01 | 0.926 |
| R-HSA-3700989 | Transcriptional Regulation by TP53 | 1.402223e-01 | 0.853 |
| R-HSA-6811440 | Retrograde transport at the Trans-Golgi-Network | 1.516668e-01 | 0.819 |
| R-HSA-9673768 | Signaling by membrane-tethered fusions of PDGFRA or PDGFRB | 1.567064e-01 | 0.805 |
| R-HSA-182218 | Nef Mediated CD8 Down-regulation | 1.769964e-01 | 0.752 |
| R-HSA-9833576 | CDH11 homotypic and heterotypic interactions | 1.769964e-01 | 0.752 |
| R-HSA-9017802 | Noncanonical activation of NOTCH3 | 1.769964e-01 | 0.752 |
| R-HSA-111957 | Cam-PDE 1 activation | 1.769964e-01 | 0.752 |
| R-HSA-177539 | Autointegration results in viral DNA circles | 1.967995e-01 | 0.706 |
| R-HSA-3595174 | Defective CHST14 causes EDS, musculocontractural type | 1.967995e-01 | 0.706 |
| R-HSA-9912529 | H139Hfs13* PPM1K causes a mild variant of MSUD | 1.967995e-01 | 0.706 |
| R-HSA-8951430 | RUNX3 regulates WNT signaling | 2.161272e-01 | 0.665 |
| R-HSA-4411364 | Binding of TCF/LEF:CTNNB1 to target gene promoters | 2.161272e-01 | 0.665 |
| R-HSA-9031528 | NR1H2 & NR1H3 regulate gene expression linked to triglyceride lipolysis in adipo... | 2.161272e-01 | 0.665 |
| R-HSA-72731 | Recycling of eIF2:GDP | 2.161272e-01 | 0.665 |
| R-HSA-9031525 | NR1H2 & NR1H3 regulate gene expression to limit cholesterol uptake | 2.161272e-01 | 0.665 |
| R-HSA-196025 | Formation of annular gap junctions | 2.349910e-01 | 0.629 |
| R-HSA-190873 | Gap junction degradation | 2.534020e-01 | 0.596 |
| R-HSA-5218900 | CASP8 activity is inhibited | 2.534020e-01 | 0.596 |
| R-HSA-9027277 | Erythropoietin activates Phospholipase C gamma (PLCG) | 2.713710e-01 | 0.566 |
| R-HSA-389960 | Formation of tubulin folding intermediates by CCT/TriC | 1.663139e-01 | 0.779 |
| R-HSA-9623433 | NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis | 3.060251e-01 | 0.514 |
| R-HSA-2514853 | Condensation of Prometaphase Chromosomes | 3.060251e-01 | 0.514 |
| R-HSA-5358493 | Synthesis of diphthamide-EEF2 | 3.060251e-01 | 0.514 |
| R-HSA-5357956 | TNFR1-induced NF-kappa-B signaling pathway | 1.923321e-01 | 0.716 |
| R-HSA-171306 | Packaging Of Telomere Ends | 1.923321e-01 | 0.716 |
| R-HSA-9709570 | Impaired BRCA2 binding to RAD51 | 2.099559e-01 | 0.678 |
| R-HSA-159227 | Transport of the SLBP independent Mature mRNA | 2.456075e-01 | 0.610 |
| R-HSA-72187 | mRNA 3'-end processing | 1.810794e-01 | 0.742 |
| R-HSA-112382 | Formation of RNA Pol II elongation complex | 1.810794e-01 | 0.742 |
| R-HSA-159230 | Transport of the SLBP Dependant Mature mRNA | 2.545664e-01 | 0.594 |
| R-HSA-390471 | Association of TriC/CCT with target proteins during biosynthesis | 2.545664e-01 | 0.594 |
| R-HSA-75955 | RNA Polymerase II Transcription Elongation | 1.871378e-01 | 0.728 |
| R-HSA-194441 | Metabolism of non-coding RNA | 2.244821e-01 | 0.649 |
| R-HSA-191859 | snRNP Assembly | 2.244821e-01 | 0.649 |
| R-HSA-72202 | Transport of Mature Transcript to Cytoplasm | 1.784148e-01 | 0.749 |
| R-HSA-159231 | Transport of Mature mRNA Derived from an Intronless Transcript | 3.082730e-01 | 0.511 |
| R-HSA-141444 | Amplification of signal from unattached kinetochores via a MAD2 inhibitory si... | 1.978489e-01 | 0.704 |
| R-HSA-141424 | Amplification of signal from the kinetochores | 1.978489e-01 | 0.704 |
| R-HSA-1799339 | SRP-dependent cotranslational protein targeting to membrane | 1.670482e-01 | 0.777 |
| R-HSA-9954714 | PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA | 2.281098e-01 | 0.642 |
| R-HSA-975956 | Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) | 2.332649e-01 | 0.632 |
| R-HSA-9954716 | ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri... | 2.541536e-01 | 0.595 |
| R-HSA-192823 | Viral mRNA Translation | 3.023569e-01 | 0.519 |
| R-HSA-167172 | Transcription of the HIV genome | 2.827301e-01 | 0.549 |
| R-HSA-9013508 | NOTCH3 Intracellular Domain Regulates Transcription | 2.188286e-01 | 0.660 |
| R-HSA-3214842 | HDMs demethylate histones | 1.749203e-01 | 0.757 |
| R-HSA-3134973 | LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production | 1.567064e-01 | 0.805 |
| R-HSA-9762292 | Regulation of CDH11 function | 2.713710e-01 | 0.566 |
| R-HSA-3769402 | Deactivation of the beta-catenin transactivating complex | 2.904133e-01 | 0.537 |
| R-HSA-1234176 | Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha | 1.750757e-01 | 0.757 |
| R-HSA-8856828 | Clathrin-mediated endocytosis | 2.015486e-01 | 0.696 |
| R-HSA-3247509 | Chromatin modifying enzymes | 1.706582e-01 | 0.768 |
| R-HSA-162599 | Late Phase of HIV Life Cycle | 1.978287e-01 | 0.704 |
| R-HSA-1606341 | IRF3 mediated activation of type 1 IFN | 1.567064e-01 | 0.805 |
| R-HSA-8849473 | PTK6 Expression | 2.161272e-01 | 0.665 |
| R-HSA-2025928 | Calcineurin activates NFAT | 2.534020e-01 | 0.596 |
| R-HSA-113501 | Inhibition of replication initiation of damaged DNA by RB1/E2F1 | 3.060251e-01 | 0.514 |
| R-HSA-1221632 | Meiotic synapsis | 1.871378e-01 | 0.728 |
| R-HSA-9735869 | SARS-CoV-1 modulates host translation machinery | 2.635318e-01 | 0.579 |
| R-HSA-4839726 | Chromatin organization | 2.127259e-01 | 0.672 |
| R-HSA-75893 | TNF signaling | 2.056137e-01 | 0.687 |
| R-HSA-167590 | Nef Mediated CD4 Down-regulation | 2.161272e-01 | 0.665 |
| R-HSA-450341 | Activation of the AP-1 family of transcription factors | 2.534020e-01 | 0.596 |
| R-HSA-72764 | Eukaryotic Translation Termination | 2.594361e-01 | 0.586 |
| R-HSA-9012852 | Signaling by NOTCH3 | 1.994078e-01 | 0.700 |
| R-HSA-3371511 | HSF1 activation | 2.814604e-01 | 0.551 |
| R-HSA-9675136 | Diseases of DNA Double-Strand Break Repair | 2.635318e-01 | 0.579 |
| R-HSA-8941855 | RUNX3 regulates CDKN1A transcription | 1.769964e-01 | 0.752 |
| R-HSA-1614603 | Cysteine formation from homocysteine | 2.161272e-01 | 0.665 |
| R-HSA-3371378 | Regulation by c-FLIP | 2.349910e-01 | 0.629 |
| R-HSA-8875656 | MET receptor recycling | 2.349910e-01 | 0.629 |
| R-HSA-193697 | p75NTR regulates axonogenesis | 2.534020e-01 | 0.596 |
| R-HSA-5140745 | WNT5A-dependent internalization of FZD2, FZD5 and ROR2 | 2.713710e-01 | 0.566 |
| R-HSA-192905 | vRNP Assembly | 2.889086e-01 | 0.539 |
| R-HSA-211733 | Regulation of activated PAK-2p34 by proteasome mediated degradation | 2.277324e-01 | 0.643 |
| R-HSA-9701190 | Defective homologous recombination repair (HRR) due to BRCA2 loss of function | 2.635318e-01 | 0.579 |
| R-HSA-165054 | Rev-mediated nuclear export of HIV RNA | 2.993524e-01 | 0.524 |
| R-HSA-73856 | RNA Polymerase II Transcription Termination | 2.372429e-01 | 0.625 |
| R-HSA-9725554 | Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin | 3.082730e-01 | 0.511 |
| R-HSA-9917777 | Epigenetic regulation by WDR5-containing histone modifying complexes | 2.440294e-01 | 0.613 |
| R-HSA-446388 | Regulation of cytoskeletal remodeling and cell spreading by IPP complex componen... | 1.769964e-01 | 0.752 |
| R-HSA-9634597 | GPER1 signaling | 1.574223e-01 | 0.803 |
| R-HSA-416482 | G alpha (12/13) signalling events | 1.596760e-01 | 0.797 |
| R-HSA-5693579 | Homologous DNA Pairing and Strand Exchange | 2.993524e-01 | 0.524 |
| R-HSA-2980766 | Nuclear Envelope Breakdown | 2.118632e-01 | 0.674 |
| R-HSA-5620971 | Pyroptosis | 2.011213e-01 | 0.697 |
| R-HSA-1236974 | ER-Phagosome pathway | 2.178897e-01 | 0.662 |
| R-HSA-9008059 | Interleukin-37 signaling | 2.188286e-01 | 0.660 |
| R-HSA-175567 | Integration of viral DNA into host genomic DNA | 1.967995e-01 | 0.706 |
| R-HSA-8847453 | Synthesis of PIPs in the nucleus | 2.161272e-01 | 0.665 |
| R-HSA-193634 | Axonal growth inhibition (RHOA activation) | 2.349910e-01 | 0.629 |
| R-HSA-9734207 | Nucleotide salvage defects | 2.349910e-01 | 0.629 |
| R-HSA-69416 | Dimerization of procaspase-8 | 2.349910e-01 | 0.629 |
| R-HSA-164843 | 2-LTR circle formation | 2.713710e-01 | 0.566 |
| R-HSA-9821993 | Replacement of protamines by nucleosomes in the male pronucleus | 1.663139e-01 | 0.779 |
| R-HSA-180689 | APOBEC3G mediated resistance to HIV-1 infection | 3.060251e-01 | 0.514 |
| R-HSA-350562 | Regulation of ornithine decarboxylase (ODC) | 2.366609e-01 | 0.626 |
| R-HSA-8854050 | FBXL7 down-regulates AURKA during mitotic entry and in early mitosis | 2.724982e-01 | 0.565 |
| R-HSA-174113 | SCF-beta-TrCP mediated degradation of Emi1 | 2.724982e-01 | 0.565 |
| R-HSA-8943724 | Regulation of PTEN gene transcription | 2.308461e-01 | 0.637 |
| R-HSA-9711097 | Cellular response to starvation | 2.600953e-01 | 0.585 |
| R-HSA-168928 | DDX58/IFIH1-mediated induction of interferon-alpha/beta | 2.541536e-01 | 0.595 |
| R-HSA-418597 | G alpha (z) signalling events | 1.994078e-01 | 0.700 |
| R-HSA-264870 | Caspase-mediated cleavage of cytoskeletal proteins | 2.534020e-01 | 0.596 |
| R-HSA-8934903 | Receptor Mediated Mitophagy | 2.713710e-01 | 0.566 |
| R-HSA-5693616 | Presynaptic phase of homologous DNA pairing and strand exchange | 2.724982e-01 | 0.565 |
| R-HSA-4641258 | Degradation of DVL | 2.904133e-01 | 0.537 |
| R-HSA-1236978 | Cross-presentation of soluble exogenous antigens (endosomes) | 3.082730e-01 | 0.511 |
| R-HSA-2408557 | Selenocysteine synthesis | 2.915347e-01 | 0.535 |
| R-HSA-1660514 | Synthesis of PIPs at the Golgi membrane | 1.835958e-01 | 0.736 |
| R-HSA-381042 | PERK regulates gene expression | 2.724982e-01 | 0.565 |
| R-HSA-111457 | Release of apoptotic factors from the mitochondria | 1.769964e-01 | 0.752 |
| R-HSA-9820962 | Assembly and release of respiratory syncytial virus (RSV) virions | 2.713710e-01 | 0.566 |
| R-HSA-450408 | AUF1 (hnRNP D0) binds and destabilizes mRNA | 2.814604e-01 | 0.551 |
| R-HSA-4641257 | Degradation of AXIN | 2.904133e-01 | 0.537 |
| R-HSA-977443 | GABA receptor activation | 2.308461e-01 | 0.637 |
| R-HSA-5675482 | Regulation of necroptotic cell death | 2.456075e-01 | 0.610 |
| R-HSA-9020702 | Interleukin-1 signaling | 2.915347e-01 | 0.535 |
| R-HSA-9637687 | Suppression of phagosomal maturation | 1.835958e-01 | 0.736 |
| R-HSA-9664873 | Pexophagy | 2.713710e-01 | 0.566 |
| R-HSA-1660516 | Synthesis of PIPs at the early endosome membrane | 1.749203e-01 | 0.757 |
| R-HSA-975871 | MyD88 cascade initiated on plasma membrane | 2.754068e-01 | 0.560 |
| R-HSA-168176 | Toll Like Receptor 5 (TLR5) Cascade | 2.754068e-01 | 0.560 |
| R-HSA-168142 | Toll Like Receptor 10 (TLR10) Cascade | 2.754068e-01 | 0.560 |
| R-HSA-9768777 | Regulation of NPAS4 gene transcription | 2.534020e-01 | 0.596 |
| R-HSA-9619665 | EGR2 and SOX10-mediated initiation of Schwann cell myelination | 2.545664e-01 | 0.594 |
| R-HSA-110331 | Cleavage of the damaged purine | 2.904133e-01 | 0.537 |
| R-HSA-5663202 | Diseases of signal transduction by growth factor receptors and second messengers | 2.376826e-01 | 0.624 |
| R-HSA-73927 | Depurination | 2.993524e-01 | 0.524 |
| R-HSA-5213460 | RIPK1-mediated regulated necrosis | 2.993524e-01 | 0.524 |
| R-HSA-446652 | Interleukin-1 family signaling | 2.361097e-01 | 0.627 |
| R-HSA-9764302 | Regulation of CDH19 Expression and Function | 1.769964e-01 | 0.752 |
| R-HSA-8964011 | HDL clearance | 1.967995e-01 | 0.706 |
| R-HSA-442729 | CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde | 2.349910e-01 | 0.629 |
| R-HSA-9834752 | Respiratory syncytial virus genome replication | 2.534020e-01 | 0.596 |
| R-HSA-9754560 | SARS-CoV-2 modulates autophagy | 2.889086e-01 | 0.539 |
| R-HSA-2022923 | DS-GAG biosynthesis | 3.060251e-01 | 0.514 |
| R-HSA-110330 | Recognition and association of DNA glycosylase with site containing an affected ... | 2.366609e-01 | 0.626 |
| R-HSA-180534 | Vpu mediated degradation of CD4 | 2.545664e-01 | 0.594 |
| R-HSA-2142845 | Hyaluronan metabolism | 2.635318e-01 | 0.579 |
| R-HSA-349425 | Autodegradation of the E3 ubiquitin ligase COP1 | 2.635318e-01 | 0.579 |
| R-HSA-2408508 | Metabolism of ingested SeMet, Sec, MeSec into H2Se | 2.724982e-01 | 0.565 |
| R-HSA-169911 | Regulation of Apoptosis | 2.724982e-01 | 0.565 |
| R-HSA-1168372 | Downstream signaling events of B Cell Receptor (BCR) | 2.958824e-01 | 0.529 |
| R-HSA-1296071 | Potassium Channels | 2.647400e-01 | 0.577 |
| R-HSA-9705683 | SARS-CoV-2-host interactions | 2.601068e-01 | 0.585 |
| R-HSA-5365859 | RA biosynthesis pathway | 2.635318e-01 | 0.579 |
| R-HSA-111933 | Calmodulin induced events | 2.814604e-01 | 0.551 |
| R-HSA-373755 | Semaphorin interactions | 2.501250e-01 | 0.602 |
| R-HSA-8866904 | Negative regulation of activity of TFAP2 (AP-2) family transcription factors | 2.349910e-01 | 0.629 |
| R-HSA-9840373 | Cellular response to mitochondrial stress | 2.534020e-01 | 0.596 |
| R-HSA-2160916 | Hyaluronan degradation | 1.749203e-01 | 0.757 |
| R-HSA-9748787 | Azathioprine ADME | 1.691297e-01 | 0.772 |
| R-HSA-111997 | CaM pathway | 2.814604e-01 | 0.551 |
| R-HSA-74217 | Purine salvage | 2.993524e-01 | 0.524 |
| R-HSA-1643685 | Disease | 1.758724e-01 | 0.755 |
| R-HSA-6794361 | Neurexins and neuroligins | 1.810794e-01 | 0.742 |
| R-HSA-73929 | Base-Excision Repair, AP Site Formation | 1.932483e-01 | 0.714 |
| R-HSA-111932 | CaMK IV-mediated phosphorylation of CREB | 2.713710e-01 | 0.566 |
| R-HSA-6804756 | Regulation of TP53 Activity through Phosphorylation | 2.028057e-01 | 0.693 |
| R-HSA-450531 | Regulation of mRNA stability by proteins that bind AU-rich elements | 3.090707e-01 | 0.510 |
| R-HSA-69202 | Cyclin E associated events during G1/S transition | 2.958824e-01 | 0.529 |
| R-HSA-8878166 | Transcriptional regulation by RUNX2 | 2.255546e-01 | 0.647 |
| R-HSA-157579 | Telomere Maintenance | 2.700640e-01 | 0.569 |
| R-HSA-9764790 | Positive Regulation of CDH1 Gene Transcription | 2.713710e-01 | 0.566 |
| R-HSA-9820960 | Respiratory syncytial virus (RSV) attachment and entry | 2.277324e-01 | 0.643 |
| R-HSA-8876198 | RAB GEFs exchange GTP for GDP on RABs | 1.978489e-01 | 0.704 |
| R-HSA-9006925 | Intracellular signaling by second messengers | 2.704192e-01 | 0.568 |
| R-HSA-5601884 | PIWI-interacting RNA (piRNA) biogenesis | 1.749203e-01 | 0.757 |
| R-HSA-69190 | DNA strand elongation | 2.366609e-01 | 0.626 |
| R-HSA-9692916 | SARS-CoV-1 activates/modulates innate immune responses | 1.810794e-01 | 0.742 |
| R-HSA-6804757 | Regulation of TP53 Degradation | 2.814604e-01 | 0.551 |
| R-HSA-110357 | Displacement of DNA glycosylase by APEX1 | 2.161272e-01 | 0.665 |
| R-HSA-6794362 | Protein-protein interactions at synapses | 1.929300e-01 | 0.715 |
| R-HSA-2408522 | Selenoamino acid metabolism | 2.846897e-01 | 0.546 |
| R-HSA-445717 | Aquaporin-mediated transport | 2.372429e-01 | 0.625 |
| R-HSA-452723 | Transcriptional regulation of pluripotent stem cells | 2.993524e-01 | 0.524 |
| R-HSA-6806003 | Regulation of TP53 Expression and Degradation | 3.082730e-01 | 0.511 |
| R-HSA-5674400 | Constitutive Signaling by AKT1 E17K in Cancer | 1.577852e-01 | 0.802 |
| R-HSA-69656 | Cyclin A:Cdk2-associated events at S phase entry | 3.090707e-01 | 0.510 |
| R-HSA-9009391 | Extra-nuclear estrogen signaling | 2.915347e-01 | 0.535 |
| R-HSA-351906 | Apoptotic cleavage of cell adhesion proteins | 2.349910e-01 | 0.629 |
| R-HSA-9693928 | Defective RIPK1-mediated regulated necrosis | 2.713710e-01 | 0.566 |
| R-HSA-5687128 | MAPK6/MAPK4 signaling | 1.929300e-01 | 0.715 |
| R-HSA-15869 | Metabolism of nucleotides | 1.760283e-01 | 0.754 |
| R-HSA-69580 | p53-Dependent G1/S DNA damage checkpoint | 1.632443e-01 | 0.787 |
| R-HSA-69563 | p53-Dependent G1 DNA Damage Response | 1.632443e-01 | 0.787 |
| R-HSA-9694516 | SARS-CoV-2 Infection | 2.905502e-01 | 0.537 |
| R-HSA-376176 | Signaling by ROBO receptors | 2.983353e-01 | 0.525 |
| R-HSA-9711123 | Cellular response to chemical stress | 2.711524e-01 | 0.567 |
| R-HSA-9022699 | MECP2 regulates neuronal receptors and channels | 1.835958e-01 | 0.736 |
| R-HSA-9755511 | KEAP1-NFE2L2 pathway | 2.321802e-01 | 0.634 |
| R-HSA-69205 | G1/S-Specific Transcription | 2.814604e-01 | 0.551 |
| R-HSA-1169410 | Antiviral mechanism by IFN-stimulated genes | 2.440294e-01 | 0.613 |
| R-HSA-9820952 | Respiratory Syncytial Virus Infection Pathway | 1.760762e-01 | 0.754 |
| R-HSA-75205 | Dissolution of Fibrin Clot | 2.889086e-01 | 0.539 |
| R-HSA-6791226 | Major pathway of rRNA processing in the nucleolus and cytosol | 3.139828e-01 | 0.503 |
| R-HSA-159236 | Transport of Mature mRNA derived from an Intron-Containing Transcript | 3.156731e-01 | 0.501 |
| R-HSA-159234 | Transport of Mature mRNAs Derived from Intronless Transcripts | 3.171710e-01 | 0.499 |
| R-HSA-177243 | Interactions of Rev with host cellular proteins | 3.171710e-01 | 0.499 |
| R-HSA-9646399 | Aggrephagy | 3.171710e-01 | 0.499 |
| R-HSA-9604323 | Negative regulation of NOTCH4 signaling | 3.171710e-01 | 0.499 |
| R-HSA-1251985 | Nuclear signaling by ERBB4 | 3.171710e-01 | 0.499 |
| R-HSA-109582 | Hemostasis | 3.195159e-01 | 0.496 |
| R-HSA-674695 | RNA Polymerase II Pre-transcription Events | 3.222782e-01 | 0.492 |
| R-HSA-2197563 | NOTCH2 intracellular domain regulates transcription | 3.227307e-01 | 0.491 |
| R-HSA-9820865 | Z-decay: degradation of maternal mRNAs by zygotically expressed factors | 3.227307e-01 | 0.491 |
| R-HSA-3000484 | Scavenging by Class F Receptors | 3.227307e-01 | 0.491 |
| R-HSA-9634285 | Constitutive Signaling by Overexpressed ERBB2 | 3.227307e-01 | 0.491 |
| R-HSA-380615 | Serotonin clearance from the synaptic cleft | 3.227307e-01 | 0.491 |
| R-HSA-9865114 | Maple Syrup Urine Disease | 3.227307e-01 | 0.491 |
| R-HSA-1247673 | Erythrocytes take up oxygen and release carbon dioxide | 3.227307e-01 | 0.491 |
| R-HSA-209543 | p75NTR recruits signalling complexes | 3.227307e-01 | 0.491 |
| R-HSA-198323 | AKT phosphorylates targets in the cytosol | 3.227307e-01 | 0.491 |
| R-HSA-73943 | Reversal of alkylation damage by DNA dioxygenases | 3.227307e-01 | 0.491 |
| R-HSA-73894 | DNA Repair | 3.229890e-01 | 0.491 |
| R-HSA-418346 | Platelet homeostasis | 3.241250e-01 | 0.489 |
| R-HSA-168271 | Transport of Ribonucleoproteins into the Host Nucleus | 3.260421e-01 | 0.487 |
| R-HSA-9929491 | SPOP-mediated proteasomal degradation of PD-L1(CD274) | 3.260421e-01 | 0.487 |
| R-HSA-5362768 | Hh mutants are degraded by ERAD | 3.260421e-01 | 0.487 |
| R-HSA-5676590 | NIK-->noncanonical NF-kB signaling | 3.260421e-01 | 0.487 |
| R-HSA-6807070 | PTEN Regulation | 3.314873e-01 | 0.480 |
| R-HSA-9932298 | Degradation of CRY and PER proteins | 3.348827e-01 | 0.475 |
| R-HSA-5610780 | Degradation of GLI1 by the proteasome | 3.348827e-01 | 0.475 |
| R-HSA-1236975 | Antigen processing-Cross presentation | 3.350515e-01 | 0.475 |
| R-HSA-975138 | TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation | 3.350515e-01 | 0.475 |
| R-HSA-5685939 | HDR through MMEJ (alt-NHEJ) | 3.390351e-01 | 0.470 |
| R-HSA-9029558 | NR1H2 & NR1H3 regulate gene expression linked to lipogenesis | 3.390351e-01 | 0.470 |
| R-HSA-9659787 | Aberrant regulation of mitotic G1/S transition in cancer due to RB1 defects | 3.390351e-01 | 0.470 |
| R-HSA-9661069 | Defective binding of RB1 mutants to E2F1,(E2F2, E2F3) | 3.390351e-01 | 0.470 |
| R-HSA-174490 | Membrane binding and targetting of GAG proteins | 3.390351e-01 | 0.470 |
| R-HSA-9933947 | Formation of the non-canonical BAF (ncBAF) complex | 3.390351e-01 | 0.470 |
| R-HSA-5676594 | TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway | 3.390351e-01 | 0.470 |
| R-HSA-6811555 | PI5P Regulates TP53 Acetylation | 3.390351e-01 | 0.470 |
| R-HSA-9683610 | Maturation of nucleoprotein | 3.390351e-01 | 0.470 |
| R-HSA-9735804 | Diseases of nucleotide metabolism | 3.390351e-01 | 0.470 |
| R-HSA-9682706 | Replication of the SARS-CoV-1 genome | 3.390351e-01 | 0.470 |
| R-HSA-975155 | MyD88 dependent cascade initiated on endosome | 3.405212e-01 | 0.468 |
| R-HSA-9648025 | EML4 and NUDC in mitotic spindle formation | 3.405212e-01 | 0.468 |
| R-HSA-111996 | Ca-dependent events | 3.436890e-01 | 0.464 |
| R-HSA-4086400 | PCP/CE pathway | 3.486866e-01 | 0.458 |
| R-HSA-9705671 | SARS-CoV-2 activates/modulates innate and adaptive immune responses | 3.505405e-01 | 0.455 |
| R-HSA-5387390 | Hh mutants abrogate ligand secretion | 3.524576e-01 | 0.453 |
| R-HSA-9637690 | Response of Mtb to phagocytosis | 3.524576e-01 | 0.453 |
| R-HSA-177504 | Retrograde neurotrophin signalling | 3.549480e-01 | 0.450 |
| R-HSA-174495 | Synthesis And Processing Of GAG, GAGPOL Polyproteins | 3.549480e-01 | 0.450 |
| R-HSA-391160 | Signal regulatory protein family interactions | 3.549480e-01 | 0.450 |
| R-HSA-399956 | CRMPs in Sema3A signaling | 3.549480e-01 | 0.450 |
| R-HSA-9933937 | Formation of the canonical BAF (cBAF) complex | 3.549480e-01 | 0.450 |
| R-HSA-9933939 | Formation of the polybromo-BAF (pBAF) complex | 3.549480e-01 | 0.450 |
| R-HSA-9856872 | Malate-aspartate shuttle | 3.549480e-01 | 0.450 |
| R-HSA-9679514 | SARS-CoV-1 Genome Replication and Transcription | 3.549480e-01 | 0.450 |
| R-HSA-5688426 | Deubiquitination | 3.554599e-01 | 0.449 |
| R-HSA-927802 | Nonsense-Mediated Decay (NMD) | 3.569430e-01 | 0.447 |
| R-HSA-975957 | Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) | 3.569430e-01 | 0.447 |
| R-HSA-1257604 | PIP3 activates AKT signaling | 3.607760e-01 | 0.443 |
| R-HSA-69236 | G1 Phase | 3.611852e-01 | 0.442 |
| R-HSA-69231 | Cyclin D associated events in G1 | 3.611852e-01 | 0.442 |
| R-HSA-187577 | SCF(Skp2)-mediated degradation of p27/p21 | 3.611852e-01 | 0.442 |
| R-HSA-3928662 | EPHB-mediated forward signaling | 3.611852e-01 | 0.442 |
| R-HSA-2995410 | Nuclear Envelope (NE) Reassembly | 3.618574e-01 | 0.441 |
| R-HSA-168181 | Toll Like Receptor 7/8 (TLR7/8) Cascade | 3.624175e-01 | 0.441 |
| R-HSA-9824585 | Regulation of MITF-M-dependent genes involved in pigmentation | 3.698687e-01 | 0.432 |
| R-HSA-1489509 | DAG and IP3 signaling | 3.698687e-01 | 0.432 |
| R-HSA-4608870 | Asymmetric localization of PCP proteins | 3.698687e-01 | 0.432 |
| R-HSA-5678895 | Defective CFTR causes cystic fibrosis | 3.698687e-01 | 0.432 |
| R-HSA-5607761 | Dectin-1 mediated noncanonical NF-kB signaling | 3.698687e-01 | 0.432 |
| R-HSA-73780 | RNA Polymerase III Chain Elongation | 3.704787e-01 | 0.431 |
| R-HSA-399954 | Sema3A PAK dependent Axon repulsion | 3.704787e-01 | 0.431 |
| R-HSA-2173791 | TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) | 3.704787e-01 | 0.431 |
| R-HSA-446353 | Cell-extracellular matrix interactions | 3.704787e-01 | 0.431 |
| R-HSA-9735871 | SARS-CoV-1 targets host intracellular signalling and regulatory pathways | 3.704787e-01 | 0.431 |
| R-HSA-450513 | Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA | 3.704787e-01 | 0.431 |
| R-HSA-171007 | p38MAPK events | 3.704787e-01 | 0.431 |
| R-HSA-9933946 | Formation of the embryonic stem cell BAF (esBAF) complex | 3.704787e-01 | 0.431 |
| R-HSA-937072 | TRAF6-mediated induction of TAK1 complex within TLR4 complex | 3.704787e-01 | 0.431 |
| R-HSA-450385 | Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA | 3.704787e-01 | 0.431 |
| R-HSA-193639 | p75NTR signals via NF-kB | 3.704787e-01 | 0.431 |
| R-HSA-73942 | DNA Damage Reversal | 3.704787e-01 | 0.431 |
| R-HSA-168249 | Innate Immune System | 3.740381e-01 | 0.427 |
| R-HSA-72165 | mRNA Splicing - Minor Pathway | 3.785051e-01 | 0.422 |
| R-HSA-168138 | Toll Like Receptor 9 (TLR9) Cascade | 3.788272e-01 | 0.422 |
| R-HSA-5668541 | TNFR2 non-canonical NF-kB pathway | 3.815326e-01 | 0.418 |
| R-HSA-9707564 | Cytoprotection by HMOX1 | 3.815326e-01 | 0.418 |
| R-HSA-140534 | Caspase activation via Death Receptors in the presence of ligand | 3.856364e-01 | 0.414 |
| R-HSA-5099900 | WNT5A-dependent internalization of FZD4 | 3.856364e-01 | 0.414 |
| R-HSA-450604 | KSRP (KHSRP) binds and destabilizes mRNA | 3.856364e-01 | 0.414 |
| R-HSA-9733458 | Induction of Cell-Cell Fusion | 3.856364e-01 | 0.414 |
| R-HSA-70350 | Fructose catabolism | 3.856364e-01 | 0.414 |
| R-HSA-71262 | Carnitine synthesis | 3.856364e-01 | 0.414 |
| R-HSA-9664420 | Killing mechanisms | 3.856364e-01 | 0.414 |
| R-HSA-9673324 | WNT5:FZD7-mediated leishmania damping | 3.856364e-01 | 0.414 |
| R-HSA-9758274 | Regulation of NF-kappa B signaling | 3.856364e-01 | 0.414 |
| R-HSA-8868773 | rRNA processing in the nucleus and cytosol | 3.909350e-01 | 0.408 |
| R-HSA-8878171 | Transcriptional regulation by RUNX1 | 3.918244e-01 | 0.407 |
| R-HSA-9031628 | NGF-stimulated transcription | 3.956261e-01 | 0.403 |
| R-HSA-389356 | Co-stimulation by CD28 | 3.956261e-01 | 0.403 |
| R-HSA-1266738 | Developmental Biology | 3.959930e-01 | 0.402 |
| R-HSA-9675108 | Nervous system development | 3.984230e-01 | 0.400 |
| R-HSA-9912633 | Antigen processing: Ub, ATP-independent proteasomal degradation | 4.004301e-01 | 0.397 |
| R-HSA-77595 | Processing of Intronless Pre-mRNAs | 4.004301e-01 | 0.397 |
| R-HSA-975110 | TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling | 4.004301e-01 | 0.397 |
| R-HSA-918233 | TRAF3-dependent IRF activation pathway | 4.004301e-01 | 0.397 |
| R-HSA-3134975 | Regulation of innate immune responses to cytosolic DNA | 4.004301e-01 | 0.397 |
| R-HSA-9927020 | Heme assimilation | 4.004301e-01 | 0.397 |
| R-HSA-9690406 | Transcriptional regulation of testis differentiation | 4.004301e-01 | 0.397 |
| R-HSA-9909615 | Regulation of PD-L1(CD274) Post-translational modification | 4.010718e-01 | 0.397 |
| R-HSA-2122947 | NOTCH1 Intracellular Domain Regulates Transcription | 4.041056e-01 | 0.394 |
| R-HSA-166058 | MyD88:MAL(TIRAP) cascade initiated on plasma membrane | 4.060711e-01 | 0.391 |
| R-HSA-168188 | Toll Like Receptor TLR6:TLR2 Cascade | 4.060711e-01 | 0.391 |
| R-HSA-73887 | Death Receptor Signaling | 4.078477e-01 | 0.390 |
| R-HSA-68877 | Mitotic Prometaphase | 4.124112e-01 | 0.385 |
| R-HSA-5658442 | Regulation of RAS by GAPs | 4.125279e-01 | 0.385 |
| R-HSA-5637812 | Signaling by EGFRvIII in Cancer | 4.148684e-01 | 0.382 |
| R-HSA-5637810 | Constitutive Signaling by EGFRvIII | 4.148684e-01 | 0.382 |
| R-HSA-5358565 | Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) | 4.148684e-01 | 0.382 |
| R-HSA-164938 | Nef-mediates down modulation of cell surface receptors by recruiting them to cla... | 4.148684e-01 | 0.382 |
| R-HSA-9909505 | Modulation of host responses by IFN-stimulated genes | 4.148684e-01 | 0.382 |
| R-HSA-9768759 | Regulation of NPAS4 gene expression | 4.148684e-01 | 0.382 |
| R-HSA-3229121 | Glycogen storage diseases | 4.148684e-01 | 0.382 |
| R-HSA-9694686 | Replication of the SARS-CoV-2 genome | 4.148684e-01 | 0.382 |
| R-HSA-2500257 | Resolution of Sister Chromatid Cohesion | 4.169092e-01 | 0.380 |
| R-HSA-73886 | Chromosome Maintenance | 4.169092e-01 | 0.380 |
| R-HSA-9759194 | Nuclear events mediated by NFE2L2 | 4.169092e-01 | 0.380 |
| R-HSA-3371571 | HSF1-dependent transactivation | 4.208909e-01 | 0.376 |
| R-HSA-1169091 | Activation of NF-kappaB in B cells | 4.208909e-01 | 0.376 |
| R-HSA-5358346 | Hedgehog ligand biogenesis | 4.208909e-01 | 0.376 |
| R-HSA-9610379 | HCMV Late Events | 4.221091e-01 | 0.375 |
| R-HSA-168179 | Toll Like Receptor TLR1:TLR2 Cascade | 4.223118e-01 | 0.374 |
| R-HSA-181438 | Toll Like Receptor 2 (TLR2) Cascade | 4.223118e-01 | 0.374 |
| R-HSA-76002 | Platelet activation, signaling and aggregation | 4.248671e-01 | 0.372 |
| R-HSA-73980 | RNA Polymerase III Transcription Termination | 4.289599e-01 | 0.368 |
| R-HSA-5358508 | Mismatch Repair | 4.289599e-01 | 0.368 |
| R-HSA-1606322 | ZBP1(DAI) mediated induction of type I IFNs | 4.289599e-01 | 0.368 |
| R-HSA-4419969 | Depolymerization of the Nuclear Lamina | 4.289599e-01 | 0.368 |
| R-HSA-416993 | Trafficking of GluR2-containing AMPA receptors | 4.289599e-01 | 0.368 |
| R-HSA-9665348 | Signaling by ERBB2 ECD mutants | 4.289599e-01 | 0.368 |
| R-HSA-428643 | Organic anion transport by SLC5/17/25 transporters | 4.289599e-01 | 0.368 |
| R-HSA-8849932 | Synaptic adhesion-like molecules | 4.289599e-01 | 0.368 |
| R-HSA-432142 | Platelet sensitization by LDL | 4.289599e-01 | 0.368 |
| R-HSA-9679504 | Translation of Replicase and Assembly of the Replication Transcription Complex | 4.289599e-01 | 0.368 |
| R-HSA-9931269 | AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) | 4.291927e-01 | 0.367 |
| R-HSA-5339562 | Uptake and actions of bacterial toxins | 4.291927e-01 | 0.367 |
| R-HSA-5620912 | Anchoring of the basal body to the plasma membrane | 4.332275e-01 | 0.363 |
| R-HSA-73884 | Base Excision Repair | 4.332275e-01 | 0.363 |
| R-HSA-373080 | Class B/2 (Secretin family receptors) | 4.332275e-01 | 0.363 |
| R-HSA-9006936 | Signaling by TGFB family members | 4.363091e-01 | 0.360 |
| R-HSA-8948751 | Regulation of PTEN stability and activity | 4.374312e-01 | 0.359 |
| R-HSA-167242 | Abortive elongation of HIV-1 transcript in the absence of Tat | 4.427129e-01 | 0.354 |
| R-HSA-9709603 | Impaired BRCA2 binding to PALB2 | 4.427129e-01 | 0.354 |
| R-HSA-113510 | E2F mediated regulation of DNA replication | 4.427129e-01 | 0.354 |
| R-HSA-8851708 | Signaling by FGFR2 IIIa TM | 4.427129e-01 | 0.354 |
| R-HSA-9834899 | Specification of the neural plate border | 4.427129e-01 | 0.354 |
| R-HSA-937041 | IKK complex recruitment mediated by RIP1 | 4.427129e-01 | 0.354 |
| R-HSA-429958 | mRNA decay by 3' to 5' exoribonuclease | 4.427129e-01 | 0.354 |
| R-HSA-1237044 | Erythrocytes take up carbon dioxide and release oxygen | 4.427129e-01 | 0.354 |
| R-HSA-844456 | The NLRP3 inflammasome | 4.427129e-01 | 0.354 |
| R-HSA-1480926 | O2/CO2 exchange in erythrocytes | 4.427129e-01 | 0.354 |
| R-HSA-9694631 | Maturation of nucleoprotein | 4.427129e-01 | 0.354 |
| R-HSA-392517 | Rap1 signalling | 4.427129e-01 | 0.354 |
| R-HSA-1912420 | Pre-NOTCH Processing in Golgi | 4.427129e-01 | 0.354 |
| R-HSA-9694682 | SARS-CoV-2 Genome Replication and Transcription | 4.427129e-01 | 0.354 |
| R-HSA-9754678 | SARS-CoV-2 modulates host translation machinery | 4.456048e-01 | 0.351 |
| R-HSA-9658195 | Leishmania infection | 4.503926e-01 | 0.346 |
| R-HSA-9824443 | Parasitic Infection Pathways | 4.503926e-01 | 0.346 |
| R-HSA-2682334 | EPH-Ephrin signaling | 4.522176e-01 | 0.345 |
| R-HSA-174824 | Plasma lipoprotein assembly, remodeling, and clearance | 4.522176e-01 | 0.345 |
| R-HSA-9934037 | Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) | 4.561355e-01 | 0.341 |
| R-HSA-9701193 | Defective homologous recombination repair (HRR) due to PALB2 loss of function | 4.561355e-01 | 0.341 |
| R-HSA-9704646 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 4.561355e-01 | 0.341 |
| R-HSA-9701192 | Defective homologous recombination repair (HRR) due to BRCA1 loss of function | 4.561355e-01 | 0.341 |
| R-HSA-9704331 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 4.561355e-01 | 0.341 |
| R-HSA-389513 | Co-inhibition by CTLA4 | 4.561355e-01 | 0.341 |
| R-HSA-416572 | Sema4D induced cell migration and growth-cone collapse | 4.561355e-01 | 0.341 |
| R-HSA-3322077 | Glycogen synthesis | 4.561355e-01 | 0.341 |
| R-HSA-187037 | Signaling by NTRK1 (TRKA) | 4.597454e-01 | 0.337 |
| R-HSA-5578775 | Ion homeostasis | 4.617506e-01 | 0.336 |
| R-HSA-109606 | Intrinsic Pathway for Apoptosis | 4.617506e-01 | 0.336 |
| R-HSA-5637815 | Signaling by Ligand-Responsive EGFR Variants in Cancer | 4.692356e-01 | 0.329 |
| R-HSA-1236382 | Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants | 4.692356e-01 | 0.329 |
| R-HSA-2161541 | Abacavir metabolism | 4.692356e-01 | 0.329 |
| R-HSA-210991 | Basigin interactions | 4.692356e-01 | 0.329 |
| R-HSA-167044 | Signalling to RAS | 4.692356e-01 | 0.329 |
| R-HSA-9636383 | Prevention of phagosomal-lysosomal fusion | 4.692356e-01 | 0.329 |
| R-HSA-6782135 | Dual incision in TC-NER | 4.776183e-01 | 0.321 |
| R-HSA-9772572 | Early SARS-CoV-2 Infection Events | 4.776183e-01 | 0.321 |
| R-HSA-162582 | Signal Transduction | 4.804222e-01 | 0.318 |
| R-HSA-5603041 | IRAK4 deficiency (TLR2/4) | 4.820209e-01 | 0.317 |
| R-HSA-450302 | activated TAK1 mediates p38 MAPK activation | 4.820209e-01 | 0.317 |
| R-HSA-76066 | RNA Polymerase III Transcription Initiation From Type 2 Promoter | 4.820209e-01 | 0.317 |
| R-HSA-9705462 | Inactivation of CSF3 (G-CSF) signaling | 4.820209e-01 | 0.317 |
| R-HSA-175474 | Assembly Of The HIV Virion | 4.820209e-01 | 0.317 |
| R-HSA-8949215 | Mitochondrial calcium ion transport | 4.820209e-01 | 0.317 |
| R-HSA-9671555 | Signaling by PDGFR in disease | 4.820209e-01 | 0.317 |
| R-HSA-5607764 | CLEC7A (Dectin-1) signaling | 4.832632e-01 | 0.316 |
| R-HSA-429914 | Deadenylation-dependent mRNA decay | 4.854446e-01 | 0.314 |
| R-HSA-352230 | Amino acid transport across the plasma membrane | 4.854446e-01 | 0.314 |
| R-HSA-186712 | Regulation of beta-cell development | 4.854446e-01 | 0.314 |
| R-HSA-9609646 | HCMV Infection | 4.856477e-01 | 0.314 |
| R-HSA-2894858 | Signaling by NOTCH1 HD+PEST Domain Mutants in Cancer | 4.931978e-01 | 0.307 |
| R-HSA-2644602 | Signaling by NOTCH1 PEST Domain Mutants in Cancer | 4.931978e-01 | 0.307 |
| R-HSA-2644606 | Constitutive Signaling by NOTCH1 PEST Domain Mutants | 4.931978e-01 | 0.307 |
| R-HSA-2894862 | Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants | 4.931978e-01 | 0.307 |
| R-HSA-2644603 | Signaling by NOTCH1 in Cancer | 4.931978e-01 | 0.307 |
| R-HSA-5362517 | Signaling by Retinoic Acid | 4.931978e-01 | 0.307 |
| R-HSA-351202 | Metabolism of polyamines | 4.931978e-01 | 0.307 |
| R-HSA-9938206 | Developmental Lineage of Mammary Stem Cells | 4.944991e-01 | 0.306 |
| R-HSA-76071 | RNA Polymerase III Transcription Initiation From Type 3 Promoter | 4.944991e-01 | 0.306 |
| R-HSA-76061 | RNA Polymerase III Transcription Initiation From Type 1 Promoter | 4.944991e-01 | 0.306 |
| R-HSA-3238698 | WNT ligand biogenesis and trafficking | 4.944991e-01 | 0.306 |
| R-HSA-8964038 | LDL clearance | 4.944991e-01 | 0.306 |
| R-HSA-5652084 | Fructose metabolism | 4.944991e-01 | 0.306 |
| R-HSA-9013507 | NOTCH3 Activation and Transmission of Signal to the Nucleus | 4.944991e-01 | 0.306 |
| R-HSA-71384 | Ethanol oxidation | 4.944991e-01 | 0.306 |
| R-HSA-6803205 | TP53 regulates transcription of several additional cell death genes whose specif... | 4.944991e-01 | 0.306 |
| R-HSA-9694676 | Translation of Replicase and Assembly of the Replication Transcription Complex | 4.944991e-01 | 0.306 |
| R-HSA-422356 | Regulation of insulin secretion | 4.954467e-01 | 0.305 |
| R-HSA-397014 | Muscle contraction | 4.969968e-01 | 0.304 |
| R-HSA-1483257 | Phospholipid metabolism | 5.007934e-01 | 0.300 |
| R-HSA-168325 | Viral Messenger RNA Synthesis | 5.008767e-01 | 0.300 |
| R-HSA-450294 | MAP kinase activation | 5.008767e-01 | 0.300 |
| R-HSA-112043 | PLC beta mediated events | 5.008767e-01 | 0.300 |
| R-HSA-3214847 | HATs acetylate histones | 5.014846e-01 | 0.300 |
| R-HSA-9614085 | FOXO-mediated transcription | 5.014846e-01 | 0.300 |
| R-HSA-77075 | RNA Pol II CTD phosphorylation and interaction with CE | 5.066773e-01 | 0.295 |
| R-HSA-167160 | RNA Pol II CTD phosphorylation and interaction with CE during HIV infection | 5.066773e-01 | 0.295 |
| R-HSA-164952 | The role of Nef in HIV-1 replication and disease pathogenesis | 5.066773e-01 | 0.295 |
| R-HSA-9648895 | Response of EIF2AK1 (HRI) to heme deficiency | 5.066773e-01 | 0.295 |
| R-HSA-5610787 | Hedgehog 'off' state | 5.074856e-01 | 0.295 |
| R-HSA-382556 | ABC-family proteins mediated transport | 5.074856e-01 | 0.295 |
| R-HSA-1268020 | Mitochondrial protein import | 5.084806e-01 | 0.294 |
| R-HSA-422475 | Axon guidance | 5.133796e-01 | 0.290 |
| R-HSA-380284 | Loss of proteins required for interphase microtubule organization from the centr... | 5.160085e-01 | 0.287 |
| R-HSA-380259 | Loss of Nlp from mitotic centrosomes | 5.160085e-01 | 0.287 |
| R-HSA-429947 | Deadenylation of mRNA | 5.185630e-01 | 0.285 |
| R-HSA-933542 | TRAF6 mediated NF-kB activation | 5.185630e-01 | 0.285 |
| R-HSA-75067 | Processing of Capped Intronless Pre-mRNA | 5.185630e-01 | 0.285 |
| R-HSA-9665686 | Signaling by ERBB2 TMD/JMD mutants | 5.185630e-01 | 0.285 |
| R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | 5.193736e-01 | 0.285 |
| R-HSA-1280218 | Adaptive Immune System | 5.266995e-01 | 0.278 |
| R-HSA-5693554 | Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD... | 5.301629e-01 | 0.276 |
| R-HSA-420029 | Tight junction interactions | 5.301629e-01 | 0.276 |
| R-HSA-400685 | Sema4D in semaphorin signaling | 5.301629e-01 | 0.276 |
| R-HSA-9932444 | ATP-dependent chromatin remodelers | 5.301629e-01 | 0.276 |
| R-HSA-9932451 | SWI/SNF chromatin remodelers | 5.301629e-01 | 0.276 |
| R-HSA-9839394 | TGFBR3 expression | 5.301629e-01 | 0.276 |
| R-HSA-203927 | MicroRNA (miRNA) biogenesis | 5.301629e-01 | 0.276 |
| R-HSA-9830364 | Formation of the nephric duct | 5.301629e-01 | 0.276 |
| R-HSA-8856825 | Cargo recognition for clathrin-mediated endocytosis | 5.311051e-01 | 0.275 |
| R-HSA-9833110 | RSV-host interactions | 5.369105e-01 | 0.270 |
| R-HSA-8854518 | AURKA Activation by TPX2 | 5.381294e-01 | 0.269 |
| R-HSA-6782315 | tRNA modification in the nucleus and cytosol | 5.381294e-01 | 0.269 |
| R-HSA-1643713 | Signaling by EGFR in Cancer | 5.414841e-01 | 0.266 |
| R-HSA-9703465 | Signaling by FLT3 fusion proteins | 5.414841e-01 | 0.266 |
| R-HSA-525793 | Myogenesis | 5.414841e-01 | 0.266 |
| R-HSA-5357769 | Caspase activation via extrinsic apoptotic signalling pathway | 5.414841e-01 | 0.266 |
| R-HSA-9615933 | Postmitotic nuclear pore complex (NPC) reformation | 5.414841e-01 | 0.266 |
| R-HSA-1855183 | Synthesis of IP2, IP, and Ins in the cytosol | 5.414841e-01 | 0.266 |
| R-HSA-2161522 | Abacavir ADME | 5.414841e-01 | 0.266 |
| R-HSA-9865118 | Diseases of branched-chain amino acid catabolism | 5.414841e-01 | 0.266 |
| R-HSA-5685942 | HDR through Homologous Recombination (HRR) | 5.453468e-01 | 0.263 |
| R-HSA-9958863 | SLC-mediated transport of amino acids | 5.453468e-01 | 0.263 |
| R-HSA-112040 | G-protein mediated events | 5.453468e-01 | 0.263 |
| R-HSA-73863 | RNA Polymerase I Transcription Termination | 5.525332e-01 | 0.258 |
| R-HSA-445095 | Interaction between L1 and Ankyrins | 5.525332e-01 | 0.258 |
| R-HSA-8949613 | Cristae formation | 5.525332e-01 | 0.258 |
| R-HSA-3928663 | EPHA-mediated growth cone collapse | 5.525332e-01 | 0.258 |
| R-HSA-389357 | CD28 dependent PI3K/Akt signaling | 5.525332e-01 | 0.258 |
| R-HSA-9841251 | Mitochondrial unfolded protein response (UPRmt) | 5.525332e-01 | 0.258 |
| R-HSA-69275 | G2/M Transition | 5.589322e-01 | 0.253 |
| R-HSA-9925563 | Developmental Lineage of Pancreatic Ductal Cells | 5.595443e-01 | 0.252 |
| R-HSA-167158 | Formation of the HIV-1 Early Elongation Complex | 5.633166e-01 | 0.249 |
| R-HSA-113418 | Formation of the Early Elongation Complex | 5.633166e-01 | 0.249 |
| R-HSA-8940973 | RUNX2 regulates osteoblast differentiation | 5.633166e-01 | 0.249 |
| R-HSA-622312 | Inflammasomes | 5.633166e-01 | 0.249 |
| R-HSA-380994 | ATF4 activates genes in response to endoplasmic reticulum stress | 5.633166e-01 | 0.249 |
| R-HSA-448424 | Interleukin-17 signaling | 5.665237e-01 | 0.247 |
| R-HSA-453274 | Mitotic G2-G2/M phases | 5.675046e-01 | 0.246 |
| R-HSA-202403 | TCR signaling | 5.708630e-01 | 0.243 |
| R-HSA-9856649 | Transcriptional and post-translational regulation of MITF-M expression and activ... | 5.734232e-01 | 0.242 |
| R-HSA-5632684 | Hedgehog 'on' state | 5.734232e-01 | 0.242 |
| R-HSA-72086 | mRNA Capping | 5.738409e-01 | 0.241 |
| R-HSA-917729 | Endosomal Sorting Complex Required For Transport (ESCRT) | 5.738409e-01 | 0.241 |
| R-HSA-9759475 | Regulation of CDH11 Expression and Function | 5.738409e-01 | 0.241 |
| R-HSA-9664565 | Signaling by ERBB2 KD Mutants | 5.738409e-01 | 0.241 |
| R-HSA-450282 | MAPK targets/ Nuclear events mediated by MAP kinases | 5.738409e-01 | 0.241 |
| R-HSA-9006335 | Signaling by Erythropoietin | 5.738409e-01 | 0.241 |
| R-HSA-9674555 | Signaling by CSF3 (G-CSF) | 5.738409e-01 | 0.241 |
| R-HSA-166520 | Signaling by NTRKs | 5.755392e-01 | 0.240 |
| R-HSA-72312 | rRNA processing | 5.770814e-01 | 0.239 |
| R-HSA-198725 | Nuclear Events (kinase and transcription factor activation) | 5.802427e-01 | 0.236 |
| R-HSA-499943 | Interconversion of nucleotide di- and triphosphates | 5.802427e-01 | 0.236 |
| R-HSA-74259 | Purine catabolism | 5.802427e-01 | 0.236 |
| R-HSA-9006934 | Signaling by Receptor Tyrosine Kinases | 5.809088e-01 | 0.236 |
| R-HSA-1483249 | Inositol phosphate metabolism | 5.818338e-01 | 0.235 |
| R-HSA-5619107 | Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC... | 5.841121e-01 | 0.234 |
| R-HSA-2424491 | DAP12 signaling | 5.841121e-01 | 0.234 |
| R-HSA-76046 | RNA Polymerase III Transcription Initiation | 5.841121e-01 | 0.234 |
| R-HSA-1227990 | Signaling by ERBB2 in Cancer | 5.841121e-01 | 0.234 |
| R-HSA-380972 | Energy dependent regulation of mTOR by LKB1-AMPK | 5.841121e-01 | 0.234 |
| R-HSA-8863795 | Downregulation of ERBB2 signaling | 5.841121e-01 | 0.234 |
| R-HSA-1474151 | Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation | 5.841121e-01 | 0.234 |
| R-HSA-112311 | Neurotransmitter clearance | 5.841121e-01 | 0.234 |
| R-HSA-9856651 | MITF-M-dependent gene expression | 5.849410e-01 | 0.233 |
| R-HSA-380270 | Recruitment of mitotic centrosome proteins and complexes | 5.869818e-01 | 0.231 |
| R-HSA-1445148 | Translocation of SLC2A4 (GLUT4) to the plasma membrane | 5.869818e-01 | 0.231 |
| R-HSA-1236394 | Signaling by ERBB4 | 5.936406e-01 | 0.226 |
| R-HSA-1855196 | IP3 and IP4 transport between cytosol and nucleus | 5.941364e-01 | 0.226 |
| R-HSA-1855229 | IP6 and IP7 transport between cytosol and nucleus | 5.941364e-01 | 0.226 |
| R-HSA-162588 | Budding and maturation of HIV virion | 5.941364e-01 | 0.226 |
| R-HSA-399719 | Trafficking of AMPA receptors | 5.941364e-01 | 0.226 |
| R-HSA-9833109 | Evasion by RSV of host interferon responses | 5.941364e-01 | 0.226 |
| R-HSA-8963693 | Aspartate and asparagine metabolism | 5.941364e-01 | 0.226 |
| R-HSA-936440 | Negative regulators of DDX58/IFIH1 signaling | 5.941364e-01 | 0.226 |
| R-HSA-9609507 | Protein localization | 5.988157e-01 | 0.223 |
| R-HSA-6781827 | Transcription-Coupled Nucleotide Excision Repair (TC-NER) | 6.002190e-01 | 0.222 |
| R-HSA-380287 | Centrosome maturation | 6.002190e-01 | 0.222 |
| R-HSA-9609690 | HCMV Early Events | 6.009151e-01 | 0.221 |
| R-HSA-983168 | Antigen processing: Ubiquitination & Proteasome degradation | 6.030731e-01 | 0.220 |
| R-HSA-1980143 | Signaling by NOTCH1 | 6.067170e-01 | 0.217 |
| R-HSA-5689603 | UCH proteinases | 6.067170e-01 | 0.217 |
| R-HSA-1855170 | IPs transport between nucleus and cytosol | 6.134677e-01 | 0.212 |
| R-HSA-5693568 | Resolution of D-loop Structures through Holliday Junction Intermediates | 6.134677e-01 | 0.212 |
| R-HSA-9930044 | Nuclear RNA decay | 6.134677e-01 | 0.212 |
| R-HSA-9764260 | Regulation of Expression and Function of Type II Classical Cadherins | 6.134677e-01 | 0.212 |
| R-HSA-6804758 | Regulation of TP53 Activity through Acetylation | 6.134677e-01 | 0.212 |
| R-HSA-8939243 | RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not kno... | 6.134677e-01 | 0.212 |
| R-HSA-399721 | Glutamate binding, activation of AMPA receptors and synaptic plasticity | 6.134677e-01 | 0.212 |
| R-HSA-1855204 | Synthesis of IP3 and IP4 in the cytosol | 6.134677e-01 | 0.212 |
| R-HSA-9733709 | Cardiogenesis | 6.134677e-01 | 0.212 |
| R-HSA-9022692 | Regulation of MECP2 expression and activity | 6.134677e-01 | 0.212 |
| R-HSA-354192 | Integrin signaling | 6.134677e-01 | 0.212 |
| R-HSA-5619084 | ABC transporter disorders | 6.194721e-01 | 0.208 |
| R-HSA-983705 | Signaling by the B Cell Receptor (BCR) | 6.213135e-01 | 0.207 |
| R-HSA-5693537 | Resolution of D-Loop Structures | 6.227861e-01 | 0.206 |
| R-HSA-9768727 | Regulation of CDH1 posttranslational processing and trafficking to plasma membra... | 6.227861e-01 | 0.206 |
| R-HSA-170822 | Regulation of Glucokinase by Glucokinase Regulatory Protein | 6.227861e-01 | 0.206 |
| R-HSA-114508 | Effects of PIP2 hydrolysis | 6.227861e-01 | 0.206 |
| R-HSA-189483 | Heme degradation | 6.227861e-01 | 0.206 |
| R-HSA-2454202 | Fc epsilon receptor (FCERI) signaling | 6.289216e-01 | 0.201 |
| R-HSA-5696400 | Dual Incision in GG-NER | 6.318805e-01 | 0.199 |
| R-HSA-203615 | eNOS activation | 6.318805e-01 | 0.199 |
| R-HSA-1980145 | Signaling by NOTCH2 | 6.318805e-01 | 0.199 |
| R-HSA-180746 | Nuclear import of Rev protein | 6.318805e-01 | 0.199 |
| R-HSA-9680350 | Signaling by CSF1 (M-CSF) in myeloid cells | 6.318805e-01 | 0.199 |
| R-HSA-5673000 | RAF activation | 6.318805e-01 | 0.199 |
| R-HSA-5686938 | Regulation of TLR by endogenous ligand | 6.318805e-01 | 0.199 |
| R-HSA-2393930 | Phosphate bond hydrolysis by NUDT proteins | 6.318805e-01 | 0.199 |
| R-HSA-5654738 | Signaling by FGFR2 | 6.319068e-01 | 0.199 |
| R-HSA-3301854 | Nuclear Pore Complex (NPC) Disassembly | 6.407561e-01 | 0.193 |
| R-HSA-9860927 | Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZ... | 6.407561e-01 | 0.193 |
| R-HSA-187687 | Signalling to ERKs | 6.407561e-01 | 0.193 |
| R-HSA-112316 | Neuronal System | 6.457470e-01 | 0.190 |
| R-HSA-6811558 | PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling | 6.486898e-01 | 0.188 |
| R-HSA-2132295 | MHC class II antigen presentation | 6.486898e-01 | 0.188 |
| R-HSA-749476 | RNA Polymerase III Abortive And Retractive Initiation | 6.494183e-01 | 0.187 |
| R-HSA-74158 | RNA Polymerase III Transcription | 6.494183e-01 | 0.187 |
| R-HSA-9682385 | FLT3 signaling in disease | 6.494183e-01 | 0.187 |
| R-HSA-8941326 | RUNX2 regulates bone development | 6.494183e-01 | 0.187 |
| R-HSA-114604 | GPVI-mediated activation cascade | 6.494183e-01 | 0.187 |
| R-HSA-1839126 | FGFR2 mutant receptor activation | 6.494183e-01 | 0.187 |
| R-HSA-983169 | Class I MHC mediated antigen processing & presentation | 6.509773e-01 | 0.186 |
| R-HSA-6809371 | Formation of the cornified envelope | 6.535053e-01 | 0.185 |
| R-HSA-2565942 | Regulation of PLK1 Activity at G2/M Transition | 6.558218e-01 | 0.183 |
| R-HSA-1296072 | Voltage gated Potassium channels | 6.578722e-01 | 0.182 |
| R-HSA-202131 | Metabolism of nitric oxide: NOS3 activation and regulation | 6.661226e-01 | 0.176 |
| R-HSA-112314 | Neurotransmitter receptors and postsynaptic signal transmission | 6.668077e-01 | 0.176 |
| R-HSA-9730414 | MITF-M-regulated melanocyte development | 6.704543e-01 | 0.174 |
| R-HSA-114608 | Platelet degranulation | 6.722940e-01 | 0.172 |
| R-HSA-381771 | Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) | 6.741747e-01 | 0.171 |
| R-HSA-9648002 | RAS processing | 6.741747e-01 | 0.171 |
| R-HSA-9820965 | Respiratory syncytial virus (RSV) genome replication, transcription and translat... | 6.741747e-01 | 0.171 |
| R-HSA-8956319 | Nucleotide catabolism | 6.814042e-01 | 0.167 |
| R-HSA-73779 | RNA Polymerase II Transcription Pre-Initiation And Promoter Opening | 6.820330e-01 | 0.166 |
| R-HSA-5696395 | Formation of Incision Complex in GG-NER | 6.820330e-01 | 0.166 |
| R-HSA-3371568 | Attenuation phase | 6.820330e-01 | 0.166 |
| R-HSA-5602358 | Diseases associated with the TLR signaling cascade | 6.820330e-01 | 0.166 |
| R-HSA-5260271 | Diseases of Immune System | 6.820330e-01 | 0.166 |
| R-HSA-8982491 | Glycogen metabolism | 6.820330e-01 | 0.166 |
| R-HSA-202433 | Generation of second messenger molecules | 6.820330e-01 | 0.166 |
| R-HSA-380320 | Recruitment of NuMA to mitotic centrosomes | 6.839529e-01 | 0.165 |
| R-HSA-199418 | Negative regulation of the PI3K/AKT network | 6.858884e-01 | 0.164 |
| R-HSA-9664433 | Leishmania parasite growth and survival | 6.877862e-01 | 0.163 |
| R-HSA-9662851 | Anti-inflammatory response favouring Leishmania parasite infection | 6.877862e-01 | 0.163 |
| R-HSA-73817 | Purine ribonucleoside monophosphate biosynthesis | 6.897022e-01 | 0.161 |
| R-HSA-73933 | Resolution of Abasic Sites (AP sites) | 6.897022e-01 | 0.161 |
| R-HSA-2029480 | Fcgamma receptor (FCGR) dependent phagocytosis | 6.916542e-01 | 0.160 |
| R-HSA-202424 | Downstream TCR signaling | 6.946675e-01 | 0.158 |
| R-HSA-167162 | RNA Polymerase II HIV Promoter Escape | 6.971870e-01 | 0.157 |
| R-HSA-167161 | HIV Transcription Initiation | 6.971870e-01 | 0.157 |
| R-HSA-75953 | RNA Polymerase II Transcription Initiation | 6.971870e-01 | 0.157 |
| R-HSA-6811438 | Intra-Golgi traffic | 6.971870e-01 | 0.157 |
| R-HSA-442660 | SLC-mediated transport of neurotransmitters | 6.971870e-01 | 0.157 |
| R-HSA-5675221 | Negative regulation of MAPK pathway | 6.971870e-01 | 0.157 |
| R-HSA-9683701 | Translation of Structural Proteins | 6.971870e-01 | 0.157 |
| R-HSA-76005 | Response to elevated platelet cytosolic Ca2+ | 7.033540e-01 | 0.153 |
| R-HSA-73762 | RNA Polymerase I Transcription Initiation | 7.044916e-01 | 0.152 |
| R-HSA-400508 | Incretin synthesis, secretion, and inactivation | 7.044916e-01 | 0.152 |
| R-HSA-611105 | Respiratory electron transport | 7.067853e-01 | 0.151 |
| R-HSA-9772573 | Late SARS-CoV-2 Infection Events | 7.101757e-01 | 0.149 |
| R-HSA-73776 | RNA Polymerase II Promoter Escape | 7.116205e-01 | 0.148 |
| R-HSA-73621 | Pyrimidine catabolism | 7.116205e-01 | 0.148 |
| R-HSA-2172127 | DAP12 interactions | 7.185778e-01 | 0.144 |
| R-HSA-190828 | Gap junction trafficking | 7.185778e-01 | 0.144 |
| R-HSA-373752 | Netrin-1 signaling | 7.185778e-01 | 0.144 |
| R-HSA-8864260 | Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors | 7.185778e-01 | 0.144 |
| R-HSA-163685 | Integration of energy metabolism | 7.200706e-01 | 0.143 |
| R-HSA-76042 | RNA Polymerase II Transcription Initiation And Promoter Clearance | 7.253677e-01 | 0.139 |
| R-HSA-774815 | Nucleosome assembly | 7.253677e-01 | 0.139 |
| R-HSA-606279 | Deposition of new CENPA-containing nucleosomes at the centromere | 7.253677e-01 | 0.139 |
| R-HSA-168333 | NEP/NS2 Interacts with the Cellular Export Machinery | 7.253677e-01 | 0.139 |
| R-HSA-6783310 | Fanconi Anemia Pathway | 7.253677e-01 | 0.139 |
| R-HSA-3560782 | Diseases associated with glycosaminoglycan metabolism | 7.253677e-01 | 0.139 |
| R-HSA-76009 | Platelet Aggregation (Plug Formation) | 7.253677e-01 | 0.139 |
| R-HSA-5358351 | Signaling by Hedgehog | 7.281508e-01 | 0.138 |
| R-HSA-6781823 | Formation of TC-NER Pre-Incision Complex | 7.319942e-01 | 0.135 |
| R-HSA-168274 | Export of Viral Ribonucleoproteins from Nucleus | 7.319942e-01 | 0.135 |
| R-HSA-9660826 | Purinergic signaling in leishmaniasis infection | 7.319942e-01 | 0.135 |
| R-HSA-9664424 | Cell recruitment (pro-inflammatory response) | 7.319942e-01 | 0.135 |
| R-HSA-9861718 | Regulation of pyruvate metabolism | 7.319942e-01 | 0.135 |
| R-HSA-2514859 | Inactivation, recovery and regulation of the phototransduction cascade | 7.319942e-01 | 0.135 |
| R-HSA-9839373 | Signaling by TGFBR3 | 7.319942e-01 | 0.135 |
| R-HSA-6807878 | COPI-mediated anterograde transport | 7.345570e-01 | 0.134 |
| R-HSA-437239 | Recycling pathway of L1 | 7.384612e-01 | 0.132 |
| R-HSA-1483191 | Synthesis of PC | 7.384612e-01 | 0.132 |
| R-HSA-3928665 | EPH-ephrin mediated repulsion of cells | 7.384612e-01 | 0.132 |
| R-HSA-445989 | TAK1-dependent IKK and NF-kappa-B activation | 7.384612e-01 | 0.132 |
| R-HSA-2029482 | Regulation of actin dynamics for phagocytic cup formation | 7.399275e-01 | 0.131 |
| R-HSA-190236 | Signaling by FGFR | 7.438108e-01 | 0.129 |
| R-HSA-9725371 | Nuclear events stimulated by ALK signaling in cancer | 7.447725e-01 | 0.128 |
| R-HSA-193704 | p75 NTR receptor-mediated signalling | 7.483334e-01 | 0.126 |
| R-HSA-157858 | Gap junction trafficking and regulation | 7.509320e-01 | 0.124 |
| R-HSA-389661 | Glyoxylate metabolism and glycine degradation | 7.509320e-01 | 0.124 |
| R-HSA-199991 | Membrane Trafficking | 7.534844e-01 | 0.123 |
| R-HSA-2871837 | FCERI mediated NF-kB activation | 7.549971e-01 | 0.122 |
| R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | 7.554753e-01 | 0.122 |
| R-HSA-5655253 | Signaling by FGFR2 in disease | 7.569431e-01 | 0.121 |
| R-HSA-9864848 | Complex IV assembly | 7.628095e-01 | 0.118 |
| R-HSA-156584 | Cytosolic sulfonation of small molecules | 7.628095e-01 | 0.118 |
| R-HSA-70895 | Branched-chain amino acid catabolism | 7.628095e-01 | 0.118 |
| R-HSA-2514856 | The phototransduction cascade | 7.628095e-01 | 0.118 |
| R-HSA-8866654 | E3 ubiquitin ligases ubiquitinate target proteins | 7.685347e-01 | 0.114 |
| R-HSA-9634815 | Transcriptional Regulation by NPAS4 | 7.685347e-01 | 0.114 |
| R-HSA-9639288 | Amino acids regulate mTORC1 | 7.741220e-01 | 0.111 |
| R-HSA-8956320 | Nucleotide biosynthesis | 7.741220e-01 | 0.111 |
| R-HSA-445355 | Smooth Muscle Contraction | 7.741220e-01 | 0.111 |
| R-HSA-5696398 | Nucleotide Excision Repair | 7.781078e-01 | 0.109 |
| R-HSA-6811442 | Intra-Golgi and retrograde Golgi-to-ER traffic | 7.803742e-01 | 0.108 |
| R-HSA-9820448 | Developmental Cell Lineages of the Exocrine Pancreas | 7.830249e-01 | 0.106 |
| R-HSA-6811436 | COPI-independent Golgi-to-ER retrograde traffic | 7.848963e-01 | 0.105 |
| R-HSA-1793185 | Chondroitin sulfate/dermatan sulfate metabolism | 7.848963e-01 | 0.105 |
| R-HSA-9725370 | Signaling by ALK fusions and activated point mutants | 7.860302e-01 | 0.105 |
| R-HSA-9700206 | Signaling by ALK in cancer | 7.860302e-01 | 0.105 |
| R-HSA-6782210 | Gap-filling DNA repair synthesis and ligation in TC-NER | 7.900897e-01 | 0.102 |
| R-HSA-9662361 | Sensory processing of sound by outer hair cells of the cochlea | 7.900897e-01 | 0.102 |
| R-HSA-177929 | Signaling by EGFR | 7.900897e-01 | 0.102 |
| R-HSA-5683057 | MAPK family signaling cascades | 7.902843e-01 | 0.102 |
| R-HSA-5621480 | Dectin-2 family | 7.951579e-01 | 0.100 |
| R-HSA-9029569 | NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflu... | 8.001041e-01 | 0.097 |
| R-HSA-2871796 | FCERI mediated MAPK activation | 8.047574e-01 | 0.094 |
| R-HSA-983189 | Kinesins | 8.096420e-01 | 0.092 |
| R-HSA-1227986 | Signaling by ERBB2 | 8.096420e-01 | 0.092 |
| R-HSA-1660661 | Sphingolipid de novo biosynthesis | 8.096420e-01 | 0.092 |
| R-HSA-5628897 | TP53 Regulates Metabolic Genes | 8.186772e-01 | 0.087 |
| R-HSA-375165 | NCAM signaling for neurite out-growth | 8.187259e-01 | 0.087 |
| R-HSA-6784531 | tRNA processing in the nucleus | 8.187259e-01 | 0.087 |
| R-HSA-9707616 | Heme signaling | 8.187259e-01 | 0.087 |
| R-HSA-6799198 | Complex I biogenesis | 8.231043e-01 | 0.085 |
| R-HSA-8848021 | Signaling by PTK6 | 8.231043e-01 | 0.085 |
| R-HSA-9006927 | Signaling by Non-Receptor Tyrosine Kinases | 8.231043e-01 | 0.085 |
| R-HSA-373760 | L1CAM interactions | 8.252989e-01 | 0.083 |
| R-HSA-168643 | Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali... | 8.273773e-01 | 0.082 |
| R-HSA-936837 | Ion transport by P-type ATPases | 8.273773e-01 | 0.082 |
| R-HSA-9748784 | Drug ADME | 8.314653e-01 | 0.080 |
| R-HSA-2219528 | PI3K/AKT Signaling in Cancer | 8.317028e-01 | 0.080 |
| R-HSA-72306 | tRNA processing | 8.390833e-01 | 0.076 |
| R-HSA-9830369 | Kidney development | 8.395883e-01 | 0.076 |
| R-HSA-9635486 | Infection with Mycobacterium tuberculosis | 8.409127e-01 | 0.075 |
| R-HSA-112315 | Transmission across Chemical Synapses | 8.416194e-01 | 0.075 |
| R-HSA-418555 | G alpha (s) signalling events | 8.416544e-01 | 0.075 |
| R-HSA-5621481 | C-type lectin receptors (CLRs) | 8.416544e-01 | 0.075 |
| R-HSA-9662360 | Sensory processing of sound by inner hair cells of the cochlea | 8.434641e-01 | 0.074 |
| R-HSA-9638482 | Metal ion assimilation from the host | 8.545398e-01 | 0.068 |
| R-HSA-8978934 | Metabolism of cofactors | 8.545398e-01 | 0.068 |
| R-HSA-189445 | Metabolism of porphyrins | 8.545398e-01 | 0.068 |
| R-HSA-5653656 | Vesicle-mediated transport | 8.593125e-01 | 0.066 |
| R-HSA-392499 | Metabolism of proteins | 8.606739e-01 | 0.065 |
| R-HSA-5663084 | Diseases of carbohydrate metabolism | 8.614858e-01 | 0.065 |
| R-HSA-1226099 | Signaling by FGFR in disease | 8.648337e-01 | 0.063 |
| R-HSA-8852135 | Protein ubiquitination | 8.681009e-01 | 0.061 |
| R-HSA-917937 | Iron uptake and transport | 8.681009e-01 | 0.061 |
| R-HSA-5633008 | TP53 Regulates Transcription of Cell Death Genes | 8.681009e-01 | 0.061 |
| R-HSA-5673001 | RAF/MAP kinase cascade | 8.719912e-01 | 0.059 |
| R-HSA-5576891 | Cardiac conduction | 8.733539e-01 | 0.059 |
| R-HSA-9824439 | Bacterial Infection Pathways | 8.734196e-01 | 0.059 |
| R-HSA-9024446 | NR1H2 and NR1H3-mediated signaling | 8.744009e-01 | 0.058 |
| R-HSA-9694635 | Translation of Structural Proteins | 8.744009e-01 | 0.058 |
| R-HSA-8856688 | Golgi-to-ER retrograde transport | 8.757630e-01 | 0.058 |
| R-HSA-9909396 | Circadian clock | 8.757630e-01 | 0.058 |
| R-HSA-9955298 | SLC-mediated transport of organic anions | 8.774374e-01 | 0.057 |
| R-HSA-9925561 | Developmental Lineage of Pancreatic Acinar Cells | 8.804007e-01 | 0.055 |
| R-HSA-9659379 | Sensory processing of sound | 8.804007e-01 | 0.055 |
| R-HSA-9833482 | PKR-mediated signaling | 8.832925e-01 | 0.054 |
| R-HSA-6806834 | Signaling by MET | 8.832925e-01 | 0.054 |
| R-HSA-5684996 | MAPK1/MAPK3 signaling | 8.837787e-01 | 0.054 |
| R-HSA-5617833 | Cilium Assembly | 8.841516e-01 | 0.053 |
| R-HSA-1630316 | Glycosaminoglycan metabolism | 8.898461e-01 | 0.051 |
| R-HSA-5619115 | Disorders of transmembrane transporters | 8.901308e-01 | 0.051 |
| R-HSA-381119 | Unfolded Protein Response (UPR) | 8.935679e-01 | 0.049 |
| R-HSA-5696399 | Global Genome Nucleotide Excision Repair (GG-NER) | 8.941788e-01 | 0.049 |
| R-HSA-9664422 | FCGR3A-mediated phagocytosis | 8.956191e-01 | 0.048 |
| R-HSA-9664417 | Leishmania phagocytosis | 8.956191e-01 | 0.048 |
| R-HSA-9664407 | Parasite infection | 8.956191e-01 | 0.048 |
| R-HSA-6807505 | RNA polymerase II transcribes snRNA genes | 9.016734e-01 | 0.045 |
| R-HSA-163841 | Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation | 9.016734e-01 | 0.045 |
| R-HSA-1614635 | Sulfur amino acid metabolism | 9.016734e-01 | 0.045 |
| R-HSA-70268 | Pyruvate metabolism | 9.040521e-01 | 0.044 |
| R-HSA-438064 | Post NMDA receptor activation events | 9.040521e-01 | 0.044 |
| R-HSA-71291 | Metabolism of amino acids and derivatives | 9.105867e-01 | 0.041 |
| R-HSA-199977 | ER to Golgi Anterograde Transport | 9.107530e-01 | 0.041 |
| R-HSA-6805567 | Keratinization | 9.132413e-01 | 0.039 |
| R-HSA-416476 | G alpha (q) signalling events | 9.155062e-01 | 0.038 |
| R-HSA-2173782 | Binding and Uptake of Ligands by Scavenger Receptors | 9.158796e-01 | 0.038 |
| R-HSA-983695 | Antigen activates B Cell Receptor (BCR) leading to generation of second messenge... | 9.191704e-01 | 0.037 |
| R-HSA-9837999 | Mitochondrial protein degradation | 9.211267e-01 | 0.036 |
| R-HSA-1989781 | PPARA activates gene expression | 9.238150e-01 | 0.034 |
| R-HSA-2168880 | Scavenging of heme from plasma | 9.248988e-01 | 0.034 |
| R-HSA-381340 | Transcriptional regulation of white adipocyte differentiation | 9.267168e-01 | 0.033 |
| R-HSA-6811434 | COPI-dependent Golgi-to-ER retrograde traffic | 9.267168e-01 | 0.033 |
| R-HSA-400206 | Regulation of lipid metabolism by PPARalpha | 9.267875e-01 | 0.033 |
| R-HSA-382551 | Transport of small molecules | 9.306708e-01 | 0.031 |
| R-HSA-8951664 | Neddylation | 9.332252e-01 | 0.030 |
| R-HSA-70171 | Glycolysis | 9.335603e-01 | 0.030 |
| R-HSA-442755 | Activation of NMDA receptors and postsynaptic events | 9.367392e-01 | 0.028 |
| R-HSA-1428517 | Aerobic respiration and respiratory electron transport | 9.394823e-01 | 0.027 |
| R-HSA-5619102 | SLC transporter disorders | 9.400789e-01 | 0.027 |
| R-HSA-2672351 | Stimuli-sensing channels | 9.467168e-01 | 0.024 |
| R-HSA-2871809 | FCERI mediated Ca+2 mobilization | 9.572733e-01 | 0.019 |
| R-HSA-2029485 | Role of phospholipids in phagocytosis | 9.572733e-01 | 0.019 |
| R-HSA-70326 | Glucose metabolism | 9.593198e-01 | 0.018 |
| R-HSA-1592230 | Mitochondrial biogenesis | 9.593198e-01 | 0.018 |
| R-HSA-2980736 | Peptide hormone metabolism | 9.593198e-01 | 0.018 |
| R-HSA-983712 | Ion channel transport | 9.624939e-01 | 0.017 |
| R-HSA-1852241 | Organelle biogenesis and maintenance | 9.662245e-01 | 0.015 |
| R-HSA-9664323 | FCGR3A-mediated IL10 synthesis | 9.681755e-01 | 0.014 |
| R-HSA-948021 | Transport to the Golgi and subsequent modification | 9.713417e-01 | 0.013 |
| R-HSA-9843745 | Adipogenesis | 9.725365e-01 | 0.012 |
| R-HSA-1474228 | Degradation of the extracellular matrix | 9.732030e-01 | 0.012 |
| R-HSA-71387 | Metabolism of carbohydrates and carbohydrate derivatives | 9.752835e-01 | 0.011 |
| R-HSA-418594 | G alpha (i) signalling events | 9.789875e-01 | 0.009 |
| R-HSA-2187338 | Visual phototransduction | 9.823561e-01 | 0.008 |
| R-HSA-877300 | Interferon gamma signaling | 9.868669e-01 | 0.006 |
| R-HSA-597592 | Post-translational protein modification | 9.897010e-01 | 0.004 |
| R-HSA-425407 | SLC-mediated transmembrane transport | 9.915268e-01 | 0.004 |
| R-HSA-3781865 | Diseases of glycosylation | 9.930783e-01 | 0.003 |
| R-HSA-5668914 | Diseases of metabolism | 9.951500e-01 | 0.002 |
| R-HSA-428157 | Sphingolipid metabolism | 9.954492e-01 | 0.002 |
| R-HSA-9640148 | Infection with Enterobacteria | 9.956684e-01 | 0.002 |
| R-HSA-1483206 | Glycerophospholipid biosynthesis | 9.956684e-01 | 0.002 |
| R-HSA-198933 | Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell | 9.977769e-01 | 0.001 |
| R-HSA-202733 | Cell surface interactions at the vascular wall | 9.981759e-01 | 0.001 |
| R-HSA-156580 | Phase II - Conjugation of compounds | 9.982640e-01 | 0.001 |
| R-HSA-211945 | Phase I - Functionalization of compounds | 9.993393e-01 | 0.000 |
| R-HSA-388396 | GPCR downstream signalling | 9.996824e-01 | 0.000 |
| R-HSA-446203 | Asparagine N-linked glycosylation | 9.997846e-01 | 0.000 |
| R-HSA-1474244 | Extracellular matrix organization | 9.998229e-01 | 0.000 |
| R-HSA-196854 | Metabolism of vitamins and cofactors | 9.999222e-01 | 0.000 |
| R-HSA-372790 | Signaling by GPCR | 9.999318e-01 | 0.000 |
| R-HSA-500792 | GPCR ligand binding | 9.999640e-01 | 0.000 |
| R-HSA-211859 | Biological oxidations | 9.999793e-01 | 0.000 |
| R-HSA-556833 | Metabolism of lipids | 9.999999e-01 | 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 |
|---|---|---|---|---|
GAK |
0.844 | 0.039 | 1 | 0.798 |
JNK2 |
0.834 | 0.322 | 1 | 0.800 |
JNK3 |
0.831 | 0.302 | 1 | 0.829 |
VRK2 |
0.830 | -0.142 | 1 | 0.825 |
TAK1 |
0.829 | -0.089 | 1 | 0.736 |
P38B |
0.828 | 0.303 | 1 | 0.828 |
CAMKK2 |
0.825 | 0.029 | -2 | 0.772 |
ALK4 |
0.824 | 0.057 | -2 | 0.807 |
MOS |
0.824 | 0.132 | 1 | 0.830 |
PKR |
0.824 | -0.096 | 1 | 0.767 |
P38A |
0.823 | 0.274 | 1 | 0.861 |
MEK1 |
0.823 | -0.107 | 2 | 0.832 |
LRRK2 |
0.823 | -0.132 | 2 | 0.818 |
ALK2 |
0.822 | 0.095 | -2 | 0.820 |
TGFBR1 |
0.822 | 0.123 | -2 | 0.796 |
BIKE |
0.821 | 0.026 | 1 | 0.689 |
CAMKK1 |
0.821 | -0.009 | -2 | 0.777 |
BMPR1B |
0.821 | 0.151 | 1 | 0.773 |
LKB1 |
0.820 | -0.054 | -3 | 0.803 |
P38D |
0.820 | 0.324 | 1 | 0.760 |
GCK |
0.820 | -0.097 | 1 | 0.730 |
NLK |
0.819 | 0.228 | 1 | 0.891 |
VRK1 |
0.819 | -0.209 | 2 | 0.802 |
BMPR2 |
0.819 | -0.153 | -2 | 0.830 |
PASK |
0.819 | 0.043 | -3 | 0.798 |
DAPK2 |
0.818 | -0.035 | -3 | 0.810 |
BRAF |
0.818 | -0.126 | -4 | 0.720 |
NEK5 |
0.818 | -0.090 | 1 | 0.748 |
NEK1 |
0.817 | -0.125 | 1 | 0.713 |
NIK |
0.816 | -0.110 | -3 | 0.813 |
ALPHAK3 |
0.815 | -0.068 | -1 | 0.758 |
PRPK |
0.815 | -0.050 | -1 | 0.821 |
MINK |
0.815 | -0.138 | 1 | 0.704 |
MST2 |
0.815 | -0.142 | 1 | 0.729 |
PRP4 |
0.815 | 0.130 | -3 | 0.716 |
ASK1 |
0.814 | -0.188 | 1 | 0.673 |
LATS1 |
0.814 | 0.020 | -3 | 0.783 |
MPSK1 |
0.814 | 0.020 | 1 | 0.738 |
PDK1 |
0.814 | -0.133 | 1 | 0.728 |
CAMLCK |
0.814 | -0.037 | -2 | 0.784 |
EEF2K |
0.814 | -0.094 | 3 | 0.786 |
TNIK |
0.814 | -0.118 | 3 | 0.829 |
MEKK2 |
0.813 | -0.166 | 2 | 0.769 |
P38G |
0.813 | 0.284 | 1 | 0.757 |
ERK5 |
0.813 | 0.217 | 1 | 0.886 |
MEK5 |
0.813 | -0.259 | 2 | 0.800 |
ICK |
0.812 | 0.106 | -3 | 0.797 |
TTK |
0.812 | -0.122 | -2 | 0.769 |
AAK1 |
0.812 | 0.060 | 1 | 0.604 |
PBK |
0.811 | -0.022 | 1 | 0.723 |
ATR |
0.811 | 0.001 | 1 | 0.780 |
HPK1 |
0.811 | -0.091 | 1 | 0.713 |
MAP3K15 |
0.811 | -0.161 | 1 | 0.684 |
ACVR2B |
0.810 | 0.054 | -2 | 0.771 |
NEK11 |
0.810 | -0.122 | 1 | 0.715 |
DLK |
0.810 | -0.164 | 1 | 0.765 |
JNK1 |
0.810 | 0.254 | 1 | 0.801 |
CAMK1B |
0.810 | -0.023 | -3 | 0.802 |
KHS1 |
0.809 | -0.115 | 1 | 0.700 |
CDKL1 |
0.808 | 0.036 | -3 | 0.755 |
DYRK2 |
0.808 | 0.274 | 1 | 0.855 |
HGK |
0.808 | -0.143 | 3 | 0.826 |
MST1 |
0.807 | -0.210 | 1 | 0.708 |
TAO2 |
0.807 | -0.204 | 2 | 0.811 |
HIPK1 |
0.807 | 0.227 | 1 | 0.859 |
ANKRD3 |
0.807 | -0.181 | 1 | 0.773 |
BMPR1A |
0.807 | 0.098 | 1 | 0.745 |
ERK1 |
0.806 | 0.272 | 1 | 0.813 |
TAO3 |
0.806 | -0.157 | 1 | 0.729 |
MEKK6 |
0.806 | -0.159 | 1 | 0.726 |
NEK4 |
0.806 | -0.137 | 1 | 0.699 |
KHS2 |
0.806 | -0.093 | 1 | 0.717 |
MEKK3 |
0.806 | -0.135 | 1 | 0.728 |
MEK2 |
0.806 | -0.209 | 2 | 0.788 |
MST3 |
0.805 | -0.115 | 2 | 0.802 |
ACVR2A |
0.805 | 0.022 | -2 | 0.752 |
MEKK1 |
0.805 | -0.201 | 1 | 0.722 |
OSR1 |
0.804 | -0.176 | 2 | 0.773 |
YSK4 |
0.804 | -0.133 | 1 | 0.691 |
ERK2 |
0.803 | 0.219 | 1 | 0.840 |
NEK8 |
0.803 | -0.215 | 2 | 0.779 |
SKMLCK |
0.803 | 0.003 | -2 | 0.795 |
MAK |
0.803 | 0.186 | -2 | 0.669 |
MYO3B |
0.802 | -0.141 | 2 | 0.781 |
GRK7 |
0.802 | 0.049 | 1 | 0.750 |
CLK3 |
0.801 | 0.206 | 1 | 0.899 |
CDK1 |
0.801 | 0.254 | 1 | 0.823 |
DAPK3 |
0.800 | -0.051 | -3 | 0.736 |
MLK2 |
0.800 | -0.121 | 2 | 0.789 |
GRK6 |
0.799 | 0.003 | 1 | 0.787 |
STLK3 |
0.799 | -0.246 | 1 | 0.660 |
SMMLCK |
0.798 | -0.076 | -3 | 0.759 |
CAMK2G |
0.798 | -0.020 | 2 | 0.828 |
RAF1 |
0.798 | -0.120 | 1 | 0.759 |
MYO3A |
0.798 | -0.192 | 1 | 0.696 |
HIPK3 |
0.797 | 0.218 | 1 | 0.838 |
TLK2 |
0.797 | -0.080 | 1 | 0.720 |
YSK1 |
0.796 | -0.191 | 2 | 0.762 |
CHAK2 |
0.796 | -0.004 | -1 | 0.807 |
PLK1 |
0.796 | -0.071 | -2 | 0.745 |
PDHK4 |
0.795 | -0.118 | 1 | 0.797 |
DMPK1 |
0.795 | -0.044 | -3 | 0.686 |
PERK |
0.795 | -0.147 | -2 | 0.813 |
CDC7 |
0.795 | 0.066 | 1 | 0.802 |
MOK |
0.795 | 0.152 | 1 | 0.861 |
DYRK4 |
0.795 | 0.284 | 1 | 0.812 |
CDK5 |
0.795 | 0.215 | 1 | 0.850 |
NEK9 |
0.794 | -0.077 | 2 | 0.795 |
COT |
0.794 | 0.002 | 2 | 0.854 |
MASTL |
0.794 | -0.184 | -2 | 0.774 |
DYRK1A |
0.794 | 0.186 | 1 | 0.860 |
ZAK |
0.793 | -0.239 | 1 | 0.696 |
GRK5 |
0.793 | -0.110 | -3 | 0.797 |
HIPK4 |
0.793 | 0.201 | 1 | 0.861 |
DAPK1 |
0.792 | -0.036 | -3 | 0.724 |
PINK1 |
0.792 | 0.005 | 1 | 0.824 |
CDK14 |
0.792 | 0.232 | 1 | 0.819 |
GRK1 |
0.791 | 0.120 | -2 | 0.794 |
CDKL5 |
0.791 | 0.074 | -3 | 0.750 |
LOK |
0.791 | -0.164 | -2 | 0.731 |
TSSK2 |
0.791 | -0.027 | -5 | 0.717 |
GRK2 |
0.790 | -0.013 | -2 | 0.708 |
ROCK2 |
0.790 | -0.077 | -3 | 0.712 |
TLK1 |
0.789 | -0.108 | -2 | 0.806 |
DYRK1B |
0.789 | 0.213 | 1 | 0.827 |
DNAPK |
0.789 | 0.031 | 1 | 0.648 |
HIPK2 |
0.789 | 0.265 | 1 | 0.797 |
CHK1 |
0.789 | 0.012 | -3 | 0.756 |
DSTYK |
0.789 | -0.027 | 2 | 0.871 |
MLK1 |
0.789 | -0.156 | 2 | 0.773 |
CDK17 |
0.788 | 0.257 | 1 | 0.760 |
CDK8 |
0.788 | 0.259 | 1 | 0.828 |
PDHK1 |
0.787 | -0.161 | 1 | 0.767 |
GSK3A |
0.787 | 0.105 | 4 | 0.526 |
PKN3 |
0.786 | -0.043 | -3 | 0.798 |
ERK7 |
0.786 | 0.063 | 2 | 0.512 |
PIM3 |
0.786 | -0.013 | -3 | 0.772 |
CLK4 |
0.786 | 0.118 | -3 | 0.713 |
MTOR |
0.786 | -0.002 | 1 | 0.784 |
BUB1 |
0.786 | 0.016 | -5 | 0.659 |
GSK3B |
0.785 | 0.059 | 4 | 0.518 |
RIPK1 |
0.785 | -0.173 | 1 | 0.729 |
HRI |
0.785 | -0.220 | -2 | 0.800 |
DYRK3 |
0.785 | 0.164 | 1 | 0.848 |
CDK18 |
0.785 | 0.259 | 1 | 0.797 |
AMPKA1 |
0.785 | -0.032 | -3 | 0.787 |
NEK2 |
0.784 | -0.120 | 2 | 0.773 |
HUNK |
0.784 | -0.075 | 2 | 0.804 |
CDK3 |
0.784 | 0.223 | 1 | 0.777 |
SMG1 |
0.784 | -0.021 | 1 | 0.730 |
CDK13 |
0.784 | 0.231 | 1 | 0.820 |
ATM |
0.784 | -0.005 | 1 | 0.716 |
PIM1 |
0.784 | -0.010 | -3 | 0.718 |
RIPK3 |
0.783 | -0.098 | 3 | 0.744 |
DCAMKL1 |
0.783 | -0.062 | -3 | 0.722 |
SRPK1 |
0.782 | 0.137 | -3 | 0.705 |
CAMK2D |
0.782 | 0.007 | -3 | 0.785 |
NEK3 |
0.782 | -0.114 | 1 | 0.675 |
PLK3 |
0.782 | -0.076 | 2 | 0.788 |
SLK |
0.782 | -0.156 | -2 | 0.681 |
MARK4 |
0.782 | -0.013 | 4 | 0.866 |
CDK6 |
0.782 | 0.190 | 1 | 0.800 |
CDK7 |
0.782 | 0.231 | 1 | 0.837 |
WNK4 |
0.782 | -0.190 | -2 | 0.800 |
WNK1 |
0.781 | -0.113 | -2 | 0.802 |
NUAK2 |
0.781 | -0.019 | -3 | 0.788 |
CDK12 |
0.781 | 0.230 | 1 | 0.801 |
CDK4 |
0.781 | 0.195 | 1 | 0.794 |
CDK16 |
0.779 | 0.229 | 1 | 0.774 |
SRPK3 |
0.779 | 0.071 | -3 | 0.682 |
CDK2 |
0.779 | 0.130 | 1 | 0.864 |
DRAK1 |
0.779 | -0.087 | 1 | 0.724 |
TSSK1 |
0.778 | -0.033 | -3 | 0.808 |
CDK9 |
0.778 | 0.220 | 1 | 0.823 |
CAMK2B |
0.777 | 0.041 | 2 | 0.819 |
CDK19 |
0.777 | 0.266 | 1 | 0.803 |
PLK2 |
0.777 | -0.009 | -3 | 0.752 |
ULK2 |
0.777 | -0.092 | 2 | 0.755 |
IRAK4 |
0.777 | -0.187 | 1 | 0.713 |
TBK1 |
0.777 | -0.111 | 1 | 0.650 |
MLK4 |
0.776 | -0.153 | 2 | 0.682 |
TAO1 |
0.776 | -0.223 | 1 | 0.640 |
CLK2 |
0.776 | 0.195 | -3 | 0.693 |
NEK7 |
0.776 | -0.157 | -3 | 0.810 |
PIM2 |
0.776 | -0.040 | -3 | 0.688 |
MLK3 |
0.776 | -0.130 | 2 | 0.698 |
HASPIN |
0.775 | -0.080 | -1 | 0.656 |
IKKE |
0.775 | -0.071 | 1 | 0.646 |
TGFBR2 |
0.774 | -0.083 | -2 | 0.773 |
CRIK |
0.774 | -0.046 | -3 | 0.650 |
MYLK4 |
0.774 | -0.043 | -2 | 0.708 |
CHAK1 |
0.774 | -0.157 | 2 | 0.749 |
PRKD1 |
0.773 | 0.096 | -3 | 0.783 |
CLK1 |
0.773 | 0.129 | -3 | 0.689 |
DCAMKL2 |
0.773 | -0.094 | -3 | 0.744 |
CAMK2A |
0.773 | 0.041 | 2 | 0.826 |
NEK6 |
0.773 | -0.081 | -2 | 0.812 |
P70S6KB |
0.773 | -0.082 | -3 | 0.729 |
IKKB |
0.772 | -0.059 | -2 | 0.728 |
ROCK1 |
0.772 | -0.096 | -3 | 0.676 |
CDK10 |
0.771 | 0.206 | 1 | 0.811 |
AMPKA2 |
0.771 | -0.035 | -3 | 0.749 |
GRK4 |
0.771 | -0.089 | -2 | 0.803 |
PKCD |
0.771 | -0.121 | 2 | 0.746 |
PDHK3_TYR |
0.770 | 0.113 | 4 | 0.915 |
MST4 |
0.770 | -0.111 | 2 | 0.817 |
IKKA |
0.770 | -0.019 | -2 | 0.720 |
MAPKAPK3 |
0.769 | 0.006 | -3 | 0.716 |
PKN2 |
0.769 | -0.122 | -3 | 0.766 |
CK1D |
0.769 | 0.055 | -3 | 0.511 |
MRCKA |
0.768 | -0.094 | -3 | 0.677 |
AKT2 |
0.768 | -0.016 | -3 | 0.639 |
GRK3 |
0.768 | -0.003 | -2 | 0.679 |
RSK2 |
0.768 | -0.003 | -3 | 0.712 |
ULK1 |
0.767 | -0.036 | -3 | 0.861 |
KIS |
0.767 | 0.307 | 1 | 0.841 |
P90RSK |
0.767 | -0.023 | -3 | 0.731 |
MRCKB |
0.767 | -0.080 | -3 | 0.667 |
MARK2 |
0.766 | -0.021 | 4 | 0.775 |
SGK3 |
0.766 | -0.068 | -3 | 0.689 |
IRAK1 |
0.766 | -0.231 | -1 | 0.695 |
SBK |
0.765 | 0.049 | -3 | 0.527 |
WNK3 |
0.765 | -0.296 | 1 | 0.732 |
MAP2K6_TYR |
0.764 | 0.067 | -1 | 0.844 |
QSK |
0.764 | -0.008 | 4 | 0.839 |
CAMK4 |
0.764 | -0.127 | -3 | 0.755 |
TTBK2 |
0.764 | -0.199 | 2 | 0.676 |
BMPR2_TYR |
0.764 | 0.092 | -1 | 0.862 |
MSK1 |
0.763 | -0.003 | -3 | 0.691 |
CAMK1D |
0.763 | -0.044 | -3 | 0.621 |
CHK2 |
0.763 | -0.029 | -3 | 0.583 |
PAK1 |
0.763 | -0.099 | -2 | 0.699 |
MAP2K4_TYR |
0.763 | 0.022 | -1 | 0.833 |
PDHK4_TYR |
0.763 | 0.033 | 2 | 0.888 |
PAK2 |
0.763 | -0.148 | -2 | 0.689 |
CK2A2 |
0.762 | 0.082 | 1 | 0.696 |
IRE1 |
0.762 | -0.175 | 1 | 0.718 |
SSTK |
0.762 | -0.058 | 4 | 0.828 |
SGK1 |
0.761 | -0.023 | -3 | 0.555 |
MELK |
0.761 | -0.105 | -3 | 0.733 |
PKCZ |
0.761 | -0.139 | 2 | 0.736 |
PDHK1_TYR |
0.760 | 0.023 | -1 | 0.865 |
NIM1 |
0.760 | -0.111 | 3 | 0.771 |
MARK1 |
0.760 | -0.048 | 4 | 0.817 |
PRKD3 |
0.760 | -0.027 | -3 | 0.697 |
QIK |
0.760 | -0.126 | -3 | 0.773 |
MAPKAPK2 |
0.759 | 0.051 | -3 | 0.666 |
MARK3 |
0.759 | -0.016 | 4 | 0.802 |
CK1A2 |
0.758 | 0.030 | -3 | 0.511 |
PRKD2 |
0.758 | 0.042 | -3 | 0.717 |
AURB |
0.758 | -0.052 | -2 | 0.583 |
CAMK1G |
0.758 | -0.067 | -3 | 0.714 |
GCN2 |
0.758 | -0.161 | 2 | 0.787 |
NDR1 |
0.757 | -0.126 | -3 | 0.760 |
PAK3 |
0.757 | -0.129 | -2 | 0.703 |
PKACG |
0.757 | -0.063 | -2 | 0.681 |
IRE2 |
0.757 | -0.201 | 2 | 0.699 |
RIPK2 |
0.756 | -0.259 | 1 | 0.642 |
NDR2 |
0.756 | -0.035 | -3 | 0.770 |
RSK4 |
0.756 | -0.018 | -3 | 0.689 |
SRPK2 |
0.756 | 0.081 | -3 | 0.632 |
TESK1_TYR |
0.756 | -0.120 | 3 | 0.870 |
PKMYT1_TYR |
0.756 | -0.051 | 3 | 0.847 |
LATS2 |
0.756 | -0.055 | -5 | 0.635 |
CK2A1 |
0.755 | 0.073 | 1 | 0.678 |
PKCA |
0.755 | -0.131 | 2 | 0.682 |
PKCB |
0.755 | -0.102 | 2 | 0.685 |
STK33 |
0.755 | -0.178 | 2 | 0.615 |
PLK4 |
0.755 | -0.165 | 2 | 0.626 |
EPHA6 |
0.754 | 0.045 | -1 | 0.852 |
CK1E |
0.754 | 0.034 | -3 | 0.558 |
AURA |
0.754 | -0.048 | -2 | 0.555 |
RSK3 |
0.754 | -0.045 | -3 | 0.716 |
PKCH |
0.753 | -0.161 | 2 | 0.671 |
MSK2 |
0.753 | -0.059 | -3 | 0.695 |
MAP2K7_TYR |
0.753 | -0.228 | 2 | 0.853 |
BCKDK |
0.752 | -0.166 | -1 | 0.715 |
AURC |
0.752 | -0.004 | -2 | 0.588 |
AKT1 |
0.751 | -0.055 | -3 | 0.647 |
PKACB |
0.750 | -0.008 | -2 | 0.603 |
PKG2 |
0.749 | -0.062 | -2 | 0.603 |
EPHB4 |
0.748 | -0.026 | -1 | 0.804 |
FAM20C |
0.748 | 0.070 | 2 | 0.661 |
NUAK1 |
0.748 | -0.051 | -3 | 0.728 |
PKCG |
0.747 | -0.147 | 2 | 0.691 |
PKCI |
0.747 | -0.126 | 2 | 0.695 |
TXK |
0.747 | 0.025 | 1 | 0.794 |
CAMK1A |
0.746 | -0.044 | -3 | 0.596 |
LIMK2_TYR |
0.746 | -0.095 | -3 | 0.814 |
SIK |
0.746 | -0.055 | -3 | 0.701 |
PINK1_TYR |
0.746 | -0.267 | 1 | 0.791 |
ABL2 |
0.745 | -0.023 | -1 | 0.774 |
MNK1 |
0.745 | -0.104 | -2 | 0.714 |
MNK2 |
0.745 | -0.093 | -2 | 0.707 |
EPHA4 |
0.745 | -0.008 | 2 | 0.801 |
PKCE |
0.744 | -0.104 | 2 | 0.674 |
YANK3 |
0.744 | -0.066 | 2 | 0.420 |
MAPKAPK5 |
0.743 | -0.059 | -3 | 0.683 |
SRMS |
0.743 | -0.026 | 1 | 0.795 |
BRSK1 |
0.743 | -0.036 | -3 | 0.731 |
BLK |
0.742 | 0.036 | -1 | 0.840 |
FGR |
0.742 | -0.085 | 1 | 0.798 |
FER |
0.742 | -0.103 | 1 | 0.818 |
YES1 |
0.741 | -0.083 | -1 | 0.814 |
RET |
0.741 | -0.206 | 1 | 0.738 |
ABL1 |
0.741 | -0.039 | -1 | 0.762 |
HCK |
0.741 | -0.032 | -1 | 0.818 |
SNRK |
0.740 | -0.188 | 2 | 0.675 |
P70S6K |
0.739 | -0.104 | -3 | 0.650 |
LCK |
0.739 | -0.008 | -1 | 0.833 |
CSF1R |
0.739 | -0.134 | 3 | 0.784 |
DDR1 |
0.739 | -0.175 | 4 | 0.844 |
FYN |
0.738 | 0.032 | -1 | 0.823 |
JAK2 |
0.738 | -0.166 | 1 | 0.731 |
BRSK2 |
0.738 | -0.101 | -3 | 0.747 |
PKCT |
0.737 | -0.170 | 2 | 0.680 |
INSRR |
0.737 | -0.109 | 3 | 0.727 |
MST1R |
0.737 | -0.200 | 3 | 0.798 |
PKACA |
0.737 | -0.027 | -2 | 0.553 |
PHKG1 |
0.737 | -0.148 | -3 | 0.754 |
JAK3 |
0.737 | -0.122 | 1 | 0.722 |
LIMK1_TYR |
0.737 | -0.266 | 2 | 0.826 |
PTK2 |
0.736 | 0.092 | -1 | 0.820 |
EPHB2 |
0.736 | -0.054 | -1 | 0.788 |
TTBK1 |
0.736 | -0.204 | 2 | 0.600 |
TYK2 |
0.736 | -0.259 | 1 | 0.728 |
TYRO3 |
0.735 | -0.223 | 3 | 0.774 |
TNK2 |
0.735 | -0.095 | 3 | 0.752 |
EPHB1 |
0.735 | -0.099 | 1 | 0.783 |
EPHB3 |
0.735 | -0.084 | -1 | 0.790 |
ROS1 |
0.734 | -0.209 | 3 | 0.746 |
ITK |
0.734 | -0.091 | -1 | 0.770 |
FGFR2 |
0.733 | -0.149 | 3 | 0.790 |
KIT |
0.733 | -0.132 | 3 | 0.786 |
AKT3 |
0.733 | -0.037 | -3 | 0.579 |
YANK2 |
0.733 | -0.091 | 2 | 0.434 |
SYK |
0.732 | 0.071 | -1 | 0.803 |
MERTK |
0.731 | -0.105 | 3 | 0.773 |
PRKX |
0.731 | 0.014 | -3 | 0.607 |
PAK6 |
0.731 | -0.057 | -2 | 0.624 |
MET |
0.730 | -0.111 | 3 | 0.777 |
BMX |
0.730 | -0.068 | -1 | 0.698 |
FLT1 |
0.729 | -0.097 | -1 | 0.826 |
KDR |
0.729 | -0.155 | 3 | 0.751 |
EPHA7 |
0.728 | -0.074 | 2 | 0.792 |
FGFR1 |
0.727 | -0.167 | 3 | 0.754 |
FGFR3 |
0.727 | -0.120 | 3 | 0.759 |
TEK |
0.727 | -0.164 | 3 | 0.712 |
PTK2B |
0.727 | -0.037 | -1 | 0.728 |
PKN1 |
0.727 | -0.102 | -3 | 0.670 |
ERBB2 |
0.726 | -0.128 | 1 | 0.712 |
NEK10_TYR |
0.726 | -0.150 | 1 | 0.617 |
TEC |
0.725 | -0.115 | -1 | 0.691 |
LYN |
0.725 | -0.071 | 3 | 0.707 |
EPHA3 |
0.725 | -0.123 | 2 | 0.769 |
JAK1 |
0.724 | -0.120 | 1 | 0.664 |
SRC |
0.724 | -0.053 | -1 | 0.802 |
FRK |
0.724 | -0.090 | -1 | 0.827 |
EPHA5 |
0.724 | -0.064 | 2 | 0.790 |
EPHA8 |
0.724 | -0.049 | -1 | 0.801 |
FLT3 |
0.723 | -0.237 | 3 | 0.770 |
EGFR |
0.723 | -0.064 | 1 | 0.635 |
PDGFRB |
0.722 | -0.273 | 3 | 0.786 |
BTK |
0.722 | -0.202 | -1 | 0.715 |
AXL |
0.722 | -0.206 | 3 | 0.769 |
NTRK1 |
0.722 | -0.202 | -1 | 0.759 |
TNK1 |
0.721 | -0.194 | 3 | 0.764 |
ALK |
0.719 | -0.198 | 3 | 0.698 |
LTK |
0.719 | -0.190 | 3 | 0.733 |
TNNI3K_TYR |
0.718 | -0.157 | 1 | 0.745 |
DDR2 |
0.718 | -0.106 | 3 | 0.723 |
EPHA1 |
0.718 | -0.154 | 3 | 0.753 |
PTK6 |
0.717 | -0.246 | -1 | 0.684 |
FLT4 |
0.717 | -0.194 | 3 | 0.749 |
PAK5 |
0.716 | -0.101 | -2 | 0.573 |
ERBB4 |
0.716 | -0.020 | 1 | 0.668 |
FGFR4 |
0.716 | -0.109 | -1 | 0.741 |
MATK |
0.716 | -0.147 | -1 | 0.702 |
EPHA2 |
0.715 | -0.051 | -1 | 0.765 |
PDGFRA |
0.715 | -0.291 | 3 | 0.781 |
INSR |
0.715 | -0.196 | 3 | 0.704 |
NTRK3 |
0.715 | -0.171 | -1 | 0.717 |
WEE1_TYR |
0.714 | -0.190 | -1 | 0.692 |
CK1G3 |
0.714 | -0.021 | -3 | 0.381 |
PHKG2 |
0.714 | -0.167 | -3 | 0.730 |
CSK |
0.714 | -0.154 | 2 | 0.789 |
CK1G1 |
0.713 | -0.040 | -3 | 0.539 |
NTRK2 |
0.711 | -0.268 | 3 | 0.737 |
ZAP70 |
0.710 | 0.006 | -1 | 0.711 |
PAK4 |
0.708 | -0.087 | -2 | 0.576 |
IGF1R |
0.704 | -0.161 | 3 | 0.645 |
PKG1 |
0.704 | -0.081 | -2 | 0.521 |
CK1G2 |
0.703 | 0.003 | -3 | 0.465 |
CK1A |
0.700 | 0.019 | -3 | 0.427 |
MUSK |
0.699 | -0.159 | 1 | 0.625 |
FES |
0.698 | -0.118 | -1 | 0.667 |