Motif 720 (n=432)
Position-wise Probabilities
Download
| uniprot | genes | site | source | protein | function |
|---|---|---|---|---|---|
| O00566 | MPHOSPH10 | S61 | ochoa | U3 small nucleolar ribonucleoprotein protein MPP10 (M phase phosphoprotein 10) | Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing (PubMed:12655004). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:12655004, ECO:0000269|PubMed:34516797}. |
| O15085 | ARHGEF11 | S225 | ochoa | Rho guanine nucleotide exchange factor 11 (PDZ-RhoGEF) | May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:0000269|PubMed:21670212}. |
| O43432 | EIF4G3 | S371 | ochoa | Eukaryotic translation initiation factor 4 gamma 3 (eIF-4-gamma 3) (eIF-4G 3) (eIF4G 3) (eIF-4-gamma II) (eIF4GII) | 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 (PubMed:9418880). Functional homolog of EIF4G1 (PubMed:9418880). {ECO:0000269|PubMed:9418880}. |
| O43707 | ACTN4 | S461 | ochoa | Alpha-actinin-4 (Non-muscle alpha-actinin 4) | F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (PubMed:22351778). Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation (PubMed:22689882). {ECO:0000250|UniProtKB:P57780, ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:22689882, ECO:0000305|PubMed:9508771}. |
| O60361 | NME2P1 | S105 | ochoa | Putative nucleoside diphosphate kinase (NDK) (NDP kinase) (EC 2.7.4.6) | 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). {ECO:0000250}. |
| O75122 | CLASP2 | S1092 | psp | CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2) | Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:17543864, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:26003921}. |
| O75150 | RNF40 | S819 | psp | E3 ubiquitin-protein ligase BRE1B (BRE1-B) (EC 2.3.2.27) (95 kDa retinoblastoma-associated protein) (RBP95) (RING finger protein 40) (RING-type E3 ubiquitin transferase BRE1B) | Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19410543}.; FUNCTION: (Microbial infection) Promotes the human herpesvirus 8 (KSHV) lytic cycle by inducing the expression of lytic viral genes including the latency switch gene RTA/ORF50. {ECO:0000269|PubMed:37888983}. |
| O75340 | PDCD6 | S107 | ochoa | Programmed cell death protein 6 (Apoptosis-linked gene 2 protein homolog) (ALG-2) | Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair. Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes (PubMed:20691033, PubMed:25667979). Involved in ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes (PubMed:19520058). Together with PEF1, acts as a calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats (PubMed:27716508). In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (PubMed:27716508). Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway (PubMed:19864416). Promotes localization and polymerization of TFG at endoplasmic reticulum exit site (PubMed:27813252). Required for T-cell receptor-, Fas-, and glucocorticoid-induced apoptosis (By similarity). May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity (PubMed:16132846). Its role in apoptosis may however be indirect, as suggested by knockout experiments (By similarity). May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway (PubMed:21893193). In case of infection by HIV-1 virus, indirectly inhibits HIV-1 production by affecting viral Gag expression and distribution (PubMed:27784779). {ECO:0000250|UniProtKB:P12815, ECO:0000269|PubMed:16132846, ECO:0000269|PubMed:19520058, ECO:0000269|PubMed:19864416, ECO:0000269|PubMed:20691033, ECO:0000269|PubMed:21893193, ECO:0000269|PubMed:25667979, ECO:0000269|PubMed:27716508, ECO:0000269|PubMed:27784779, ECO:0000269|PubMed:27813252}.; FUNCTION: [Isoform 2]: Has a lower Ca(2+) affinity than isoform 1 (By similarity). {ECO:0000250|UniProtKB:P12815}. |
| O75348 | ATP6V1G1 | S65 | ochoa | V-type proton ATPase subunit G 1 (V-ATPase subunit G 1) (V-ATPase 13 kDa subunit 1) (Vacuolar proton pump subunit G 1) (Vacuolar proton pump subunit M16) | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:32001091, PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (PubMed:32001091). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633). {ECO:0000269|PubMed:28296633, ECO:0000269|PubMed:33065002, ECO:0000303|PubMed:32001091}. |
| O75385 | ULK1 | S881 | ochoa | Serine/threonine-protein kinase ULK1 (EC 2.7.11.1) (Autophagy-related protein 1 homolog) (ATG1) (hATG1) (Unc-51-like kinase 1) | Serine/threonine-protein kinase involved in autophagy in response to starvation (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:23524951, PubMed:25040165, PubMed:29487085, PubMed:31123703). Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:25040165). Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR (PubMed:21795849). Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity (PubMed:21460634). May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences (PubMed:18936157). Plays a role early in neuronal differentiation and is required for granule cell axon formation (PubMed:11146101). Also phosphorylates SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165, PubMed:37306101). Phosphorylates FLCN, promoting autophagy (PubMed:25126726). Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation (PubMed:20921139). Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B (PubMed:28821708). {ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:20921139, ECO:0000269|PubMed:21460634, ECO:0000269|PubMed:21795849, ECO:0000269|PubMed:23524951, ECO:0000269|PubMed:25040165, ECO:0000269|PubMed:25126726, ECO:0000269|PubMed:28821708, ECO:0000269|PubMed:29487085, ECO:0000269|PubMed:31123703, ECO:0000269|PubMed:37306101}. |
| O75396 | SEC22B | S168 | ochoa | Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1) | SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER. {ECO:0000269|PubMed:15272311}. |
| O75439 | PMPCB | S44 | ochoa | Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (P-52) | Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (Probable) (PubMed:29576218). Preferentially, cleaves after an arginine at position P2 (By similarity). Required for PINK1 turnover by coupling PINK1 mitochondrial import and cleavage, which results in subsequent PINK1 proteolysis (PubMed:22354088). {ECO:0000250|UniProtKB:Q03346, ECO:0000269|PubMed:22354088, ECO:0000269|PubMed:29576218, ECO:0000305|PubMed:22354088}. |
| O75691 | UTP20 | S788 | ochoa | Small subunit processome component 20 homolog (Down-regulated in metastasis protein) (Novel nucleolar protein 73) (NNP73) (Protein Key-1A6) | Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. Involved in 18S pre-rRNA processing. Associates with U3 snoRNA. {ECO:0000269|PubMed:17498821, ECO:0000269|PubMed:34516797}. |
| O75899 | GABBR2 | S779 | ochoa | Gamma-aminobutyric acid type B receptor subunit 2 (GABA-B receptor 2) (GABA-B-R2) (GABA-BR2) (GABABR2) (Gb2) (G-protein coupled receptor 51) (HG20) | Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054, PubMed:9872316, PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:18165688). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644, PubMed:10773016, PubMed:24305054). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644, PubMed:10773016, PubMed:10906333, PubMed:9872744). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (PubMed:22660477, PubMed:9872744). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10075644, PubMed:22660477, PubMed:9872316, PubMed:9872744). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (Probable). {ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10328880, ECO:0000269|PubMed:15617512, ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477, ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:9872316, ECO:0000269|PubMed:9872744, ECO:0000305}. |
| O75899 | GABBR2 | S793 | ochoa | Gamma-aminobutyric acid type B receptor subunit 2 (GABA-B receptor 2) (GABA-B-R2) (GABA-BR2) (GABABR2) (Gb2) (G-protein coupled receptor 51) (HG20) | Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054, PubMed:9872316, PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:18165688). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644, PubMed:10773016, PubMed:24305054). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644, PubMed:10773016, PubMed:10906333, PubMed:9872744). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (PubMed:22660477, PubMed:9872744). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10075644, PubMed:22660477, PubMed:9872316, PubMed:9872744). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (Probable). {ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10328880, ECO:0000269|PubMed:15617512, ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477, ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:9872316, ECO:0000269|PubMed:9872744, ECO:0000305}. |
| O95049 | TJP3 | S212 | ochoa | Tight junction protein ZO-3 (Tight junction protein 3) (Zona occludens protein 3) (Zonula occludens protein 3) | TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:16129888). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions (PubMed:16129888). Promotes cell-cycle progression through the sequestration of cyclin D1 (CCND1) at tight junctions during mitosis which prevents CCND1 degradation during M-phase and enables S-phase transition (PubMed:21411630). With TJP1 and TJP2, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). Contrary to TJP2, TJP3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment (By similarity). {ECO:0000250|UniProtKB:O62683, ECO:0000250|UniProtKB:Q9QXY1, ECO:0000269|PubMed:16129888, ECO:0000269|PubMed:21411630}. |
| O95235 | KIF20A | S677 | ochoa | Kinesin-like protein KIF20A (GG10_2) (Mitotic kinesin-like protein 2) (MKlp2) (Rab6-interacting kinesin-like protein) (Rabkinesin-6) | Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. {ECO:0000269|PubMed:12939256}. |
| O95239 | KIF4A | S951 | ochoa | Chromosome-associated kinesin KIF4A (Chromokinesin-A) | Iron-sulfur (Fe-S) cluster binding motor protein that has a role in chromosome segregation during mitosis (PubMed:29848660). Translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis (PubMed:15297875, PubMed:15625105). May play a role in mitotic chromosomal positioning and bipolar spindle stabilization (By similarity). {ECO:0000250|UniProtKB:P33174, ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:29848660}. |
| P02545 | LMNA | S143 | ochoa | Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)] | [Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:18551513, ECO:0000269|PubMed:18611980, ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:23666920, ECO:0000269|PubMed:23990565, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:31434876, ECO:0000269|PubMed:31548606, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269|PubMed:20458013}. |
| P02545 | LMNA | S153 | ochoa | Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)] | [Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:18551513, ECO:0000269|PubMed:18611980, ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:23666920, ECO:0000269|PubMed:23990565, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:31434876, ECO:0000269|PubMed:31548606, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269|PubMed:20458013}. |
| P02545 | LMNA | S301 | ochoa|psp | Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)] | [Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:18551513, ECO:0000269|PubMed:18611980, ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:23666920, ECO:0000269|PubMed:23990565, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:31434876, ECO:0000269|PubMed:31548606, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269|PubMed:20458013}. |
| P04843 | RPN1 | S514 | ochoa | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit) (Ribophorin I) (RPN-I) (Ribophorin-1) | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). {ECO:0000250|UniProtKB:E2RQ08, ECO:0000269|PubMed:31831667, ECO:0000269|PubMed:39567208}. |
| P04843 | RPN1 | S535 | ochoa | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit) (Ribophorin I) (RPN-I) (Ribophorin-1) | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). {ECO:0000250|UniProtKB:E2RQ08, ECO:0000269|PubMed:31831667, ECO:0000269|PubMed:39567208}. |
| P05023 | ATP1A1 | S369 | ochoa | Sodium/potassium-transporting ATPase subunit alpha-1 (Na(+)/K(+) ATPase alpha-1 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-1) | This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (PubMed:29499166, PubMed:30388404). Could also be part of an osmosensory signaling pathway that senses body-fluid sodium levels and controls salt intake behavior as well as voluntary water intake to regulate sodium homeostasis (By similarity). {ECO:0000250|UniProtKB:Q8VDN2, ECO:0000269|PubMed:29499166, ECO:0000269|PubMed:30388404}. |
| P07951 | TPM2 | S188 | ochoa | Tropomyosin beta chain (Beta-tropomyosin) (Tropomyosin-2) | Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization. {ECO:0000250|UniProtKB:P58774, ECO:0000250|UniProtKB:P58775}. |
| P08235 | NR3C2 | S843 | psp | Mineralocorticoid receptor (MR) (Nuclear receptor subfamily 3 group C member 2) | Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels. {ECO:0000269|PubMed:3037703}. |
| P08631 | HCK | S214 | ochoa | Tyrosine-protein kinase HCK (EC 2.7.10.2) (Hematopoietic cell kinase) (Hemopoietic cell kinase) (p59-HCK/p60-HCK) (p59Hck) (p61Hck) | Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS. {ECO:0000269|PubMed:10092522, ECO:0000269|PubMed:10779760, ECO:0000269|PubMed:10973280, ECO:0000269|PubMed:11741929, ECO:0000269|PubMed:11896602, ECO:0000269|PubMed:12411494, ECO:0000269|PubMed:15010462, ECO:0000269|PubMed:15952790, ECO:0000269|PubMed:15998323, ECO:0000269|PubMed:17310994, ECO:0000269|PubMed:17535448, ECO:0000269|PubMed:19114024, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:20452982, ECO:0000269|PubMed:21338576, ECO:0000269|PubMed:7535819, ECO:0000269|PubMed:8132624, ECO:0000269|PubMed:9406996, ECO:0000269|PubMed:9407116}. |
| P11413 | G6PD | S123 | ochoa | Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49) | Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. {ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:26479991, ECO:0000269|PubMed:35122041, ECO:0000269|PubMed:38066190, ECO:0000269|PubMed:743300}. |
| P12814 | ACTN1 | S442 | ochoa | Alpha-actinin-1 (Alpha-actinin cytoskeletal isoform) (F-actin cross-linking protein) (Non-muscle alpha-actinin-1) | F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation (PubMed:22689882). {ECO:0000269|PubMed:22689882}. |
| P12883 | MYH7 | S1261 | ochoa | Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000305|PubMed:26150528, ECO:0000305|PubMed:26246073}. |
| P12883 | MYH7 | S1275 | ochoa | Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000305|PubMed:26150528, ECO:0000305|PubMed:26246073}. |
| P12883 | MYH7 | S1465 | ochoa | Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000305|PubMed:26150528, ECO:0000305|PubMed:26246073}. |
| P12883 | MYH7 | S1718 | ochoa | Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000305|PubMed:26150528, ECO:0000305|PubMed:26246073}. |
| P13533 | MYH6 | S1467 | ochoa | Myosin-6 (Myosin heavy chain 6) (Myosin heavy chain, cardiac muscle alpha isoform) (MyHC-alpha) | Muscle contraction. |
| P13533 | MYH6 | S1720 | ochoa | Myosin-6 (Myosin heavy chain 6) (Myosin heavy chain, cardiac muscle alpha isoform) (MyHC-alpha) | Muscle contraction. |
| P13637 | ATP1A3 | S359 | ochoa | Sodium/potassium-transporting ATPase subunit alpha-3 (Na(+)/K(+) ATPase alpha-3 subunit) (EC 7.2.2.13) (Na(+)/K(+) ATPase alpha(III) subunit) (Sodium pump subunit alpha-3) | This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. {ECO:0000269|PubMed:33880529}. |
| P15531 | NME1 | S120 | ochoa|psp | Nucleoside diphosphate kinase A (NDK A) (NDP kinase A) (EC 2.7.4.6) (Granzyme A-activated DNase) (GAAD) (Metastasis inhibition factor nm23) (NM23-H1) (Tumor metastatic process-associated protein) | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair. {ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:8810265}. |
| P15924 | DSP | S1708 | ochoa | Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen) | Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250|UniProtKB:F1LMV6}. |
| P18583 | SON | S353 | ochoa | Protein SON (Bax antagonist selected in saccharomyces 1) (BASS1) (Negative regulatory element-binding protein) (NRE-binding protein) (Protein DBP-5) (SON3) | RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'-GA[GT]AN[CG][AG]CC-3'. May indirectly repress hepatitis B virus (HBV) core promoter activity and transcription of HBV genes and production of HBV virions. Essential for correct RNA splicing of multiple genes critical for brain development, neuronal migration and metabolism, including TUBG1, FLNA, PNKP, WDR62, PSMD3, PCK2, PFKL, IDH2, and ACY1 (PubMed:27545680). {ECO:0000269|PubMed:20581448, ECO:0000269|PubMed:21504830, ECO:0000269|PubMed:27545680}. |
| P19367 | HK1 | S337 | ochoa | Hexokinase-1 (EC 2.7.1.1) (Brain form hexokinase) (Hexokinase type I) (HK I) (Hexokinase-A) | Catalyzes the phosphorylation of various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate, respectively) (PubMed:1637300, PubMed:25316723, PubMed:27374331). Does not phosphorylate N-acetyl-D-glucosamine (PubMed:27374331). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (By similarity). Involved in innate immunity and inflammation by acting as a pattern recognition receptor for bacterial peptidoglycan (PubMed:27374331). When released in the cytosol, N-acetyl-D-glucosamine component of bacterial peptidoglycan inhibits the hexokinase activity of HK1 and causes its dissociation from mitochondrial outer membrane, thereby activating the NLRP3 inflammasome (PubMed:27374331). {ECO:0000250|UniProtKB:P05708, ECO:0000269|PubMed:1637300, ECO:0000269|PubMed:25316723, ECO:0000269|PubMed:27374331}. |
| P19429 | TNNI3 | S42 | psp | Troponin I, cardiac muscle (Cardiac troponin I) | Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. |
| P20700 | LMNB1 | S305 | 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}. |
| P20929 | NEB | S923 | ochoa | Nebulin | This giant muscle protein may be involved in maintaining the structural integrity of sarcomeres and the membrane system associated with the myofibrils. Binds and stabilize F-actin. |
| P20936 | RASA1 | S833 | ochoa | Ras GTPase-activating protein 1 (GAP) (GTPase-activating protein) (RasGAP) (Ras p21 protein activator) (p120GAP) | Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase of normal but not oncogenic Ras p21; this stimulation may be further increased in the presence of NCK1. {ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:8360177}. |
| P21462 | FPR1 | S328 | psp | fMet-Leu-Phe receptor (fMLP receptor) (N-formyl peptide receptor) (FPR) (N-formylpeptide chemoattractant receptor) | High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors (PubMed:10514456, PubMed:15153520, PubMed:2161213, PubMed:2176894). Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release (PubMed:15153520, PubMed:15210802, PubMed:1712023, PubMed:2161213). This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system (PubMed:10514456, PubMed:1712023). Receptor for TAFA4, mediates its effects on chemoattracting macrophages, promoting phagocytosis and increasing ROS release (PubMed:25109685). Receptor for cathepsin CTSG, leading to increased phagocyte chemotaxis (PubMed:15210802). {ECO:0000269|PubMed:10514456, ECO:0000269|PubMed:15153520, ECO:0000269|PubMed:2161213, ECO:0000269|PubMed:2176894, ECO:0000269|PubMed:25109685, ECO:0000303|PubMed:10514456, ECO:0000303|PubMed:1712023, ECO:0000303|PubMed:2161213, ECO:0000303|PubMed:2176894}. |
| P22392 | NME2 | S120 | 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}. |
| P28290 | ITPRID2 | S1010 | ochoa | Protein ITPRID2 (Cleavage signal-1 protein) (CS-1) (ITPR-interacting domain-containing protein 2) (Ki-ras-induced actin-interacting protein) (Sperm-specific antigen 2) | None |
| P30305 | CDC25B | S373 | ochoa | M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B) | Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression (PubMed:1836978, PubMed:20360007). Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:20360007). Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner (PubMed:17332740). The three isoforms seem to have a different level of activity (PubMed:1836978). {ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:1836978, ECO:0000269|PubMed:20360007}. |
| P30622 | CLIP1 | S348 | ochoa | CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 1) (Cytoplasmic linker protein 170 alpha-2) (CLIP-170) (Reed-Sternberg intermediate filament-associated protein) (Restin) | Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269|PubMed:12433698, ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:17889670}. |
| P30622 | CLIP1 | S1271 | ochoa | CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 1) (Cytoplasmic linker protein 170 alpha-2) (CLIP-170) (Reed-Sternberg intermediate filament-associated protein) (Restin) | Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269|PubMed:12433698, ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:17889670}. |
| P31040 | SDHA | S530 | ochoa | Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (Fp) (Malate dehydrogenase [quinone] flavoprotein subunit) (EC 1.1.5.-) | Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (PubMed:10746566, PubMed:24781757). SDH also oxidizes malate to the non-canonical enol form of oxaloacetate, enol-oxaloacetate (By similarity). Enol-oxaloacetate, which is a potent inhibitor of the succinate dehydrogenase activity, is further isomerized into keto-oxaloacetate (By similarity). Can act as a tumor suppressor (PubMed:20484225). {ECO:0000250|UniProtKB:P31039, ECO:0000269|PubMed:10746566, ECO:0000269|PubMed:20484225, ECO:0000269|PubMed:24781757}. |
| P35236 | PTPN7 | S63 | ochoa | Tyrosine-protein phosphatase non-receptor type 7 (EC 3.1.3.48) (Hematopoietic protein-tyrosine phosphatase) (HEPTP) (Protein-tyrosine phosphatase LC-PTP) | Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction. {ECO:0000269|PubMed:10206983, ECO:0000269|PubMed:10559944, ECO:0000269|PubMed:10702794, ECO:0000269|PubMed:1510684, ECO:0000269|PubMed:1530918, ECO:0000269|PubMed:9624114}. |
| P35609 | ACTN2 | S449 | ochoa | Alpha-actinin-2 (Alpha-actinin skeletal muscle isoform 2) (F-actin cross-linking protein) | F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. |
| P35749 | MYH11 | S1266 | ochoa | Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) | Muscle contraction. |
| P35749 | MYH11 | S1385 | ochoa | Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) | Muscle contraction. |
| P35749 | MYH11 | S1722 | ochoa | Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) | Muscle contraction. |
| P38398 | BRCA1 | S1211 | ochoa | Breast cancer type 1 susceptibility protein (EC 2.3.2.27) (RING finger protein 53) (RING-type E3 ubiquitin transferase BRCA1) | E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage (PubMed:10500182, PubMed:12887909, PubMed:12890688, PubMed:14976165, PubMed:16818604, PubMed:17525340, PubMed:19261748). It is unclear whether it also mediates the formation of other types of polyubiquitin chains (PubMed:12890688). The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:12890688, PubMed:14976165, PubMed:20351172). Regulates centrosomal microtubule nucleation (PubMed:18056443). Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle (PubMed:10724175, PubMed:11836499, PubMed:12183412, PubMed:19261748). Required for FANCD2 targeting to sites of DNA damage (PubMed:12887909). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation (PubMed:16326698). Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks (PubMed:19369211). Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8 (PubMed:16818604). Acts as a transcriptional activator (PubMed:20160719). {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:11836499, ECO:0000269|PubMed:12183412, ECO:0000269|PubMed:12887909, ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14976165, ECO:0000269|PubMed:16326698, ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:20351172}. |
| P41279 | MAP3K8 | S400 | psp | Mitogen-activated protein kinase kinase kinase 8 (EC 2.7.11.25) (Cancer Osaka thyroid oncogene) (Proto-oncogene c-Cot) (Serine/threonine-protein kinase cot) (Tumor progression locus 2) (TPL-2) | Required for lipopolysaccharide (LPS)-induced, TLR4-mediated activation of the MAPK/ERK pathway in macrophages, thus being critical for production of the pro-inflammatory cytokine TNF-alpha (TNF) during immune responses. Involved in the regulation of T-helper cell differentiation and IFNG expression in T-cells. Involved in mediating host resistance to bacterial infection through negative regulation of type I interferon (IFN) production. In vitro, activates MAPK/ERK pathway in response to IL1 in an IRAK1-independent manner, leading to up-regulation of IL8 and CCL4. Transduces CD40 and TNFRSF1A signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. May also play a role in the transduction of TNF signals that activate JNK and NF-kappa-B in some cell types. In adipocytes, activates MAPK/ERK pathway in an IKBKB-dependent manner in response to IL1B and TNF, but not insulin, leading to induction of lipolysis. Plays a role in the cell cycle. Isoform 1 shows some transforming activity, although it is much weaker than that of the activated oncogenic variant. {ECO:0000269|PubMed:11342626, ECO:0000269|PubMed:12667451, ECO:0000269|PubMed:15169888, ECO:0000269|PubMed:16371247, ECO:0000269|PubMed:1833717, ECO:0000269|PubMed:19001140, ECO:0000269|PubMed:19808894}. |
| P42566 | EPS15 | S368 | ochoa | Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p) | Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:18362181, ECO:0000269|PubMed:19458185, ECO:0000269|PubMed:22648170}. |
| P42566 | EPS15 | S435 | ochoa | Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p) | Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:18362181, ECO:0000269|PubMed:19458185, ECO:0000269|PubMed:22648170}. |
| P42566 | EPS15 | S470 | ochoa | Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p) | Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:18362181, ECO:0000269|PubMed:19458185, ECO:0000269|PubMed:22648170}. |
| P43686 | PSMC4 | S28 | ochoa | 26S proteasome regulatory subunit 6B (26S proteasome AAA-ATPase subunit RPT3) (MB67-interacting protein) (MIP224) (Proteasome 26S subunit ATPase 4) (Tat-binding protein 7) (TBP-7) | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC4 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000269|PubMed:1317798, ECO:0000269|PubMed:8060531}. |
| P46060 | RANGAP1 | S504 | psp | Ran GTPase-activating protein 1 (RanGAP1) | GTPase activator for RAN (PubMed:16428860, PubMed:8146159, PubMed:8896452). Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export (PubMed:27160050, PubMed:8896452). Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (PubMed:27160050). {ECO:0000269|PubMed:16428860, ECO:0000269|PubMed:27160050, ECO:0000269|PubMed:8146159, ECO:0000269|PubMed:8896452}. |
| P46939 | UTRN | S1695 | ochoa | Utrophin (Dystrophin-related protein 1) (DRP-1) | May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}. |
| P49327 | FASN | S1129 | ochoa | Fatty acid synthase (EC 2.3.1.85) (Type I fatty acid synthase) [Includes: [Acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.39); Acyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14)] | Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000269|PubMed:16215233, ECO:0000269|PubMed:16969344, ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448}.; FUNCTION: (Microbial infection) Fatty acid synthetase activity is required for SARS coronavirus-2/SARS-CoV-2 replication. {ECO:0000269|PubMed:34320401}. |
| P49327 | FASN | S2198 | ochoa | Fatty acid synthase (EC 2.3.1.85) (Type I fatty acid synthase) [Includes: [Acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.39); Acyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14)] | Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000269|PubMed:16215233, ECO:0000269|PubMed:16969344, ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448}.; FUNCTION: (Microbial infection) Fatty acid synthetase activity is required for SARS coronavirus-2/SARS-CoV-2 replication. {ECO:0000269|PubMed:34320401}. |
| P50748 | KNTC1 | S1047 | ochoa | Kinetochore-associated protein 1 (Rough deal homolog) (HsROD) (Rod) (hRod) | Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores (PubMed:11146660, PubMed:11590237, PubMed:15824131). Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex. {ECO:0000269|PubMed:11146660, ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15824131, ECO:0000305}. |
| P50993 | ATP1A2 | S367 | ochoa | Sodium/potassium-transporting ATPase subunit alpha-2 (Na(+)/K(+) ATPase alpha-2 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-2) | This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients. {ECO:0000269|PubMed:33880529}. |
| P52789 | HK2 | S122 | ochoa | Hexokinase-2 (EC 2.7.1.1) (Hexokinase type II) (HK II) (Hexokinase-B) (Muscle form hexokinase) | Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively) (PubMed:23185017, PubMed:26985301, PubMed:29298880). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:29298880). Plays a key role in maintaining the integrity of the outer mitochondrial membrane by preventing the release of apoptogenic molecules from the intermembrane space and subsequent apoptosis (PubMed:18350175). {ECO:0000269|PubMed:18350175, ECO:0000269|PubMed:23185017, ECO:0000269|PubMed:26985301, ECO:0000269|PubMed:29298880}. |
| P55211 | CASP9 | S195 | psp | Caspase-9 (CASP-9) (EC 3.4.22.62) (Apoptotic protease Mch-6) (Apoptotic protease-activating factor 3) (APAF-3) (ICE-like apoptotic protease 6) (ICE-LAP6) [Cleaved into: Caspase-9 subunit p35; Caspase-9 subunit p10] | Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates effector caspases caspase-3 (CASP3) or caspase-7 (CASP7). Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (PubMed:36758105, PubMed:36758106). {ECO:0000269|PubMed:15657060, ECO:0000269|PubMed:16352606, ECO:0000269|PubMed:16916640, ECO:0000269|PubMed:23516580, ECO:0000269|PubMed:27889207, ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120}.; FUNCTION: [Isoform 2]: Lacks activity is an dominant-negative inhibitor of caspase-9. {ECO:0000269|PubMed:10070954}. |
| P60880 | SNAP25 | S28 | psp | Synaptosomal-associated protein 25 (SNAP-25) (Super protein) (SUP) (Synaptosomal-associated 25 kDa protein) | t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells. {ECO:0000250|UniProtKB:P60881}. |
| P61978 | HNRNPK | S89 | 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}. |
| Q00987 | MDM2 | S256 | psp | E3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27) (Double minute 2 protein) (Hdm2) (Oncoprotein Mdm2) (RING-type E3 ubiquitin transferase Mdm2) (p53-binding protein Mdm2) | E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome (PubMed:29681526). Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation (PubMed:12821780, PubMed:15053880, PubMed:15195100, PubMed:15632057, PubMed:16337594, PubMed:17290220, PubMed:19098711, PubMed:19219073, PubMed:19837670, PubMed:19965871, PubMed:20173098, PubMed:20385133, PubMed:20858735, PubMed:22128911). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (By similarity). Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis (PubMed:30879903). Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis (PubMed:30879903). {ECO:0000250|UniProtKB:P23804, ECO:0000269|PubMed:12821780, ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:15632057, ECO:0000269|PubMed:16337594, ECO:0000269|PubMed:17290220, ECO:0000269|PubMed:19098711, ECO:0000269|PubMed:19219073, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:19965871, ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:20385133, ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:22128911, ECO:0000269|PubMed:29681526, ECO:0000269|PubMed:30879903}. |
| Q01628 | IFITM3 | S101 | 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 | S100 | 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}. |
| Q03252 | LMNB2 | Y319 | ochoa | Lamin-B2 | 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:33033404). 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:33033404). 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:33033404). {ECO:0000269|PubMed:33033404}. |
| Q03701 | CEBPZ | S320 | ochoa | CCAAT/enhancer-binding protein zeta (CCAAT-box-binding transcription factor) (CBF) (CCAAT-binding factor) | Stimulates transcription from the HSP70 promoter. |
| Q04917 | YWHAH | S25 | psp | 14-3-3 protein eta (Protein AS1) | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1. {ECO:0000269|PubMed:12177059}. |
| Q08043 | ACTN3 | S456 | ochoa | Alpha-actinin-3 (Alpha-actinin skeletal muscle isoform 3) (F-actin cross-linking protein) | F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. |
| Q08AD1 | CAMSAP2 | S900 | ochoa | Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1) | Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:24706919, ECO:0000269|PubMed:24908486, ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28726242}. |
| Q12846 | STX4 | S208 | ochoa | Syntaxin-4 (Renal carcinoma antigen NY-REN-31) | Plasma membrane t-SNARE that mediates docking of transport vesicles (By similarity). Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane (By similarity). In neurons, recruited at neurite tips to membrane domains rich in the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) which promotes neurite tip surface expression of the dopamine transporter SLC6A3/DAT by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity). Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones (By similarity). Required for normal hearing (PubMed:36355422). {ECO:0000250|UniProtKB:P70452, ECO:0000250|UniProtKB:Q08850, ECO:0000269|PubMed:36355422}. |
| Q13021 | MALL | S66 | ochoa | MAL-like protein (Protein BENE) | None |
| Q13136 | PPFIA1 | S275 | ochoa | Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1) | May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269|PubMed:7796809}. |
| Q13464 | ROCK1 | S479 | 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}. |
| Q13576 | IQGAP2 | S1061 | ochoa | Ras GTPase-activating-like protein IQGAP2 | Binds to activated CDC42 and RAC1 but does not seem to stimulate their GTPase activity. Associates with calmodulin. |
| Q13586 | STIM1 | Y316 | psp | Stromal interaction molecule 1 | Acts as a Ca(2+) sensor that gates two major inward rectifying Ca(2+) channels at the plasma membrane: Ca(2+) release-activated Ca(2+) (CRAC) channels and arachidonate-regulated Ca(2+)-selective (ARC) channels (PubMed:15866891, PubMed:16005298, PubMed:16208375, PubMed:16537481, PubMed:16733527, PubMed:16766533, PubMed:16807233, PubMed:18854159, PubMed:19182790, PubMed:19249086, PubMed:19622606, PubMed:19706554, PubMed:22464749, PubMed:24069340, PubMed:24351972, PubMed:24591628, PubMed:25326555, PubMed:26322679, PubMed:28219928, PubMed:32415068). Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates CRAC channel pore-forming subunits ORA1, ORA2 and ORAI3 to generate sustained and oscillatory Ca(2+) entry (PubMed:16208375, PubMed:16537481, PubMed:32415068). Involved in enamel formation (PubMed:24621671). {ECO:0000269|PubMed:15866891, ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:16537481, ECO:0000269|PubMed:16733527, ECO:0000269|PubMed:16766533, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19182790, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19622606, ECO:0000269|PubMed:19706554, ECO:0000269|PubMed:22464749, ECO:0000269|PubMed:24069340, ECO:0000269|PubMed:24351972, ECO:0000269|PubMed:24591628, ECO:0000269|PubMed:24621671, ECO:0000269|PubMed:25326555, ECO:0000269|PubMed:26322679, ECO:0000269|PubMed:28219928, ECO:0000269|PubMed:32415068}. |
| Q13733 | ATP1A4 | S377 | ochoa | Sodium/potassium-transporting ATPase subunit alpha-4 (Na(+)/K(+) ATPase alpha-4 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-4) | This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. Plays a role in sperm motility. |
| Q14149 | MORC3 | S771 | ochoa | MORC family CW-type zinc finger protein 3 (Nuclear matrix protein 2) (Zinc finger CW-type coiled-coil domain protein 3) | Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response (PubMed:27440897, PubMed:34759314). Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function (PubMed:34759314). Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity (PubMed:17332504, PubMed:20501696). Binds RNA in vitro (PubMed:11927593). Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3 (PubMed:26933034). The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0 (PubMed:26933034). {ECO:0000269|PubMed:11927593, ECO:0000269|PubMed:17332504, ECO:0000269|PubMed:20501696, ECO:0000269|PubMed:26933034, ECO:0000269|PubMed:27440897, ECO:0000269|PubMed:34759314}.; FUNCTION: (Microbial infection) May be required for influenza A transcription during viral infection (PubMed:26202233). {ECO:0000269|PubMed:26202233}. |
| Q14203 | DCTN1 | S351 | ochoa | Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (DAP-150) (DP-150) (p135) (p150-glued) | Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule (PubMed:25185702). Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon (PubMed:23874158). Plays a role in metaphase spindle orientation (PubMed:22327364). Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole (PubMed:23386061). Plays a role in primary cilia formation (PubMed:25774020). {ECO:0000250|UniProtKB:A0A287B8J2, ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:23874158, ECO:0000269|PubMed:25185702, ECO:0000269|PubMed:25774020}. |
| Q14258 | TRIM25 | S433 | ochoa | E3 ubiquitin/ISG15 ligase TRIM25 (EC 6.3.2.n3) (Estrogen-responsive finger protein) (RING finger protein 147) (RING-type E3 ubiquitin transferase) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM25) (Tripartite motif-containing protein 25) (Ubiquitin/ISG15-conjugating enzyme TRIM25) (Zinc finger protein 147) | Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase (PubMed:16352599). Involved in innate immune defense against viruses by mediating ubiquitination of RIGI and IFIH1 (PubMed:17392790, PubMed:29357390, PubMed:30193849, PubMed:31710640, PubMed:33849980, PubMed:36045682). Mediates 'Lys-63'-linked polyubiquitination of the RIGI N-terminal CARD-like region and may play a role in signal transduction that leads to the production of interferons in response to viral infection (PubMed:17392790, PubMed:23950712). Mediates 'Lys-63'-linked polyubiquitination of IFIH1 (PubMed:30193849). Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway (PubMed:16352599, PubMed:17069755). Mediates estrogen action in various target organs (PubMed:22452784). Mediates the ubiquitination and subsequent proteasomal degradation of ZFHX3 (PubMed:22452784). Plays a role in promoting the restart of stalled replication forks via interaction with the KHDC3L-OOEP scaffold and subsequent ubiquitination of BLM, resulting in the recruitment and retainment of BLM at DNA replication forks (By similarity). Plays an essential role in the antiviral activity of ZAP/ZC3HAV1; an antiviral protein which inhibits the replication of certain viruses. Mechanistically, mediates 'Lys-63'-linked polyubiquitination of ZAP/ZC3HAV1 that is required for its optimal binding to target mRNA (PubMed:28060952, PubMed:28202764). Also mediates the ubiquitination of various substrates implicated in stress granule formation, nonsense-mediated mRNA decay, nucleoside synthesis and mRNA translation and stability (PubMed:36067236). {ECO:0000250|UniProtKB:Q61510, ECO:0000269|PubMed:16352599, ECO:0000269|PubMed:17069755, ECO:0000269|PubMed:17392790, ECO:0000269|PubMed:22452784, ECO:0000269|PubMed:23950712, ECO:0000269|PubMed:29357390, ECO:0000269|PubMed:30193849, ECO:0000269|PubMed:31710640, ECO:0000269|PubMed:33849980, ECO:0000269|PubMed:36045682, ECO:0000269|PubMed:36067236}. |
| Q14676 | MDC1 | S760 | ochoa | 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}. |
| Q14789 | GOLGB1 | S1567 | ochoa | Golgin subfamily B member 1 (372 kDa Golgi complex-associated protein) (GCP372) (Giantin) (Macrogolgin) | May participate in forming intercisternal cross-bridges of the Golgi complex. |
| Q14789 | GOLGB1 | S1956 | ochoa | Golgin subfamily B member 1 (372 kDa Golgi complex-associated protein) (GCP372) (Giantin) (Macrogolgin) | May participate in forming intercisternal cross-bridges of the Golgi complex. |
| Q14980 | NUMA1 | S83 | ochoa | Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen) | Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250|UniProtKB:E9Q7G0, ECO:0000269|PubMed:11163243, ECO:0000269|PubMed:11229403, ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386, ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:17172455, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23027904, ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901, ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:27462074, ECO:0000269|PubMed:7769006, ECO:0000305|PubMed:10075938, ECO:0000305|PubMed:21816348}. |
| Q14980 | NUMA1 | S1225 | ochoa | Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen) | Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250|UniProtKB:E9Q7G0, ECO:0000269|PubMed:11163243, ECO:0000269|PubMed:11229403, ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386, ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:17172455, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23027904, ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901, ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:27462074, ECO:0000269|PubMed:7769006, ECO:0000305|PubMed:10075938, ECO:0000305|PubMed:21816348}. |
| Q15149 | PLEC | S201 | ochoa | Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1) | Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:21109228}. |
| Q15149 | PLEC | S647 | ochoa | Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1) | Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:21109228}. |
| Q15149 | PLEC | S1444 | ochoa | Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1) | Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:21109228}. |
| Q15643 | TRIP11 | S464 | ochoa | Thyroid receptor-interacting protein 11 (TR-interacting protein 11) (TRIP-11) (Clonal evolution-related gene on chromosome 14 protein) (Golgi-associated microtubule-binding protein 210) (GMAP-210) (Trip230) | Is a membrane tether required for vesicle tethering to Golgi. Has an essential role in the maintenance of Golgi structure and function (PubMed:25473115, PubMed:30728324). It is required for efficient anterograde and retrograde trafficking in the early secretory pathway, functioning at both the ER-to-Golgi intermediate compartment (ERGIC) and Golgi complex (PubMed:25717001). Binds the ligand binding domain of the thyroid receptor (THRB) in the presence of triiodothyronine and enhances THRB-modulated transcription. {ECO:0000269|PubMed:10189370, ECO:0000269|PubMed:25473115, ECO:0000269|PubMed:25717001, ECO:0000269|PubMed:30728324, ECO:0000269|PubMed:9256431}. |
| Q15643 | TRIP11 | S527 | ochoa | Thyroid receptor-interacting protein 11 (TR-interacting protein 11) (TRIP-11) (Clonal evolution-related gene on chromosome 14 protein) (Golgi-associated microtubule-binding protein 210) (GMAP-210) (Trip230) | Is a membrane tether required for vesicle tethering to Golgi. Has an essential role in the maintenance of Golgi structure and function (PubMed:25473115, PubMed:30728324). It is required for efficient anterograde and retrograde trafficking in the early secretory pathway, functioning at both the ER-to-Golgi intermediate compartment (ERGIC) and Golgi complex (PubMed:25717001). Binds the ligand binding domain of the thyroid receptor (THRB) in the presence of triiodothyronine and enhances THRB-modulated transcription. {ECO:0000269|PubMed:10189370, ECO:0000269|PubMed:25473115, ECO:0000269|PubMed:25717001, ECO:0000269|PubMed:30728324, ECO:0000269|PubMed:9256431}. |
| Q16625 | OCLN | S445 | ochoa | Occludin | May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions. {ECO:0000269|PubMed:19114660}.; FUNCTION: (Microbial infection) Acts as a coreceptor for hepatitis C virus (HCV) in hepatocytes. {ECO:0000269|PubMed:19182773, ECO:0000269|PubMed:20375010}. |
| Q16828 | DUSP6 | S328 | ochoa | Dual specificity protein phosphatase 6 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase PYST1) (Mitogen-activated protein kinase phosphatase 3) (MAP kinase phosphatase 3) (MKP-3) | Dual specificity protein phosphatase, which mediates dephosphorylation and inactivation of MAP kinases (PubMed:8670865). Has a specificity for the ERK family (PubMed:8670865). Plays an important role in alleviating chronic postoperative pain (By similarity). Necessary for the normal dephosphorylation of the long-lasting phosphorylated forms of spinal MAPK1/3 and MAP kinase p38 induced by peripheral surgery, which drives the resolution of acute postoperative allodynia (By similarity). Also important for dephosphorylation of MAPK1/3 in local wound tissue, which further contributes to resolution of acute pain (By similarity). Promotes cell differentiation by regulating MAPK1/MAPK3 activity and regulating the expression of AP1 transcription factors (PubMed:29043977). {ECO:0000250|UniProtKB:Q9DBB1, ECO:0000269|PubMed:29043977, ECO:0000269|PubMed:8670865}. |
| Q16829 | DUSP7 | S366 | ochoa | Dual specificity protein phosphatase 7 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase PYST2) | Dual specificity protein phosphatase (PubMed:9788880). Shows high activity towards MAPK1/ERK2 (PubMed:9788880). Also has lower activity towards MAPK14 and MAPK8 (PubMed:9788880). In arrested oocytes, plays a role in meiotic resumption (By similarity). Promotes nuclear envelope breakdown and activation of the CDK1/Cyclin-B complex in oocytes, probably by dephosphorylating and inactivating the conventional protein kinase C (cPKC) isozyme PRKCB (By similarity). May also inactivate PRKCA and/or PRKCG (By similarity). Also important in oocytes for normal chromosome alignment on the metaphase plate and progression to anaphase, where it might regulate activity of the spindle-assembly checkpoint (SAC) complex (By similarity). {ECO:0000250|UniProtKB:Q91Z46, ECO:0000269|PubMed:9788880}. |
| Q53QZ3 | ARHGAP15 | S343 | 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}. |
| Q63HN8 | RNF213 | S1128 | ochoa | E3 ubiquitin-protein ligase RNF213 (EC 2.3.2.27) (EC 3.6.4.-) (ALK lymphoma oligomerization partner on chromosome 17) (E3 ubiquitin-lipopolysaccharide ligase RNF213) (EC 2.3.2.-) (Mysterin) (RING finger protein 213) | Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (PubMed:21799892, PubMed:26126547, PubMed:26278786, PubMed:26766444, PubMed:30705059, PubMed:32139119, PubMed:34012115). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS (PubMed:34012115). Also acts indirectly by mediating the recruitment of the LUBAC complex, which conjugates linear polyubiquitin chains (PubMed:34012115). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (PubMed:34012115). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (PubMed:30705059). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (PubMed:30846318). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys-63'-linked ubiquitination of target proteins (PubMed:32139119, PubMed:33842849). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of FLNA and NFATC2 downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression (PubMed:26766444). Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (PubMed:34012115). {ECO:0000269|PubMed:21799892, ECO:0000269|PubMed:26126547, ECO:0000269|PubMed:26278786, ECO:0000269|PubMed:26766444, ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:30846318, ECO:0000269|PubMed:32139119, ECO:0000269|PubMed:33842849, ECO:0000269|PubMed:34012115}. |
| Q66GS9 | CEP135 | S356 | ochoa | Centrosomal protein of 135 kDa (Cep135) (Centrosomal protein 4) | Centrosomal microtubule-binding protein involved in centriole biogenesis (PubMed:27477386). Acts as a scaffolding protein during early centriole biogenesis. Required for the targeting of centriole satellite proteins to centrosomes such as of PCM1, SSX2IP and CEP290 and recruitment of WRAP73 to centrioles. Also required for centriole-centriole cohesion during interphase by acting as a platform protein for CEP250 at the centriole. Required for the recruitment of CEP295 to the proximal end of new-born centrioles at the centriolar microtubule wall during early S phase in a PLK4-dependent manner (PubMed:27185865). {ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:18851962, ECO:0000269|PubMed:26675238, ECO:0000269|PubMed:27185865, ECO:0000269|PubMed:27477386}. |
| Q6NZI2 | CAVIN1 | S167 | ochoa | Caveolae-associated protein 1 (Cavin-1) (Polymerase I and transcript release factor) | Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:19726876). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (By similarity) (PubMed:18056712, PubMed:18191225, PubMed:19726876). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (By similarity). {ECO:0000250|UniProtKB:O54724, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19726876}. |
| Q6P2H3 | CEP85 | S623 | ochoa | Centrosomal protein of 85 kDa (Cep85) (Coiled-coil domain-containing protein 21) | Acts as a regulator of centriole duplication through a direct interaction with STIL, a key factor involved in the early steps of centriole formation. The CEP85-STIL protein complex acts as a modulator of PLK4-driven cytoskeletal rearrangements and directional cell motility (PubMed:29712910, PubMed:32107292). Acts as a negative regulator of NEK2 to maintain the centrosome integrity in interphase. Suppresses centrosome disjunction by inhibiting NEK2 kinase activity (PubMed:26220856). {ECO:0000269|PubMed:26220856, ECO:0000269|PubMed:29712910, ECO:0000269|PubMed:32107292}. |
| Q6PKG0 | LARP1 | S596 | 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}. |
| Q6WCQ1 | MPRIP | S265 | ochoa | Myosin phosphatase Rho-interacting protein (M-RIP) (Rho-interacting protein 3) (RIP3) (p116Rip) | Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells. {ECO:0000250|UniProtKB:P97434, ECO:0000269|PubMed:15545284, ECO:0000269|PubMed:16257966}. |
| Q6ZSZ5 | ARHGEF18 | S98 | ochoa | Rho guanine nucleotide exchange factor 18 (114 kDa Rho-specific guanine nucleotide exchange factor) (p114-Rho-GEF) (p114RhoGEF) (Septin-associated RhoGEF) (SA-RhoGEF) | Acts as a guanine nucleotide exchange factor (GEF) for RhoA GTPases. Its activation induces formation of actin stress fibers. Also acts as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Does not act as a GEF for CDC42. The G protein beta-gamma (Gbetagamma) subunits of heterotrimeric G proteins act as activators, explaining the integrated effects of LPA and other G-protein coupled receptor agonists on actin stress fiber formation, cell shape change and ROS production. Required for EPB41L4B-mediated regulation of the circumferential actomyosin belt in epithelial cells (PubMed:22006950). {ECO:0000269|PubMed:11085924, ECO:0000269|PubMed:14512443, ECO:0000269|PubMed:15558029, ECO:0000269|PubMed:22006950, ECO:0000269|PubMed:28132693}. |
| Q6ZU80 | CEP128 | S463 | ochoa | Centrosomal protein of 128 kDa (Cep128) | None |
| Q6ZVD8 | PHLPP2 | S299 | ochoa | PH domain leucine-rich repeat-containing protein phosphatase 2 (EC 3.1.3.16) (PH domain leucine-rich repeat-containing protein phosphatase-like) (PHLPP-like) | Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-II and 'Ser-657' of PRKCA. Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and decreases cell proliferation. Also controls the phosphorylation of AKT3. Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis (PubMed:20513427). Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation (PubMed:21986499). Inhibits cancer cell proliferation and may act as a tumor suppressor. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Dephosphorylates RAF1 inhibiting its kinase activity (PubMed:24530606). {ECO:0000269|PubMed:17386267, ECO:0000269|PubMed:18162466, ECO:0000269|PubMed:19079341, ECO:0000269|PubMed:20513427, ECO:0000269|PubMed:21986499, ECO:0000269|PubMed:24530606}. |
| Q702N8 | XIRP1 | S205 | ochoa | Xin actin-binding repeat-containing protein 1 (Cardiomyopathy-associated protein 1) | Protects actin filaments from depolymerization (PubMed:15454575). Required for correct cardiac intercalated disk ultrastructure via maintenance of cell-cell adhesion stability, and as a result maintains cardiac organ morphology, conductance and heart beat rhythm (By similarity). Required for development of normal skeletal muscle morphology and muscle fiber type composition (By similarity). Plays a role in regulating muscle satellite cell activation and survival, as a result promotes muscle fiber recovery from injury and fatigue (By similarity). {ECO:0000250|UniProtKB:O70373, ECO:0000269|PubMed:15454575}. |
| Q76I76 | SSH2 | S1353 | ochoa | Protein phosphatase Slingshot homolog 2 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 2) (SSH-2L) (hSSH-2L) | Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein (PubMed:11832213). Required for spermatogenesis (By similarity). Involved in acrosome biogenesis, probably by regulating cofilin-mediated actin cytoskeleton remodeling during proacrosomal vesicle fusion and/or Golgi to perinuclear vesicle trafficking (By similarity). {ECO:0000250|UniProtKB:Q5SW75, ECO:0000269|PubMed:11832213}. |
| Q7L4E1 | MIGA2 | S228 | ochoa | Mitoguardin 2 (Protein FAM73B) | Regulator of mitochondrial fusion: acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of PLD6/MitoPLD dimers. May act by regulating phospholipid metabolism via PLD6/MitoPLD. {ECO:0000269|PubMed:26711011}. |
| Q7L7X3 | TAOK1 | S554 | psp | Serine/threonine-protein kinase TAO1 (EC 2.7.11.1) (Kinase from chicken homolog B) (hKFC-B) (MARK Kinase) (MARKK) (Prostate-derived sterile 20-like kinase 2) (PSK-2) (PSK2) (Prostate-derived STE20-like kinase 2) (Thousand and one amino acid protein kinase 1) (TAOK1) (hTAOK1) | Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade. Plays an essential role in the regulation of neuronal development in the central nervous system (PubMed:33565190). Also plays a role in the regulation of neuronal migration to the cortical plate (By similarity). {ECO:0000250|UniProtKB:Q5F2E8, ECO:0000269|PubMed:12665513, ECO:0000269|PubMed:13679851, ECO:0000269|PubMed:16407310, ECO:0000269|PubMed:17396146, ECO:0000269|PubMed:17900936, ECO:0000269|PubMed:33565190}. |
| Q7Z3U7 | MON2 | S207 | 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}. |
| Q7Z6Z7 | HUWE1 | S2339 | psp | E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1) | E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250|UniProtKB:P51593, ECO:0000250|UniProtKB:Q7TMY8, ECO:0000269|PubMed:15567145, ECO:0000269|PubMed:15767685, ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:15989957, ECO:0000269|PubMed:17567951, ECO:0000269|PubMed:18488021, ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:20534529, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:27746020, ECO:0000269|PubMed:30217973, ECO:0000269|PubMed:35776542}. |
| Q86VP1 | TAX1BP1 | S240 | ochoa | Tax1-binding protein 1 (TRAF6-binding protein) | Ubiquitin-binding adapter that participates in inflammatory, antiviral and innate immune processes as well as selective autophagy regulation (PubMed:29940186, PubMed:30459273, PubMed:30909570). Plays a key role in the negative regulation of NF-kappa-B and IRF3 signalings by acting as an adapter for the ubiquitin-editing enzyme A20/TNFAIP3 to bind and inactivate its substrates (PubMed:17703191). Disrupts the interactions between the E3 ubiquitin ligase TRAF3 and TBK1/IKBKE to attenuate 'Lys63'-linked polyubiquitination of TBK1 and thereby IFN-beta production (PubMed:21885437). Also recruits A20/TNFAIP3 to ubiquitinated signaling proteins TRAF6 and RIPK1, leading to their deubiquitination and disruption of IL-1 and TNF-induced NF-kappa-B signaling pathways (PubMed:17703191). Inhibits virus-induced apoptosis by inducing the 'Lys-48'-linked polyubiquitination and degradation of MAVS via recruitment of the E3 ligase ITCH, thereby attenuating MAVS-mediated apoptosis signaling (PubMed:27736772). As a macroautophagy/autophagy receptor, facilitates the xenophagic clearance of pathogenic bacteria such as Salmonella typhimurium and Mycobacterium tuberculosis (PubMed:26451915). Upon NBR1 recruitment to the SQSTM1-ubiquitin condensates, acts as the major recruiter of RB1CC1 to these ubiquitin condensates to promote their autophagic degradation (PubMed:33226137, PubMed:34471133). Mediates the autophagic degradation of other substrates including TICAM1 (PubMed:28898289). {ECO:0000269|PubMed:10435631, ECO:0000269|PubMed:10920205, ECO:0000269|PubMed:17703191, ECO:0000269|PubMed:21885437, ECO:0000269|PubMed:26451915, ECO:0000269|PubMed:27736772, ECO:0000269|PubMed:28898289, ECO:0000269|PubMed:29940186, ECO:0000269|PubMed:30459273, ECO:0000269|PubMed:30909570, ECO:0000269|PubMed:33226137, ECO:0000269|PubMed:34471133}. |
| Q8IUC4 | RHPN2 | S82 | ochoa | Rhophilin-2 (76 kDa RhoB effector protein) (GTP-Rho-binding protein 2) (p76RBE) | Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity. {ECO:0000269|PubMed:12221077}. |
| Q8IUG5 | MYO18B | S1545 | ochoa | Unconventional myosin-XVIIIb | May be involved in intracellular trafficking of the muscle cell when in the cytoplasm, whereas entering the nucleus, may be involved in the regulation of muscle specific genes. May play a role in the control of tumor development and progression; restored MYO18B expression in lung cancer cells suppresses anchorage-independent growth. |
| Q8IWP9 | CCDC28A | S241 | ochoa | Coiled-coil domain-containing protein 28A (CCRL1AP) | None |
| Q8IY18 | SMC5 | S793 | ochoa | Structural maintenance of chromosomes protein 5 (SMC protein 5) (SMC-5) (hSMC5) | Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6. SMC5-SMC6 complex may prevent transcription of episomal DNA, such as circular viral DNA genome (PubMed:26983541). {ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:19502785, ECO:0000269|PubMed:26983541}. |
| Q8N6Q8 | METTL25 | S357 | ochoa | Probable methyltransferase-like protein 25 (EC 2.1.1.-) | Probable methyltransferase. {ECO:0000305}. |
| Q8NCN4 | RNF169 | S644 | ochoa | E3 ubiquitin-protein ligase RNF169 (EC 2.3.2.27) (RING finger protein 169) (RING-type E3 ubiquitin transferase RNF169) | Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization (PubMed:22492721, PubMed:30773093). Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1 (PubMed:30104380, PubMed:30773093). E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair. {ECO:0000269|PubMed:22492721, ECO:0000269|PubMed:22733822, ECO:0000269|PubMed:22742833, ECO:0000269|PubMed:30104380, ECO:0000269|PubMed:30773093}. |
| Q8NCY6 | MSANTD4 | S286 | ochoa | Myb/SANT-like DNA-binding domain-containing protein 4 (Myb/SANT-like DNA-binding domain containing 4 with coiled-coils) | None |
| Q8NHV4 | NEDD1 | S637 | psp | Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1) | Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269|PubMed:19029337, ECO:0000269|PubMed:19509060}. |
| Q8TD55 | PLEKHO2 | S439 | ochoa | Pleckstrin homology domain-containing family O member 2 (PH domain-containing family O member 2) (Pleckstrin homology domain-containing family Q member 1) (PH domain-containing family Q member 1) | None |
| Q8TDY2 | RB1CC1 | S1160 | ochoa | RB1-inducible coiled-coil protein 1 (FAK family kinase-interacting protein of 200 kDa) (FIP200) | Involved in autophagy (PubMed:21775823). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (By similarity). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (PubMed:10769033, PubMed:12221124). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (By similarity). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:14533007). Plays a crucial role in muscular differentiation (PubMed:12163359). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity). {ECO:0000250|UniProtKB:Q9ESK9, ECO:0000269|PubMed:10769033, ECO:0000269|PubMed:12095676, ECO:0000269|PubMed:12163359, ECO:0000269|PubMed:12221124, ECO:0000269|PubMed:14533007, ECO:0000269|PubMed:21775823, ECO:0000269|PubMed:23392225}. |
| Q8TF21 | ANKRD24 | S393 | ochoa | Ankyrin repeat domain-containing protein 24 | Component of the stereocilia rootlet in hair cells of inner ear. Bridges the apical plasma membrane with the lower rootlet and maintains normal distribution of TRIOBP, thereby reinforcing stereocilia insertion points and organizing rootlets for hearing with long-term resilience. {ECO:0000250|UniProtKB:Q80VM7}. |
| Q8WWI1 | LMO7 | S540 | ochoa | LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP) | None |
| Q8WYP3 | RIN2 | S79 | ochoa | Ras and Rab interactor 2 (Ras association domain family 4) (Ras inhibitor JC265) (Ras interaction/interference protein 2) | Ras effector protein. May function as an upstream activator and/or downstream effector for RAB5B in endocytic pathway. May function as a guanine nucleotide exchange (GEF) of RAB5B, required for activating the RAB5 proteins by exchanging bound GDP for free GTP. {ECO:0000269|PubMed:11733506}. |
| Q92543 | SNX19 | S375 | ochoa | Sorting nexin-19 | Plays a role in intracellular vesicle trafficking and exocytosis (PubMed:24843546). May play a role in maintaining insulin-containing dense core vesicles in pancreatic beta-cells and in preventing their degradation. May play a role in insulin secretion (PubMed:24843546). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (By similarity). {ECO:0000250|UniProtKB:Q6P4T1, ECO:0000269|PubMed:24843546}. |
| Q92614 | MYO18A | S1528 | ochoa | Unconventional myosin-XVIIIa (Molecule associated with JAK3 N-terminus) (MAJN) (Myosin containing a PDZ domain) (Surfactant protein receptor SP-R210) (SP-R210) | May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (PubMed:19837035, PubMed:23345592). Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346). Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:16087679, PubMed:21123169). Strongly enhances natural killer cell cytotoxicity (PubMed:27467939). {ECO:0000250|UniProtKB:Q9JMH9, ECO:0000269|PubMed:16087679, ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:21123169, ECO:0000269|PubMed:23345592, ECO:0000269|PubMed:25965346, ECO:0000269|PubMed:27467939}. |
| Q92734 | TFG | S100 | ochoa | Protein TFG (TRK-fused gene protein) | Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules (PubMed:23479643, PubMed:27813252). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:21478858). {ECO:0000269|PubMed:21478858, ECO:0000269|PubMed:23479643, ECO:0000269|PubMed:27813252}. |
| Q96AA8 | JAKMIP2 | S42 | ochoa | Janus kinase and microtubule-interacting protein 2 (CTCL tumor antigen HD-CL-04) (Neuroendocrine long coiled-coil protein 1) | None |
| Q96CV9 | OPTN | S342 | ochoa | Optineurin (E3-14.7K-interacting protein) (FIP-2) (Huntingtin yeast partner L) (Huntingtin-interacting protein 7) (HIP-7) (Huntingtin-interacting protein L) (NEMO-related protein) (Optic neuropathy-inducing protein) (Transcription factor IIIA-interacting protein) (TFIIIA-IntP) | Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8 (PubMed:27534431). Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation (PubMed:27534431). Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation (PubMed:27538435). In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta/IFNB1. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and huntingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as that of transferrin receptor (TFRC/TfR); regulates Rab8 recruitment to tubules emanating from the endocytic recycling compartment (PubMed:22854040). Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000269|PubMed:11834836, ECO:0000269|PubMed:15837803, ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:21617041, ECO:0000269|PubMed:22854040, ECO:0000269|PubMed:27534431, ECO:0000269|PubMed:27538435}.; FUNCTION: (Microbial infection) May constitute a cellular target for various viruses, such as adenovirus E3 14.7 or Bluetongue virus, to inhibit innate immune response (PubMed:27538435, PubMed:9488477). During RNA virus infection, such as that of Sendai virus, negatively regulates the induction of IFNB1 (PubMed:20174559). {ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:27538435, ECO:0000269|PubMed:9488477}. |
| Q96D09 | GPRASP2 | S512 | ochoa | G-protein coupled receptor-associated sorting protein 2 (GASP-2) | May play a role in regulation of a variety of G-protein coupled receptors. {ECO:0000269|PubMed:15086532}. |
| Q96MK2 | RIPOR3 | S381 | ochoa | RIPOR family member 3 | None |
| Q96MR9 | ZNF560 | T170 | ochoa | Zinc finger protein 560 | May be involved in transcriptional regulation. |
| Q96ST8 | CEP89 | S292 | ochoa | Centrosomal protein of 89 kDa (Cep89) (Centrosomal protein 123) (Cep123) (Coiled-coil domain-containing protein 123) | Required for ciliogenesis. Also plays a role in mitochondrial metabolism where it may modulate complex IV activity. {ECO:0000269|PubMed:23348840, ECO:0000269|PubMed:23575228}. |
| Q96TC7 | RMDN3 | S393 | ochoa | Regulator of microtubule dynamics protein 3 (RMD-3) (hRMD-3) (Cerebral protein 10) (Protein FAM82A2) (Protein FAM82C) (Protein tyrosine phosphatase-interacting protein 51) (TCPTP-interacting protein 51) | Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis. {ECO:0000269|PubMed:16820967, ECO:0000269|PubMed:22131369}. |
| Q99698 | LYST | S2627 | ochoa | Lysosomal-trafficking regulator (Beige homolog) | Adapter protein that regulates and/or fission of intracellular vesicles such as lysosomes (PubMed:11984006, PubMed:25216107). Might regulate trafficking of effectors involved in exocytosis (PubMed:25425525). In cytotoxic T-cells and natural killer (NK) cells, has role in the regulation of size, number and exocytosis of lytic granules (PubMed:26478006). In macrophages and dendritic cells, regulates phagosome maturation by controlling the conversion of early phagosomal compartments into late phagosomes (By similarity). In macrophages and dendritic cells, specifically involved in TLR3- and TLR4-induced production of pro-inflammatory cytokines by regulating the endosomal TLR3- TICAM1/TRIF and TLR4- TICAM1/TRIF signaling pathways (PubMed:27881733). {ECO:0000250|UniProtKB:P97412, ECO:0000269|PubMed:11984006, ECO:0000269|PubMed:25216107, ECO:0000269|PubMed:25425525, ECO:0000269|PubMed:26478006, ECO:0000269|PubMed:27881733}. |
| Q9BT73 | PSMG3 | S55 | ochoa | Proteasome assembly chaperone 3 (PAC-3) (hPAC3) (Proteasome chaperone homolog 3) (Pba3) | Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes. {ECO:0000269|PubMed:17189198}. |
| Q9BUR4 | WRAP53 | S491 | ochoa | Telomerase Cajal body protein 1 (WD repeat-containing protein 79) (WD40 repeat-containing protein antisense to TP53 gene) (WRAP53beta) | RNA chaperone that plays a key role in telomere maintenance and RNA localization to Cajal bodies (PubMed:29695869, PubMed:29804836). Specifically recognizes and binds the Cajal body box (CAB box) present in both small Cajal body RNAs (scaRNAs) and telomerase RNA template component (TERC) (PubMed:19285445, PubMed:20351177, PubMed:29695869, PubMed:29804836). Essential component of the telomerase holoenzyme complex, a ribonucleoprotein complex essential for the replication of chromosome termini that elongates telomeres in most eukaryotes (PubMed:19179534, PubMed:20351177, PubMed:26170453, PubMed:29695869). In the telomerase holoenzyme complex, required to stimulate the catalytic activity of the complex (PubMed:27525486, PubMed:29804836). Acts by specifically binding the CAB box of the TERC RNA and controlling the folding of the CR4/CR5 region of the TERC RNA, a critical step for telomerase activity (PubMed:29804836). In addition, also controls telomerase holoenzyme complex localization to Cajal body (PubMed:22547674). During S phase, required for delivery of TERC to telomeres during S phase and for telomerase activity (PubMed:29804836). In addition to its role in telomere maintenance, also required for Cajal body formation, probably by mediating localization of scaRNAs to Cajal bodies (PubMed:19285445, PubMed:21072240). Also plays a role in DNA repair: phosphorylated by ATM in response to DNA damage and relocalizes to sites of DNA double-strand breaks to promote the repair of DNA double-strand breaks (PubMed:25512560, PubMed:27715493). Acts by recruiting the ubiquitin ligase RNF8 to DNA breaks and promote both homologous recombination (HR) and non-homologous end joining (NHEJ) (PubMed:25512560, PubMed:27715493). {ECO:0000269|PubMed:19179534, ECO:0000269|PubMed:19285445, ECO:0000269|PubMed:20351177, ECO:0000269|PubMed:21072240, ECO:0000269|PubMed:22547674, ECO:0000269|PubMed:25512560, ECO:0000269|PubMed:26170453, ECO:0000269|PubMed:27525486, ECO:0000269|PubMed:27715493, ECO:0000269|PubMed:29695869, ECO:0000269|PubMed:29804836}. |
| Q9BVJ6 | UTP14A | S451 | ochoa | U3 small nucleolar RNA-associated protein 14 homolog A (Antigen NY-CO-16) (Serologically defined colon cancer antigen 16) | May be required for ribosome biogenesis. {ECO:0000250}. |
| Q9BXL6 | CARD14 | S255 | ochoa | Caspase recruitment domain-containing protein 14 (CARD-containing MAGUK protein 2) (Carma 2) | Acts as a scaffolding protein that can activate the inflammatory transcription factor NF-kappa-B and p38/JNK MAP kinase signaling pathways. Forms a signaling complex with BCL10 and MALT1, and activates MALT1 proteolytic activity and inflammatory gene expression. MALT1 is indispensable for CARD14-induced activation of NF-kappa-B and p38/JNK MAP kinases (PubMed:11278692, PubMed:21302310, PubMed:27071417, PubMed:27113748). May play a role in signaling mediated by TRAF2, TRAF3 and TRAF6 and protects cells against apoptosis. {ECO:0000269|PubMed:11278692, ECO:0000269|PubMed:21302310, ECO:0000269|PubMed:27071417, ECO:0000269|PubMed:27113748}.; FUNCTION: [Isoform 3]: Not able to activate the inflammatory transcription factor NF-kappa-B and may function as a dominant negative regulator (PubMed:21302310, PubMed:26358359). {ECO:0000269|PubMed:21302310, ECO:0000269|PubMed:26358359}. |
| Q9BXW9 | FANCD2 | S222 | ochoa|psp | Fanconi anemia group D2 protein (Protein FACD2) | Required for maintenance of chromosomal stability (PubMed:11239453, PubMed:14517836). Promotes accurate and efficient pairing of homologs during meiosis (PubMed:14517836). Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing (PubMed:15671039, PubMed:15650050, PubMed:30335751, PubMed:36385258). The FANCI-FANCD2 complex binds and scans double-stranded DNA (dsDNA) for DNA damage; this complex stalls at DNA junctions between double-stranded DNA and single-stranded DNA (By similarity). May participate in S phase and G2 phase checkpoint activation upon DNA damage (PubMed:15377654). Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress (PubMed:15454491, PubMed:15661754). Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress (PubMed:15661754, PubMed:19465921). Promotes BRCA2/FANCD1 loading onto damaged chromatin (PubMed:11239454, PubMed:12239151, PubMed:12086603, PubMed:15115758, PubMed:15199141, PubMed:15671039, PubMed:18212739). May also be involved in B-cell immunoglobulin isotype switching. {ECO:0000250|UniProtKB:Q68Y81, ECO:0000269|PubMed:11239453, ECO:0000269|PubMed:11239454, ECO:0000269|PubMed:12086603, ECO:0000269|PubMed:12239151, ECO:0000269|PubMed:14517836, ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15314022, ECO:0000269|PubMed:15377654, ECO:0000269|PubMed:15454491, ECO:0000269|PubMed:15650050, ECO:0000269|PubMed:15661754, ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:19465921, ECO:0000269|PubMed:30335751, ECO:0000269|PubMed:36385258}. |
| Q9BZD4 | NUF2 | S171 | ochoa | Kinetochore protein Nuf2 (hNuf2) (hNuf2R) (hsNuf2) (Cell division cycle-associated protein 1) | Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:12438418, PubMed:14654001, PubMed:15062103, PubMed:15235793, PubMed:15239953, PubMed:15548592, PubMed:17535814). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:15548592). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020). {ECO:0000269|PubMed:12438418, ECO:0000269|PubMed:14654001, ECO:0000269|PubMed:15062103, ECO:0000269|PubMed:15235793, ECO:0000269|PubMed:15239953, ECO:0000269|PubMed:15548592, ECO:0000269|PubMed:17535814, ECO:0000269|PubMed:23085020}. |
| Q9H0A0 | NAT10 | S675 | ochoa | RNA cytidine acetyltransferase (EC 2.3.1.-) (18S rRNA cytosine acetyltransferase) (N-acetyltransferase 10) (N-acetyltransferase-like protein) (hALP) | RNA cytidine acetyltransferase that catalyzes the formation of N(4)-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs (PubMed:25411247, PubMed:25653167, PubMed:30449621, PubMed:35679869). Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed:30449621, PubMed:35679869). mRNA ac4C modification is frequently present within wobble cytidine sites and promotes translation efficiency (PubMed:30449621). Mediates the formation of ac4C at position 1842 in 18S rRNA (PubMed:25411247). May also catalyze the formation of ac4C at position 1337 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25411247, PubMed:25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMPD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167). In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). The relevance of the protein lysine acetyltransferase activity is however unsure in vivo (PubMed:30449621). Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization (PubMed:14592445, PubMed:18082603). Involved in the regulation of centrosome duplication by acetylating CENATAC during mitosis, promoting SASS6 proteasome degradation (PubMed:31722219). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000250|UniProtKB:P53914, ECO:0000269|PubMed:14592445, ECO:0000269|PubMed:17631499, ECO:0000269|PubMed:18082603, ECO:0000269|PubMed:19303003, ECO:0000269|PubMed:25411247, ECO:0000269|PubMed:25653167, ECO:0000269|PubMed:26882543, ECO:0000269|PubMed:27993683, ECO:0000269|PubMed:30165671, ECO:0000269|PubMed:30449621, ECO:0000269|PubMed:31722219, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:35679869}. |
| Q9H4Z2 | ZNF335 | S1153 | ochoa | Zinc finger protein 335 (NRC-interacting factor 1) (NIF-1) | Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters (PubMed:19131338, PubMed:23178126). Enhances ligand-dependent transcriptional activation by nuclear hormone receptors (PubMed:12215545, PubMed:18180299, PubMed:19131338). Plays an important role in neural progenitor cell proliferation and self-renewal through the regulation of specific genes involved brain development, including REST (PubMed:23178126). Also controls the expression of genes involved in somatic development and regulates, for instance, lymphoblast proliferation (PubMed:23178126). {ECO:0000269|PubMed:12215545, ECO:0000269|PubMed:18180299, ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:23178126}. |
| Q9H814 | PHAX | S226 | ochoa | Phosphorylated adapter RNA export protein (RNA U small nuclear RNA export adapter protein) | A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus (PubMed:39011894). Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Also binds to telomerase RNA. {ECO:0000250, ECO:0000269|PubMed:15574332, ECO:0000269|PubMed:15574333}. |
| Q9NQG5 | RPRD1B | S134 | ochoa | Regulation of nuclear pre-mRNA domain-containing protein 1B (Cell cycle-related and expression-elevated protein in tumor) | Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD by RPAP2. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation. {ECO:0000269|PubMed:22231121, ECO:0000269|PubMed:22264791, ECO:0000269|PubMed:24399136, ECO:0000269|PubMed:24997600}. |
| Q9NQS7 | INCENP | S452 | ochoa | Inner centromere protein | Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with AURKB or AURKC, the N-terminus associated with BIRC5/survivin and CDCA8/borealin tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs AURKB/C toward substrates near microtubules (PubMed:12925766, PubMed:15316025, PubMed:27332895). The flexibility of the SAH domain is proposed to allow AURKB/C to follow substrates on dynamic microtubules while ensuring CPC docking to static chromatin (By similarity). Activates AURKB and AURKC (PubMed:27332895). Required for localization of CBX5 to mitotic centromeres (PubMed:21346195). Controls the kinetochore localization of BUB1 (PubMed:16760428). {ECO:0000250|UniProtKB:P53352, ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:15316025, ECO:0000269|PubMed:16760428, ECO:0000269|PubMed:21346195, ECO:0000269|PubMed:27332895}. |
| Q9NQW6 | ANLN | S419 | ochoa | Anillin | Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis (PubMed:23870127). May play a significant role in podocyte cell migration (PubMed:24676636). {ECO:0000269|PubMed:10931866, ECO:0000269|PubMed:12479805, ECO:0000269|PubMed:15496454, ECO:0000269|PubMed:16040610, ECO:0000269|PubMed:16357138, ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:24676636}. |
| Q9NSG2 | FIRRM | S43 | ochoa|psp | FIGNL1-interacting regulator of recombination and mitosis (FIDGETIN-like-1 interacting protein) (FLIP) (POLO1-associating protein) | Regulates PLK1 kinase activity at kinetochores and promotes faithful chromosome segregation in prometaphase by bridging kinase and phosphatase activities (PubMed:34260926). Phosphorylation of FIRRM by PLK1 negatively regulates its interaction with the phosphatase, PPP1CC, thus creating a negative feedback loop for maintaining proper PLK1 kinase activity during mitosis (PubMed:34260926). In complex with FIGL1 may regulate homologous recombination (PubMed:29608566). {ECO:0000269|PubMed:29608566, ECO:0000269|PubMed:34260926}. |
| Q9P0K7 | RAI14 | S340 | ochoa | Ankycorbin (Ankyrin repeat and coiled-coil structure-containing protein) (Novel retinal pigment epithelial cell protein) (Retinoic acid-induced protein 14) | Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier. {ECO:0000250|UniProtKB:Q5U312}. |
| Q9P0K7 | RAI14 | S520 | ochoa | Ankycorbin (Ankyrin repeat and coiled-coil structure-containing protein) (Novel retinal pigment epithelial cell protein) (Retinoic acid-induced protein 14) | Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier. {ECO:0000250|UniProtKB:Q5U312}. |
| Q9P0K8 | FOXJ2 | S439 | ochoa | Forkhead box protein J2 (Fork head homologous X) | [Isoform FOXJ2.L]: Transcriptional activator. Able to bind to two different type of DNA binding sites. More effective than isoform FOXJ2.S in transcriptional activation (PubMed:10777590, PubMed:10966786). Plays an important role in spermatogenesis, especially in spermatocyte meiosis (By similarity). {ECO:0000250|UniProtKB:Q9ES18, ECO:0000269|PubMed:10777590, ECO:0000269|PubMed:10966786}.; FUNCTION: [Isoform FOXJ2.S]: Transcriptional activator. {ECO:0000269|PubMed:10966786}. |
| Q9P2F6 | ARHGAP20 | S730 | ochoa | Rho GTPase-activating protein 20 (Rho-type GTPase-activating protein 20) | GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. |
| Q9UBS5 | GABBR1 | S879 | ochoa | Gamma-aminobutyric acid type B receptor subunit 1 (GABA-B receptor 1) (GABA-B-R1) (GABA-BR1) (GABABR1) (Gb1) | Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054, PubMed:36103875, PubMed:9872316, PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:18165688). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644, PubMed:10773016, PubMed:10906333, PubMed:24305054, PubMed:9872744). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (PubMed:9844003). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10075644, PubMed:22660477, PubMed:9844003, PubMed:9872316, PubMed:9872744). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (Probable). Activated by (-)-baclofen, cgp27492 and blocked by phaclofen (PubMed:24305054, PubMed:9844003, PubMed:9872316). {ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10773016, ECO:0000269|PubMed:10906333, ECO:0000269|PubMed:15617512, ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477, ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:36103875, ECO:0000269|PubMed:9844003, ECO:0000269|PubMed:9872316, ECO:0000269|PubMed:9872744, ECO:0000305}.; FUNCTION: Isoform 1E may regulate the formation of functional GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This could explain the observation that certain small molecule ligands exhibit differential affinity for central versus peripheral sites. |
| Q9UDT6 | CLIP2 | S352 | ochoa | CAP-Gly domain-containing linker protein 2 (Cytoplasmic linker protein 115) (CLIP-115) (Cytoplasmic linker protein 2) (Williams-Beuren syndrome chromosomal region 3 protein) (Williams-Beuren syndrome chromosomal region 4 protein) | Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations (By similarity). {ECO:0000250}. |
| Q9UGN4 | CD300A | S217 | ochoa | CMRF35-like molecule 8 (CLM-8) (CD300 antigen-like family member A) (CMRF-35-H9) (CMRF35-H9) (CMRF35-H) (IRC1/IRC2) (Immunoglobulin superfamily member 12) (IgSF12) (Inhibitory receptor protein 60) (IRp60) (NK inhibitory receptor) (CD antigen CD300a) | Inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation (PubMed:10746781, PubMed:16339535, PubMed:9701027). Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 but not TRIF through activation of PTPN6 (PubMed:22043923). {ECO:0000269|PubMed:10746781, ECO:0000269|PubMed:16339535, ECO:0000269|PubMed:22043923, ECO:0000269|PubMed:9701027}. |
| Q9UHY7 | ENOPH1 | S154 | ochoa | Enolase-phosphatase E1 (EC 3.1.3.77) (2,3-diketo-5-methylthio-1-phosphopentane phosphatase) (MASA homolog) | Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). {ECO:0000255|HAMAP-Rule:MF_03117, ECO:0000269|PubMed:15843022}. |
| Q9UKL3 | CASP8AP2 | S1326 | ochoa | CASP8-associated protein 2 (FLICE-associated huge protein) | Participates in TNF-alpha-induced blockade of glucocorticoid receptor (GR) transactivation at the nuclear receptor coactivator level, upstream and independently of NF-kappa-B. Suppresses both NCOA2- and NCOA3-induced enhancement of GR transactivation. Involved in TNF-alpha-induced activation of NF-kappa-B via a TRAF2-dependent pathway. Acts as a downstream mediator for CASP8-induced activation of NF-kappa-B. Required for the activation of CASP8 in FAS-mediated apoptosis. Required for histone gene transcription and progression through S phase. {ECO:0000269|PubMed:12477726, ECO:0000269|PubMed:15698540, ECO:0000269|PubMed:17003125, ECO:0000269|PubMed:17245429}. |
| Q9UKX2 | MYH2 | S1267 | ochoa | Myosin-2 (Myosin heavy chain 2) (Myosin heavy chain 2a) (MyHC-2a) (Myosin heavy chain IIa) (MyHC-IIa) (Myosin heavy chain, skeletal muscle, adult 2) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. {ECO:0000250|UniProtKB:P12883}. |
| Q9ULU8 | CADPS | S377 | ochoa | Calcium-dependent secretion activator 1 (Calcium-dependent activator protein for secretion 1) (CAPS-1) | Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates in DCVs-membrane fusion. However, it may also participate in small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering (By similarity). {ECO:0000250}. |
| Q9UPN3 | MACF1 | S1376 | ochoa | Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5 (620 kDa actin-binding protein) (ABP620) (Actin cross-linking family protein 7) (Macrophin-1) (Trabeculin-alpha) | [Isoform 2]: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:15265687, PubMed:20937854). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (PubMed:15265687). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity). As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity). {ECO:0000250|UniProtKB:Q9QXZ0, ECO:0000269|PubMed:15265687, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:27693509}. |
| Q9Y217 | MTMR6 | S556 | ochoa | Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR6 (EC 3.1.3.95) (Myotubularin-related protein 6) (Phosphatidylinositol-3-phosphate phosphatase) | Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate (PubMed:19038970, PubMed:22647598). Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), phosphatidic acid and phosphatidylserine (PubMed:19038970). Negatively regulates ER-Golgi protein transport (By similarity). Probably in association with MTMR9, plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3-phosphate in membrane ruffles (PubMed:24591580). Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4(+) T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3-phosphate (PubMed:15831468). Negatively regulates proliferation of reactivated CD4(+) T-cells (PubMed:16847315). In complex with MTMR9, negatively regulates DNA damage-induced apoptosis (PubMed:19038970, PubMed:22647598). The formation of the MTMR6-MTMR9 complex stabilizes both MTMR6 and MTMR9 protein levels (PubMed:19038970). {ECO:0000250|UniProtKB:A0A0G2JXT6, ECO:0000269|PubMed:15831468, ECO:0000269|PubMed:16847315, ECO:0000269|PubMed:19038970, ECO:0000269|PubMed:22647598, ECO:0000269|PubMed:24591580, ECO:0000305|PubMed:24591580}. |
| Q9Y2J4 | AMOTL2 | S759 | ochoa|psp | Angiomotin-like protein 2 (Leman coiled-coil protein) (LCCP) | Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Plays a role in coupling actin fibers to cell junctions in endothelial cells and is therefore required for correct endothelial cell morphology via facilitating transcellular transmission of mechanical force resulting in endothelial cell elongation (By similarity). Required for the anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane which facilitates organization of radial actin fiber structure and cellular response to contractile forces (PubMed:28842668). This contributes to maintenance of cell area, size, shape, epithelial sheet organization and trophectoderm cell properties that facilitate blastocyst zona hatching (PubMed:28842668). Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. Activates the Hippo signaling pathway in response to cell contact inhibition via interaction with and ubiquitination by Crumbs complex-bound WWP1 (PubMed:34404733). Ubiquitinated AMOTL2 then interacts with LATS2 which in turn phosphorylates YAP1, excluding it from the nucleus and localizing it to the cytoplasm and tight junctions, therefore ultimately repressing YAP1-driven transcription of target genes (PubMed:17293535, PubMed:21205866, PubMed:26598551). Acts to inhibit WWTR1/TAZ transcriptional coactivator activity via sequestering WWTR1/TAZ in the cytoplasm and at tight junctions (PubMed:23911299). Regulates the size and protein composition of the podosome cortex and core at myofibril neuromuscular junctions (PubMed:23525008). Selectively promotes FGF-induced MAPK activation through SRC (PubMed:17293535). May play a role in the polarity, proliferation and migration of endothelial cells. {ECO:0000250|UniProtKB:Q8K371, ECO:0000269|PubMed:17293535, ECO:0000269|PubMed:21205866, ECO:0000269|PubMed:21937427, ECO:0000269|PubMed:22362771, ECO:0000269|PubMed:23525008, ECO:0000269|PubMed:23911299, ECO:0000269|PubMed:26598551, ECO:0000269|PubMed:28842668, ECO:0000269|PubMed:34404733}. |
| Q9Y343 | SNX24 | S116 | ochoa | Sorting nexin-24 | May be involved in several stages of intracellular trafficking. {ECO:0000250}. |
| Q9Y3F4 | STRAP | S219 | ochoa | Serine-threonine kinase receptor-associated protein (MAP activator with WD repeats) (UNR-interacting protein) (WD-40 repeat protein PT-WD) | The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein. {ECO:0000269|PubMed:16251192, ECO:0000269|PubMed:18984161}. |
| Q9Y4B5 | MTCL1 | S345 | ochoa | Microtubule cross-linking factor 1 (Coiled-coil domain-containing protein 165) (PAR-1-interacting protein) (SOGA family member 2) | Microtubule-associated factor involved in the late phase of epithelial polarization and microtubule dynamics regulation (PubMed:23902687). Plays a role in the development and maintenance of non-centrosomal microtubule bundles at the lateral membrane in polarized epithelial cells (PubMed:23902687). Required for faithful chromosome segregation during mitosis (PubMed:33587225). {ECO:0000269|PubMed:23902687, ECO:0000269|PubMed:33587225}. |
| Q9Y4F9 | RIPOR2 | S585 | ochoa | Rho family-interacting cell polarization regulator 2 | Acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization (PubMed:17150207, PubMed:23241886, PubMed:24687993, PubMed:24958875, PubMed:25588844, PubMed:27556504). Inhibits chemokine-induced T lymphocyte responses, such as cell adhesion, polarization and migration (PubMed:23241886). Involved also in the regulation of neutrophil polarization, chemotaxis and adhesion (By similarity). Required for normal development of inner and outer hair cell stereocilia within the cochlea of the inner ear (By similarity). Plays a role for maintaining the structural organization of the basal domain of stereocilia (By similarity). Involved in mechanosensory hair cell function (By similarity). Required for normal hearing (PubMed:24958875). {ECO:0000250|UniProtKB:Q80U16, ECO:0000269|PubMed:17150207, ECO:0000269|PubMed:23241886, ECO:0000269|PubMed:24687993, ECO:0000269|PubMed:24958875, ECO:0000269|PubMed:27556504}.; FUNCTION: [Isoform 2]: Acts as an inhibitor of the small GTPase RHOA (PubMed:25588844). Plays a role in fetal mononuclear myoblast differentiation by promoting filopodia and myotube formation (PubMed:17150207). Maintains naive T lymphocytes in a quiescent state (PubMed:27556504). {ECO:0000269|PubMed:17150207, ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:27556504}. |
| Q9Y616 | IRAK3 | S151 | ochoa | Interleukin-1 receptor-associated kinase 3 (IRAK-3) (IL-1 receptor-associated kinase M) (IRAK-M) (Inactive IL-1 receptor-associated kinase 3) | Putative inactive protein kinase which regulates signaling downstream of immune receptors including IL1R and Toll-like receptors (PubMed:10383454, PubMed:29686383). Inhibits dissociation of IRAK1 and IRAK4 from the Toll-like receptor signaling complex by either inhibiting the phosphorylation of IRAK1 and IRAK4 or stabilizing the receptor complex (By similarity). Upon IL33-induced lung inflammation, positively regulates expression of IL6, CSF3, CXCL2 and CCL5 mRNAs in dendritic cells (PubMed:29686383). {ECO:0000250|UniProtKB:Q8K4B2, ECO:0000269|PubMed:10383454, ECO:0000269|PubMed:29686383}. |
| Q9Y6Q9 | NCOA3 | S1042 | psp | Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (ACTR) (Amplified in breast cancer 1 protein) (AIB-1) (CBP-interacting protein) (pCIP) (Class E basic helix-loop-helix protein 42) (bHLHe42) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (TRAM-1) | Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit. |
| Q9Y6X4 | FAM169A | S350 | ochoa | Soluble lamin-associated protein of 75 kDa (SLAP75) (Protein FAM169A) | None |
| P35579 | MYH9 | S1308 | Sugiyama | Myosin-9 (Cellular myosin heavy chain, type A) (Myosin heavy chain 9) (Myosin heavy chain, non-muscle IIa) (Non-muscle myosin heavy chain A) (NMMHC-A) (Non-muscle myosin heavy chain IIa) (NMMHC II-a) (NMMHC-IIA) | Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Required for cortical actin clearance prior to oocyte exocytosis (By similarity). Promotes cell motility in conjunction with S100A4 (PubMed:16707441). During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (PubMed:20052411). {ECO:0000250|UniProtKB:Q8VDD5, ECO:0000269|PubMed:16707441, ECO:0000269|PubMed:20052411}.; FUNCTION: (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1 envelope glycoprotein B. {ECO:0000269|PubMed:20944748, ECO:0000269|PubMed:39048823}. |
| P33176 | KIF5B | S532 | Sugiyama | Kinesin-1 heavy chain (Conventional kinesin heavy chain) (Ubiquitous kinesin heavy chain) (UKHC) | Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner (By similarity). Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of the cell cycle in a BICD2-dependent manner, antagonizes dynein function and drives the separation of nuclei and centrosomes (PubMed:20386726). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity). Through binding with PLEKHM2 and ARL8B, directs lysosome movement toward microtubule plus ends (Probable). Involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (PubMed:24088571). {ECO:0000250|UniProtKB:Q2PQA9, ECO:0000250|UniProtKB:Q61768, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:24088571, ECO:0000305|PubMed:22172677, ECO:0000305|PubMed:24088571}. |
| Q9UBC2 | EPS15L1 | S479 | Sugiyama | Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R) | Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:9407958}. |
| O00507 | USP9Y | S647 | Sugiyama | Ubiquitin carboxyl-terminal hydrolase 9Y (EC 3.4.19.12) (Deubiquitinating enzyme FAF-Y) (Fat facets protein-related, Y-linked) (Ubiquitin thioesterase FAF-Y) (Ubiquitin-specific protease 9, Y chromosome) (Ubiquitin-specific-processing protease FAF-Y) | Deubiquitinase that mediates deubiquitination of target proteins (PubMed:12895410). May stabilize target proteins that are important for male germ cell development (PubMed:12895410). {ECO:0000269|PubMed:12895410}. |
| O15111 | CHUK | S596 | Sugiyama | Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK-1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA) (Transcription factor 16) (TCF-16) | Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues (PubMed:18626576, PubMed:35952808, PubMed:9244310, PubMed:9252186, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11) (PubMed:21765415). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes (PubMed:20501937). In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Also participates in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities (PubMed:17434128). Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP (PubMed:12789342). Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor (PubMed:15084260). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates AMBRA1 following mitophagy induction, promoting AMBRA1 interaction with ATG8 family proteins and its mitophagic activity (PubMed:30217973). {ECO:0000250|UniProtKB:Q60680, ECO:0000269|PubMed:12789342, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:17434128, ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:20501937, ECO:0000269|PubMed:21765415, ECO:0000269|PubMed:30217973, ECO:0000269|PubMed:35952808, ECO:0000269|PubMed:9244310, ECO:0000269|PubMed:9252186, ECO:0000269|PubMed:9346484, ECO:0000303|PubMed:18626576}. |
| Q8TDY2 | RB1CC1 | S943 | PSP | RB1-inducible coiled-coil protein 1 (FAK family kinase-interacting protein of 200 kDa) (FIP200) | Involved in autophagy (PubMed:21775823). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (By similarity). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (PubMed:10769033, PubMed:12221124). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (By similarity). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:14533007). Plays a crucial role in muscular differentiation (PubMed:12163359). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity). {ECO:0000250|UniProtKB:Q9ESK9, ECO:0000269|PubMed:10769033, ECO:0000269|PubMed:12095676, ECO:0000269|PubMed:12163359, ECO:0000269|PubMed:12221124, ECO:0000269|PubMed:14533007, ECO:0000269|PubMed:21775823, ECO:0000269|PubMed:23392225}. |
| Q5T8P6 | RBM26 | Y822 | Sugiyama | RNA-binding protein 26 (CTCL tumor antigen se70-2) (RNA-binding motif protein 26) | May be involved in the turnover of nuclear polyadenylated (pA+) RNA. {ECO:0000269|PubMed:31950173}. |
| A0AVT1 | UBA6 | S697 | Sugiyama | Ubiquitin-like modifier-activating enzyme 6 (Ubiquitin-activating enzyme 6) (EC 6.2.1.45) (Monocyte protein 4) (MOP-4) (Ubiquitin-activating enzyme E1-like protein 2) (E1-L2) | Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP (PubMed:35970836, PubMed:35986001). Specific for ubiquitin, does not activate ubiquitin-like peptides. Also activates UBD/FAT10 conjugation via adenylation of its C-terminal glycine (PubMed:17889673, PubMed:35970836, PubMed:35986001). Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34. Essential for embryonic development. Isoform 2 may play a key role in ubiquitin system and may influence spermatogenesis and male fertility. {ECO:0000269|PubMed:15202508, ECO:0000269|PubMed:17597759, ECO:0000269|PubMed:17889673, ECO:0000269|PubMed:35970836, ECO:0000269|PubMed:35986001}. |
| Q9Y6K9 | IKBKG | S141 | GPS6 | NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier) | Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor (PubMed:14695475, PubMed:20724660, PubMed:21518757, PubMed:9751060). Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways (PubMed:16547522, PubMed:18287044, PubMed:19033441, PubMed:19185524, PubMed:21606507, PubMed:27777308, PubMed:33567255). Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much higher affinity for linear polyubiquitin (PubMed:16547522, PubMed:18287044, PubMed:19033441, PubMed:19185524, PubMed:21606507, PubMed:27777308). Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3 (PubMed:19854139). Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination (PubMed:20724660). {ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:16547522, ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:19033441, ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20724660, ECO:0000269|PubMed:21518757, ECO:0000269|PubMed:21606507, ECO:0000269|PubMed:27777308, ECO:0000269|PubMed:33567255, ECO:0000269|PubMed:9751060}.; FUNCTION: (Microbial infection) Also considered to be a mediator for HTLV-1 Tax oncoprotein activation of NF-kappa-B. {ECO:0000269|PubMed:10364167, ECO:0000269|PubMed:11064457}. |
| P19525 | EIF2AK2 | S462 | Sugiyama | Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase) | IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (PubMed:18835251, PubMed:19189853, PubMed:19507191, PubMed:21072047, PubMed:21123651, PubMed:22381929, PubMed:22948139, PubMed:23229543). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (PubMed:19189853, PubMed:21123651, PubMed:22948139, PubMed:23229543). Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1) (PubMed:11836380, PubMed:19189853, PubMed:19840259, PubMed:20171114, PubMed:21710204, PubMed:23115276, PubMed:23399035). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11 (PubMed:11836380, PubMed:19229320, PubMed:22214662). In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteasomal degradation (PubMed:20395957). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (PubMed:22948139, PubMed:23084476, PubMed:23372823). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (PubMed:10848580, PubMed:15121867, PubMed:15229216). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (PubMed:20685959). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (PubMed:20685959). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (PubMed:22801494). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (By similarity). {ECO:0000250|UniProtKB:Q03963, ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:11836380, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15229216, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:19189853, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19507191, ECO:0000269|PubMed:19840259, ECO:0000269|PubMed:20171114, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20685959, ECO:0000269|PubMed:21072047, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21710204, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:22381929, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948139, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:23115276, ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:23372823, ECO:0000269|PubMed:23399035, ECO:0000269|PubMed:32197074}. |
| Q92614 | MYO18A | S1465 | Sugiyama | Unconventional myosin-XVIIIa (Molecule associated with JAK3 N-terminus) (MAJN) (Myosin containing a PDZ domain) (Surfactant protein receptor SP-R210) (SP-R210) | May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (PubMed:19837035, PubMed:23345592). Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346). Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:16087679, PubMed:21123169). Strongly enhances natural killer cell cytotoxicity (PubMed:27467939). {ECO:0000250|UniProtKB:Q9JMH9, ECO:0000269|PubMed:16087679, ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:21123169, ECO:0000269|PubMed:23345592, ECO:0000269|PubMed:25965346, ECO:0000269|PubMed:27467939}. |
| Q3V6T2 | CCDC88A | S1172 | Sugiyama | Girdin (Akt phosphorylation enhancer) (APE) (Coiled-coil domain-containing protein 88A) (G alpha-interacting vesicle-associated protein) (GIV) (Girders of actin filament) (Hook-related protein 1) (HkRP1) | Bifunctional modulator of guanine nucleotide-binding proteins (G proteins) (PubMed:19211784, PubMed:27621449). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits (PubMed:19211784, PubMed:21954290, PubMed:23509302, PubMed:25187647). Also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS (PubMed:27621449). Essential for cell migration (PubMed:16139227, PubMed:19211784, PubMed:20462955, PubMed:21954290). Interacts in complex with G(i) alpha subunits with the EGFR receptor, retaining EGFR at the cell membrane following ligand stimulation and promoting EGFR signaling which triggers cell migration (PubMed:20462955). Binding to Gi-alpha subunits displaces the beta and gamma subunits from the heterotrimeric G-protein complex which enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB (PubMed:19211784). Phosphorylation of AKT1/PKB induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation (By similarity). Binds in its tyrosine-phosphorylated form to the phosphatidylinositol 3-kinase (PI3K) regulatory subunit PIK3R1 which enables recruitment of PIK3R1 to the EGFR receptor, enhancing PI3K activity and cell migration (PubMed:21954290). Plays a role as a key modulator of the AKT-mTOR signaling pathway, controlling the tempo of the process of newborn neuron integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Inhibition of G(s) subunit alpha GNAS leads to reduced cellular levels of cAMP and suppression of cell proliferation (PubMed:27621449). Essential for the integrity of the actin cytoskeleton (PubMed:16139227, PubMed:19211784). Required for formation of actin stress fibers and lamellipodia (PubMed:15882442). May be involved in membrane sorting in the early endosome (PubMed:15882442). Plays a role in ciliogenesis and cilium morphology and positioning and this may partly be through regulation of the localization of scaffolding protein CROCC/Rootletin (PubMed:27623382). {ECO:0000250|UniProtKB:Q5SNZ0, ECO:0000269|PubMed:15882442, ECO:0000269|PubMed:16139227, ECO:0000269|PubMed:19211784, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:21954290, ECO:0000269|PubMed:23509302, ECO:0000269|PubMed:25187647, ECO:0000269|PubMed:27621449, ECO:0000269|PubMed:27623382}. |
| P35580 | MYH10 | S1315 | Sugiyama | Myosin-10 (Cellular myosin heavy chain, type B) (Myosin heavy chain 10) (Myosin heavy chain, non-muscle IIb) (Non-muscle myosin heavy chain B) (NMMHC-B) (Non-muscle myosin heavy chain IIb) (NMMHC II-b) (NMMHC-IIB) | Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9. {ECO:0000269|PubMed:20052411, ECO:0000269|PubMed:20603131}.; FUNCTION: (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1 envelope glycoprotein B. {ECO:0000305|PubMed:25428876, ECO:0000305|PubMed:39048823}. |
| Q96K76 | USP47 | S868 | Sugiyama | Ubiquitin carboxyl-terminal hydrolase 47 (EC 3.4.19.12) (Deubiquitinating enzyme 47) (Ubiquitin thioesterase 47) (Ubiquitin-specific-processing protease 47) | Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER). Acts as a regulator of cell growth and genome integrity. May also indirectly regulate CDC25A expression at a transcriptional level. {ECO:0000269|PubMed:19966869, ECO:0000269|PubMed:21362556}. |
| P42261 | GRIA1 | S645 | SIGNOR|iPTMNet | Glutamate receptor 1 (GluR-1) (AMPA-selective glutamate receptor 1) (GluR-A) (GluR-K1) (Glutamate receptor ionotropic, AMPA 1) | Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid (PubMed:1311100, PubMed:20805473, PubMed:21172611, PubMed:28628100, PubMed:35675825). L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse upon entry of monovalent and divalent cations such as sodium and calcium. The receptor then desensitizes rapidly and enters in a transient inactive state, characterized by the presence of bound agonist (By similarity). In the presence of CACNG2 or CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of L-glutamate (PubMed:21172611). Resensitization is blocked by CNIH2 through interaction with CACNG8 in the CACNG8-containing AMPA receptors complex (PubMed:21172611). Calcium (Ca(2+)) permeability depends on subunits composition and, heteromeric channels containing edited GRIA2 subunit are calcium-impermeable. Also permeable to other divalents cations such as strontium(2+) and magnesium(2+) and monovalent cations such as potassium(1+) and lithium(1+) (By similarity). {ECO:0000250|UniProtKB:P19490, ECO:0000269|PubMed:1311100, ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:21172611, ECO:0000269|PubMed:28628100, ECO:0000269|PubMed:35675825}. |
| Q9UNH7 | SNX6 | S343 | Sugiyama | Sorting nexin-6 (TRAF4-associated factor 2) [Cleaved into: Sorting nexin-6, N-terminally processed] | Involved in several stages of intracellular trafficking. Interacts with membranes phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate (Probable). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex (PubMed:19935774). 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 SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Does not have in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptor IGF2R (PubMed:17148574). May function as link between transport vesicles and dynactin (Probable). Negatively regulates retrograde transport of BACE1 from the cell surface to the trans-Golgi network (PubMed:20354142). Involved in E-cadherin sorting and degradation; inhibits PIP5K1C isoform 3-mediated E-cadherin degradation (PubMed:24610942). In association with GIT1 involved in EGFR degradation. Promotes lysosomal degradation of CDKN1B (By similarity). May contribute to transcription regulation (Probable). {ECO:0000250|UniProtKB:Q6P8X1, ECO:0000269|PubMed:17148574, ECO:0000269|PubMed:19935774, ECO:0000269|PubMed:20354142, ECO:0000269|PubMed:23085988, ECO:0000269|PubMed:24610942, ECO:0000303|PubMed:19935774, ECO:0000303|PubMed:20830743, ECO:0000305}. |
| Q8TBC4 | UBA3 | S417 | Sugiyama | NEDD8-activating enzyme E1 catalytic subunit (EC 6.2.1.64) (NEDD8-activating enzyme E1C) (Ubiquitin-activating enzyme E1C) (Ubiquitin-like modifier-activating enzyme 3) (Ubiquitin-activating enzyme 3) | Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression. {ECO:0000269|PubMed:10207026, ECO:0000269|PubMed:12740388, ECO:0000269|PubMed:9694792}. |
| Q9GZM8 | NDEL1 | S162 | PSP | Nuclear distribution protein nudE-like 1 (Protein Nudel) (Mitosin-associated protein 1) | Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts (By similarity). Plays a role, together with DISC1, in the regulation of neurite outgrowth (By similarity). May act as a RAB9A/B effector that tethers RAB9-associated late endosomes to the dynein motor for their retrograde transport to the trans-Golgi network (PubMed:34793709). {ECO:0000250|UniProtKB:Q78PB6, ECO:0000250|UniProtKB:Q9ERR1, ECO:0000269|PubMed:12556484, ECO:0000269|PubMed:14970193, ECO:0000269|PubMed:16291865, ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:34793709}. |
| P30622 | CLIP1 | S1321 | Sugiyama | CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 1) (Cytoplasmic linker protein 170 alpha-2) (CLIP-170) (Reed-Sternberg intermediate filament-associated protein) (Restin) | Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269|PubMed:12433698, ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:17889670}. |
| P30622 | CLIP1 | S1328 | Sugiyama | CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 1) (Cytoplasmic linker protein 170 alpha-2) (CLIP-170) (Reed-Sternberg intermediate filament-associated protein) (Restin) | Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269|PubMed:12433698, ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:17889670}. |
| Q9P2E9 | RRBP1 | S872 | Sugiyama | Ribosome-binding protein 1 (180 kDa ribosome receptor homolog) (RRp) (ES/130-related protein) (Ribosome receptor protein) | Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane. {ECO:0000250}. |
| Q6XUX3 | DSTYK | S291 | Sugiyama | Dual serine/threonine and tyrosine protein kinase (EC 2.7.12.1) (Dusty protein kinase) (Dusty PK) (RIP-homologous kinase) (Receptor-interacting serine/threonine-protein kinase 5) (Sugen kinase 496) (SgK496) | Acts as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation (PubMed:23862974, PubMed:28157540). Involved in the regulation of both caspase-dependent apoptosis and caspase-independent cell death (PubMed:15178406). In the skin, it plays a predominant role in suppressing caspase-dependent apoptosis in response to UV stress in a range of dermal cell types (PubMed:28157540). {ECO:0000269|PubMed:15178406, ECO:0000269|PubMed:23862974, ECO:0000269|PubMed:28157540}. |
| Q8IWW6 | ARHGAP12 | S656 | Sugiyama | Rho GTPase-activating protein 12 (Rho-type GTPase-activating protein 12) | GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. |
| Q14980 | NUMA1 | T1166 | Sugiyama | Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen) | Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250|UniProtKB:E9Q7G0, ECO:0000269|PubMed:11163243, ECO:0000269|PubMed:11229403, ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386, ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:17172455, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23027904, ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901, ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:27462074, ECO:0000269|PubMed:7769006, ECO:0000305|PubMed:10075938, ECO:0000305|PubMed:21816348}. |
| P17275 | JUNB | S312 | Sugiyama | Transcription factor JunB (Transcription factor AP-1 subunit JunB) | Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[GC]TCA-3'. Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to an AP-1 consensus sequence and its transcriptional activity (By similarity). {ECO:0000250|UniProtKB:P09450}. |
| Q9H0H5 | RACGAP1 | S410 | ELM|iPTMNet|EPSD | Rac GTPase-activating protein 1 (Male germ cell RacGap) (MgcRacGAP) (Protein CYK4 homolog) (CYK4) (HsCYK-4) | Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Sequentially binds to ECT2 and RAB11FIP3 which regulates cleavage furrow ingression and abscission during cytokinesis (PubMed:18511905). Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity (PubMed:10979956). Has a critical role in erythropoiesis (PubMed:34818416). Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269|PubMed:10979956, ECO:0000269|PubMed:11085985, ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:11782313, ECO:0000269|PubMed:14729465, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16129829, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:18511905, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:23235882, ECO:0000269|PubMed:9497316}. |
| Q9BQI3 | EIF2AK1 | S151 | Sugiyama | Eukaryotic translation initiation factor 2-alpha kinase 1 (EC 2.7.11.1) (Heme-controlled repressor) (HCR) (Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase) (Heme-regulated inhibitor) (hHRI) (Hemin-sensitive initiation factor 2-alpha kinase) | Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress conditions (PubMed:32132706, PubMed:32132707, PubMed:37327776, PubMed:37550454, PubMed:38340717). Key activator of the integrated stress response (ISR) required for adaptation to various stress, such as heme deficiency, oxidative stress, osmotic shock, mitochondrial dysfunction and heat shock (PubMed:32132706, PubMed:32132707, PubMed:37327776, PubMed:37550454, PubMed:38340717). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming (PubMed:32132706, PubMed:32132707, PubMed:37327776). Acts as a key sensor of heme-deficiency: in normal conditions, binds hemin via a cysteine thiolate and histidine nitrogenous coordination, leading to inhibit the protein kinase activity (By similarity). This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell: heme depletion relieves inhibition and stimulates kinase activity, activating the ISR (By similarity). Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions (By similarity). In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties (By similarity). It thereby plays an essential protective role for RBC survival in anemias of iron deficiency (By similarity). Iron deficiency also triggers activation by full-length DELE1 (PubMed:37327776). Also activates the ISR in response to mitochondrial dysfunction: HRI/EIF2AK1 protein kinase activity is activated upon binding to the processed form of DELE1 (S-DELE1), thereby promoting the ATF4-mediated reprogramming (PubMed:32132706, PubMed:32132707). Also acts as an activator of mitophagy in response to mitochondrial damage: catalyzes phosphorylation of eIF-2-alpha (EIF2S1) following activation by S-DELE1, thereby promoting mitochondrial localization of EIF2S1, triggering PRKN-independent mitophagy (PubMed:38340717). {ECO:0000250|UniProtKB:Q9Z2R9, ECO:0000269|PubMed:32132706, ECO:0000269|PubMed:32132707, ECO:0000269|PubMed:32197074, ECO:0000269|PubMed:37550454, ECO:0000269|PubMed:38340717}. |
| Q15075 | EEA1 | S76 | Sugiyama | Early endosome antigen 1 (Endosome-associated protein p162) (Zinc finger FYVE domain-containing protein 2) | Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking. |
| Q9HBH9 | MKNK2 | S394 | Sugiyama | MAP kinase-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (MAP kinase signal-integrating kinase 2) (MAPK signal-integrating kinase 2) (Mnk2) | Serine/threonine-protein kinase that phosphorylates SFPQ/PSF, HNRNPA1 and EIF4E. May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. Required for mediating PP2A-inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from cytoplasm to nucleus. Isoform 1 displays a high basal kinase activity, but isoform 2 exhibits a very low kinase activity. Acts as a mediator of the suppressive effects of IFNgamma on hematopoiesis. Negative regulator for signals that control generation of arsenic trioxide As(2)O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal. {ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:11463832, ECO:0000269|PubMed:12897141, ECO:0000269|PubMed:16111636, ECO:0000269|PubMed:17965020, ECO:0000269|PubMed:18299328, ECO:0000269|PubMed:20823271, ECO:0000269|PubMed:20927323, ECO:0000269|PubMed:21149447}. |
| O60763 | USO1 | S883 | Sugiyama | General vesicular transport factor p115 (Protein USO1 homolog) (Transcytosis-associated protein) (TAP) (Vesicle-docking protein) | General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity. {ECO:0000250|UniProtKB:P41542}. |
| Q13136 | PPFIA1 | S846 | Sugiyama | Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1) | May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269|PubMed:7796809}. |
| A0A0G2JPF8 | HNRNPCL4 | S196 | ochoa | Heterogeneous nuclear ribonucleoprotein C like 4 | None |
| A6H8Y1 | BDP1 | S938 | ochoa | Transcription factor TFIIIB component B'' homolog (Transcription factor IIIB 150) (TFIIIB150) (Transcription factor-like nuclear regulator) | General activator of RNA polymerase III transcription. Requires for transcription from all three types of polymerase III promoters. Requires for transcription of genes with internal promoter elements and with promoter elements upstream of the initiation site. {ECO:0000269|PubMed:11040218}. |
| A6NMY6 | ANXA2P2 | Y109 | 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}. |
| A8K0Z3 | WASHC1 | S219 | ochoa | WASH complex subunit 1 (CXYorf1-like protein on chromosome 9) (Protein FAM39E) (WAS protein family homolog 1) | Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922874, PubMed:19922875, PubMed:20498093, PubMed:23452853). Involved in endocytic trafficking of EGF (By similarity). Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (PubMed:22114305). In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation (By similarity). Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling. Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (PubMed:24344185). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). {ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8, ECO:0000269|PubMed:19922874, ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093, ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:23452853, ECO:0000305|PubMed:20498093}. |
| A8MWX3 | WASH4P | S232 | ochoa | Putative WAS protein family homolog 4 (Protein FAM39CP) | May act as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7}. |
| B2RXH8 | HNRNPCL2 | S196 | ochoa | Heterogeneous nuclear ribonucleoprotein C-like 2 (hnRNP C-like-2) | May play a role in nucleosome assembly by neutralizing basic proteins such as A and B core hnRNPs. {ECO:0000250}. |
| B7ZW38 | HNRNPCL3 | S196 | ochoa | Heterogeneous nuclear ribonucleoprotein C-like 3 | None |
| C4AMC7 | WASH3P | S217 | ochoa | Putative WAS protein family homolog 3 (Protein FAM39DP) | Acts as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:18159949, PubMed:20175130). Involved in endocytic trafficking of EGF (PubMed:20175130). Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (By similarity). In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling (By similarity). Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (By similarity). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:Q8VDD8, ECO:0000269|PubMed:18159949, ECO:0000269|PubMed:20175130}. |
| O14775 | GNB5 | S63 | ochoa | Guanine nucleotide-binding protein subunit beta-5 (Gbeta5) (Transducin beta chain 5) | Enhances GTPase-activating protein (GAP) activity of regulator of G protein signaling (RGS) proteins, such as RGS7 and RGS9, hence involved in the termination of the signaling initiated by the G protein coupled receptors (GPCRs) by accelerating the GTP hydrolysis on the G-alpha subunits, thereby promoting their inactivation (PubMed:27677260). Increases RGS7 GTPase-activating protein (GAP) activity, thereby regulating mood and cognition (By similarity). Increases RGS9 GTPase-activating protein (GAP) activity, hence contributes to the deactivation of G protein signaling initiated by D(2) dopamine receptors (PubMed:27677260). May play an important role in neuronal signaling, including in the parasympathetic, but not sympathetic, control of heart rate (By similarity). {ECO:0000250|UniProtKB:A1L271, ECO:0000250|UniProtKB:P62881, ECO:0000269|PubMed:27677260}. |
| O15085 | ARHGEF11 | S232 | ochoa | Rho guanine nucleotide exchange factor 11 (PDZ-RhoGEF) | May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:0000269|PubMed:21670212}. |
| O15360 | FANCA | S165 | psp | Fanconi anemia group A protein (Protein FACA) | DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be involved in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. |
| O15400 | STX7 | S173 | 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. |
| O15503 | INSIG1 | S209 | psp | Insulin-induced gene 1 protein (INSIG-1) | Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR (PubMed:12202038, PubMed:12535518, PubMed:16168377, PubMed:16399501, PubMed:16606821, PubMed:32322062). Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:12202038, PubMed:16399501, PubMed:26311497, PubMed:32322062). Binds oxysterol, including 25-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum (PubMed:32322062). In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi (PubMed:15899885, PubMed:32322062). Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG1 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:26311497, PubMed:32322062). Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligases AMFR/gp78 and/or RNF139 (PubMed:12535518, PubMed:16168377, PubMed:22143767). Also regulates degradation of SOAT2/ACAT2 when the lipid levels are low: initiates the ubiquitin-mediated degradation of SOAT2/ACAT2 via recruitment of the ubiquitin ligases AMFR/gp78 (PubMed:28604676). {ECO:0000269|PubMed:12202038, ECO:0000269|PubMed:12535518, ECO:0000269|PubMed:15899885, ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:16399501, ECO:0000269|PubMed:16606821, ECO:0000269|PubMed:22143767, ECO:0000269|PubMed:26311497, ECO:0000269|PubMed:28604676, ECO:0000269|PubMed:32322062}. |
| O15553 | MEFV | S242 | ochoa|psp | Pyrin (Marenostrin) | Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma (PubMed:10807793, PubMed:11468188, PubMed:16037825, PubMed:16785446, PubMed:17431422, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923, PubMed:26347139, PubMed:27030597, PubMed:28835462). Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy (PubMed:16785446, PubMed:17431422, PubMed:26347139). Acts as an autophagy receptor for the degradation of several inflammasome components, including CASP1, NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18-mediated inflammation (PubMed:16785446, PubMed:17431422, PubMed:26347139). However, it can also have a positive effect in the inflammatory pathway, acting as an innate immune sensor that triggers PYCARD/ASC specks formation, caspase-1 activation, and IL1B and IL18 production (PubMed:16037825, PubMed:27030597, PubMed:28835462). Together with AIM2, also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). It is required for PSTPIP1-induced PYCARD/ASC oligomerization and inflammasome formation (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). Recruits PSTPIP1 to inflammasomes, and is required for PSTPIP1 oligomerization (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). {ECO:0000250|UniProtKB:Q9JJ26, ECO:0000269|PubMed:10807793, ECO:0000269|PubMed:11468188, ECO:0000269|PubMed:16037825, ECO:0000269|PubMed:16785446, ECO:0000269|PubMed:17431422, ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18577712, ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:26347139, ECO:0000269|PubMed:27030597, ECO:0000269|PubMed:28835462}. |
| O43264 | ZW10 | S356 | ochoa | Centromere/kinetochore protein zw10 homolog | Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (PubMed:11590237, PubMed:15485811, PubMed:15824131). Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:15029241). {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15029241, ECO:0000269|PubMed:15094189, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131, ECO:0000305}. |
| O43353 | RIPK2 | S485 | ochoa | Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (CARD-containing interleukin-1 beta-converting enzyme-associated kinase) (CARD-containing IL-1 beta ICE-kinase) (RIP-like-interacting CLARP kinase) (Receptor-interacting protein 2) (RIP-2) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2) | Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:14638696, PubMed:17054981, PubMed:21123652, PubMed:28656966, PubMed:9575181, PubMed:9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17054981, PubMed:17562858, PubMed:21123652, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed:22607974, PubMed:28545134, PubMed:29452636, PubMed:30026309, PubMed:30279485, PubMed:30478312). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:17562858, PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed:18079694). In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18079694). The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed:29452636, PubMed:30026309). Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed:21887730). Also involved in adaptive immunity: plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed:14638696). Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed:26646181). {ECO:0000269|PubMed:14638696, ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:17562858, ECO:0000269|PubMed:18079694, ECO:0000269|PubMed:21123652, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:22607974, ECO:0000269|PubMed:26646181, ECO:0000269|PubMed:28545134, ECO:0000269|PubMed:28656966, ECO:0000269|PubMed:29452636, ECO:0000269|PubMed:30026309, ECO:0000269|PubMed:30279485, ECO:0000269|PubMed:30478312, ECO:0000269|PubMed:9575181, ECO:0000269|PubMed:9642260}. |
| O43379 | WDR62 | S1048 | ochoa | WD repeat-containing protein 62 | Required for cerebral cortical development. Plays a role in neuronal proliferation and migration (PubMed:20729831, PubMed:20890278). Plays a role in mother-centriole-dependent centriole duplication; the function also seems to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:26297806}. |
| O43379 | WDR62 | S1101 | ochoa | WD repeat-containing protein 62 | Required for cerebral cortical development. Plays a role in neuronal proliferation and migration (PubMed:20729831, PubMed:20890278). Plays a role in mother-centriole-dependent centriole duplication; the function also seems to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:26297806}. |
| O43379 | WDR62 | S1436 | ochoa | WD repeat-containing protein 62 | Required for cerebral cortical development. Plays a role in neuronal proliferation and migration (PubMed:20729831, PubMed:20890278). Plays a role in mother-centriole-dependent centriole duplication; the function also seems to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:26297806}. |
| O43663 | PRC1 | S472 | ochoa | Protein regulator of cytokinesis 1 | Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436). {ECO:0000269|PubMed:12082078, ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:17409436, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:20691902, ECO:0000269|PubMed:9885575}. |
| O60271 | SPAG9 | S183 | ochoa | C-Jun-amino-terminal kinase-interacting protein 4 (JIP-4) (JNK-interacting protein 4) (Cancer/testis antigen 89) (CT89) (Human lung cancer oncogene 6 protein) (HLC-6) (JNK-associated leucine-zipper protein) (JLP) (Mitogen-activated protein kinase 8-interacting protein 4) (Proliferation-inducing protein 6) (Protein highly expressed in testis) (PHET) (Sperm surface protein) (Sperm-associated antigen 9) (Sperm-specific protein) (Sunday driver 1) | The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module (PubMed:14743216). Regulates lysosomal positioning by acting as an adapter protein which links PIP4P1-positive lysosomes to the dynein-dynactin complex (PubMed:29146937). Assists PIKFYVE selective functionality in microtubule-based endosome-to-TGN trafficking (By similarity). {ECO:0000250|UniProtKB:Q58A65, ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:29146937}. |
| O60563 | CCNT1 | S352 | ochoa | Cyclin-T1 (CycT1) (Cyclin-T) | Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II) (PubMed:16109376, PubMed:16109377, PubMed:30134174, PubMed:35393539). Required to activate the protein kinase activity of CDK9: acts by mediating formation of liquid-liquid phase separation (LLPS) that enhances binding of P-TEFb to the CTD of RNA Pol II (PubMed:29849146, PubMed:35393539). {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:29849146, ECO:0000269|PubMed:30134174, ECO:0000269|PubMed:35393539}.; FUNCTION: (Microbial infection) In case of HIV or SIV infections, binds to the transactivation domain of the viral nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA Pol II activation, allowing transcription of viral genes. {ECO:0000269|PubMed:10329125, ECO:0000269|PubMed:10329126}. |
| O60664 | PLIN3 | S91 | ochoa | Perilipin-3 (47 kDa mannose 6-phosphate receptor-binding protein) (47 kDa MPR-binding protein) (Cargo selection protein TIP47) (Mannose-6-phosphate receptor-binding protein 1) (Placental protein 17) (PP17) | Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets (PubMed:34077757). Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network (PubMed:9590177). {ECO:0000269|PubMed:34077757, ECO:0000269|PubMed:9590177}. |
| O60812 | HNRNPCL1 | S196 | ochoa | Heterogeneous nuclear ribonucleoprotein C-like 1 (hnRNP C-like-1) (hnRNP core protein C-like 1) | May play a role in nucleosome assembly by neutralizing basic proteins such as A and B core hnRNPs. {ECO:0000250}. |
| O76003 | GLRX3 | S117 | ochoa | Glutaredoxin-3 (PKC-interacting cousin of thioredoxin) (PICOT) (PKC-theta-interacting protein) (PKCq-interacting protein) (Thioredoxin-like protein 2) | Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins (PubMed:26613676, PubMed:27519415). Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). Required for hemoglobin maturation (PubMed:23615448). Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity. {ECO:0000250|UniProtKB:Q9CQM9, ECO:0000269|PubMed:23615448, ECO:0000269|PubMed:26613676, ECO:0000269|PubMed:27519415}. |
| O94885 | SASH1 | S743 | ochoa | SAM and SH3 domain-containing protein 1 (Proline-glutamate repeat-containing protein) | Is a positive regulator of NF-kappa-B signaling downstream of TLR4 activation. It acts as a scaffold molecule to assemble a molecular complex that includes TRAF6, MAP3K7, CHUK and IKBKB, thereby facilitating NF-kappa-B signaling activation (PubMed:23776175). Regulates TRAF6 and MAP3K7 ubiquitination (PubMed:23776175). Involved in the regulation of cell mobility (PubMed:23333244, PubMed:23776175, PubMed:25315659). Regulates lipolysaccharide (LPS)-induced endothelial cell migration (PubMed:23776175). Is involved in the regulation of skin pigmentation through the control of melanocyte migration in the epidermis (PubMed:23333244). {ECO:0000269|PubMed:23333244, ECO:0000269|PubMed:23776175, ECO:0000269|PubMed:25315659}. |
| O94887 | FARP2 | S27 | ochoa | FERM, ARHGEF and pleckstrin domain-containing protein 2 (FERM domain-including RhoGEF) (FIR) (FERM, RhoGEF and pleckstrin domain-containing protein 2) (Pleckstrin homology domain-containing family C member 3) (PH domain-containing family C member 3) | Functions as a guanine nucleotide exchange factor that activates RAC1. May have relatively low activity. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton. Plays a role in TNFSF11-mediated osteoclast differentiation, especially in podosome rearrangement and reorganization of the actin cytoskeleton. Regulates the activation of ITGB3, integrin signaling and cell adhesion (By similarity). {ECO:0000250}. |
| O95155 | UBE4B | S1256 | ochoa | Ubiquitin conjugation factor E4 B (EC 2.3.2.27) (Homozygously deleted in neuroblastoma 1) (RING-type E3 ubiquitin transferase E4 B) (Ubiquitin fusion degradation protein 2) | Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases (By similarity). May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00, ECO:0000269|PubMed:17369820}. |
| O95239 | KIF4A | S941 | ochoa | Chromosome-associated kinesin KIF4A (Chromokinesin-A) | Iron-sulfur (Fe-S) cluster binding motor protein that has a role in chromosome segregation during mitosis (PubMed:29848660). Translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis (PubMed:15297875, PubMed:15625105). May play a role in mitotic chromosomal positioning and bipolar spindle stabilization (By similarity). {ECO:0000250|UniProtKB:P33174, ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:29848660}. |
| O95466 | FMNL1 | S921 | ochoa | Formin-like protein 1 (CLL-associated antigen KW-13) (Leukocyte formin) | May play a role in the control of cell motility and survival of macrophages (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. {ECO:0000250, ECO:0000269|PubMed:21834987}. |
| O95613 | PCNT | S682 | ochoa | Pericentrin (Kendrin) (Pericentrin-B) | Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome. {ECO:0000269|PubMed:10823944, ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:20599736, ECO:0000269|PubMed:30420784}. |
| O95613 | PCNT | S3014 | ochoa | Pericentrin (Kendrin) (Pericentrin-B) | Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome. {ECO:0000269|PubMed:10823944, ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:20599736, ECO:0000269|PubMed:30420784}. |
| O96017 | CHEK2 | S372 | psp | Serine/threonine-protein kinase Chk2 (EC 2.7.11.1) (CHK2 checkpoint homolog) (Cds1 homolog) (Hucds1) (hCds1) (Checkpoint kinase 2) | Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest, activation of DNA repair and apoptosis in response to the presence of DNA double-strand breaks. May also negatively regulate cell cycle progression during unperturbed cell cycles. Following activation, phosphorylates numerous effectors preferentially at the consensus sequence [L-X-R-X-X-S/T] (PubMed:37943659). Regulates cell cycle checkpoint arrest through phosphorylation of CDC25A, CDC25B and CDC25C, inhibiting their activity. Inhibition of CDC25 phosphatase activity leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. May also phosphorylate NEK6 which is involved in G2/M cell cycle arrest. Regulates DNA repair through phosphorylation of BRCA2, enhancing the association of RAD51 with chromatin which promotes DNA repair by homologous recombination. Also stimulates the transcription of genes involved in DNA repair (including BRCA2) through the phosphorylation and activation of the transcription factor FOXM1. Regulates apoptosis through the phosphorylation of p53/TP53, MDM4 and PML. Phosphorylation of p53/TP53 at 'Ser-20' by CHEK2 may alleviate inhibition by MDM2, leading to accumulation of active p53/TP53. Phosphorylation of MDM4 may also reduce degradation of p53/TP53. Also controls the transcription of pro-apoptotic genes through phosphorylation of the transcription factor E2F1. Tumor suppressor, it may also have a DNA damage-independent function in mitotic spindle assembly by phosphorylating BRCA1. Its absence may be a cause of the chromosomal instability observed in some cancer cells. Promotes the CCAR2-SIRT1 association and is required for CCAR2-mediated SIRT1 inhibition (PubMed:25361978). Under oxidative stress, promotes ATG7 ubiquitination by phosphorylating the E3 ubiquitin ligase TRIM32 at 'Ser-55' leading to positive regulation of the autophagosme assembly (PubMed:37943659). {ECO:0000250|UniProtKB:Q9Z265, ECO:0000269|PubMed:10097108, ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:11298456, ECO:0000269|PubMed:12402044, ECO:0000269|PubMed:12607004, ECO:0000269|PubMed:12717439, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:16163388, ECO:0000269|PubMed:17101782, ECO:0000269|PubMed:17380128, ECO:0000269|PubMed:17715138, ECO:0000269|PubMed:18317453, ECO:0000269|PubMed:18644861, ECO:0000269|PubMed:18728393, ECO:0000269|PubMed:20364141, ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:25619829, ECO:0000269|PubMed:37943659, ECO:0000269|PubMed:9836640, ECO:0000269|PubMed:9889122}.; FUNCTION: (Microbial infection) Phosphorylates herpes simplex virus 1/HHV-1 protein ICP0 and thus activates its SUMO-targeted ubiquitin ligase activity. {ECO:0000269|PubMed:32001251}. |
| P00736 | C1R | S206 | psp | Complement C1r subcomponent (EC 3.4.21.41) (Complement component 1 subcomponent r) [Cleaved into: Complement C1r subcomponent heavy chain (Complement C1r subcomponent chain A); Complement C1r subcomponent light chain (Complement C1r subcomponent chain B)] | Serine protease component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:17996945, PubMed:19473974, PubMed:29449492). C1R catalyzes the first enzymatic step in the classical complement pathway: it is activated by the C1Q subcomplex of the C1 complex, which associates with IgG or IgM immunoglobulins complexed with antigens to form antigen-antibody complexes on the surface of pathogens (PubMed:29449492, PubMed:34155115). Immunoglobulin-binding promotes the autocatalytic cleavage and activation of C1R (PubMed:11445589, PubMed:11673533, PubMed:17996945, PubMed:20178990, PubMed:6254570, PubMed:6271784). Activated C1R then cleaves and activates C1S, the second protease of the classical complement pathway (PubMed:11445589, PubMed:11673533, PubMed:6271784). It is unclear if C1R activates C1S within single, strained C1 complexes or between neighboring C1 complexes on surfaces (PubMed:28104818, PubMed:29311313, PubMed:29449492). {ECO:0000269|PubMed:11445589, ECO:0000269|PubMed:11673533, ECO:0000269|PubMed:17996945, ECO:0000269|PubMed:19473974, ECO:0000269|PubMed:20178990, ECO:0000269|PubMed:28104818, ECO:0000269|PubMed:29311313, ECO:0000269|PubMed:29449492, ECO:0000269|PubMed:34155115, ECO:0000269|PubMed:6254570, ECO:0000269|PubMed:6271784}. |
| P02042 | HBD | S87 | ochoa | Hemoglobin subunit delta (Delta-globin) (Hemoglobin delta chain) | Involved in oxygen transport from the lung to the various peripheral tissues. |
| P04843 | RPN1 | S528 | ochoa | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit) (Ribophorin I) (RPN-I) (Ribophorin-1) | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). {ECO:0000250|UniProtKB:E2RQ08, ECO:0000269|PubMed:31831667, ECO:0000269|PubMed:39567208}. |
| P05023 | ATP1A1 | S499 | ochoa | Sodium/potassium-transporting ATPase subunit alpha-1 (Na(+)/K(+) ATPase alpha-1 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-1) | This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (PubMed:29499166, PubMed:30388404). Could also be part of an osmosensory signaling pathway that senses body-fluid sodium levels and controls salt intake behavior as well as voluntary water intake to regulate sodium homeostasis (By similarity). {ECO:0000250|UniProtKB:Q8VDN2, ECO:0000269|PubMed:29499166, ECO:0000269|PubMed:30388404}. |
| P05783 | KRT18 | S305 | 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 | S319 | 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 | S567 | 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}. |
| P06753 | TPM3 | S189 | ochoa | Tropomyosin alpha-3 chain (Gamma-tropomyosin) (Tropomyosin-3) (Tropomyosin-5) (hTM5) | Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. {ECO:0000250|UniProtKB:P09493}. |
| P07355 | ANXA2 | Y109 | 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}. |
| P07900 | HSP90AA1 | S391 | 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}. |
| P07910 | HNRNPC | S209 | ochoa | Heterogeneous nuclear ribonucleoproteins C1/C2 (hnRNP C1/C2) | Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides (PubMed:8264621). May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671). {ECO:0000269|PubMed:12509468, ECO:0000269|PubMed:16010978, ECO:0000269|PubMed:25719671, ECO:0000269|PubMed:7567451, ECO:0000269|PubMed:8264621}. |
| P08670 | VIM | S144 | 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}. |
| P09382 | LGALS1 | S30 | ochoa | Galectin-1 (Gal-1) (14 kDa laminin-binding protein) (HLBP14) (14 kDa lectin) (Beta-galactoside-binding lectin L-14-I) (Galaptin) (HBL) (HPL) (Lactose-binding lectin 1) (Lectin galactoside-binding soluble 1) (Putative MAPK-activating protein PM12) (S-Lac lectin 1) | Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. Plays a negative role in Th17 cell differentiation via activation of the receptor CD69 (PubMed:24752896). {ECO:0000269|PubMed:14617626, ECO:0000269|PubMed:18796645, ECO:0000269|PubMed:19497882, ECO:0000269|PubMed:24752896, ECO:0000269|PubMed:24945728}. |
| P09874 | PARP1 | S274 | ochoa | Poly [ADP-ribose] polymerase 1 (PARP-1) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 1) (ARTD1) (DNA ADP-ribosyltransferase PARP1) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 1) (ADPRT 1) (Poly[ADP-ribose] synthase 1) (Protein poly-ADP-ribosyltransferase PARP1) (EC 2.4.2.-) [Cleaved into: Poly [ADP-ribose] polymerase 1, processed C-terminus (Poly [ADP-ribose] polymerase 1, 89-kDa form); Poly [ADP-ribose] polymerase 1, processed N-terminus (NT-PARP-1) (Poly [ADP-ribose] polymerase 1, 24-kDa form) (Poly [ADP-ribose] polymerase 1, 28-kDa form)] | Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:17177976, PubMed:18055453, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:20388712, PubMed:21680843, PubMed:22582261, PubMed:23230272, PubMed:25043379, PubMed:26344098, PubMed:26626479, PubMed:26626480, PubMed:30104678, PubMed:31796734, PubMed:32028527, PubMed:32241924, PubMed:32358582, PubMed:33186521, PubMed:34465625, PubMed:34737271). Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed:19764761, PubMed:25043379, PubMed:28190768, PubMed:29954836, PubMed:35393539, PubMed:7852410, PubMed:9315851). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:33186521, PubMed:34874266). Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 (PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33186521, PubMed:33589610, PubMed:34625544, PubMed:34874266). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site (PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33186521, PubMed:33589610, PubMed:34625544, PubMed:34874266). Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (PubMed:29954836, PubMed:30257210). Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity (By similarity). PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272, PubMed:27067600, PubMed:34465625, PubMed:34874266). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains (PubMed:33683197, PubMed:34732825, PubMed:34795260). In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation (PubMed:26344098, PubMed:30356214). Mediates the poly-ADP-ribosylation of a number of proteins, including itself, APLF, CHFR, RPA1 and NFAT5 (PubMed:17396150, PubMed:19764761, PubMed:24906880, PubMed:34049076). In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively (PubMed:27471034). Required for PARP9 and DTX3L recruitment to DNA damage sites (PubMed:23230272). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272). PARP1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity (PubMed:15607977, PubMed:17177976, PubMed:19344625, PubMed:27256882, PubMed:32315358, PubMed:32844745, PubMed:35124853, PubMed:35393539, PubMed:35460603). Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II (PubMed:15607977, PubMed:22464733). Acts both as a positive and negative regulator of transcription elongation, depending on the context (PubMed:27256882, PubMed:35393539). Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing (PubMed:27256882). Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9 (PubMed:35393539). Involved in replication fork progression following interaction with CARM1: mediates poly-ADP-ribosylation at replication forks, slowing fork progression (PubMed:33412112). Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos (By similarity). Also acts as a negative regulator of the cGAS-STING pathway (PubMed:32315358, PubMed:32844745, PubMed:35460603). Acts by mediating poly-ADP-ribosylation of CGAS: PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS (PubMed:35460603). Acts as a negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). {ECO:0000250|UniProtKB:P11103, ECO:0000269|PubMed:15607977, ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:18055453, ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19344625, ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:19764761, ECO:0000269|PubMed:20388712, ECO:0000269|PubMed:21680843, ECO:0000269|PubMed:22464733, ECO:0000269|PubMed:22582261, ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:24906880, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:26344098, ECO:0000269|PubMed:26626479, ECO:0000269|PubMed:26626480, ECO:0000269|PubMed:27067600, ECO:0000269|PubMed:27256882, ECO:0000269|PubMed:27257257, ECO:0000269|PubMed:27471034, ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:30104678, ECO:0000269|PubMed:30257210, ECO:0000269|PubMed:30356214, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32028527, ECO:0000269|PubMed:32241924, ECO:0000269|PubMed:32315358, ECO:0000269|PubMed:32358582, ECO:0000269|PubMed:32844745, ECO:0000269|PubMed:33186521, ECO:0000269|PubMed:33412112, ECO:0000269|PubMed:33589610, ECO:0000269|PubMed:33683197, ECO:0000269|PubMed:34049076, ECO:0000269|PubMed:34465625, ECO:0000269|PubMed:34625544, ECO:0000269|PubMed:34732825, ECO:0000269|PubMed:34737271, ECO:0000269|PubMed:34795260, ECO:0000269|PubMed:34874266, ECO:0000269|PubMed:35124853, ECO:0000269|PubMed:35393539, ECO:0000269|PubMed:35460603, ECO:0000269|PubMed:7852410, ECO:0000269|PubMed:9315851}.; FUNCTION: [Poly [ADP-ribose] polymerase 1, processed C-terminus]: Promotes AIFM1-mediated apoptosis (PubMed:33168626). This form, which translocates into the cytoplasm following cleavage by caspase-3 (CASP3) and caspase-7 (CASP7) in response to apoptosis, is auto-poly-ADP-ribosylated and serves as a poly-ADP-ribose carrier to induce AIFM1-mediated apoptosis (PubMed:33168626). {ECO:0000269|PubMed:33168626}.; FUNCTION: [Poly [ADP-ribose] polymerase 1, processed N-terminus]: This cleavage form irreversibly binds to DNA breaks and interferes with DNA repair, promoting DNA damage-induced apoptosis. {ECO:0000269|PubMed:35104452}. |
| P0DMR1 | HNRNPCL4 | S196 | ochoa | Heterogeneous nuclear ribonucleoprotein C-like 4 | None |
| P10114 | RAP2A | S129 | ochoa | Ras-related protein Rap-2a (EC 3.6.5.2) (RbBP-30) | Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form (PubMed:14966141, PubMed:15342639, PubMed:16246175, PubMed:16540189, PubMed:18930710, PubMed:20159449, PubMed:35293963). In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK (PubMed:14966141, PubMed:15342639, PubMed:18930710, PubMed:20159449). Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development (PubMed:20159449). More generally, it is part of several signaling cascades and regulates cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading (PubMed:14966141, PubMed:15342639, PubMed:16246175, PubMed:16540189, PubMed:18930710, PubMed:20159449, PubMed:35293963). {ECO:0000269|PubMed:14966141, ECO:0000269|PubMed:15342639, ECO:0000269|PubMed:16246175, ECO:0000269|PubMed:16540189, ECO:0000269|PubMed:18930710, ECO:0000269|PubMed:20159449, ECO:0000269|PubMed:35293963}. |
| P11055 | MYH3 | S1477 | ochoa | Myosin-3 (Muscle embryonic myosin heavy chain) (Myosin heavy chain 3) (Myosin heavy chain, fast skeletal muscle, embryonic) (SMHCE) | Muscle contraction. |
| P11277 | SPTB | S1829 | ochoa | Spectrin beta chain, erythrocytic (Beta-I spectrin) | Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. |
| P12270 | TPR | S1495 | ochoa | Nucleoprotein TPR (Megator) (NPC-associated intranuclear protein) (Translocated promoter region protein) | Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:11952838, PubMed:22253824). Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases. {ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:18794356, ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:20407419, ECO:0000269|PubMed:21613532, ECO:0000269|PubMed:22253824, ECO:0000269|PubMed:9864356}. |
| P12882 | MYH1 | S1480 | ochoa | Myosin-1 (Myosin heavy chain 1) (Myosin heavy chain 2x) (MyHC-2x) (Myosin heavy chain IIx/d) (MyHC-IIx/d) (Myosin heavy chain, skeletal muscle, adult 1) | Required for normal hearing. It plays a role in cochlear amplification of auditory stimuli, likely through the positive regulation of prestin (SLC26A5) activity and outer hair cell (OHC) electromotility. {ECO:0000250|UniProtKB:Q5SX40}. |
| P12883 | MYH7 | S1476 | ochoa | Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000305|PubMed:26150528, ECO:0000305|PubMed:26246073}. |
| P13533 | MYH6 | S1478 | ochoa | Myosin-6 (Myosin heavy chain 6) (Myosin heavy chain, cardiac muscle alpha isoform) (MyHC-alpha) | Muscle contraction. |
| P13535 | MYH8 | S1479 | ochoa | Myosin-8 (Myosin heavy chain 8) (Myosin heavy chain, skeletal muscle, perinatal) (MyHC-perinatal) | Muscle contraction. |
| P13688 | CEACAM1 | S461 | psp | Cell adhesion molecule CEACAM1 (Biliary glycoprotein 1) (BGP-1) (Carcinoembryonic antigen-related cell adhesion molecule 1) (CEA cell adhesion molecule 1) (CD antigen CD66a) | [Isoform 1]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and also functions as an activator during angiogenesis (PubMed:18424730, PubMed:23696226, PubMed:25363763). Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors. Plays a role in immune response, of T cells, natural killer (NK) and neutrophils (PubMed:18424730, PubMed:23696226). Upon TCR/CD3 complex stimulation, inhibits TCR-mediated cytotoxicity by blocking granule exocytosis by mediating homophilic binding to adjacent cells, allowing interaction with and phosphorylation by LCK and interaction with the TCR/CD3 complex which recruits PTPN6 resulting in dephosphorylation of CD247 and ZAP70 (PubMed:18424730). Also inhibits T cell proliferation and cytokine production through inhibition of JNK cascade and plays a crucial role in regulating autoimmunity and anti-tumor immunity by inhibiting T cell through its interaction with HAVCR2 (PubMed:25363763). Upon natural killer (NK) cells activation, inhibit KLRK1-mediated cytolysis of CEACAM1-bearing tumor cells by trans-homophilic interactions with CEACAM1 on the target cell and lead to cis-interaction between CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1 dephosphorylation (PubMed:23696226). Upon neutrophils activation negatively regulates IL1B production by recruiting PTPN6 to a SYK-TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome. Down-regulates neutrophil production by acting as a coinhibitory receptor for CSF3R by down-regulating the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (By similarity). Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (By similarity). Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis. This inernalization promotes interaction with FASN leading to receptor-mediated insulin degradation and to reduction of FASN activity leading to negative regulation of fatty acid synthesis. INSR-mediated phosphorylation also provokes a down-regulation of cell proliferation through SHC1 interaction resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways (By similarity). Functions as activator in angiogenesis by promoting blood vessel remodeling through endothelial cell differentiation and migration and in arteriogenesis by increasing the number of collateral arteries and collateral vessel calibers after ischemia. Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (By similarity). Down-regulates cell growth in response to EGF through its interaction with SHC1 that mediates interaction with EGFR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (By similarity). Negatively regulates platelet aggregation by decreasing platelet adhesion on type I collagen through the GPVI-FcRgamma complex (By similarity). Inhibits cell migration and cell scattering through interaction with FLNA; interferes with the interaction of FLNA with RALA (PubMed:16291724). Mediates bile acid transport activity in a phosphorylation dependent manner (By similarity). Negatively regulates osteoclastogenesis (By similarity). {ECO:0000250|UniProtKB:P16573, ECO:0000250|UniProtKB:P31809, ECO:0000269|PubMed:16291724, ECO:0000269|PubMed:18424730, ECO:0000269|PubMed:23696226, ECO:0000269|PubMed:25363763}.; FUNCTION: [Isoform 8]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Promotes populations of T cells regulating IgA production and secretion associated with control of the commensal microbiota and resistance to enteropathogens (By similarity). {ECO:0000250|UniProtKB:P16573, ECO:0000250|UniProtKB:P31809}. |
| P14625 | HSP90B1 | S172 | ochoa | Endoplasmin (EC 3.6.4.-) (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Heat shock protein family C member 4) (Tumor rejection antigen 1) (gp96 homolog) | ATP-dependent chaperone involved in the processing of proteins in the endoplasmic reticulum, regulating their transport (PubMed:23572575, PubMed:39509507). Together with MESD, acts as a modulator of the Wnt pathway by promoting the folding of LRP6, a coreceptor of the canonical Wnt pathway (PubMed:23572575, PubMed:39509507). When associated with CNPY3, required for proper folding of Toll-like receptors (PubMed:11584270). Promotes folding and trafficking of TLR4 to the cell surface (PubMed:11584270). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:11584270, ECO:0000269|PubMed:23572575, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:39509507}. |
| P14625 | HSP90B1 | S439 | ochoa | Endoplasmin (EC 3.6.4.-) (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Heat shock protein family C member 4) (Tumor rejection antigen 1) (gp96 homolog) | ATP-dependent chaperone involved in the processing of proteins in the endoplasmic reticulum, regulating their transport (PubMed:23572575, PubMed:39509507). Together with MESD, acts as a modulator of the Wnt pathway by promoting the folding of LRP6, a coreceptor of the canonical Wnt pathway (PubMed:23572575, PubMed:39509507). When associated with CNPY3, required for proper folding of Toll-like receptors (PubMed:11584270). Promotes folding and trafficking of TLR4 to the cell surface (PubMed:11584270). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:11584270, ECO:0000269|PubMed:23572575, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:39509507}. |
| P15924 | DSP | S2231 | ochoa | Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen) | Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250|UniProtKB:F1LMV6}. |
| P18031 | PTPN1 | Y153 | psp | Tyrosine-protein phosphatase non-receptor type 1 (EC 3.1.3.48) (Protein-tyrosine phosphatase 1B) (PTP-1B) | Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET. {ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:21135139, ECO:0000269|PubMed:22169477}. |
| P18206 | VCL | S443 | ochoa | Vinculin (Metavinculin) (MV) | Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. {ECO:0000269|PubMed:20484056}. |
| P19634 | SLC9A1 | S648 | ochoa|psp | Sodium/hydrogen exchanger 1 (APNH) (Na(+)/H(+) antiporter, amiloride-sensitive) (Na(+)/H(+) exchanger 1) (NHE-1) (Solute carrier family 9 member 1) | Electroneutral Na(+) /H(+) antiporter that extrudes Na(+) in exchange for external protons driven by the inward sodium ion chemical gradient, protecting cells from acidification that occurs from metabolism (PubMed:11350981, PubMed:11532004, PubMed:14680478, PubMed:15035633, PubMed:15677483, PubMed:17073455, PubMed:17493937, PubMed:22020933, PubMed:27650500, PubMed:32130622, PubMed:7110335, PubMed:7603840). Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry (By similarity). Plays a key role in maintening intracellular pH neutral and cell volume, and thus is important for cell growth, proliferation, migration and survival (PubMed:12947095, PubMed:15096511, PubMed:22020933, PubMed:8901634). In addition, can transport lithium Li(+) and also functions as a Na(+)/Li(+) antiporter (PubMed:7603840). SLC9A1 also functions in membrane anchoring and organization of scaffolding complexes that coordinate signaling inputs (PubMed:15096511). {ECO:0000250|UniProtKB:P26431, ECO:0000269|PubMed:11350981, ECO:0000269|PubMed:11532004, ECO:0000269|PubMed:12947095, ECO:0000269|PubMed:14680478, ECO:0000269|PubMed:15035633, ECO:0000269|PubMed:15096511, ECO:0000269|PubMed:15677483, ECO:0000269|PubMed:17073455, ECO:0000269|PubMed:17493937, ECO:0000269|PubMed:22020933, ECO:0000269|PubMed:27650500, ECO:0000269|PubMed:32130622, ECO:0000269|PubMed:7110335, ECO:0000269|PubMed:7603840, ECO:0000269|PubMed:8901634}. |
| P20585 | MSH3 | S155 | ochoa | DNA mismatch repair protein Msh3 (hMSH3) (Divergent upstream protein) (DUP) (Mismatch repair protein 1) (MRP1) | Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to 13 nucleotides long. 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. |
| P20700 | LMNB1 | S158 | 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}. |
| P20700 | LMNB1 | S288 | 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}. |
| P20700 | LMNB1 | S302 | 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}. |
| P21757 | MSR1 | S27 | ochoa | Macrophage scavenger receptor types I and II (Macrophage acetylated LDL receptor I and II) (Scavenger receptor class A member 1) (CD antigen CD204) | Membrane glycoproteins implicated in the pathologic deposition of cholesterol in arterial walls during atherogenesis. Two types of receptor subunits exist. These receptors mediate the endocytosis of a diverse group of macromolecules, including modified low density lipoproteins (LDL) (PubMed:2251254). Isoform III does not internalize acetylated LDL (PubMed:9548586). {ECO:0000269|PubMed:2251254, ECO:0000269|PubMed:9548586}. |
| P26038 | MSN | S384 | ochoa | Moesin (Membrane-organizing extension spike protein) | Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (PubMed:10212266). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:9298994, PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By similarity). Also participates in immunologic synapse formation (PubMed:27405666). {ECO:0000250|UniProtKB:P26041, ECO:0000269|PubMed:10212266, ECO:0000269|PubMed:12387735, ECO:0000269|PubMed:15039356, ECO:0000269|PubMed:27405666, ECO:0000269|PubMed:9298994, ECO:0000269|PubMed:9616160}. |
| P30304 | CDC25A | S107 | psp | M-phase inducer phosphatase 1 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25A) | Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression (PubMed:12676925, PubMed:14559997, PubMed:1836978, PubMed:20360007). Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:20360007). Also dephosphorylates CDK2 in complex with cyclin-E, in vitro (PubMed:20360007). {ECO:0000269|PubMed:12676925, ECO:0000269|PubMed:14559997, ECO:0000269|PubMed:1836978, ECO:0000269|PubMed:20360007}. |
| P33076 | CIITA | S373 | psp | MHC class II transactivator (CIITA) (EC 2.3.1.-) (EC 2.7.11.1) | Essential for transcriptional activity of the HLA class II promoter; activation is via the proximal promoter (PubMed:16600381, PubMed:17493635, PubMed:7749984, PubMed:8402893). Does not bind DNA (PubMed:16600381, PubMed:17493635, PubMed:7749984, PubMed:8402893). May act in a coactivator-like fashion through protein-protein interactions by contacting factors binding to the proximal MHC class II promoter, to elements of the transcription machinery, or both PubMed:8402893, PubMed:7749984, (PubMed:16600381, PubMed:17493635). Alternatively it may activate HLA class II transcription by modifying proteins that bind to the MHC class II promoter (PubMed:16600381, PubMed:17493635, PubMed:7749984, PubMed:8402893). Also mediates enhanced MHC class I transcription; the promoter element requirements for CIITA-mediated transcription are distinct from those of constitutive MHC class I transcription, and CIITA can functionally replace TAF1 at these genes. Activates CD74 transcription (PubMed:32855215). Exhibits intrinsic GTP-stimulated acetyltransferase activity (PubMed:11172716). Exhibits serine/threonine protein kinase activity: can phosphorylate the TFIID component TAF7, the RAP74 subunit of the general transcription factor TFIIF, histone H2B at 'Ser-37' and other histones (in vitro) (PubMed:24036077). Has antiviral activity against Ebola virus and coronaviruses, including SARS-CoV-2 (PubMed:32855215). Induces resistance by up-regulation of the p41 isoform of CD74, which blocks cathepsin-mediated cleavage of viral glycoproteins, thereby preventing viral fusion (PubMed:32855215). {ECO:0000269|PubMed:11172716, ECO:0000269|PubMed:16600381, ECO:0000269|PubMed:17493635, ECO:0000269|PubMed:24036077, ECO:0000269|PubMed:32855215, ECO:0000269|PubMed:7749984, ECO:0000269|PubMed:8402893}.; FUNCTION: [Isoform 3]: Exhibits dominant-negative suppression of MHC class II gene expression. {ECO:0000269|PubMed:12919287}. |
| P35573 | AGL | S1028 | ochoa | Glycogen debranching enzyme (Glycogen debrancher) [Includes: 4-alpha-glucanotransferase (EC 2.4.1.25) (Oligo-1,4-1,4-glucantransferase); Amylo-alpha-1,6-glucosidase (Amylo-1,6-glucosidase) (EC 3.2.1.33) (Dextrin 6-alpha-D-glucosidase)] | Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. |
| P35579 | MYH9 | S1326 | ochoa | Myosin-9 (Cellular myosin heavy chain, type A) (Myosin heavy chain 9) (Myosin heavy chain, non-muscle IIa) (Non-muscle myosin heavy chain A) (NMMHC-A) (Non-muscle myosin heavy chain IIa) (NMMHC II-a) (NMMHC-IIA) | Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Required for cortical actin clearance prior to oocyte exocytosis (By similarity). Promotes cell motility in conjunction with S100A4 (PubMed:16707441). During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (PubMed:20052411). {ECO:0000250|UniProtKB:Q8VDD5, ECO:0000269|PubMed:16707441, ECO:0000269|PubMed:20052411}.; FUNCTION: (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1 envelope glycoprotein B. {ECO:0000269|PubMed:20944748, ECO:0000269|PubMed:39048823}. |
| P35749 | MYH11 | S1034 | ochoa | Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) | Muscle contraction. |
| P35749 | MYH11 | S1684 | ochoa | Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) | Muscle contraction. |
| P36871 | PGM1 | S408 | ochoa | Phosphoglucomutase-1 (PGM 1) (EC 5.4.2.2) (Glucose phosphomutase 1) | Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (PubMed:15378030, PubMed:25288802). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (Probable) (PubMed:25288802). This enzyme participates in both the breakdown and synthesis of glucose (PubMed:17924679, PubMed:25288802). {ECO:0000269|PubMed:15378030, ECO:0000269|PubMed:17924679, ECO:0000269|PubMed:25288802, ECO:0000305|PubMed:15378030}. |
| P38398 | BRCA1 | S1423 | psp | Breast cancer type 1 susceptibility protein (EC 2.3.2.27) (RING finger protein 53) (RING-type E3 ubiquitin transferase BRCA1) | E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage (PubMed:10500182, PubMed:12887909, PubMed:12890688, PubMed:14976165, PubMed:16818604, PubMed:17525340, PubMed:19261748). It is unclear whether it also mediates the formation of other types of polyubiquitin chains (PubMed:12890688). The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:12890688, PubMed:14976165, PubMed:20351172). Regulates centrosomal microtubule nucleation (PubMed:18056443). Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle (PubMed:10724175, PubMed:11836499, PubMed:12183412, PubMed:19261748). Required for FANCD2 targeting to sites of DNA damage (PubMed:12887909). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation (PubMed:16326698). Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks (PubMed:19369211). Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8 (PubMed:16818604). Acts as a transcriptional activator (PubMed:20160719). {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:11836499, ECO:0000269|PubMed:12183412, ECO:0000269|PubMed:12887909, ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14976165, ECO:0000269|PubMed:16326698, ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:20351172}. |
| P43243 | MATR3 | S509 | ochoa | Matrin-3 | May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:32245947}. |
| P48047 | ATP5PO | S166 | ochoa | ATP synthase peripheral stalk subunit OSCP, mitochondrial (ATP synthase subunit O) (Oligomycin sensitivity conferral protein) (OSCP) | Subunit OSCP, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (PubMed:37244256). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity). {ECO:0000250|UniProtKB:P13621, ECO:0000250|UniProtKB:P19483, ECO:0000269|PubMed:37244256, ECO:0000305|PubMed:37244256}. |
| P48681 | NES | S731 | ochoa | Nestin | Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity). {ECO:0000250}. |
| P49792 | RANBP2 | S3053 | ochoa | E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270) | E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22194619, ECO:0000269|PubMed:22902403, ECO:0000269|PubMed:23353830, ECO:0000269|PubMed:7775481, ECO:0000303|PubMed:10078529}. |
| P52789 | HK2 | S415 | ochoa | Hexokinase-2 (EC 2.7.1.1) (Hexokinase type II) (HK II) (Hexokinase-B) (Muscle form hexokinase) | Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively) (PubMed:23185017, PubMed:26985301, PubMed:29298880). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:29298880). Plays a key role in maintaining the integrity of the outer mitochondrial membrane by preventing the release of apoptogenic molecules from the intermembrane space and subsequent apoptosis (PubMed:18350175). {ECO:0000269|PubMed:18350175, ECO:0000269|PubMed:23185017, ECO:0000269|PubMed:26985301, ECO:0000269|PubMed:29298880}. |
| P54886 | ALDH18A1 | S136 | ochoa | Delta-1-pyrroline-5-carboxylate synthase (P5CS) (Aldehyde dehydrogenase family 18 member A1) [Includes: Glutamate 5-kinase (GK) (EC 2.7.2.11) (Gamma-glutamyl kinase); Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase)] | Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine. {ECO:0000269|PubMed:10037775, ECO:0000269|PubMed:11092761, ECO:0000269|PubMed:26297558, ECO:0000269|PubMed:26320891, ECO:0000269|PubMed:39506109}. |
| P78527 | PRKDC | S2117 | ochoa | DNA-dependent protein kinase catalytic subunit (DNA-PK catalytic subunit) (DNA-PKcs) (EC 2.7.11.1) (DNPK1) (Ser-473 kinase) (S473K) (p460) | Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234). Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234, PubMed:34352203). Must be bound to DNA to express its catalytic properties (PubMed:11955432). Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C) (PubMed:11955432). Recruited by XRCC5 and XRCC6 to DNA ends and is required to (1) protect and align broken ends of DNA, thereby preventing their degradation, (2) and sequester the DSB for repair by NHEJ (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326, PubMed:33854234). Acts as a scaffold protein to aid the localization of DNA repair proteins to the site of damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion (By similarity). Also involved in modulation of transcription (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome (PubMed:32103174). Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome (PubMed:32103174). Recognizes the substrate consensus sequence [ST]-Q (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). Phosphorylates 'Ser-139' of histone variant H2AX, thereby regulating DNA damage response mechanism (PubMed:14627815, PubMed:16046194). Phosphorylates ASF1A, DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF, NHEJ1/XLF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2 (PubMed:10026262, PubMed:10467406, PubMed:11889123, PubMed:12509254, PubMed:14599745, PubMed:14612514, PubMed:14704337, PubMed:15177042, PubMed:1597196, PubMed:16397295, PubMed:18644470, PubMed:2247066, PubMed:2507541, PubMed:26237645, PubMed:26666690, PubMed:28712728, PubMed:29478807, PubMed:30247612, PubMed:8407951, PubMed:8464713, PubMed:9139719, PubMed:9362500). Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA (PubMed:9679063). Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D (PubMed:9363941). Acts as a regulator of the phosphatidylinositol 3-kinase/protein kinase B signal transduction by mediating phosphorylation of 'Ser-473' of protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), promoting their activation (PubMed:15262962). Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Also regulates the cGAS-STING pathway by catalyzing phosphorylation of CGAS, thereby impairing CGAS oligomerization and activation (PubMed:33273464). Also regulates the cGAS-STING pathway by mediating phosphorylation of PARP1 (PubMed:35460603). {ECO:0000250|UniProtKB:P97313, ECO:0000269|PubMed:10026262, ECO:0000269|PubMed:10467406, ECO:0000269|PubMed:11889123, ECO:0000269|PubMed:11955432, ECO:0000269|PubMed:12509254, ECO:0000269|PubMed:12649176, ECO:0000269|PubMed:14599745, ECO:0000269|PubMed:14612514, ECO:0000269|PubMed:14627815, ECO:0000269|PubMed:14704337, ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:15177042, ECO:0000269|PubMed:15262962, ECO:0000269|PubMed:15574326, ECO:0000269|PubMed:1597196, ECO:0000269|PubMed:16046194, ECO:0000269|PubMed:16397295, ECO:0000269|PubMed:18644470, ECO:0000269|PubMed:2247066, ECO:0000269|PubMed:2507541, ECO:0000269|PubMed:26237645, ECO:0000269|PubMed:26666690, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:29478807, ECO:0000269|PubMed:30247612, ECO:0000269|PubMed:32103174, ECO:0000269|PubMed:33273464, ECO:0000269|PubMed:33854234, ECO:0000269|PubMed:34352203, ECO:0000269|PubMed:35460603, ECO:0000269|PubMed:8407951, ECO:0000269|PubMed:8464713, ECO:0000269|PubMed:9139719, ECO:0000269|PubMed:9362500, ECO:0000269|PubMed:9363941, ECO:0000269|PubMed:9679063}. |
| P78527 | PRKDC | S2789 | ochoa | DNA-dependent protein kinase catalytic subunit (DNA-PK catalytic subunit) (DNA-PKcs) (EC 2.7.11.1) (DNPK1) (Ser-473 kinase) (S473K) (p460) | Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234). Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234, PubMed:34352203). Must be bound to DNA to express its catalytic properties (PubMed:11955432). Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C) (PubMed:11955432). Recruited by XRCC5 and XRCC6 to DNA ends and is required to (1) protect and align broken ends of DNA, thereby preventing their degradation, (2) and sequester the DSB for repair by NHEJ (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326, PubMed:33854234). Acts as a scaffold protein to aid the localization of DNA repair proteins to the site of damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion (By similarity). Also involved in modulation of transcription (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome (PubMed:32103174). Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome (PubMed:32103174). Recognizes the substrate consensus sequence [ST]-Q (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). Phosphorylates 'Ser-139' of histone variant H2AX, thereby regulating DNA damage response mechanism (PubMed:14627815, PubMed:16046194). Phosphorylates ASF1A, DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF, NHEJ1/XLF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2 (PubMed:10026262, PubMed:10467406, PubMed:11889123, PubMed:12509254, PubMed:14599745, PubMed:14612514, PubMed:14704337, PubMed:15177042, PubMed:1597196, PubMed:16397295, PubMed:18644470, PubMed:2247066, PubMed:2507541, PubMed:26237645, PubMed:26666690, PubMed:28712728, PubMed:29478807, PubMed:30247612, PubMed:8407951, PubMed:8464713, PubMed:9139719, PubMed:9362500). Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA (PubMed:9679063). Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D (PubMed:9363941). Acts as a regulator of the phosphatidylinositol 3-kinase/protein kinase B signal transduction by mediating phosphorylation of 'Ser-473' of protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), promoting their activation (PubMed:15262962). Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Also regulates the cGAS-STING pathway by catalyzing phosphorylation of CGAS, thereby impairing CGAS oligomerization and activation (PubMed:33273464). Also regulates the cGAS-STING pathway by mediating phosphorylation of PARP1 (PubMed:35460603). {ECO:0000250|UniProtKB:P97313, ECO:0000269|PubMed:10026262, ECO:0000269|PubMed:10467406, ECO:0000269|PubMed:11889123, ECO:0000269|PubMed:11955432, ECO:0000269|PubMed:12509254, ECO:0000269|PubMed:12649176, ECO:0000269|PubMed:14599745, ECO:0000269|PubMed:14612514, ECO:0000269|PubMed:14627815, ECO:0000269|PubMed:14704337, ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:15177042, ECO:0000269|PubMed:15262962, ECO:0000269|PubMed:15574326, ECO:0000269|PubMed:1597196, ECO:0000269|PubMed:16046194, ECO:0000269|PubMed:16397295, ECO:0000269|PubMed:18644470, ECO:0000269|PubMed:2247066, ECO:0000269|PubMed:2507541, ECO:0000269|PubMed:26237645, ECO:0000269|PubMed:26666690, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:29478807, ECO:0000269|PubMed:30247612, ECO:0000269|PubMed:32103174, ECO:0000269|PubMed:33273464, ECO:0000269|PubMed:33854234, ECO:0000269|PubMed:34352203, ECO:0000269|PubMed:35460603, ECO:0000269|PubMed:8407951, ECO:0000269|PubMed:8464713, ECO:0000269|PubMed:9139719, ECO:0000269|PubMed:9362500, ECO:0000269|PubMed:9363941, ECO:0000269|PubMed:9679063}. |
| Q01658 | DR1 | S106 | ochoa | Protein Dr1 (Down-regulator of transcription 1) (Negative cofactor 2-beta) (NC2-beta) (TATA-binding protein-associated phosphoprotein) | The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. {ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:8670811}. |
| Q03001 | DST | S3920 | ochoa | Dystonin (230 kDa bullous pemphigoid antigen) (230/240 kDa bullous pemphigoid antigen) (Bullous pemphigoid antigen 1) (BPA) (Bullous pemphigoid antigen) (Dystonia musculorum protein) (Hemidesmosomal plaque protein) | Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1 (By similarity). {ECO:0000250|UniProtKB:Q91ZU6}.; FUNCTION: [Isoform 3]: Plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity.; FUNCTION: [Isoform 6]: Required for bundling actin filaments around the nucleus. {ECO:0000250, ECO:0000269|PubMed:10428034, ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692}.; FUNCTION: [Isoform 7]: Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. |
| Q03252 | LMNB2 | S316 | ochoa | Lamin-B2 | 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:33033404). 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:33033404). 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:33033404). {ECO:0000269|PubMed:33033404}. |
| Q05D60 | DEUP1 | S518 | ochoa | Deuterosome assembly protein 1 (Coiled-coil domain-containing protein 67) | Key structural component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells and can generate more than 100 centrioles. Probably sufficient for the specification and formation of the deuterosome inner core. Interacts with CEP152 and recruits PLK4 to activate centriole biogenesis (By similarity). {ECO:0000250}. |
| Q07157 | TJP1 | S686 | ochoa | Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1) | TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250|UniProtKB:O97758, ECO:0000250|UniProtKB:P39447, ECO:0000269|PubMed:20930113, ECO:0000269|PubMed:21240187}. |
| Q07666 | KHDRBS1 | S113 | ochoa | KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68) | Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (PubMed:26080397). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (By similarity). {ECO:0000250|UniProtKB:Q60749, ECO:0000269|PubMed:15021911, ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:20186123, ECO:0000269|PubMed:20610388, ECO:0000269|PubMed:22253824, ECO:0000269|PubMed:26080397, ECO:0000269|PubMed:26758068}.; FUNCTION: Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase. {ECO:0000269|PubMed:9013542}. |
| Q08378 | GOLGA3 | S878 | ochoa | Golgin subfamily A member 3 (Golgi complex-associated protein of 170 kDa) (GCP170) (Golgin-160) | Golgi auto-antigen; probably involved in maintaining Golgi structure. |
| Q09666 | AHNAK | S5261 | ochoa | Neuroblast differentiation-associated protein AHNAK (Desmoyokin) | May be required for neuronal cell differentiation. |
| Q12905 | ILF2 | S218 | ochoa | Interleukin enhancer-binding factor 2 (Nuclear factor of activated T-cells 45 kDa) | Chromatin-interacting protein that forms a stable heterodimer with interleukin enhancer-binding factor 3/ILF3 and plays a role in several biological processes including transcription, innate immunity or cell growth (PubMed:18458058, PubMed:31212927). Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. Together with ILF3, forms an RNA-binding complex that is required for mitotic progression and cytokinesis by regulating the expression of a cluster of mitotic genes. Mechanistically, competes with STAU1/STAU2-mediated mRNA decay (PubMed:32433969). Also plays a role in the inhibition of various viruses including Japanese encephalitis virus or enterovirus 71. {ECO:0000269|PubMed:10574923, ECO:0000269|PubMed:11739746, ECO:0000269|PubMed:18458058, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:31212927, ECO:0000269|PubMed:32433969, ECO:0000269|PubMed:9442054}.; FUNCTION: (Microbial infection) Plays a positive role in HIV-1 virus production by binding to and thereby stabilizing HIV-1 RNA, together with ILF3. {ECO:0000269|PubMed:26891316}. |
| Q13185 | CBX3 | S145 | 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}. |
| Q13459 | MYO9B | S1043 | ochoa | Unconventional myosin-IXb (Unconventional myosin-9b) | Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions (PubMed:9490638). Also acts as a GTPase activator for RHOA (PubMed:26529257, PubMed:9490638). Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). {ECO:0000269|PubMed:26529257, ECO:0000269|PubMed:9490638}. |
| Q13573 | SNW1 | S389 | 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}. |
| Q13615 | MTMR3 | S1173 | 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}. |
| Q13813 | SPTAN1 | S1291 | ochoa | Spectrin alpha chain, non-erythrocytic 1 (Alpha-II spectrin) (Fodrin alpha chain) (Spectrin, non-erythroid alpha subunit) | Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. |
| Q14653 | IRF3 | S396 | psp | Interferon regulatory factor 3 (IRF-3) | Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:22394562, PubMed:24049179, PubMed:25636800, PubMed:27302953, PubMed:31340999, PubMed:36603579, PubMed:8524823). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (PubMed:11846977, PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:32972995, PubMed:36603579, PubMed:8524823). Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction (PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:36603579). Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases (PubMed:22394562, PubMed:25636800, PubMed:27302953, PubMed:36603579). This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes (PubMed:16154084, PubMed:27302953, PubMed:33440148, PubMed:36603579). Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages (PubMed:16846591). In response to Sendai virus infection, is recruited by TOMM70:HSP90AA1 to mitochondrion and forms an apoptosis complex TOMM70:HSP90AA1:IRF3:BAX inducing apoptosis (PubMed:25609812). Key transcription factor regulating the IFN response during SARS-CoV-2 infection (PubMed:33440148). {ECO:0000269|PubMed:16154084, ECO:0000269|PubMed:22394562, ECO:0000269|PubMed:24049179, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27302953, ECO:0000269|PubMed:31340999, ECO:0000269|PubMed:31413131, ECO:0000269|PubMed:32972995, ECO:0000269|PubMed:33440148, ECO:0000269|PubMed:36603579, ECO:0000269|PubMed:8524823, ECO:0000303|PubMed:11846977, ECO:0000303|PubMed:16846591, ECO:0000303|PubMed:16979567, ECO:0000303|PubMed:20049431}. |
| Q14980 | NUMA1 | S1103 | ochoa | Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen) | Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250|UniProtKB:E9Q7G0, ECO:0000269|PubMed:11163243, ECO:0000269|PubMed:11229403, ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386, ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:17172455, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23027904, ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901, ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:27462074, ECO:0000269|PubMed:7769006, ECO:0000305|PubMed:10075938, ECO:0000305|PubMed:21816348}. |
| Q14980 | NUMA1 | S1187 | ochoa | Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen) | Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250|UniProtKB:E9Q7G0, ECO:0000269|PubMed:11163243, ECO:0000269|PubMed:11229403, ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386, ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:17172455, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23027904, ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901, ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:27462074, ECO:0000269|PubMed:7769006, ECO:0000305|PubMed:10075938, ECO:0000305|PubMed:21816348}. |
| Q14980 | NUMA1 | S1278 | ochoa | Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen) | Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250|UniProtKB:E9Q7G0, ECO:0000269|PubMed:11163243, ECO:0000269|PubMed:11229403, ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386, ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:17172455, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23027904, ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901, ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:27462074, ECO:0000269|PubMed:7769006, ECO:0000305|PubMed:10075938, ECO:0000305|PubMed:21816348}. |
| Q15788 | NCOA1 | S863 | psp | Nuclear receptor coactivator 1 (NCoA-1) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 74) (bHLHe74) (Protein Hin-2) (RIP160) (Renal carcinoma antigen NY-REN-52) (Steroid receptor coactivator 1) (SRC-1) | Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3. {ECO:0000269|PubMed:10449719, ECO:0000269|PubMed:12954634, ECO:0000269|PubMed:7481822, ECO:0000269|PubMed:9223281, ECO:0000269|PubMed:9223431, ECO:0000269|PubMed:9296499, ECO:0000269|PubMed:9427757}. |
| Q15911 | ZFHX3 | S1247 | ochoa | Zinc finger homeobox protein 3 (AT motif-binding factor 1) (AT-binding transcription factor 1) (Alpha-fetoprotein enhancer-binding protein) (Zinc finger homeodomain protein 3) (ZFH-3) | Transcriptional regulator which can act as an activator or a repressor. Inhibits the enhancer element of the AFP gene by binding to its AT-rich core sequence. In concert with SMAD-dependent TGF-beta signaling can repress the transcription of AFP via its interaction with SMAD2/3 (PubMed:25105025). Regulates the circadian locomotor rhythms via transcriptional activation of neuropeptidergic genes which are essential for intercellular synchrony and rhythm amplitude in the suprachiasmatic nucleus (SCN) of the brain (By similarity). Regulator of myoblasts differentiation through the binding to the AT-rich sequence of MYF6 promoter and promoter repression (PubMed:11312261). Down-regulates the MUC5AC promoter in gastric cancer (PubMed:17330845). In association with RUNX3, up-regulates CDKN1A promoter activity following TGF-beta stimulation (PubMed:20599712). Inhibits estrogen receptor (ESR1) function by selectively competing with coactivator NCOA3 for binding to ESR1 in ESR1-positive breast cancer cells (PubMed:20720010). {ECO:0000250|UniProtKB:Q61329, ECO:0000269|PubMed:11312261, ECO:0000269|PubMed:17330845, ECO:0000269|PubMed:20599712, ECO:0000269|PubMed:20720010, ECO:0000269|PubMed:25105025}. |
| Q16821 | PPP1R3A | S584 | ochoa | Protein phosphatase 1 regulatory subunit 3A (Protein phosphatase 1 glycogen-associated regulatory subunit) (Protein phosphatase type-1 glycogen targeting subunit) (RG1) | Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase (By similarity). {ECO:0000250}. |
| Q16825 | PTPN21 | S484 | ochoa | Tyrosine-protein phosphatase non-receptor type 21 (EC 3.1.3.48) (Protein-tyrosine phosphatase D1) | None |
| Q16832 | DDR2 | S758 | ochoa | Discoidin domain-containing receptor 2 (Discoidin domain receptor 2) (EC 2.7.10.1) (CD167 antigen-like family member B) (Discoidin domain-containing receptor tyrosine kinase 2) (Neurotrophic tyrosine kinase, receptor-related 3) (Receptor protein-tyrosine kinase TKT) (Tyrosine-protein kinase TYRO10) (CD antigen CD167b) | Tyrosine kinase involved in the regulation of tissues remodeling (PubMed:30449416). It functions as a cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing. {ECO:0000269|PubMed:16186104, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:17665456, ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20004161, ECO:0000269|PubMed:20564243, ECO:0000269|PubMed:20734453, ECO:0000269|PubMed:30449416, ECO:0000269|PubMed:9659899}. |
| Q32P28 | P3H1 | S706 | ochoa | Prolyl 3-hydroxylase 1 (EC 1.14.11.7) (Growth suppressor 1) (Leucine- and proline-enriched proteoglycan 1) (Leprecan-1) | Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts. {ECO:0000269|PubMed:10951563}. |
| Q3V6T2 | CCDC88A | S1702 | ochoa | Girdin (Akt phosphorylation enhancer) (APE) (Coiled-coil domain-containing protein 88A) (G alpha-interacting vesicle-associated protein) (GIV) (Girders of actin filament) (Hook-related protein 1) (HkRP1) | Bifunctional modulator of guanine nucleotide-binding proteins (G proteins) (PubMed:19211784, PubMed:27621449). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits (PubMed:19211784, PubMed:21954290, PubMed:23509302, PubMed:25187647). Also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS (PubMed:27621449). Essential for cell migration (PubMed:16139227, PubMed:19211784, PubMed:20462955, PubMed:21954290). Interacts in complex with G(i) alpha subunits with the EGFR receptor, retaining EGFR at the cell membrane following ligand stimulation and promoting EGFR signaling which triggers cell migration (PubMed:20462955). Binding to Gi-alpha subunits displaces the beta and gamma subunits from the heterotrimeric G-protein complex which enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB (PubMed:19211784). Phosphorylation of AKT1/PKB induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation (By similarity). Binds in its tyrosine-phosphorylated form to the phosphatidylinositol 3-kinase (PI3K) regulatory subunit PIK3R1 which enables recruitment of PIK3R1 to the EGFR receptor, enhancing PI3K activity and cell migration (PubMed:21954290). Plays a role as a key modulator of the AKT-mTOR signaling pathway, controlling the tempo of the process of newborn neuron integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Inhibition of G(s) subunit alpha GNAS leads to reduced cellular levels of cAMP and suppression of cell proliferation (PubMed:27621449). Essential for the integrity of the actin cytoskeleton (PubMed:16139227, PubMed:19211784). Required for formation of actin stress fibers and lamellipodia (PubMed:15882442). May be involved in membrane sorting in the early endosome (PubMed:15882442). Plays a role in ciliogenesis and cilium morphology and positioning and this may partly be through regulation of the localization of scaffolding protein CROCC/Rootletin (PubMed:27623382). {ECO:0000250|UniProtKB:Q5SNZ0, ECO:0000269|PubMed:15882442, ECO:0000269|PubMed:16139227, ECO:0000269|PubMed:19211784, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:21954290, ECO:0000269|PubMed:23509302, ECO:0000269|PubMed:25187647, ECO:0000269|PubMed:27621449, ECO:0000269|PubMed:27623382}. |
| Q52LW3 | ARHGAP29 | S983 | ochoa | Rho GTPase-activating protein 29 (PTPL1-associated RhoGAP protein 1) (Rho-type GTPase-activating protein 29) | GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. {ECO:0000269|PubMed:15752761, ECO:0000269|PubMed:9305890}. |
| Q5CZC0 | FSIP2 | S3890 | ochoa | Fibrous sheath-interacting protein 2 | Plays a role in spermatogenesis. {ECO:0000305|PubMed:30137358}. |
| Q5SWA1 | PPP1R15B | S203 | ochoa | Protein phosphatase 1 regulatory subunit 15B | Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1. {ECO:0000269|PubMed:26159176, ECO:0000269|PubMed:26307080}. |
| Q5T655 | CFAP58 | S146 | ochoa | Cilia- and flagella-associated protein 58 (Coiled-coil domain-containing protein 147) | Has an essential role in the assembly and organization of the sperm flagellar axoneme (PubMed:32791035). Required for the elongation of the primary cilium and sperm flagellar midpiece via modulation of the Notch signaling pathway (By similarity). {ECO:0000250|UniProtKB:B2RW38, ECO:0000269|PubMed:32791035}. |
| Q5TCX8 | MAP3K21 | S455 | ochoa | Mitogen-activated protein kinase kinase kinase 21 (EC 2.7.11.25) (Mitogen-activated protein kinase kinase kinase MLK4) (Mixed lineage kinase 4) | Negative regulator of TLR4 signaling. Does not activate JNK1/MAPK8 pathway, p38/MAPK14, nor ERK2/MAPK1 pathways. {ECO:0000269|PubMed:21602844}. |
| Q5THJ4 | VPS13D | S1067 | ochoa | Intermembrane lipid transfer protein VPS13D (Vacuolar protein sorting-associated protein 13D) | Mediates the transfer of lipids between membranes at organelle contact sites (By similarity). Functions in promoting mitochondrial clearance by mitochondrial autophagy (mitophagy), also possibly by positively regulating mitochondrial fission (PubMed:29307555, PubMed:29604224). Mitophagy plays an important role in regulating cell health and mitochondrial size and homeostasis. {ECO:0000250|UniProtKB:Q07878, ECO:0000269|PubMed:29307555, ECO:0000269|PubMed:29604224}. |
| Q5VT52 | RPRD2 | S1069 | ochoa | Regulation of nuclear pre-mRNA domain-containing protein 2 | None |
| Q5VVW2 | GARNL3 | S424 | ochoa | GTPase-activating Rap/Ran-GAP domain-like protein 3 | None |
| Q5VZ66 | JAKMIP3 | S383 | ochoa | Janus kinase and microtubule-interacting protein 3 (Neuroendocrine long coiled-coil protein 2) | None |
| Q5VZK9 | CARMIL1 | S1068 | ochoa | F-actin-uncapping protein LRRC16A (CARMIL homolog) (Capping protein regulator and myosin 1 linker protein 1) (Capping protein, Arp2/3 and myosin-I linker homolog 1) (Capping protein, Arp2/3 and myosin-I linker protein 1) (Leucine-rich repeat-containing protein 16A) | Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments (PubMed:16054028). Plays a role in lamellipodial protrusion formations and cell migration (PubMed:19846667). {ECO:0000269|PubMed:16054028, ECO:0000269|PubMed:19846667}. |
| Q5W0B1 | OBI1 | S115 | ochoa | ORC ubiquitin ligase 1 (OBI1) (EC 2.3.2.27) (RING finger protein 219) | E3 ubiquitin ligase essential for DNA replication origin activation during S phase (PubMed:31160578). Acts as a replication origin selector which selects the origins to be fired and catalyzes the multi-mono-ubiquitination of a subset of chromatin-bound ORC3 and ORC5 during S-phase (PubMed:31160578). {ECO:0000269|PubMed:31160578}. |
| Q68CQ4 | UTP25 | S186 | ochoa | U3 small nucleolar RNA-associated protein 25 homolog (Digestive organ expansion factor homolog) (UTP25 small subunit processor component) | Component of the ribosomal small subunit processome for the biogenesis of ribosomes, functions in pre-ribosomal RNA (pre-rRNA) processing (By similarity). Essential for embryonic development in part through the regulation of p53 pathway. Controls the expansion growth of digestive organs and liver (PubMed:23357851, PubMed:25007945, PubMed:27657329). Also involved in the sympathetic neuronal development (By similarity). Mediates, with CAPN3, the proteasome-independent degradation of p53/TP53 (PubMed:23357851, PubMed:27657329). {ECO:0000250|UniProtKB:Q6PEH4, ECO:0000269|PubMed:23357851, ECO:0000269|PubMed:25007945, ECO:0000269|PubMed:27657329}. |
| Q68DA7 | FMN1 | S199 | ochoa | Formin-1 (Limb deformity protein homolog) | Plays a role in the formation of adherens junction and the polymerization of linear actin cables. {ECO:0000250}. |
| Q6KC79 | NIPBL | S1736 | ochoa | Nipped-B-like protein (Delangin) (SCC2 homolog) | Plays an important role in the loading of the cohesin complex on to DNA. Forms a heterodimeric complex (also known as cohesin loading complex) with MAU2/SCC4 which mediates the loading of the cohesin complex onto chromatin (PubMed:22628566, PubMed:28914604). Plays a role in cohesin loading at sites of DNA damage. Its recruitment to double-strand breaks (DSBs) sites occurs in a CBX3-, RNF8- and RNF168-dependent manner whereas its recruitment to UV irradiation-induced DNA damage sites occurs in a ATM-, ATR-, RNF8- and RNF168-dependent manner (PubMed:28167679). Along with ZNF609, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others (By similarity). {ECO:0000250|UniProtKB:Q6KCD5, ECO:0000269|PubMed:22628566, ECO:0000269|PubMed:28167679, ECO:0000269|PubMed:28914604}. |
| Q6L8Q7 | PDE12 | S438 | ochoa | 2',5'-phosphodiesterase 12 (2'-PDE) (2-PDE) (EC 3.1.4.-) (Mitochondrial deadenylase) (EC 3.1.13.4) | Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. Degrades triphosphorylated 2-5A to produce AMP and ATP (PubMed:26055709). Also cleaves 3',5'-phosphodiester bond of oligoadenylates (PubMed:21666256, PubMed:26055709, PubMed:30389976). Plays a role as a negative regulator of the 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme increases cellular 2-5A levels and decreases viral replication in cultured small-airway epithelial cells and Hela cells (PubMed:26055709). {ECO:0000269|PubMed:15231837, ECO:0000269|PubMed:21245038, ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:22285541, ECO:0000269|PubMed:26055709, ECO:0000269|PubMed:30389976}. |
| Q6NZ36 | FAAP20 | S48 | psp | Fanconi anemia core complex-associated protein 20 (FANCA-associated protein of 20 kDa) (Fanconi anemia-associated protein of 20 kDa) | Component of the Fanconi anemia (FA) complex required to recruit the FA complex to DNA interstrand cross-links (ICLs) and promote ICLs repair. Following DNA damage recognizes and binds 'Lys-63'-linked ubiquitin generated by RNF8 at ICLs and recruits other components of the FA complex. Promotes translesion synthesis via interaction with REV1. {ECO:0000269|PubMed:22266823, ECO:0000269|PubMed:22343915, ECO:0000269|PubMed:22396592, ECO:0000269|PubMed:22705371}. |
| Q6P0N0 | MIS18BP1 | S729 | ochoa | Mis18-binding protein 1 (Kinetochore-associated protein KNL-2 homolog) (HsKNL-2) (P243) | Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038, ECO:0000269|PubMed:17339379}. |
| Q6P2Q9 | PRPF8 | S859 | ochoa | Pre-mRNA-processing-splicing factor 8 (220 kDa U5 snRNP-specific protein) (PRP8 homolog) (Splicing factor Prp8) (p220) | Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes, both of the predominant U2-type spliceosome and the minor U12-type spliceosome (PubMed:10411133, PubMed:11971955, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30315277, PubMed:30705154, PubMed:30728453). Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex, a building block of the spliceosome. Functions as a scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site. {ECO:0000269|PubMed:10411133, ECO:0000269|PubMed:11971955, ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, ECO:0000303|PubMed:15840809}. |
| Q6UXG2 | ELAPOR1 | S990 | ochoa | Endosome/lysosome-associated apoptosis and autophagy regulator 1 (Estrogen-induced gene 121 protein) | May protect cells from cell death by inducing cytosolic vacuolization and up-regulating the autophagy pathway (PubMed:21072319). May play a role in apoptosis and cell proliferation through its interaction with HSPA5 (PubMed:26045166). {ECO:0000269|PubMed:21072319, ECO:0000269|PubMed:26045166}. |
| Q6VEQ5 | WASH2P | S219 | ochoa | WAS protein family homolog 2 (CXYorf1-like protein on chromosome 2) (Protein FAM39B) | Acts as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Involved in endocytic trafficking of EGF. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration. In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T-cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling. Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex. Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8}. |
| Q6ZS17 | RIPOR1 | S114 | ochoa | Rho family-interacting cell polarization regulator 1 | Downstream effector protein for Rho-type small GTPases that plays a role in cell polarity and directional migration (PubMed:27807006). Acts as an adapter protein, linking active Rho proteins to STK24 and STK26 kinases, and hence positively regulates Golgi reorientation in polarized cell migration upon Rho activation (PubMed:27807006). Involved in the subcellular relocation of STK26 from the Golgi to cytoplasm punctae in a Rho- and PDCD10-dependent manner upon serum stimulation (PubMed:27807006). {ECO:0000269|PubMed:27807006}. |
| Q6ZS30 | NBEAL1 | S1842 | ochoa | Neurobeachin-like protein 1 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 16 protein) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 17 protein) | None |
| Q6ZWE6 | PLEKHM3 | S460 | ochoa | Pleckstrin homology domain-containing family M member 3 (PH domain-containing family M member 3) (Differentiation associated protein) | Involved in skeletal muscle differentiation. May act as a scaffold protein for AKT1 during muscle differentiation. {ECO:0000250|UniProtKB:Q8BM47}. |
| Q7Z6Z7 | HUWE1 | S2391 | ochoa | E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1) | E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250|UniProtKB:P51593, ECO:0000250|UniProtKB:Q7TMY8, ECO:0000269|PubMed:15567145, ECO:0000269|PubMed:15767685, ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:15989957, ECO:0000269|PubMed:17567951, ECO:0000269|PubMed:18488021, ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:20534529, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:27746020, ECO:0000269|PubMed:30217973, ECO:0000269|PubMed:35776542}. |
| Q7Z6Z7 | HUWE1 | S2636 | ochoa|psp | E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1) | E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250|UniProtKB:P51593, ECO:0000250|UniProtKB:Q7TMY8, ECO:0000269|PubMed:15567145, ECO:0000269|PubMed:15767685, ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:15989957, ECO:0000269|PubMed:17567951, ECO:0000269|PubMed:18488021, ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:20534529, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:27746020, ECO:0000269|PubMed:30217973, ECO:0000269|PubMed:35776542}. |
| Q86VP1 | TAX1BP1 | S344 | ochoa | Tax1-binding protein 1 (TRAF6-binding protein) | Ubiquitin-binding adapter that participates in inflammatory, antiviral and innate immune processes as well as selective autophagy regulation (PubMed:29940186, PubMed:30459273, PubMed:30909570). Plays a key role in the negative regulation of NF-kappa-B and IRF3 signalings by acting as an adapter for the ubiquitin-editing enzyme A20/TNFAIP3 to bind and inactivate its substrates (PubMed:17703191). Disrupts the interactions between the E3 ubiquitin ligase TRAF3 and TBK1/IKBKE to attenuate 'Lys63'-linked polyubiquitination of TBK1 and thereby IFN-beta production (PubMed:21885437). Also recruits A20/TNFAIP3 to ubiquitinated signaling proteins TRAF6 and RIPK1, leading to their deubiquitination and disruption of IL-1 and TNF-induced NF-kappa-B signaling pathways (PubMed:17703191). Inhibits virus-induced apoptosis by inducing the 'Lys-48'-linked polyubiquitination and degradation of MAVS via recruitment of the E3 ligase ITCH, thereby attenuating MAVS-mediated apoptosis signaling (PubMed:27736772). As a macroautophagy/autophagy receptor, facilitates the xenophagic clearance of pathogenic bacteria such as Salmonella typhimurium and Mycobacterium tuberculosis (PubMed:26451915). Upon NBR1 recruitment to the SQSTM1-ubiquitin condensates, acts as the major recruiter of RB1CC1 to these ubiquitin condensates to promote their autophagic degradation (PubMed:33226137, PubMed:34471133). Mediates the autophagic degradation of other substrates including TICAM1 (PubMed:28898289). {ECO:0000269|PubMed:10435631, ECO:0000269|PubMed:10920205, ECO:0000269|PubMed:17703191, ECO:0000269|PubMed:21885437, ECO:0000269|PubMed:26451915, ECO:0000269|PubMed:27736772, ECO:0000269|PubMed:28898289, ECO:0000269|PubMed:29940186, ECO:0000269|PubMed:30459273, ECO:0000269|PubMed:30909570, ECO:0000269|PubMed:33226137, ECO:0000269|PubMed:34471133}. |
| Q86X10 | RALGAPB | S1300 | ochoa | Ral GTPase-activating protein subunit beta (p170) | Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB. {ECO:0000250}. |
| Q86YC2 | PALB2 | S357 | ochoa | Partner and localizer of BRCA2 | Plays a critical role in homologous recombination repair (HRR) through its ability to recruit BRCA2 and RAD51 to DNA breaks (PubMed:16793542, PubMed:19369211, PubMed:19423707, PubMed:22941656, PubMed:24141787, PubMed:28319063). Strongly stimulates the DNA strand-invasion activity of RAD51, stabilizes the nucleoprotein filament against a disruptive BRC3-BRC4 polypeptide and helps RAD51 to overcome the suppressive effect of replication protein A (RPA) (PubMed:20871615). Functionally cooperates with RAD51AP1 in promoting of D-loop formation by RAD51 (PubMed:20871616). Serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is essential for homologous recombination (PubMed:19369211). Via its WD repeats is proposed to scaffold a HR complex containing RAD51C and BRCA2 which is thought to play a role in HR-mediated DNA repair (PubMed:24141787). Essential partner of BRCA2 that promotes the localization and stability of BRCA2 (PubMed:16793542). Also enables its recombinational repair and checkpoint functions of BRCA2 (PubMed:16793542). May act by promoting stable association of BRCA2 with nuclear structures, allowing BRCA2 to escape the effects of proteasome-mediated degradation (PubMed:16793542). Binds DNA with high affinity for D loop, which comprises single-stranded, double-stranded and branched DNA structures (PubMed:20871616). May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with BRCA2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity (PubMed:24485656). {ECO:0000269|PubMed:16793542, ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:19423707, ECO:0000269|PubMed:20871615, ECO:0000269|PubMed:20871616, ECO:0000269|PubMed:22941656, ECO:0000269|PubMed:24141787, ECO:0000269|PubMed:24485656, ECO:0000269|PubMed:28319063}. |
| Q86YV0 | RASAL3 | S949 | ochoa | RAS protein activator like-3 | Functions as a Ras GTPase-activating protein. Plays an important role in the expansion and functions of natural killer T (NKT) cells in the liver by negatively regulating RAS activity and the down-stream ERK signaling pathway. {ECO:0000250|UniProtKB:Q8C2K5}. |
| Q8IUD2 | ERC1 | S687 | ochoa | ELKS/Rab6-interacting/CAST family member 1 (ERC-1) (Rab6-interacting protein 2) | Regulatory subunit of the IKK complex. Probably recruits IkappaBalpha/NFKBIA to the complex. May be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. May be involved in vesicle trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to Golgi transport. {ECO:0000269|PubMed:15218148}. |
| Q8IV36 | HID1 | S559 | ochoa | Protein HID1 (Down-regulated in multiple cancers 1) (HID1 domain-containing protein) (Protein hid-1 homolog) | May play an important role in the development of cancers in a broad range of tissues. {ECO:0000269|PubMed:11281419}. |
| Q8IWA0 | WDR75 | S811 | ochoa | WD repeat-containing protein 75 (U3 small nucleolar RNA-associated protein 17 homolog) | Ribosome biogenesis factor. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I. {ECO:0000269|PubMed:17699751, ECO:0000269|PubMed:34516797}. |
| Q8IWJ2 | GCC2 | S236 | ochoa | GRIP and coiled-coil domain-containing protein 2 (185 kDa Golgi coiled-coil protein) (GCC185) (CLL-associated antigen KW-11) (CTCL tumor antigen se1-1) (Ran-binding protein 2-like 4) (RanBP2L4) (Renal carcinoma antigen NY-REN-53) | Golgin which probably tethers transport vesicles to the trans-Golgi network (TGN) and regulates vesicular transport between the endosomes and the Golgi. As a RAB9A effector it is involved in recycling of the mannose 6-phosphate receptor from the late endosomes to the TGN. May also play a role in transport between the recycling endosomes and the Golgi. Required for maintenance of the Golgi structure, it is involved in the biogenesis of noncentrosomal, Golgi-associated microtubules through recruitment of CLASP1 and CLASP2. {ECO:0000269|PubMed:16885419, ECO:0000269|PubMed:17488291, ECO:0000269|PubMed:17543864}. |
| Q8IY92 | SLX4 | S1170 | ochoa | Structure-specific endonuclease subunit SLX4 (BTB/POZ domain-containing protein 12) | Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures originating from replication and recombination intermediates and from DNA damage. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5'-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products. Interacts with the structure-specific ERCC4-ERCC1 endonuclease and promotes the cleavage of bubble structures. Interacts with the structure-specific MUS81-EME1 endonuclease and promotes the cleavage of 3'-flap and replication fork-like structures. SLX4 is required for recovery from alkylation-induced DNA damage and is involved in the resolution of DNA double-strand breaks. {ECO:0000269|PubMed:19595721, ECO:0000269|PubMed:19595722, ECO:0000269|PubMed:19596235, ECO:0000269|PubMed:19596236}. |
| Q8N3C0 | ASCC3 | S446 | ochoa | Activating signal cointegrator 1 complex subunit 3 (EC 5.6.2.4) (ASC-1 complex subunit p200) (ASC1p200) (Helicase, ATP binding 1) (Trip4 complex subunit p200) | ATPase involved both in DNA repair and rescue of stalled ribosomes (PubMed:22055184, PubMed:28757607, PubMed:32099016, PubMed:32579943, PubMed:36302773). 3'-5' DNA helicase involved in repair of alkylated DNA: promotes DNA unwinding to generate single-stranded substrate needed for ALKBH3, enabling ALKBH3 to process alkylated N3-methylcytosine (3mC) within double-stranded regions (PubMed:22055184). Also involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation (PubMed:28757607, PubMed:32099016, PubMed:32579943, PubMed:36302773). Drives the splitting of stalled ribosomes that are ubiquitinated in a ZNF598-dependent manner, as part of the ribosome quality control trigger (RQT) complex (PubMed:28757607, PubMed:32099016, PubMed:32579943, PubMed:36302773). Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation (PubMed:12077347). {ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:22055184, ECO:0000269|PubMed:28757607, ECO:0000269|PubMed:32099016, ECO:0000269|PubMed:32579943, ECO:0000269|PubMed:36302773}. |
| Q8N3D4 | EHBP1L1 | S180 | ochoa | EH domain-binding protein 1-like protein 1 | May act as Rab effector protein and play a role in vesicle trafficking. {ECO:0000305|PubMed:27552051}. |
| Q8NB16 | MLKL | S132 | ochoa | Mixed lineage kinase domain-like protein (hMLKL) | Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process (PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:24316671). Does not have protein kinase activity (PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:24316671). Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage (PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:24316671). In addition to TNF-induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: following activation by ZBP1, MLKL is phosphorylated by RIPK3 in the nucleus, triggering disruption of the nuclear envelope and leakage of cellular DNA into the cytosol.following ZBP1 activation, which senses double-stranded Z-RNA structures, nuclear RIPK3 catalyzes phosphorylation and activation of MLKL, promoting disruption of the nuclear envelope and leakage of cellular DNA into the cytosol (By similarity). Binds to highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which is essential for its necroptotic function (PubMed:29883610). {ECO:0000250|UniProtKB:Q9D2Y4, ECO:0000269|PubMed:22265413, ECO:0000269|PubMed:22265414, ECO:0000269|PubMed:22421439, ECO:0000269|PubMed:24316671, ECO:0000269|PubMed:29883610}. |
| Q8NCN4 | RNF169 | S472 | ochoa | E3 ubiquitin-protein ligase RNF169 (EC 2.3.2.27) (RING finger protein 169) (RING-type E3 ubiquitin transferase RNF169) | Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization (PubMed:22492721, PubMed:30773093). Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1 (PubMed:30104380, PubMed:30773093). E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair. {ECO:0000269|PubMed:22492721, ECO:0000269|PubMed:22733822, ECO:0000269|PubMed:22742833, ECO:0000269|PubMed:30104380, ECO:0000269|PubMed:30773093}. |
| Q8NDI1 | EHBP1 | S243 | ochoa | EH domain-binding protein 1 | May play a role in actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton. May act as Rab effector protein and play a role in vesicle trafficking (PubMed:14676205, PubMed:27552051). Required for perinuclear sorting and insulin-regulated recycling of SLC2A4/GLUT4 in adipocytes (By similarity). {ECO:0000250|UniProtKB:Q69ZW3, ECO:0000269|PubMed:14676205, ECO:0000305|PubMed:27552051}. |
| Q8NI35 | PATJ | S522 | ochoa | InaD-like protein (Inadl protein) (hINADL) (Channel-interacting PDZ domain-containing protein) (Pals1-associated tight junction protein) (Protein associated to tight junctions) | Scaffolding protein that facilitates the localization of proteins to the cell membrane (PubMed:11927608, PubMed:16678097, PubMed:22006950). Required for the correct formation of tight junctions and epithelial apico-basal polarity (PubMed:11927608, PubMed:16678097). Acts (via its L27 domain) as an apical connector and elongation factor for multistranded TJP1/ZO1 condensates that form a tight junction belt, thereby required for the formation of the tight junction-mediated cell barrier (By similarity). Positively regulates epithelial cell microtubule elongation and cell migration, possibly via facilitating localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells (By similarity). Plays a role in the correct reorientation of the microtubule-organizing center during epithelial migration (By similarity). May regulate the surface expression and/or function of ASIC3 in sensory neurons (By similarity). May recruit ARHGEF18 to apical cell-cell boundaries (PubMed:22006950). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7, ECO:0000269|PubMed:11927608, ECO:0000269|PubMed:16678097, ECO:0000269|PubMed:22006950}. |
| Q8TC07 | TBC1D15 | S203 | ochoa | TBC1 domain family member 15 (GTPase-activating protein RAB7) (GAP for RAB7) (Rab7-GAP) | Acts as a GTPase activating protein for RAB7A. Does not act on RAB4, RAB5 or RAB6 (By similarity). {ECO:0000250}. |
| Q8TCN5 | ZNF507 | S73 | ochoa | Zinc finger protein 507 | May be involved in transcriptional regulation. |
| Q8TDC0 | MYOZ3 | S31 | ochoa | Myozenin-3 (Calsarcin-3) (FATZ-related protein 3) | Myozenins may serve as intracellular binding proteins involved in linking Z line 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. |
| Q8TER5 | ARHGEF40 | S1443 | ochoa | Rho guanine nucleotide exchange factor 40 (Protein SOLO) | May act as a guanine nucleotide exchange factor (GEF). {ECO:0000250}. |
| Q8TEV9 | SMCR8 | S421 | ochoa | Guanine nucleotide exchange protein SMCR8 (Smith-Magenis syndrome chromosomal region candidate gene 8 protein) | Component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy (PubMed:20562859, PubMed:27103069, PubMed:27193190, PubMed:27559131, PubMed:27617292, PubMed:28195531, PubMed:32303654). In the complex, C9orf72 and SMCR8 probably constitute the catalytic subunits that promote the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation (PubMed:20562859, PubMed:27103069, PubMed:27617292, PubMed:28195531). The C9orf72-SMCR8 complex also acts as a negative regulator of autophagy initiation by interacting with the ULK1/ATG1 kinase complex and inhibiting its protein kinase activity (PubMed:27617292, PubMed:28195531). As part of the C9orf72-SMCR8 complex, stimulates RAB8A and RAB11A GTPase activity in vitro (PubMed:32303654). Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates (PubMed:27559131, PubMed:28195531). In addition to its activity in the cytoplasm within the C9orf72-SMCR8 complex, SMCR8 also localizes in the nucleus, where it associates with chromatin and negatively regulates expression of suppresses ULK1 and WIPI2 genes (PubMed:28195531). {ECO:0000269|PubMed:20562859, ECO:0000269|PubMed:27103069, ECO:0000269|PubMed:27193190, ECO:0000269|PubMed:27559131, ECO:0000269|PubMed:27617292, ECO:0000269|PubMed:28195531, ECO:0000269|PubMed:32303654}. |
| Q8TF72 | SHROOM3 | S1137 | ochoa | Protein Shroom3 (Shroom-related protein) (hShrmL) | Controls cell shape changes in the neuroepithelium during neural tube closure. Induces apical constriction in epithelial cells by promoting the apical accumulation of F-actin and myosin II, and probably by bundling stress fibers (By similarity). Induces apicobasal cell elongation by redistributing gamma-tubulin and directing the assembly of robust apicobasal microtubule arrays (By similarity). {ECO:0000250|UniProtKB:Q27IV2, ECO:0000250|UniProtKB:Q9QXN0}. |
| Q8WUM0 | NUP133 | S499 | ochoa | Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133) | Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222). {ECO:0000269|PubMed:11684705, ECO:0000269|PubMed:30179222}. |
| Q8WUM0 | NUP133 | S1021 | ochoa | Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133) | Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222). {ECO:0000269|PubMed:11684705, ECO:0000269|PubMed:30179222}. |
| Q8WWI1 | LMO7 | S751 | ochoa | LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP) | None |
| Q8WWN9 | IPCEF1 | S209 | ochoa | Interactor protein for cytohesin exchange factors 1 (Phosphoinositide-binding protein PIP3-E) | Enhances the promotion of guanine-nucleotide exchange by PSCD2 on ARF6 in a concentration-dependent manner. {ECO:0000250}. |
| Q8WXE1 | ATRIP | S72 | psp | ATR-interacting protein (ATM and Rad3-related-interacting protein) | Required for checkpoint signaling after DNA damage. Required for ATR expression, possibly by stabilizing the protein. {ECO:0000269|PubMed:12791985}. |
| Q8WXH0 | SYNE2 | S1111 | ochoa | Nesprin-2 (KASH domain-containing protein 2) (KASH2) (Nuclear envelope spectrin repeat protein 2) (Nucleus and actin connecting element protein) (Protein NUANCE) (Synaptic nuclear envelope protein 2) (Syne-2) | Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (PubMed:34818527). Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. May be involved in nucleus-centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probable association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 may act redundantly. During INM at G1 phase mediates respective LINC complex association with kinesin to push the nucleus away from the centrosome. Involved in nuclear migration in retinal photoreceptor progenitors. Required for centrosome migration to the apical cell surface during early ciliogenesis. Facilitates the relaxation of mechanical stress imposed by compressive actin fibers at the rupture site through its nteraction with SYN2 (PubMed:34818527). {ECO:0000250|UniProtKB:Q6ZWQ0, ECO:0000269|PubMed:12118075, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:22945352, ECO:0000269|PubMed:34818527}. |
| Q8WZA9 | IRGQ | S44 | ochoa | Immunity-related GTPase family Q protein | Autophagy receptor that specifically promotes clearance of misfolded MHC class I molecules by targeting them to the lysosome for degradation (PubMed:39481378). Acts as a molecular adapter that specifically recognizes and binds (1) misfolded MHC class I molecules following their ubiquitination, as well as (2) autophagy-related proteins, promoting the recruitment of misfolded MHC class I molecules to autophagy machinery for degradation (PubMed:39481378). Degradation of misfolded MHC class I molecules is essential to prevent accumulation of defective MHC class I complexes at the surface of CD8(+) T-cells and prevent a stronger T-cell-mediated response (PubMed:39481378). In contrast to other members of the family, does not show GTPase activity (PubMed:39481378). {ECO:0000269|PubMed:39481378}. |
| Q93052 | LPP | S126 | ochoa | Lipoma-preferred partner (LIM domain-containing preferred translocation partner in lipoma) | May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus. {ECO:0000269|PubMed:10637295}. |
| Q969G5 | CAVIN3 | S62 | ochoa | Caveolae-associated protein 3 (Cavin-3) (Protein kinase C delta-binding protein) (Serum deprivation response factor-related gene product that binds to C-kinase) (hSRBC) | Regulates the traffic and/or budding of caveolae (PubMed:19262564). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in smooth muscle but not in the lung and heart endothelial cells. Regulates the equilibrium between cell surface-associated and cell surface-dissociated caveolae by promoting the rapid release of caveolae from the cell surface. Plays a role in the regulation of the circadian clock. Modulates the period length and phase of circadian gene expression and also regulates expression and interaction of the core clock components PER1/2 and CRY1/2 (By similarity). {ECO:0000250|UniProtKB:Q91VJ2, ECO:0000250|UniProtKB:Q9Z1H9, ECO:0000269|PubMed:19262564}. |
| Q969G9 | NKD1 | S169 | ochoa | Protein naked cuticle homolog 1 (Naked-1) (hNkd) (hNkd1) | Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity. {ECO:0000269|PubMed:11752446, ECO:0000269|PubMed:15687260, ECO:0000269|PubMed:16567647}. |
| Q96AD5 | PNPLA2 | S428 | ochoa | Patatin-like phospholipase domain-containing protein 2 (EC 3.1.1.3) (Adipose triglyceride lipase) (Calcium-independent phospholipase A2-zeta) (iPLA2-zeta) (EC 3.1.1.4) (Desnutrin) (Pigment epithelium-derived factor receptor) (PEDF-R) (TTS2.2) (Transport-secretion protein 2) (TTS2) | Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets (PubMed:15364929, PubMed:15550674, PubMed:16150821, PubMed:16239926, PubMed:17603008, PubMed:34903883). Exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone and acts coordinately with LIPE/HLS and DGAT2 within the lipolytic cascade (By similarity). Also possesses acylglycerol transacylase and phospholipase A2 activities (PubMed:15364929, PubMed:17032652, PubMed:17603008). Transfers fatty acid from triglyceride to retinol, hydrolyzes retinylesters, and generates 1,3-diacylglycerol from triglycerides (PubMed:17603008). Regulates adiposome size and may be involved in the degradation of adiposomes (PubMed:16239926). Catalyzes the formation of an ester bond between hydroxy fatty acids and fatty acids derived from triglycerides or diglycerides to generate fatty acid esters of hydroxy fatty acids (FAHFAs) in adipocytes (PubMed:35676490). Acts antagonistically with LDAH in regulation of cellular lipid stores (PubMed:28578400). Inhibits LDAH-stimulated lipid droplet fusion (PubMed:28578400). May play an important role in energy homeostasis (By similarity). May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion (By similarity). {ECO:0000250|UniProtKB:Q8BJ56, ECO:0000269|PubMed:15364929, ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16239926, ECO:0000269|PubMed:17032652, ECO:0000269|PubMed:17603008, ECO:0000269|PubMed:28578400, ECO:0000269|PubMed:34903883, ECO:0000269|PubMed:35676490}. |
| Q96BX8 | MOB3A | S38 | psp | MOB kinase activator 3A (MOB-LAK) (Mob1 homolog 2A) (Mps one binder kinase activator-like 2A) | May regulate the activity of kinases. {ECO:0000250}. |
| Q96BZ8 | LENG1 | S59 | ochoa | Leukocyte receptor cluster member 1 | None |
| Q96FI4 | NEIL1 | S207 | ochoa|psp | Endonuclease 8-like 1 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil1) (DNA-(apurinic or apyrimidinic site) lyase Neil1) (Endonuclease VIII-like 1) (FPG1) (Nei homolog 1) (NEH1) (Nei-like protein 1) | Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. {ECO:0000269|PubMed:11904416, ECO:0000269|PubMed:12200441, ECO:0000269|PubMed:12509226, ECO:0000269|PubMed:14522990}. |
| Q96MT3 | PRICKLE1 | S597 | ochoa | Prickle-like protein 1 (REST/NRSF-interacting LIM domain protein 1) | Involved in the planar cell polarity pathway that controls convergent extension during gastrulation and neural tube closure. Convergent extension is a complex morphogenetic process during which cells elongate, move mediolaterally, and intercalate between neighboring cells, leading to convergence toward the mediolateral axis and extension along the anteroposterior axis. Necessary for nuclear localization of REST. May serve as nuclear receptor. {ECO:0000269|PubMed:21901791}. |
| Q96PV0 | SYNGAP1 | S1204 | ochoa | Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1) | Major constituent of the PSD essential for postsynaptic signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of the NMDAR signaling complex in excitatory synapses, it may play a role in NMDAR-dependent control of AMPAR potentiation, AMPAR membrane trafficking and synaptic plasticity. Regulates AMPAR-mediated miniature excitatory postsynaptic currents. Exhibits dual GTPase-activating specificity for Ras and Rap. May be involved in certain forms of brain injury, leading to long-term learning and memory deficits (By similarity). {ECO:0000250}. |
| Q96QT4 | TRPM7 | S1660 | psp | Transient receptor potential cation channel subfamily M member 7 (EC 2.7.11.1) (Channel-kinase 1) (Long transient receptor potential channel 7) (LTrpC-7) (LTrpC7) [Cleaved into: TRPM7 kinase, cleaved form (M7CK); TRPM7 channel, cleaved form] | Bifunctional protein that combines an ion channel with an intrinsic kinase domain, enabling it to modulate cellular functions either by conducting ions through the pore or by phosphorylating downstream proteins via its kinase domain. The channel is highly permeable to divalent cations, specifically calcium (Ca2+), magnesium (Mg2+) and zinc (Zn2+) and mediates their influx (PubMed:11385574, PubMed:12887921, PubMed:15485879, PubMed:24316671, PubMed:35561741, PubMed:36027648). Controls a wide range of biological processes such as Ca2(+), Mg(2+) and Zn(2+) homeostasis, vesicular Zn(2+) release channel and intracellular Ca(2+) signaling, embryonic development, immune responses, cell motility, proliferation and differentiation (By similarity). The C-terminal alpha-kinase domain autophosphorylates cytoplasmic residues of TRPM7 (PubMed:18365021). In vivo, TRPM7 phosphorylates SMAD2, suggesting that TRPM7 kinase may play a role in activating SMAD signaling pathways. In vitro, TRPM7 kinase phosphorylates ANXA1 (annexin A1), myosin II isoforms and a variety of proteins with diverse cellular functions (PubMed:15485879, PubMed:18394644). {ECO:0000250|UniProtKB:Q923J1, ECO:0000269|PubMed:11385574, ECO:0000269|PubMed:12887921, ECO:0000269|PubMed:15485879, ECO:0000269|PubMed:18365021, ECO:0000269|PubMed:18394644, ECO:0000269|PubMed:24316671, ECO:0000269|PubMed:35561741, ECO:0000269|PubMed:36027648}.; FUNCTION: [TRPM7 channel, cleaved form]: The cleaved channel exhibits substantially higher current and potentiates Fas receptor signaling. {ECO:0000250|UniProtKB:Q923J1}.; FUNCTION: [TRPM7 kinase, cleaved form]: The C-terminal kinase domain can be cleaved from the channel segment in a cell-type-specific fashion. In immune cells, the TRPM7 kinase domain is clipped from the channel domain by caspases in response to Fas-receptor stimulation. The cleaved kinase fragments can translocate to the nucleus, and bind chromatin-remodeling complex proteins in a Zn(2+)-dependent manner to ultimately phosphorylate specific Ser/Thr residues of histones known to be functionally important for cell differentiation and embryonic development. {ECO:0000250|UniProtKB:Q923J1}. |
| Q99733 | NAP1L4 | S54 | ochoa | Nucleosome assembly protein 1-like 4 (Nucleosome assembly protein 2) (NAP-2) | Acts as a histone chaperone in nucleosome assembly. {ECO:0000269|PubMed:9325046}. |
| Q99983 | OMD | S233 | ochoa | Osteomodulin (Keratan sulfate proteoglycan osteomodulin) (KSPG osteomodulin) (Osteoadherin) (OSAD) | May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin. {ECO:0000250|UniProtKB:O77742}. |
| Q9BXW9 | FANCD2 | S898 | psp | Fanconi anemia group D2 protein (Protein FACD2) | Required for maintenance of chromosomal stability (PubMed:11239453, PubMed:14517836). Promotes accurate and efficient pairing of homologs during meiosis (PubMed:14517836). Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing (PubMed:15671039, PubMed:15650050, PubMed:30335751, PubMed:36385258). The FANCI-FANCD2 complex binds and scans double-stranded DNA (dsDNA) for DNA damage; this complex stalls at DNA junctions between double-stranded DNA and single-stranded DNA (By similarity). May participate in S phase and G2 phase checkpoint activation upon DNA damage (PubMed:15377654). Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress (PubMed:15454491, PubMed:15661754). Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress (PubMed:15661754, PubMed:19465921). Promotes BRCA2/FANCD1 loading onto damaged chromatin (PubMed:11239454, PubMed:12239151, PubMed:12086603, PubMed:15115758, PubMed:15199141, PubMed:15671039, PubMed:18212739). May also be involved in B-cell immunoglobulin isotype switching. {ECO:0000250|UniProtKB:Q68Y81, ECO:0000269|PubMed:11239453, ECO:0000269|PubMed:11239454, ECO:0000269|PubMed:12086603, ECO:0000269|PubMed:12239151, ECO:0000269|PubMed:14517836, ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15314022, ECO:0000269|PubMed:15377654, ECO:0000269|PubMed:15454491, ECO:0000269|PubMed:15650050, ECO:0000269|PubMed:15661754, ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:19465921, ECO:0000269|PubMed:30335751, ECO:0000269|PubMed:36385258}. |
| Q9BZF1 | OSBPL8 | S32 | ochoa | Oxysterol-binding protein-related protein 8 (ORP-8) (OSBP-related protein 8) | Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206935). Binds oxysterol, 25-hydroxycholesterol and cholesterol (PubMed:17428193, PubMed:17991739, PubMed:21698267). {ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:17991739, ECO:0000269|PubMed:21698267, ECO:0000269|PubMed:26206935}. |
| Q9H6A9 | PCNX3 | S244 | ochoa | Pecanex-like protein 3 (Pecanex homolog protein 3) | None |
| Q9NPI1 | BRD7 | S380 | ochoa | Bromodomain-containing protein 7 (75 kDa bromodomain protein) (Protein CELTIX-1) | Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR (By similarity). Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase. {ECO:0000250, ECO:0000269|PubMed:16265664, ECO:0000269|PubMed:16475162, ECO:0000269|PubMed:20215511, ECO:0000269|PubMed:20228809, ECO:0000269|PubMed:20660729}. |
| Q9NQA3 | WASH6P | S201 | ochoa | WAS protein family homolog 6 (Protein FAM39A) | May act as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7}. |
| Q9NUQ9 | CYRIB | S117 | ochoa | CYFIP-related Rac1 interactor B (L1) | Negatively regulates RAC1 signaling and RAC1-driven cytoskeletal remodeling (PubMed:30250061, PubMed:31285585). Regulates chemotaxis, cell migration and epithelial polarization by controlling the polarity, plasticity, duration and extent of protrusions. Limits Rac1 mediated activation of the Scar/WAVE complex, focuses protrusion signals and regulates pseudopod complexity by inhibiting Scar/WAVE-induced actin polymerization (PubMed:30250061). Protects against Salmonella bacterial infection. Attenuates processes such as macropinocytosis, phagocytosis and cell migration and restrict sopE-mediated bacterial entry (PubMed:31285585). Also restricts infection mediated by Mycobacterium tuberculosis and Listeria monocytogenes (By similarity). Involved in the regulation of mitochondrial dynamics and oxidative stress (PubMed:29059164). {ECO:0000250|UniProtKB:Q921M7, ECO:0000269|PubMed:29059164, ECO:0000269|PubMed:30250061, ECO:0000269|PubMed:31285585}. |
| Q9NWB7 | IFT57 | Y168 | ochoa | Intraflagellar transport protein 57 homolog (Dermal papilla-derived protein 8) (Estrogen-related receptor beta-like protein 1) (HIP1-interacting protein) (MHS4R2) | Required for the formation of cilia. Plays an indirect role in sonic hedgehog signaling, cilia being required for all activity of the hedgehog pathway (By similarity). Has pro-apoptotic function via its interaction with HIP1, leading to recruit caspase-8 (CASP8) and trigger apoptosis. Has the ability to bind DNA sequence motif 5'-AAAGACATG-3' present in the promoter of caspase genes such as CASP1, CASP8 and CASP10, suggesting that it may act as a transcription regulator; however the relevance of such function remains unclear. {ECO:0000250, ECO:0000269|PubMed:11788820, ECO:0000269|PubMed:17107665, ECO:0000269|PubMed:17623017}. |
| Q9NXD2 | MTMR10 | S582 | ochoa | Myotubularin-related protein 10 (Inactive phosphatidylinositol 3-phosphatase 10) | None |
| Q9NYV6 | RRN3 | S199 | psp | RNA polymerase I-specific transcription initiation factor RRN3 (Transcription initiation factor IA) (TIF-IA) | Required for efficient transcription initiation by RNA polymerase I (Pol I). Required for the formation of the competent pre-initiation complex (PIC). {ECO:0000250, ECO:0000269|PubMed:10758157, ECO:0000269|PubMed:11250903, ECO:0000269|PubMed:11265758, ECO:0000269|PubMed:15805466}. |
| Q9P2E9 | RRBP1 | S165 | ochoa | Ribosome-binding protein 1 (180 kDa ribosome receptor homolog) (RRp) (ES/130-related protein) (Ribosome receptor protein) | Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane. {ECO:0000250}. |
| Q9UBB4 | ATXN10 | S430 | ochoa | Ataxin-10 (Brain protein E46 homolog) (Spinocerebellar ataxia type 10 protein) | May play a role in the regulation of cytokinesis (PubMed:21857149, PubMed:25666058). May play a role in signaling by stimulating protein glycosylation. Induces neuritogenesis by activating the Ras-MAP kinase pathway and is necessary for the survival of cerebellar neurons (By similarity). Does not appear to play a major role in ciliogenesis (By similarity). {ECO:0000250|UniProtKB:P28658, ECO:0000250|UniProtKB:Q9ER24, ECO:0000269|PubMed:21857149, ECO:0000269|PubMed:25666058}. |
| Q9UER7 | DAXX | S564 | psp | Death domain-associated protein 6 (Daxx) (hDaxx) (ETS1-associated protein 1) (EAP1) (Fas death domain-associated protein) | Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (PubMed:15016915). {ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:15364927, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:17081986, ECO:0000269|PubMed:17942542, ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:24530302}. |
| Q9UGN5 | PARP2 | S353 | ochoa | Poly [ADP-ribose] polymerase 2 (PARP-2) (hPARP-2) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 2) (ARTD2) (DNA ADP-ribosyltransferase PARP2) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 2) (ADPRT-2) (Poly[ADP-ribose] synthase 2) (pADPRT-2) (Protein poly-ADP-ribosyltransferase PARP2) (EC 2.4.2.-) | Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:10364231, PubMed:25043379, PubMed:27471034, PubMed:30104678, PubMed:32028527, PubMed:32939087, PubMed:34108479, PubMed:34486521, PubMed:34874266). Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed:25043379, PubMed:30104678, PubMed:30321391). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:32939087). Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 (PubMed:25043379). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site (PubMed:28190768, PubMed:32028527, PubMed:34108479, PubMed:34486521, PubMed:34874266). PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed:10364231, PubMed:32939087, PubMed:34108479). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains (PubMed:34732825, PubMed:34795260). Specifically mediates formation of branched poly-ADP-ribosylation (PubMed:30104678). Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF (PubMed:30104678). In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex (PubMed:27471034, PubMed:29361132). {ECO:0000269|PubMed:10364231, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:27471034, ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29361132, ECO:0000269|PubMed:30104678, ECO:0000269|PubMed:30321391, ECO:0000269|PubMed:32028527, ECO:0000269|PubMed:32939087, ECO:0000269|PubMed:34108479, ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34732825, ECO:0000269|PubMed:34795260, ECO:0000269|PubMed:34874266}. |
| Q9UIF8 | BAZ2B | S1467 | ochoa | Bromodomain adjacent to zinc finger domain protein 2B (hWALp4) | Regulatory subunit of the ATP-dependent BRF-1 and BRF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). The BRF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the BRF-5 ISWI chromatin remodeling complex (PubMed:28801535). Chromatin reader protein, which may play a role in transcriptional regulation via interaction with ISWI (By similarity) (PubMed:10662543). Involved in positively modulating the rate of age-related behavioral deterioration (By similarity). Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with histone methyltransferase EHMT1 (By similarity). {ECO:0000250|UniProtKB:A2AUY4, ECO:0000269|PubMed:28801535, ECO:0000303|PubMed:10662543}. |
| Q9UJS0 | SLC25A13 | S472 | ochoa | Electrogenic aspartate/glutamate antiporter SLC25A13, mitochondrial (Calcium-binding mitochondrial carrier protein Aralar2) (ARALAR-related gene 2) (ARALAR2) (Citrin) (Mitochondrial aspartate glutamate carrier 2) (Solute carrier family 25 member 13) | Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle (PubMed:11566871, PubMed:38945283). Also mediates the uptake of L-cysteinesulfinate (3-sulfino-L-alanine) by mitochondria in exchange of L-glutamate and proton (PubMed:11566871). Can also exchange L-cysteinesulfinate with aspartate in their anionic form without any proton translocation (PubMed:11566871). Lacks transport activity towards gamma-aminobutyric acid (GABA) (PubMed:38945283). {ECO:0000269|PubMed:11566871, ECO:0000269|PubMed:38945283}. |
| Q9UKL3 | CASP8AP2 | S1674 | ochoa | CASP8-associated protein 2 (FLICE-associated huge protein) | Participates in TNF-alpha-induced blockade of glucocorticoid receptor (GR) transactivation at the nuclear receptor coactivator level, upstream and independently of NF-kappa-B. Suppresses both NCOA2- and NCOA3-induced enhancement of GR transactivation. Involved in TNF-alpha-induced activation of NF-kappa-B via a TRAF2-dependent pathway. Acts as a downstream mediator for CASP8-induced activation of NF-kappa-B. Required for the activation of CASP8 in FAS-mediated apoptosis. Required for histone gene transcription and progression through S phase. {ECO:0000269|PubMed:12477726, ECO:0000269|PubMed:15698540, ECO:0000269|PubMed:17003125, ECO:0000269|PubMed:17245429}. |
| Q9UKX2 | MYH2 | S1239 | ochoa | Myosin-2 (Myosin heavy chain 2) (Myosin heavy chain 2a) (MyHC-2a) (Myosin heavy chain IIa) (MyHC-IIa) (Myosin heavy chain, skeletal muscle, adult 2) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. {ECO:0000250|UniProtKB:P12883}. |
| Q9UKX2 | MYH2 | S1482 | ochoa | Myosin-2 (Myosin heavy chain 2) (Myosin heavy chain 2a) (MyHC-2a) (Myosin heavy chain IIa) (MyHC-IIa) (Myosin heavy chain, skeletal muscle, adult 2) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. {ECO:0000250|UniProtKB:P12883}. |
| Q9UKX3 | MYH13 | S1480 | ochoa | Myosin-13 (Myosin heavy chain 13) (Myosin heavy chain, skeletal muscle, extraocular) (MyHC-EO) (Myosin heavy chain, skeletal muscle, laryngeal) (MyHC-IIL) (Superfast myosin) | Fast twitching myosin mediating the high-velocity and low-tension contractions of specific striated muscles. {ECO:0000269|PubMed:23908353}. |
| Q9ULD2 | MTUS1 | S1083 | ochoa | Microtubule-associated tumor suppressor 1 (AT2 receptor-binding protein) (Angiotensin-II type 2 receptor-interacting protein) (Mitochondrial tumor suppressor 1) | Cooperates with AGTR2 to inhibit ERK2 activation and cell proliferation. May be required for AGTR2 cell surface expression. Together with PTPN6, induces UBE2V2 expression upon angiotensin-II stimulation. Isoform 1 inhibits breast cancer cell proliferation, delays the progression of mitosis by prolonging metaphase and reduces tumor growth. {ECO:0000269|PubMed:12692079, ECO:0000269|PubMed:19794912}. |
| Q9ULL1 | PLEKHG1 | S930 | ochoa | Pleckstrin homology domain-containing family G member 1 | None |
| Q9ULL8 | SHROOM4 | S1019 | ochoa | Protein Shroom4 (Second homolog of apical protein) | Probable regulator of cytoskeletal architecture that plays an important role in development. May regulate cellular and cytoskeletal architecture by modulating the spatial distribution of myosin II (By similarity). {ECO:0000250, ECO:0000269|PubMed:16684770}. |
| Q9UPQ0 | LIMCH1 | S377 | ochoa | LIM and calponin homology domains-containing protein 1 | Actin stress fibers-associated protein that activates non-muscle myosin IIa. Activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. Through the activation of non-muscle myosin IIa, positively regulates actin stress fibers assembly and stabilizes focal adhesions. It therefore negatively regulates cell spreading and cell migration. {ECO:0000269|PubMed:28228547}. |
| Q9Y2H5 | PLEKHA6 | S591 | ochoa | Pleckstrin homology domain-containing family A member 6 (PH domain-containing family A member 6) (Phosphoinositol 3-phosphate-binding protein 3) (PEPP-3) | None |
| Q9Y2I6 | NINL | S448 | psp | Ninein-like protein | Involved in the microtubule organization in interphase cells. Overexpression induces the fragmentation of the Golgi, and causes lysosomes to disperse toward the cell periphery; it also interferes with mitotic spindle assembly. Involved in vesicle transport in photoreceptor cells (By similarity). May play a role in ovarian carcinogenesis. {ECO:0000250|UniProtKB:G9G127, ECO:0000269|PubMed:12852856, ECO:0000269|PubMed:16254247, ECO:0000269|PubMed:18538832}. |
| Q9Y623 | MYH4 | S1480 | ochoa | Myosin-4 (Myosin heavy chain 2b) (MyHC-2b) (Myosin heavy chain 4) (Myosin heavy chain IIb) (MyHC-IIb) (Myosin heavy chain, skeletal muscle, fetal) | Muscle contraction. |
| Q9Y657 | SPIN1 | S109 | psp | Spindlin-1 (Ovarian cancer-related protein) (Spindlin1) | Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and 'Lys-9' (H3K4me3K9me3) and is involved in piRNA-mediated retrotransposon silencing during spermatogenesis (PubMed:33574238). Plays a key role in the initiation of the PIWIL4-piRNA pathway, a pathway that directs transposon DNA methylation and silencing in the male embryonic germ cells, by promoting recruitment of DNA methylation machinery to transposons: binds young, but not old, LINE1 transposons, which are specifically marked with H3K4me3K9me3, and promotes the recruitment of PIWIL4 and SPOCD1 to transposons, leading to piRNA-directed DNA methylation (By similarity). Also recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway downstream of PRMT2 (PubMed:22258766, PubMed:29061846). In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway (PubMed:24589551). Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes (PubMed:21960006). May play a role in cell-cycle regulation during the transition from gamete to embryo (By similarity). Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption (By similarity). {ECO:0000250|UniProtKB:Q61142, ECO:0000269|PubMed:21960006, ECO:0000269|PubMed:22258766, ECO:0000269|PubMed:24589551, ECO:0000269|PubMed:29061846, ECO:0000269|PubMed:33574238}. |
| P08238 | HSP90AB1 | S383 | Sugiyama | Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84) (Heat shock protein family C member 3) | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:19696785, ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:32272059, ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.; FUNCTION: (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes (PubMed:21949862). Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable). {ECO:0000269|PubMed:21949862, ECO:0000305|PubMed:22066472}. |
| Q9Y4L1 | HYOU1 | S763 | Sugiyama | Hypoxia up-regulated protein 1 (150 kDa oxygen-regulated protein) (ORP-150) (170 kDa glucose-regulated protein) (GRP-170) (Heat shock protein family H member 4) | Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. Promotes HSPA5/BiP-mediated ATP nucleotide exchange and thereby activates the unfolded protein response (UPR) pathway in the presence of endoplasmic reticulum stress (By similarity). May play a role as a molecular chaperone and participate in protein folding. {ECO:0000250|UniProtKB:Q9JKR6, ECO:0000269|PubMed:10037731}. |
| O43707 | ACTN4 | S511 | Sugiyama | Alpha-actinin-4 (Non-muscle alpha-actinin 4) | F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (PubMed:22351778). Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation (PubMed:22689882). {ECO:0000250|UniProtKB:P57780, ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:22689882, ECO:0000305|PubMed:9508771}. |
| O75330 | HMMR | S344 | Sugiyama | Hyaluronan mediated motility receptor (Intracellular hyaluronic acid-binding protein) (Receptor for hyaluronan-mediated motility) (CD antigen CD168) | Receptor for hyaluronic acid (HA) (By similarity). Involved in cell motility (By similarity). When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity. May act as a regulator of adipogenisis (By similarity). {ECO:0000250|UniProtKB:Q00547}. |
| P05787 | KRT8 | S404 | Sugiyama | 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}. |
| Q9NP81 | SARS2 | S53 | Sugiyama | Serine--tRNA ligase, mitochondrial (EC 6.1.1.11) (SerRSmt) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) | Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). {ECO:0000250|UniProtKB:Q9N0F3}. |
| P63241 | EIF5A | S100 | Sugiyama | Eukaryotic translation initiation factor 5A-1 (eIF-5A-1) (eIF-5A1) (Eukaryotic initiation factor 5A isoform 1) (eIF-5A) (Rev-binding factor) (eIF-4D) | Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (PubMed:33547280). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (By similarity). Acts as a ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity (PubMed:16987817). With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis (PubMed:15371445). Also regulates TNF-alpha-mediated apoptosis (PubMed:15452064, PubMed:17187778). Mediates effects of polyamines on neuronal process extension and survival (PubMed:17360499). Is required for autophagy by assisting the ribosome in translating the ATG3 protein at a specific amino acid sequence, the 'ASP-ASP-Gly' motif, leading to the increase of the efficiency of ATG3 translation and facilitation of LC3B lipidation and autophagosome formation (PubMed:29712776). {ECO:0000250|UniProtKB:P23301, ECO:0000269|PubMed:15371445, ECO:0000269|PubMed:15452064, ECO:0000269|PubMed:16987817, ECO:0000269|PubMed:17187778, ECO:0000269|PubMed:17360499, ECO:0000269|PubMed:29712776, ECO:0000269|PubMed:33547280}.; FUNCTION: (Microbial infection) Cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts. {ECO:0000269|PubMed:8253832}. |
| O95721 | SNAP29 | S204 | Sugiyama | Synaptosomal-associated protein 29 (SNAP-29) (Soluble 29 kDa NSF attachment protein) (Vesicle-membrane fusion protein SNAP-29) | SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also plays a role in ciliogenesis by regulating membrane fusions. {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686250, ECO:0000269|PubMed:25686604}. |
| P00519 | ABL1 | S1106 | Sugiyama | Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150) | Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9 (PubMed:22810897). Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (PubMed:28428613). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 also acts as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner (By similarity). Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (By similarity). Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (By similarity). {ECO:0000250|UniProtKB:P00520, ECO:0000269|PubMed:10391250, ECO:0000269|PubMed:11971963, ECO:0000269|PubMed:12379650, ECO:0000269|PubMed:12531427, ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:15556646, ECO:0000269|PubMed:15657060, ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16424036, ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:16943190, ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:17623672, ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:18945674, ECO:0000269|PubMed:19891780, ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:20417104, ECO:0000269|PubMed:22810897, ECO:0000269|PubMed:28428613, ECO:0000269|PubMed:9037071, ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9461559}. |
| Q9Y490 | TLN1 | S1891 | Sugiyama | Talin-1 | High molecular weight cytoskeletal protein concentrated at regions of cell-matrix and cell-cell contacts. Involved in connections of major cytoskeletal structures to the plasma membrane. With KANK1 co-organize the assembly of cortical microtubule stabilizing complexes (CMSCs) positioned to control microtubule-actin crosstalk at focal adhesions (FAs) rims. {ECO:0000250|UniProtKB:P26039}. |
| Q12778 | FOXO1 | S212 | GPS6|SIGNOR|EPSD|PSP | Forkhead box protein O1 (Forkhead box protein O1A) (Forkhead in rhabdomyosarcoma) | Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (PubMed:10358076, PubMed:12228231, PubMed:15220471, PubMed:15890677, PubMed:18356527, PubMed:19221179, PubMed:20543840, PubMed:21245099). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3' (PubMed:10358076). Activity suppressed by insulin (PubMed:10358076). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (PubMed:17024043). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (PubMed:18356527, PubMed:19221179). Promotes neural cell death (PubMed:18356527). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (PubMed:20543840). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). Positive regulator of apoptosis in cardiac smooth muscle cells as a result of its transcriptional activation of pro-apoptotic genes (PubMed:19483080). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). {ECO:0000250|UniProtKB:A4L7N3, ECO:0000250|UniProtKB:G3V7R4, ECO:0000250|UniProtKB:Q9R1E0, ECO:0000269|PubMed:10358076, ECO:0000269|PubMed:12228231, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:15890677, ECO:0000269|PubMed:17024043, ECO:0000269|PubMed:18356527, ECO:0000269|PubMed:19221179, ECO:0000269|PubMed:19483080, ECO:0000269|PubMed:20543840, ECO:0000269|PubMed:21245099, ECO:0000269|PubMed:31063815}. |
| P28340 | POLD1 | S1042 | Sugiyama | DNA polymerase delta catalytic subunit (EC 2.7.7.7) (3'-5' exodeoxyribonuclease) (EC 3.1.11.-) (DNA polymerase subunit delta p125) | As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair (PubMed:16510448, PubMed:19074196, PubMed:20334433, PubMed:24022480, PubMed:24035200, PubMed:31449058). Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities (PubMed:16510448, PubMed:19074196, PubMed:20334433, PubMed:24022480, PubMed:24035200). Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4 (PubMed:19074196, PubMed:20334433). Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated (PubMed:24035200). Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation (PubMed:20227374). Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR) (PubMed:24310611). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine, 8oxoG or abasic sites (PubMed:19074196, PubMed:24191025). {ECO:0000269|PubMed:16510448, ECO:0000269|PubMed:19074196, ECO:0000269|PubMed:20227374, ECO:0000269|PubMed:20334433, ECO:0000269|PubMed:24022480, ECO:0000269|PubMed:24035200, ECO:0000269|PubMed:24191025, ECO:0000269|PubMed:24310611, ECO:0000269|PubMed:31449058}. |
| Q14164 | IKBKE | S695 | Sugiyama | Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i) | Serine/threonine kinase that plays an essential role in regulating inflammatory responses to viral infection, through the activation of the type I IFN, NF-kappa-B and STAT signaling. Also involved in TNFA and inflammatory cytokines, like Interleukin-1, signaling. Following activation of viral RNA sensors, such as RIG-I-like receptors, associates with DDX3X and phosphorylates interferon regulatory factors (IRFs), IRF3 and IRF7, as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB. In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD can be recruited to the IKBKE-containing-complexes. Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway through, at least, the phosphorylation of CYLD. Phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. In addition, is also required for the induction of a subset of ISGs which displays antiviral activity, may be through the phosphorylation of STAT1 at 'Ser-708'. Phosphorylation of STAT1 at 'Ser-708' also seems to promote the assembly and DNA binding of ISGF3 (STAT1:STAT2:IRF9) complexes compared to GAF (STAT1:STAT1) complexes, in this way regulating the balance between type I and type II IFN responses. Protects cells against DNA damage-induced cell death. Also plays an important role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Phosphorylates AKT1. {ECO:0000269|PubMed:17568778, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:19153231, ECO:0000269|PubMed:20188669, ECO:0000269|PubMed:21138416, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:22532683, ECO:0000269|PubMed:23453969, ECO:0000269|PubMed:23478265}. |
| P17987 | TCP1 | S372 | Sugiyama | T-complex protein 1 subunit alpha (TCP-1-alpha) (EC 3.6.1.-) (CCT-alpha) (Chaperonin containing T-complex polypeptide 1 subunit 1) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
| Q9BVC4 | MLST8 | S43 | Sugiyama | 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}. |
| Q8NBK3 | SUMF1 | S234 | Sugiyama | Formylglycine-generating enzyme (FGE) (EC 1.8.3.7) (C-alpha-formylglycine-generating enzyme 1) (Sulfatase-modifying factor 1) | Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:16368756, PubMed:21224894, PubMed:25931126). 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:16368756, PubMed:25931126). Known substrates include GALNS, ARSA, STS and ARSE (PubMed:12757706, PubMed:15657036, PubMed:15907468). {ECO:0000269|PubMed:12757706, ECO:0000269|PubMed:15657036, ECO:0000269|PubMed:15907468, ECO:0000269|PubMed:16368756, ECO:0000269|PubMed:21224894, ECO:0000269|PubMed:25931126}. |
| P07942 | LAMB1 | S1294 | Sugiyama | Laminin subunit beta-1 (Laminin B1 chain) (Laminin-1 subunit beta) (Laminin-10 subunit beta) (Laminin-12 subunit beta) (Laminin-2 subunit beta) (Laminin-6 subunit beta) (Laminin-8 subunit beta) | Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface. {ECO:0000269|PubMed:23472759}. |
| P83436 | COG7 | S559 | Sugiyama | Conserved oligomeric Golgi complex subunit 7 (COG complex subunit 7) (Component of oligomeric Golgi complex 7) | Required for normal Golgi function. {ECO:0000269|PubMed:11980916}. |
| Q9H4B4 | PLK3 | S304 | Sugiyama | Serine/threonine-protein kinase PLK3 (EC 2.7.11.21) (Cytokine-inducible serine/threonine-protein kinase) (FGF-inducible kinase) (Polo-like kinase 3) (PLK-3) (Proliferation-related kinase) | Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1. {ECO:0000269|PubMed:10557092, ECO:0000269|PubMed:11156373, ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11551930, ECO:0000269|PubMed:11971976, ECO:0000269|PubMed:12242661, ECO:0000269|PubMed:14968113, ECO:0000269|PubMed:14980500, ECO:0000269|PubMed:15021912, ECO:0000269|PubMed:16478733, ECO:0000269|PubMed:16481012, ECO:0000269|PubMed:17264206, ECO:0000269|PubMed:17804415, ECO:0000269|PubMed:18062778, ECO:0000269|PubMed:18650425, ECO:0000269|PubMed:19103756, ECO:0000269|PubMed:19490146, ECO:0000269|PubMed:20889502, ECO:0000269|PubMed:20940307, ECO:0000269|PubMed:20951827, ECO:0000269|PubMed:21098032, ECO:0000269|PubMed:21264284, ECO:0000269|PubMed:21376736, ECO:0000269|PubMed:21840391, ECO:0000269|PubMed:9353331}. |
| Q9UK32 | RPS6KA6 | S560 | Sugiyama | Ribosomal protein S6 kinase alpha-6 (S6K-alpha-6) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 6) (p90-RSK 6) (p90RSK6) (Ribosomal S6 kinase 4) (RSK-4) (pp90RSK4) | Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis. {ECO:0000269|PubMed:15042092, ECO:0000269|PubMed:15632195}. |
| P36578 | RPL4 | S131 | Sugiyama | Large ribosomal subunit protein uL4 (60S ribosomal protein L1) (60S ribosomal protein L4) | Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}. |
Download
| reactome_id | name | p | -log10_p |
|---|---|---|---|
| R-HSA-1640170 | Cell Cycle | 1.353614e-08 | 7.869 |
| R-HSA-9725370 | Signaling by ALK fusions and activated point mutants | 1.087859e-08 | 7.963 |
| R-HSA-9700206 | Signaling by ALK in cancer | 1.087859e-08 | 7.963 |
| R-HSA-390522 | Striated Muscle Contraction | 2.494453e-07 | 6.603 |
| R-HSA-69278 | Cell Cycle, Mitotic | 5.933652e-07 | 6.227 |
| R-HSA-5663202 | Diseases of signal transduction by growth factor receptors and second messengers | 1.282103e-06 | 5.892 |
| R-HSA-111465 | Apoptotic cleavage of cellular proteins | 1.539726e-06 | 5.813 |
| R-HSA-1280215 | Cytokine Signaling in Immune system | 1.741489e-06 | 5.759 |
| R-HSA-68886 | M Phase | 3.922577e-06 | 5.406 |
| R-HSA-68877 | Mitotic Prometaphase | 1.023874e-05 | 4.990 |
| R-HSA-75153 | Apoptotic execution phase | 2.475431e-05 | 4.606 |
| R-HSA-397014 | Muscle contraction | 3.448119e-05 | 4.462 |
| R-HSA-69620 | Cell Cycle Checkpoints | 4.296324e-05 | 4.367 |
| R-HSA-141444 | Amplification of signal from unattached kinetochores via a MAD2 inhibitory si... | 7.842238e-05 | 4.106 |
| R-HSA-141424 | Amplification of signal from the kinetochores | 7.842238e-05 | 4.106 |
| R-HSA-8935964 | RUNX1 regulates expression of components of tight junctions | 8.174982e-05 | 4.088 |
| R-HSA-168256 | Immune System | 1.237103e-04 | 3.908 |
| R-HSA-449147 | Signaling by Interleukins | 1.448059e-04 | 3.839 |
| R-HSA-6796648 | TP53 Regulates Transcription of DNA Repair Genes | 1.726895e-04 | 3.763 |
| R-HSA-9860927 | Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZ... | 1.963465e-04 | 3.707 |
| R-HSA-373755 | Semaphorin interactions | 1.933867e-04 | 3.714 |
| R-HSA-69275 | G2/M Transition | 2.399319e-04 | 3.620 |
| R-HSA-453274 | Mitotic G2-G2/M phases | 2.667424e-04 | 3.574 |
| R-HSA-69618 | Mitotic Spindle Checkpoint | 3.231612e-04 | 3.491 |
| R-HSA-2500257 | Resolution of Sister Chromatid Cohesion | 4.609426e-04 | 3.336 |
| R-HSA-913531 | Interferon Signaling | 4.564920e-04 | 3.341 |
| R-HSA-9613829 | Chaperone Mediated Autophagy | 4.974105e-04 | 3.303 |
| R-HSA-109581 | Apoptosis | 5.961411e-04 | 3.225 |
| R-HSA-5357801 | Programmed Cell Death | 6.494601e-04 | 3.187 |
| R-HSA-9648025 | EML4 and NUDC in mitotic spindle formation | 6.552376e-04 | 3.184 |
| R-HSA-416572 | Sema4D induced cell migration and growth-cone collapse | 7.216780e-04 | 3.142 |
| R-HSA-373753 | Nephrin family interactions | 7.216780e-04 | 3.142 |
| R-HSA-9013973 | TICAM1-dependent activation of IRF3/IRF7 | 8.683914e-04 | 3.061 |
| R-HSA-68882 | Mitotic Anaphase | 1.062942e-03 | 2.973 |
| R-HSA-8950505 | Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulati... | 1.101653e-03 | 2.958 |
| R-HSA-2555396 | Mitotic Metaphase and Anaphase | 1.109679e-03 | 2.955 |
| R-HSA-1169410 | Antiviral mechanism by IFN-stimulated genes | 1.190479e-03 | 2.924 |
| R-HSA-5674400 | Constitutive Signaling by AKT1 E17K in Cancer | 1.386275e-03 | 2.858 |
| R-HSA-9860931 | Response of endothelial cells to shear stress | 1.572585e-03 | 2.803 |
| R-HSA-168164 | Toll Like Receptor 3 (TLR3) Cascade | 1.781164e-03 | 2.749 |
| R-HSA-400685 | Sema4D in semaphorin signaling | 1.850617e-03 | 2.733 |
| R-HSA-9705671 | SARS-CoV-2 activates/modulates innate and adaptive immune responses | 1.929910e-03 | 2.714 |
| R-HSA-2467813 | Separation of Sister Chromatids | 1.945530e-03 | 2.711 |
| R-HSA-199991 | Membrane Trafficking | 2.097771e-03 | 2.678 |
| R-HSA-166166 | MyD88-independent TLR4 cascade | 2.401689e-03 | 2.619 |
| R-HSA-937061 | TRIF (TICAM1)-mediated TLR4 signaling | 2.401689e-03 | 2.619 |
| R-HSA-9020591 | Interleukin-12 signaling | 2.614732e-03 | 2.583 |
| R-HSA-936964 | Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) | 2.932182e-03 | 2.533 |
| R-HSA-9855142 | Cellular responses to mechanical stimuli | 3.013932e-03 | 2.521 |
| R-HSA-5602636 | IKBKB deficiency causes SCID | 3.231653e-03 | 2.491 |
| R-HSA-5603027 | IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (E... | 3.231653e-03 | 2.491 |
| R-HSA-352238 | Breakdown of the nuclear lamina | 3.231653e-03 | 2.491 |
| R-HSA-5693532 | DNA Double-Strand Break Repair | 3.284784e-03 | 2.483 |
| R-HSA-909733 | Interferon alpha/beta signaling | 3.550077e-03 | 2.450 |
| R-HSA-9828211 | Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation | 3.690777e-03 | 2.433 |
| R-HSA-351906 | Apoptotic cleavage of cell adhesion proteins | 3.690777e-03 | 2.433 |
| R-HSA-5693538 | Homology Directed Repair | 4.159288e-03 | 2.381 |
| R-HSA-1606322 | ZBP1(DAI) mediated induction of type I IFNs | 4.042206e-03 | 2.393 |
| R-HSA-5357905 | Regulation of TNFR1 signaling | 4.220748e-03 | 2.375 |
| R-HSA-9705683 | SARS-CoV-2-host interactions | 4.331020e-03 | 2.363 |
| R-HSA-264870 | Caspase-mediated cleavage of cytoskeletal proteins | 4.695723e-03 | 2.328 |
| R-HSA-8854518 | AURKA Activation by TPX2 | 4.921299e-03 | 2.308 |
| R-HSA-5653656 | Vesicle-mediated transport | 5.376016e-03 | 2.270 |
| R-HSA-381038 | XBP1(S) activates chaperone genes | 5.409804e-03 | 2.267 |
| R-HSA-447115 | Interleukin-12 family signaling | 5.746759e-03 | 2.241 |
| R-HSA-9764790 | Positive Regulation of CDH1 Gene Transcription | 5.850868e-03 | 2.233 |
| R-HSA-168898 | Toll-like Receptor Cascades | 6.337590e-03 | 2.198 |
| R-HSA-933543 | NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 | 7.161737e-03 | 2.145 |
| R-HSA-9924644 | Developmental Lineages of the Mammary Gland | 7.397471e-03 | 2.131 |
| R-HSA-6804757 | Regulation of TP53 Degradation | 7.283359e-03 | 2.138 |
| R-HSA-166016 | Toll Like Receptor 4 (TLR4) Cascade | 7.192925e-03 | 2.143 |
| R-HSA-445355 | Smooth Muscle Contraction | 7.484660e-03 | 2.126 |
| R-HSA-381070 | IRE1alpha activates chaperones | 7.676943e-03 | 2.115 |
| R-HSA-9824878 | Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 | 8.633058e-03 | 2.064 |
| R-HSA-446652 | Interleukin-1 family signaling | 8.494306e-03 | 2.071 |
| R-HSA-6811442 | Intra-Golgi and retrograde Golgi-to-ER traffic | 8.797589e-03 | 2.056 |
| R-HSA-168928 | DDX58/IFIH1-mediated induction of interferon-alpha/beta | 9.543301e-03 | 2.020 |
| R-HSA-1169408 | ISG15 antiviral mechanism | 8.934375e-03 | 2.049 |
| R-HSA-6806003 | Regulation of TP53 Expression and Degradation | 9.551273e-03 | 2.020 |
| R-HSA-5578775 | Ion homeostasis | 9.329561e-03 | 2.030 |
| R-HSA-75893 | TNF signaling | 9.329561e-03 | 2.030 |
| R-HSA-2980766 | Nuclear Envelope Breakdown | 1.001082e-02 | 2.000 |
| R-HSA-8862803 | Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's dis... | 1.007766e-02 | 1.997 |
| R-HSA-8863678 | Neurodegenerative Diseases | 1.007766e-02 | 1.997 |
| R-HSA-198323 | AKT phosphorylates targets in the cytosol | 1.026881e-02 | 1.988 |
| R-HSA-73894 | DNA Repair | 1.038758e-02 | 1.983 |
| R-HSA-5684264 | MAP3K8 (TPL2)-dependent MAPK1/3 activation | 1.404606e-02 | 1.852 |
| R-HSA-380284 | Loss of proteins required for interphase microtubule organization from the centr... | 1.485650e-02 | 1.828 |
| R-HSA-380259 | Loss of Nlp from mitotic centrosomes | 1.485650e-02 | 1.828 |
| R-HSA-6798695 | Neutrophil degranulation | 1.475657e-02 | 1.831 |
| R-HSA-9833482 | PKR-mediated signaling | 1.199785e-02 | 1.921 |
| R-HSA-9705677 | SARS-CoV-2 targets PDZ proteins in cell-cell junction | 1.224295e-02 | 1.912 |
| R-HSA-2565942 | Regulation of PLK1 Activity at G2/M Transition | 1.494506e-02 | 1.826 |
| R-HSA-69615 | G1/S DNA Damage Checkpoints | 1.485650e-02 | 1.828 |
| R-HSA-450294 | MAP kinase activation | 1.309113e-02 | 1.883 |
| R-HSA-68875 | Mitotic Prophase | 1.320695e-02 | 1.879 |
| R-HSA-162909 | Host Interactions of HIV factors | 1.567044e-02 | 1.805 |
| R-HSA-168249 | Innate Immune System | 1.430343e-02 | 1.845 |
| R-HSA-3928663 | EPHA-mediated growth cone collapse | 1.384481e-02 | 1.859 |
| R-HSA-6790901 | rRNA modification in the nucleus and cytosol | 1.485650e-02 | 1.828 |
| R-HSA-9734009 | Defective Intrinsic Pathway for Apoptosis | 1.384481e-02 | 1.859 |
| R-HSA-170834 | Signaling by TGF-beta Receptor Complex | 1.115050e-02 | 1.953 |
| R-HSA-1500931 | Cell-Cell communication | 1.337666e-02 | 1.874 |
| R-HSA-381119 | Unfolded Protein Response (UPR) | 1.250364e-02 | 1.903 |
| R-HSA-168643 | Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali... | 1.579837e-02 | 1.801 |
| R-HSA-168927 | TICAM1, RIP1-mediated IKK complex recruitment | 1.619218e-02 | 1.791 |
| R-HSA-1810476 | RIP-mediated NFkB activation via ZBP1 | 1.619218e-02 | 1.791 |
| R-HSA-9854909 | Regulation of MITF-M dependent genes involved in invasion | 1.636627e-02 | 1.786 |
| R-HSA-69613 | p53-Independent G1/S DNA Damage Checkpoint | 1.663052e-02 | 1.779 |
| R-HSA-69601 | Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A | 1.663052e-02 | 1.779 |
| R-HSA-6783310 | Fanconi Anemia Pathway | 1.663052e-02 | 1.779 |
| R-HSA-9675135 | Diseases of DNA repair | 1.786449e-02 | 1.748 |
| R-HSA-9008059 | Interleukin-37 signaling | 1.840280e-02 | 1.735 |
| R-HSA-9652817 | Signaling by MAPK mutants | 2.099530e-02 | 1.678 |
| R-HSA-918233 | TRAF3-dependent IRF activation pathway | 2.100663e-02 | 1.678 |
| R-HSA-380320 | Recruitment of NuMA to mitotic centrosomes | 1.931192e-02 | 1.714 |
| R-HSA-5620912 | Anchoring of the basal body to the plasma membrane | 2.128546e-02 | 1.672 |
| R-HSA-936440 | Negative regulators of DDX58/IFIH1 signaling | 2.010549e-02 | 1.697 |
| R-HSA-5685942 | HDR through Homologous Recombination (HRR) | 1.887018e-02 | 1.724 |
| R-HSA-5603029 | IkBA variant leads to EDA-ID | 2.099530e-02 | 1.678 |
| R-HSA-9860276 | SLC15A4:TASL-dependent IRF5 activation | 2.099530e-02 | 1.678 |
| R-HSA-448424 | Interleukin-17 signaling | 2.232668e-02 | 1.651 |
| R-HSA-73887 | Death Receptor Signaling | 2.275807e-02 | 1.643 |
| R-HSA-5658442 | Regulation of RAS by GAPs | 2.340027e-02 | 1.631 |
| R-HSA-9909505 | Modulation of host responses by IFN-stimulated genes | 2.367625e-02 | 1.626 |
| R-HSA-5693568 | Resolution of D-loop Structures through Holliday Junction Intermediates | 2.379377e-02 | 1.624 |
| R-HSA-69273 | Cyclin A/B1/B2 associated events during G2/M transition | 2.379377e-02 | 1.624 |
| R-HSA-9612973 | Autophagy | 2.437329e-02 | 1.613 |
| R-HSA-69656 | Cyclin A:Cdk2-associated events at S phase entry | 2.485388e-02 | 1.605 |
| R-HSA-162582 | Signal Transduction | 2.518702e-02 | 1.599 |
| R-HSA-5693567 | HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA) | 2.523649e-02 | 1.598 |
| R-HSA-9616334 | Defective Base Excision Repair Associated with NEIL1 | 2.719668e-02 | 1.565 |
| R-HSA-9661070 | Defective translocation of RB1 mutants to the nucleus | 2.719668e-02 | 1.565 |
| R-HSA-937041 | IKK complex recruitment mediated by RIP1 | 2.954002e-02 | 1.530 |
| R-HSA-9927426 | Developmental Lineage of Mammary Gland Alveolar Cells | 2.786616e-02 | 1.555 |
| R-HSA-380270 | Recruitment of mitotic centrosome proteins and complexes | 2.618622e-02 | 1.582 |
| R-HSA-380287 | Centrosome maturation | 2.899132e-02 | 1.538 |
| R-HSA-5693537 | Resolution of D-Loop Structures | 2.578150e-02 | 1.589 |
| R-HSA-168638 | NOD1/2 Signaling Pathway | 2.786616e-02 | 1.555 |
| R-HSA-4419969 | Depolymerization of the Nuclear Lamina | 2.652088e-02 | 1.576 |
| R-HSA-168138 | Toll Like Receptor 9 (TLR9) Cascade | 2.733652e-02 | 1.563 |
| R-HSA-9694516 | SARS-CoV-2 Infection | 2.942001e-02 | 1.531 |
| R-HSA-6811434 | COPI-dependent Golgi-to-ER retrograde traffic | 3.057699e-02 | 1.515 |
| R-HSA-3700989 | Transcriptional Regulation by TP53 | 3.071063e-02 | 1.513 |
| R-HSA-428890 | Role of ABL in ROBO-SLIT signaling | 3.165003e-02 | 1.500 |
| R-HSA-5336415 | Uptake and function of diphtheria toxin | 3.165003e-02 | 1.500 |
| R-HSA-1632852 | Macroautophagy | 3.323465e-02 | 1.478 |
| R-HSA-2173793 | Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer | 3.359745e-02 | 1.474 |
| R-HSA-9764561 | Regulation of CDH1 Function | 3.552676e-02 | 1.449 |
| R-HSA-165054 | Rev-mediated nuclear export of HIV RNA | 3.718653e-02 | 1.430 |
| R-HSA-9020702 | Interleukin-1 signaling | 3.759114e-02 | 1.425 |
| R-HSA-446107 | Type I hemidesmosome assembly | 3.761865e-02 | 1.425 |
| R-HSA-9825895 | Regulation of MITF-M-dependent genes involved in DNA replication, damage repair ... | 3.761865e-02 | 1.425 |
| R-HSA-2995383 | Initiation of Nuclear Envelope (NE) Reformation | 3.963380e-02 | 1.402 |
| R-HSA-69541 | Stabilization of p53 | 3.976406e-02 | 1.401 |
| R-HSA-168276 | NS1 Mediated Effects on Host Pathways | 3.976406e-02 | 1.401 |
| R-HSA-983189 | Kinesins | 4.171856e-02 | 1.380 |
| R-HSA-199977 | ER to Golgi Anterograde Transport | 4.174033e-02 | 1.379 |
| R-HSA-204626 | Hypusine synthesis from eIF5A-lysine | 4.397871e-02 | 1.357 |
| R-HSA-5676590 | NIK-->noncanonical NF-kB signaling | 4.521711e-02 | 1.345 |
| R-HSA-9734779 | Developmental Cell Lineages of the Integumentary System | 5.087324e-02 | 1.294 |
| R-HSA-6802957 | Oncogenic MAPK signaling | 4.594959e-02 | 1.338 |
| R-HSA-69481 | G2/M Checkpoints | 4.548889e-02 | 1.342 |
| R-HSA-73933 | Resolution of Abasic Sites (AP sites) | 4.521711e-02 | 1.345 |
| R-HSA-975138 | TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation | 5.087324e-02 | 1.294 |
| R-HSA-177243 | Interactions of Rev with host cellular proteins | 4.244093e-02 | 1.372 |
| R-HSA-9820962 | Assembly and release of respiratory syncytial virus (RSV) virions | 5.070463e-02 | 1.295 |
| R-HSA-9834752 | Respiratory syncytial virus genome replication | 4.397871e-02 | 1.357 |
| R-HSA-9927418 | Developmental Lineage of Mammary Gland Luminal Epithelial Cells | 5.106669e-02 | 1.292 |
| R-HSA-933542 | TRAF6 mediated NF-kB activation | 5.124550e-02 | 1.290 |
| R-HSA-9679506 | SARS-CoV Infections | 5.139024e-02 | 1.289 |
| R-HSA-9006821 | Alternative Lengthening of Telomeres (ALT) | 5.365533e-02 | 1.270 |
| R-HSA-9673013 | Diseases of Telomere Maintenance | 5.365533e-02 | 1.270 |
| R-HSA-9670621 | Defective Inhibition of DNA Recombination at Telomere | 5.365533e-02 | 1.270 |
| R-HSA-5632927 | Defective Mismatch Repair Associated With MSH3 | 5.365533e-02 | 1.270 |
| R-HSA-9699150 | Defective DNA double strand break response due to BARD1 loss of function | 5.365533e-02 | 1.270 |
| R-HSA-9670615 | Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations | 5.365533e-02 | 1.270 |
| R-HSA-5602566 | TICAM1 deficiency - HSE | 5.365533e-02 | 1.270 |
| R-HSA-9663199 | Defective DNA double strand break response due to BRCA1 loss of function | 5.365533e-02 | 1.270 |
| R-HSA-9670613 | Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations | 5.365533e-02 | 1.270 |
| R-HSA-997272 | Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits | 5.544255e-02 | 1.256 |
| R-HSA-1296041 | Activation of G protein gated Potassium channels | 5.544255e-02 | 1.256 |
| R-HSA-1296059 | G protein gated Potassium channels | 5.544255e-02 | 1.256 |
| R-HSA-5607761 | Dectin-1 mediated noncanonical NF-kB signaling | 6.057860e-02 | 1.218 |
| R-HSA-9703465 | Signaling by FLT3 fusion proteins | 5.979816e-02 | 1.223 |
| R-HSA-110373 | Resolution of AP sites via the multiple-nucleotide patch replacement pathway | 5.979816e-02 | 1.223 |
| R-HSA-169131 | Inhibition of PKR | 5.365533e-02 | 1.270 |
| R-HSA-110362 | POLB-Dependent Long Patch Base Excision Repair | 6.515702e-02 | 1.186 |
| R-HSA-68884 | Mitotic Telophase/Cytokinesis | 6.515702e-02 | 1.186 |
| R-HSA-202670 | ERKs are inactivated | 6.515702e-02 | 1.186 |
| R-HSA-8856688 | Golgi-to-ER retrograde transport | 5.523605e-02 | 1.258 |
| R-HSA-1236974 | ER-Phagosome pathway | 5.633648e-02 | 1.249 |
| R-HSA-9663891 | Selective autophagy | 5.415515e-02 | 1.266 |
| R-HSA-5633007 | Regulation of TP53 Activity | 6.118872e-02 | 1.213 |
| R-HSA-975155 | MyD88 dependent cascade initiated on endosome | 5.271721e-02 | 1.278 |
| R-HSA-168181 | Toll Like Receptor 7/8 (TLR7/8) Cascade | 6.050921e-02 | 1.218 |
| R-HSA-9662360 | Sensory processing of sound by inner hair cells of the cochlea | 6.123616e-02 | 1.213 |
| R-HSA-9818028 | NFE2L2 regulates pentose phosphate pathway genes | 6.515702e-02 | 1.186 |
| R-HSA-381183 | ATF6 (ATF6-alpha) activates chaperone genes | 6.515702e-02 | 1.186 |
| R-HSA-5357956 | TNFR1-induced NF-kappa-B signaling pathway | 6.430921e-02 | 1.192 |
| R-HSA-163765 | ChREBP activates metabolic gene expression | 5.777188e-02 | 1.238 |
| R-HSA-1168372 | Downstream signaling events of B Cell Receptor (BCR) | 6.680156e-02 | 1.175 |
| R-HSA-69202 | Cyclin E associated events during G1/S transition | 6.680156e-02 | 1.175 |
| R-HSA-1834949 | Cytosolic sensors of pathogen-associated DNA | 6.680156e-02 | 1.175 |
| R-HSA-5617833 | Cilium Assembly | 6.727125e-02 | 1.172 |
| R-HSA-176034 | Interactions of Tat with host cellular proteins | 7.939592e-02 | 1.100 |
| R-HSA-5609974 | Defective PGM1 causes PGM1-CDG | 7.939592e-02 | 1.100 |
| R-HSA-5602571 | TRAF3 deficiency - HSE | 7.939592e-02 | 1.100 |
| R-HSA-5619056 | Defective HK1 causes hexokinase deficiency (HK deficiency) | 7.939592e-02 | 1.100 |
| R-HSA-3000484 | Scavenging by Class F Receptors | 7.283762e-02 | 1.138 |
| R-HSA-9615710 | Late endosomal microautophagy | 7.378422e-02 | 1.132 |
| R-HSA-9927432 | Developmental Lineage of Mammary Gland Myoepithelial Cells | 7.378422e-02 | 1.132 |
| R-HSA-5619107 | Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC... | 7.874112e-02 | 1.104 |
| R-HSA-1855196 | IP3 and IP4 transport between cytosol and nucleus | 8.383934e-02 | 1.077 |
| R-HSA-1855229 | IP6 and IP7 transport between cytosol and nucleus | 8.383934e-02 | 1.077 |
| R-HSA-6807878 | COPI-mediated anterograde transport | 7.832003e-02 | 1.106 |
| R-HSA-69473 | G2/M DNA damage checkpoint | 7.874699e-02 | 1.104 |
| R-HSA-5632928 | Defective Mismatch Repair Associated With MSH2 | 7.939592e-02 | 1.100 |
| R-HSA-2559584 | Formation of Senescence-Associated Heterochromatin Foci (SAHF) | 8.079224e-02 | 1.093 |
| R-HSA-77387 | Insulin receptor recycling | 6.897238e-02 | 1.161 |
| R-HSA-1296065 | Inwardly rectifying K+ channels | 8.907504e-02 | 1.050 |
| R-HSA-9833109 | Evasion by RSV of host interferon responses | 8.383934e-02 | 1.077 |
| R-HSA-69563 | p53-Dependent G1 DNA Damage Response | 7.461180e-02 | 1.127 |
| R-HSA-69580 | p53-Dependent G1/S DNA damage checkpoint | 7.461180e-02 | 1.127 |
| R-HSA-75035 | Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex | 8.079224e-02 | 1.093 |
| R-HSA-9766229 | Degradation of CDH1 | 7.461180e-02 | 1.127 |
| R-HSA-1169091 | Activation of NF-kappaB in B cells | 8.219146e-02 | 1.085 |
| R-HSA-5685939 | HDR through MMEJ (alt-NHEJ) | 8.079224e-02 | 1.093 |
| R-HSA-975871 | MyD88 cascade initiated on plasma membrane | 8.377773e-02 | 1.077 |
| R-HSA-168142 | Toll Like Receptor 10 (TLR10) Cascade | 8.377773e-02 | 1.077 |
| R-HSA-168176 | Toll Like Receptor 5 (TLR5) Cascade | 8.377773e-02 | 1.077 |
| R-HSA-166058 | MyD88:MAL(TIRAP) cascade initiated on plasma membrane | 7.810879e-02 | 1.107 |
| R-HSA-168188 | Toll Like Receptor TLR6:TLR2 Cascade | 7.810879e-02 | 1.107 |
| R-HSA-168179 | Toll Like Receptor TLR1:TLR2 Cascade | 8.540271e-02 | 1.069 |
| R-HSA-181438 | Toll Like Receptor 2 (TLR2) Cascade | 8.540271e-02 | 1.069 |
| R-HSA-975144 | IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation | 7.283762e-02 | 1.138 |
| R-HSA-937039 | IRAK1 recruits IKK complex | 7.283762e-02 | 1.138 |
| R-HSA-9029558 | NR1H2 & NR1H3 regulate gene expression linked to lipogenesis | 8.079224e-02 | 1.093 |
| R-HSA-5673001 | RAF/MAP kinase cascade | 9.007110e-02 | 1.045 |
| R-HSA-2132295 | MHC class II antigen presentation | 8.791769e-02 | 1.056 |
| R-HSA-5683057 | MAPK family signaling cascades | 8.737024e-02 | 1.059 |
| R-HSA-9692916 | SARS-CoV-1 activates/modulates innate immune responses | 8.611825e-02 | 1.065 |
| R-HSA-9725371 | Nuclear events stimulated by ALK signaling in cancer | 7.096123e-02 | 1.149 |
| R-HSA-422475 | Axon guidance | 6.987447e-02 | 1.156 |
| R-HSA-9675108 | Nervous system development | 7.605085e-02 | 1.119 |
| R-HSA-70171 | Glycolysis | 8.944100e-02 | 1.048 |
| R-HSA-9764265 | Regulation of CDH1 Expression and Function | 8.773068e-02 | 1.057 |
| R-HSA-9764274 | Regulation of Expression and Function of Type I Classical Cadherins | 8.773068e-02 | 1.057 |
| R-HSA-446728 | Cell junction organization | 7.290695e-02 | 1.137 |
| R-HSA-381033 | ATF6 (ATF6-alpha) activates chaperones | 8.079224e-02 | 1.093 |
| R-HSA-1221632 | Meiotic synapsis | 9.013469e-02 | 1.045 |
| R-HSA-416482 | G alpha (12/13) signalling events | 9.175902e-02 | 1.037 |
| R-HSA-983231 | Factors involved in megakaryocyte development and platelet production | 9.200518e-02 | 1.036 |
| R-HSA-8953897 | Cellular responses to stimuli | 9.209994e-02 | 1.036 |
| R-HSA-1855170 | IPs transport between nucleus and cytosol | 9.444426e-02 | 1.025 |
| R-HSA-159227 | Transport of the SLBP independent Mature mRNA | 9.444426e-02 | 1.025 |
| R-HSA-5685938 | HDR through Single Strand Annealing (SSA) | 9.444426e-02 | 1.025 |
| R-HSA-9659379 | Sensory processing of sound | 9.517502e-02 | 1.021 |
| R-HSA-9679191 | Potential therapeutics for SARS | 9.677311e-02 | 1.014 |
| R-HSA-9856651 | MITF-M-dependent gene expression | 9.677311e-02 | 1.014 |
| R-HSA-2173791 | TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) | 9.744236e-02 | 1.011 |
| R-HSA-3270619 | IRF3-mediated induction of type I IFN | 9.744236e-02 | 1.011 |
| R-HSA-399954 | Sema3A PAK dependent Axon repulsion | 9.744236e-02 | 1.011 |
| R-HSA-2995410 | Nuclear Envelope (NE) Reassembly | 9.865504e-02 | 1.006 |
| R-HSA-159230 | Transport of the SLBP Dependant Mature mRNA | 9.994299e-02 | 1.000 |
| R-HSA-170822 | Regulation of Glucokinase by Glucokinase Regulatory Protein | 9.994299e-02 | 1.000 |
| R-HSA-9665230 | Drug resistance in ERBB2 KD mutants | 1.044379e-01 | 0.981 |
| R-HSA-9652282 | Drug-mediated inhibition of ERBB2 signaling | 1.044379e-01 | 0.981 |
| R-HSA-9665246 | Resistance of ERBB2 KD mutants to neratinib | 1.044379e-01 | 0.981 |
| R-HSA-9665249 | Resistance of ERBB2 KD mutants to afatinib | 1.044379e-01 | 0.981 |
| R-HSA-9665737 | Drug resistance in ERBB2 TMD/JMD mutants | 1.044379e-01 | 0.981 |
| R-HSA-9665247 | Resistance of ERBB2 KD mutants to osimertinib | 1.044379e-01 | 0.981 |
| R-HSA-9665250 | Resistance of ERBB2 KD mutants to AEE788 | 1.044379e-01 | 0.981 |
| R-HSA-9665245 | Resistance of ERBB2 KD mutants to tesevatinib | 1.044379e-01 | 0.981 |
| R-HSA-3656535 | TGFBR1 LBD Mutants in Cancer | 1.044379e-01 | 0.981 |
| R-HSA-9665233 | Resistance of ERBB2 KD mutants to trastuzumab | 1.044379e-01 | 0.981 |
| R-HSA-9665251 | Resistance of ERBB2 KD mutants to lapatinib | 1.044379e-01 | 0.981 |
| R-HSA-9665244 | Resistance of ERBB2 KD mutants to sapitinib | 1.044379e-01 | 0.981 |
| R-HSA-9013957 | TLR3-mediated TICAM1-dependent programmed cell death | 1.525012e-01 | 0.817 |
| R-HSA-211163 | AKT-mediated inactivation of FOXO1A | 1.525012e-01 | 0.817 |
| R-HSA-69200 | Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 ... | 1.525012e-01 | 0.817 |
| R-HSA-399710 | Activation of AMPA receptors | 1.755588e-01 | 0.756 |
| R-HSA-8985586 | SLIT2:ROBO1 increases RHOA activity | 1.979905e-01 | 0.703 |
| R-HSA-111459 | Activation of caspases through apoptosome-mediated cleavage | 1.979905e-01 | 0.703 |
| R-HSA-9842640 | Signaling by LTK in cancer | 2.198132e-01 | 0.658 |
| R-HSA-3656244 | Defective B4GALT1 causes B4GALT1-CDG (CDG-2d) | 2.198132e-01 | 0.658 |
| R-HSA-3656225 | Defective CHST6 causes MCDC1 | 2.198132e-01 | 0.658 |
| R-HSA-3656243 | Defective ST3GAL3 causes MCT12 and EIEE15 | 2.198132e-01 | 0.658 |
| R-HSA-2562578 | TRIF-mediated programmed cell death | 2.410434e-01 | 0.618 |
| R-HSA-112126 | ALKBH3 mediated reversal of alkylation damage | 2.616971e-01 | 0.582 |
| R-HSA-444257 | RSK activation | 2.616971e-01 | 0.582 |
| R-HSA-9709603 | Impaired BRCA2 binding to PALB2 | 1.425344e-01 | 0.846 |
| R-HSA-5649702 | APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement P... | 2.817901e-01 | 0.550 |
| R-HSA-9613354 | Lipophagy | 2.817901e-01 | 0.550 |
| R-HSA-9701193 | Defective homologous recombination repair (HRR) due to PALB2 loss of function | 1.520149e-01 | 0.818 |
| R-HSA-9704646 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 1.520149e-01 | 0.818 |
| R-HSA-9704331 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 1.520149e-01 | 0.818 |
| R-HSA-9701192 | Defective homologous recombination repair (HRR) due to BRCA1 loss of function | 1.520149e-01 | 0.818 |
| R-HSA-9014325 | TICAM1,TRAF6-dependent induction of TAK1 complex | 3.013374e-01 | 0.521 |
| R-HSA-390450 | Folding of actin by CCT/TriC | 3.013374e-01 | 0.521 |
| R-HSA-438066 | Unblocking of NMDA receptors, glutamate binding and activation | 1.713209e-01 | 0.766 |
| R-HSA-5696400 | Dual Incision in GG-NER | 1.055671e-01 | 0.976 |
| R-HSA-3301854 | Nuclear Pore Complex (NPC) Disassembly | 1.113125e-01 | 0.953 |
| R-HSA-159231 | Transport of Mature mRNA Derived from an Intronless Transcript | 1.354215e-01 | 0.868 |
| R-HSA-5693554 | Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD... | 2.109568e-01 | 0.676 |
| R-HSA-159234 | Transport of Mature mRNAs Derived from Intronless Transcripts | 1.417093e-01 | 0.849 |
| R-HSA-9709570 | Impaired BRCA2 binding to RAD51 | 2.513677e-01 | 0.600 |
| R-HSA-6802952 | Signaling by BRAF and RAF1 fusions | 1.447842e-01 | 0.839 |
| R-HSA-399719 | Trafficking of AMPA receptors | 2.716738e-01 | 0.566 |
| R-HSA-5693571 | Nonhomologous End-Joining (NHEJ) | 2.020890e-01 | 0.694 |
| R-HSA-9675126 | Diseases of mitotic cell cycle | 2.818233e-01 | 0.550 |
| R-HSA-399721 | Glutamate binding, activation of AMPA receptors and synaptic plasticity | 2.919607e-01 | 0.535 |
| R-HSA-442742 | CREB1 phosphorylation through NMDA receptor-mediated activation of RAS signaling | 2.919607e-01 | 0.535 |
| R-HSA-383280 | Nuclear Receptor transcription pathway | 2.149365e-01 | 0.668 |
| R-HSA-9841922 | MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesi... | 1.926605e-01 | 0.715 |
| R-HSA-9851695 | Epigenetic regulation of adipogenesis genes by MLL3 and MLL4 complexes | 1.926605e-01 | 0.715 |
| R-HSA-3371497 | HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig... | 1.601049e-01 | 0.796 |
| R-HSA-5358606 | Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) | 1.239887e-01 | 0.907 |
| R-HSA-9818564 | Epigenetic regulation of gene expression by MLL3 and MLL4 complexes | 1.926605e-01 | 0.715 |
| R-HSA-9646399 | Aggrephagy | 1.417093e-01 | 0.849 |
| R-HSA-9627069 | Regulation of the apoptosome activity | 3.013374e-01 | 0.521 |
| R-HSA-354192 | Integrin signaling | 2.919607e-01 | 0.535 |
| R-HSA-6807505 | RNA polymerase II transcribes snRNA genes | 1.247480e-01 | 0.904 |
| R-HSA-111458 | Formation of apoptosome | 3.013374e-01 | 0.521 |
| R-HSA-9615933 | Postmitotic nuclear pore complex (NPC) reformation | 2.210122e-01 | 0.656 |
| R-HSA-5693565 | Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at... | 1.160375e-01 | 0.935 |
| R-HSA-9675136 | Diseases of DNA Double-Strand Break Repair | 1.055671e-01 | 0.976 |
| R-HSA-933541 | TRAF6 mediated IRF7 activation | 1.231500e-01 | 0.910 |
| R-HSA-191650 | Regulation of gap junction activity | 1.525012e-01 | 0.817 |
| R-HSA-164940 | Nef mediated downregulation of MHC class I complex cell surface expression | 2.616971e-01 | 0.582 |
| R-HSA-204005 | COPII-mediated vesicle transport | 1.706346e-01 | 0.768 |
| R-HSA-432722 | Golgi Associated Vesicle Biogenesis | 2.378532e-01 | 0.624 |
| R-HSA-199992 | trans-Golgi Network Vesicle Budding | 1.813986e-01 | 0.741 |
| R-HSA-1606341 | IRF3 mediated activation of type 1 IFN | 1.755588e-01 | 0.756 |
| R-HSA-8849472 | PTK6 Down-Regulation | 1.755588e-01 | 0.756 |
| R-HSA-2025928 | Calcineurin activates NFAT | 2.817901e-01 | 0.550 |
| R-HSA-5357786 | TNFR1-induced proapoptotic signaling | 1.616149e-01 | 0.792 |
| R-HSA-9639288 | Amino acids regulate mTORC1 | 2.378532e-01 | 0.624 |
| R-HSA-174178 | APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins ... | 2.378532e-01 | 0.624 |
| R-HSA-445989 | TAK1-dependent IKK and NF-kappa-B activation | 1.950939e-01 | 0.710 |
| R-HSA-5693606 | DNA Double Strand Break Response | 1.549329e-01 | 0.810 |
| R-HSA-9758274 | Regulation of NF-kappa B signaling | 1.060995e-01 | 0.974 |
| R-HSA-8937144 | Aryl hydrocarbon receptor signalling | 1.979905e-01 | 0.703 |
| R-HSA-9917777 | Epigenetic regulation by WDR5-containing histone modifying complexes | 2.002780e-01 | 0.698 |
| R-HSA-3656534 | Loss of Function of TGFBR1 in Cancer | 1.755588e-01 | 0.756 |
| R-HSA-399955 | SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion | 1.060995e-01 | 0.974 |
| R-HSA-2470946 | Cohesin Loading onto Chromatin | 2.410434e-01 | 0.618 |
| R-HSA-114516 | Disinhibition of SNARE formation | 2.410434e-01 | 0.618 |
| R-HSA-181429 | Serotonin Neurotransmitter Release Cycle | 1.331874e-01 | 0.876 |
| R-HSA-9701190 | Defective homologous recombination repair (HRR) due to BRCA2 loss of function | 1.055671e-01 | 0.976 |
| R-HSA-180910 | Vpr-mediated nuclear import of PICs | 1.231500e-01 | 0.910 |
| R-HSA-6811438 | Intra-Golgi traffic | 1.545673e-01 | 0.811 |
| R-HSA-445095 | Interaction between L1 and Ankyrins | 2.311054e-01 | 0.636 |
| R-HSA-168333 | NEP/NS2 Interacts with the Cellular Export Machinery | 1.812934e-01 | 0.742 |
| R-HSA-437239 | Recycling pathway of L1 | 1.950939e-01 | 0.710 |
| R-HSA-211733 | Regulation of activated PAK-2p34 by proteasome mediated degradation | 2.716738e-01 | 0.566 |
| R-HSA-5358508 | Mismatch Repair | 1.331874e-01 | 0.876 |
| R-HSA-977444 | GABA B receptor activation | 1.611289e-01 | 0.793 |
| R-HSA-5656169 | Termination of translesion DNA synthesis | 2.513677e-01 | 0.600 |
| R-HSA-176187 | Activation of ATR in response to replication stress | 2.919607e-01 | 0.535 |
| R-HSA-1500620 | Meiosis | 1.169911e-01 | 0.932 |
| R-HSA-8849468 | PTK6 Regulates Proteins Involved in RNA Processing | 1.755588e-01 | 0.756 |
| R-HSA-9620244 | Long-term potentiation | 2.109568e-01 | 0.676 |
| R-HSA-3295583 | TRP channels | 2.210122e-01 | 0.656 |
| R-HSA-9734767 | Developmental Cell Lineages | 2.579657e-01 | 0.588 |
| R-HSA-212676 | Dopamine Neurotransmitter Release Cycle | 1.811199e-01 | 0.742 |
| R-HSA-5693579 | Homologous DNA Pairing and Strand Exchange | 1.292337e-01 | 0.889 |
| R-HSA-9907900 | Proteasome assembly | 1.744962e-01 | 0.758 |
| R-HSA-1445148 | Translocation of SLC2A4 (GLUT4) to the plasma membrane | 1.868636e-01 | 0.728 |
| R-HSA-948021 | Transport to the Golgi and subsequent modification | 1.611618e-01 | 0.793 |
| R-HSA-5675482 | Regulation of necroptotic cell death | 2.919607e-01 | 0.535 |
| R-HSA-166208 | mTORC1-mediated signalling | 1.811199e-01 | 0.742 |
| R-HSA-1482801 | Acyl chain remodelling of PS | 2.109568e-01 | 0.676 |
| R-HSA-991365 | Activation of GABAB receptors | 1.611289e-01 | 0.793 |
| R-HSA-3371571 | HSF1-dependent transactivation | 2.234055e-01 | 0.651 |
| R-HSA-9913351 | Formation of the dystrophin-glycoprotein complex (DGC) | 2.716738e-01 | 0.566 |
| R-HSA-5602358 | Diseases associated with the TLR signaling cascade | 1.417093e-01 | 0.849 |
| R-HSA-5260271 | Diseases of Immune System | 1.417093e-01 | 0.849 |
| R-HSA-525793 | Myogenesis | 2.210122e-01 | 0.656 |
| R-HSA-6811440 | Retrograde transport at the Trans-Golgi-Network | 1.950939e-01 | 0.710 |
| R-HSA-5423599 | Diseases of Mismatch Repair (MMR) | 1.288002e-01 | 0.890 |
| R-HSA-111464 | SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes | 1.755588e-01 | 0.756 |
| R-HSA-8941855 | RUNX3 regulates CDKN1A transcription | 1.979905e-01 | 0.703 |
| R-HSA-444473 | Formyl peptide receptors bind formyl peptides and many other ligands | 2.616971e-01 | 0.582 |
| R-HSA-844456 | The NLRP3 inflammasome | 1.425344e-01 | 0.846 |
| R-HSA-9840373 | Cellular response to mitochondrial stress | 2.817901e-01 | 0.550 |
| R-HSA-264642 | Acetylcholine Neurotransmitter Release Cycle | 1.616149e-01 | 0.792 |
| R-HSA-450321 | JNK (c-Jun kinases) phosphorylation and activation mediated by activated human ... | 1.616149e-01 | 0.792 |
| R-HSA-181430 | Norepinephrine Neurotransmitter Release Cycle | 2.009493e-01 | 0.697 |
| R-HSA-8941858 | Regulation of RUNX3 expression and activity | 1.417093e-01 | 0.849 |
| R-HSA-389357 | CD28 dependent PI3K/Akt signaling | 2.311054e-01 | 0.636 |
| R-HSA-194441 | Metabolism of non-coding RNA | 1.160375e-01 | 0.935 |
| R-HSA-191859 | snRNP Assembly | 1.160375e-01 | 0.935 |
| R-HSA-350562 | Regulation of ornithine decarboxylase (ODC) | 2.818233e-01 | 0.550 |
| R-HSA-977443 | GABA receptor activation | 2.894445e-01 | 0.538 |
| R-HSA-168325 | Viral Messenger RNA Synthesis | 2.968983e-01 | 0.527 |
| R-HSA-8953750 | Transcriptional Regulation by E2F6 | 1.354215e-01 | 0.868 |
| R-HSA-8934903 | Receptor Mediated Mitophagy | 3.013374e-01 | 0.521 |
| R-HSA-180746 | Nuclear import of Rev protein | 1.055671e-01 | 0.976 |
| R-HSA-4608870 | Asymmetric localization of PCP proteins | 1.812934e-01 | 0.742 |
| R-HSA-8863795 | Downregulation of ERBB2 signaling | 2.615193e-01 | 0.582 |
| R-HSA-182971 | EGFR downregulation | 2.716738e-01 | 0.566 |
| R-HSA-73884 | Base Excision Repair | 2.922758e-01 | 0.534 |
| R-HSA-9605308 | Diseases of Base Excision Repair | 1.979905e-01 | 0.703 |
| R-HSA-1834941 | STING mediated induction of host immune responses | 1.425344e-01 | 0.846 |
| R-HSA-69242 | S Phase | 1.779726e-01 | 0.750 |
| R-HSA-9706374 | FLT3 signaling through SRC family kinases | 1.525012e-01 | 0.817 |
| R-HSA-111463 | SMAC (DIABLO) binds to IAPs | 1.755588e-01 | 0.756 |
| R-HSA-425986 | Sodium/Proton exchangers | 2.616971e-01 | 0.582 |
| R-HSA-418889 | Caspase activation via Dependence Receptors in the absence of ligand | 2.817901e-01 | 0.550 |
| R-HSA-198693 | AKT phosphorylates targets in the nucleus | 2.817901e-01 | 0.550 |
| R-HSA-176033 | Interactions of Vpr with host cellular proteins | 1.417093e-01 | 0.849 |
| R-HSA-168271 | Transport of Ribonucleoproteins into the Host Nucleus | 1.480926e-01 | 0.829 |
| R-HSA-210500 | Glutamate Neurotransmitter Release Cycle | 2.210122e-01 | 0.656 |
| R-HSA-8940973 | RUNX2 regulates osteoblast differentiation | 2.412269e-01 | 0.618 |
| R-HSA-5694530 | Cargo concentration in the ER | 2.716738e-01 | 0.566 |
| R-HSA-3000171 | Non-integrin membrane-ECM interactions | 1.979492e-01 | 0.703 |
| R-HSA-3371556 | Cellular response to heat stress | 1.723317e-01 | 0.764 |
| R-HSA-1236975 | Antigen processing-Cross presentation | 1.174065e-01 | 0.930 |
| R-HSA-2219528 | PI3K/AKT Signaling in Cancer | 3.008577e-01 | 0.522 |
| R-HSA-1852241 | Organelle biogenesis and maintenance | 2.329522e-01 | 0.633 |
| R-HSA-9686347 | Microbial modulation of RIPK1-mediated regulated necrosis | 2.410434e-01 | 0.618 |
| R-HSA-5607764 | CLEC7A (Dectin-1) signaling | 1.758694e-01 | 0.755 |
| R-HSA-6804115 | TP53 regulates transcription of additional cell cycle genes whose exact role in ... | 1.811199e-01 | 0.742 |
| R-HSA-8854214 | TBC/RABGAPs | 1.677733e-01 | 0.775 |
| R-HSA-622312 | Inflammasomes | 2.412269e-01 | 0.618 |
| R-HSA-76005 | Response to elevated platelet cytosolic Ca2+ | 1.212945e-01 | 0.916 |
| R-HSA-74160 | Gene expression (Transcription) | 2.957661e-01 | 0.529 |
| R-HSA-8878159 | Transcriptional regulation by RUNX3 | 1.804502e-01 | 0.744 |
| R-HSA-1660499 | Synthesis of PIPs at the plasma membrane | 1.300785e-01 | 0.886 |
| R-HSA-9682385 | FLT3 signaling in disease | 1.171748e-01 | 0.931 |
| R-HSA-202424 | Downstream TCR signaling | 1.409476e-01 | 0.851 |
| R-HSA-162906 | HIV Infection | 2.453760e-01 | 0.610 |
| R-HSA-5250971 | Toxicity of botulinum toxin type C (botC) | 1.755588e-01 | 0.756 |
| R-HSA-3134973 | LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production | 1.755588e-01 | 0.756 |
| R-HSA-111469 | SMAC, XIAP-regulated apoptotic response | 1.979905e-01 | 0.703 |
| R-HSA-9758919 | Epithelial-Mesenchymal Transition (EMT) during gastrulation | 1.979905e-01 | 0.703 |
| R-HSA-446388 | Regulation of cytoskeletal remodeling and cell spreading by IPP complex componen... | 1.979905e-01 | 0.703 |
| R-HSA-5250992 | Toxicity of botulinum toxin type E (botE) | 1.979905e-01 | 0.703 |
| R-HSA-164944 | Nef and signal transduction | 2.198132e-01 | 0.658 |
| R-HSA-5250968 | Toxicity of botulinum toxin type A (botA) | 2.817901e-01 | 0.550 |
| R-HSA-9693928 | Defective RIPK1-mediated regulated necrosis | 3.013374e-01 | 0.521 |
| R-HSA-450302 | activated TAK1 mediates p38 MAPK activation | 1.713209e-01 | 0.766 |
| R-HSA-164952 | The role of Nef in HIV-1 replication and disease pathogenesis | 1.909999e-01 | 0.719 |
| R-HSA-8852276 | The role of GTSE1 in G2/M progression after G2 checkpoint | 1.300785e-01 | 0.886 |
| R-HSA-168274 | Export of Viral Ribonucleoproteins from Nucleus | 1.881607e-01 | 0.725 |
| R-HSA-9856530 | High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR... | 2.264771e-01 | 0.645 |
| R-HSA-70221 | Glycogen breakdown (glycogenolysis) | 2.109568e-01 | 0.676 |
| R-HSA-373760 | L1CAM interactions | 1.529566e-01 | 0.815 |
| R-HSA-5684996 | MAPK1/MAPK3 signaling | 1.022029e-01 | 0.991 |
| R-HSA-5668541 | TNFR2 non-canonical NF-kB pathway | 2.440714e-01 | 0.612 |
| R-HSA-114608 | Platelet degranulation | 2.010381e-01 | 0.697 |
| R-HSA-5357769 | Caspase activation via extrinsic apoptotic signalling pathway | 2.210122e-01 | 0.656 |
| R-HSA-5675221 | Negative regulation of MAPK pathway | 1.545673e-01 | 0.811 |
| R-HSA-5687128 | MAPK6/MAPK4 signaling | 2.559666e-01 | 0.592 |
| R-HSA-2028269 | Signaling by Hippo | 1.239887e-01 | 0.907 |
| R-HSA-6804760 | Regulation of TP53 Activity through Methylation | 1.331874e-01 | 0.876 |
| R-HSA-1362277 | Transcription of E2F targets under negative control by DREAM complex | 1.520149e-01 | 0.818 |
| R-HSA-6807004 | Negative regulation of MET activity | 1.520149e-01 | 0.818 |
| R-HSA-2160916 | Hyaluronan degradation | 2.109568e-01 | 0.676 |
| R-HSA-2029482 | Regulation of actin dynamics for phagocytic cup formation | 2.722288e-01 | 0.565 |
| R-HSA-9645723 | Diseases of programmed cell death | 1.327359e-01 | 0.877 |
| R-HSA-9857377 | Regulation of MITF-M-dependent genes involved in lysosome biogenesis and autopha... | 1.811199e-01 | 0.742 |
| R-HSA-6804756 | Regulation of TP53 Activity through Phosphorylation | 1.247480e-01 | 0.904 |
| R-HSA-5576891 | Cardiac conduction | 2.225420e-01 | 0.653 |
| R-HSA-1643685 | Disease | 2.722317e-01 | 0.565 |
| R-HSA-2173795 | Downregulation of SMAD2/3:SMAD4 transcriptional activity | 2.818233e-01 | 0.550 |
| R-HSA-3304351 | Signaling by TGF-beta Receptor Complex in Cancer | 2.198132e-01 | 0.658 |
| R-HSA-198753 | ERK/MAPK targets | 1.616149e-01 | 0.792 |
| R-HSA-5689896 | Ovarian tumor domain proteases | 1.231500e-01 | 0.910 |
| R-HSA-193648 | NRAGE signals death through JNK | 2.598044e-01 | 0.585 |
| R-HSA-453279 | Mitotic G1 phase and G1/S transition | 3.003918e-01 | 0.522 |
| R-HSA-1655829 | Regulation of cholesterol biosynthesis by SREBP (SREBF) | 2.206866e-01 | 0.656 |
| R-HSA-156711 | Polo-like kinase mediated events | 1.331874e-01 | 0.876 |
| R-HSA-877300 | Interferon gamma signaling | 2.196505e-01 | 0.658 |
| R-HSA-2173796 | SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription | 1.231500e-01 | 0.910 |
| R-HSA-9662361 | Sensory processing of sound by outer hair cells of the cochlea | 1.027084e-01 | 0.988 |
| R-HSA-9692914 | SARS-CoV-1-host interactions | 2.284906e-01 | 0.641 |
| R-HSA-2262752 | Cellular responses to stress | 2.841986e-01 | 0.546 |
| R-HSA-983712 | Ion channel transport | 2.193417e-01 | 0.659 |
| R-HSA-2029480 | Fcgamma receptor (FCGR) dependent phagocytosis | 2.855392e-01 | 0.544 |
| R-HSA-449836 | Other interleukin signaling | 1.425344e-01 | 0.846 |
| R-HSA-936837 | Ion transport by P-type ATPases | 1.398115e-01 | 0.854 |
| R-HSA-9006936 | Signaling by TGFB family members | 1.227603e-01 | 0.911 |
| R-HSA-2682334 | EPH-Ephrin signaling | 1.536674e-01 | 0.813 |
| R-HSA-9793380 | Formation of paraxial mesoderm | 2.968983e-01 | 0.527 |
| R-HSA-1483255 | PI Metabolism | 2.039931e-01 | 0.690 |
| R-HSA-9825892 | Regulation of MITF-M-dependent genes involved in cell cycle and proliferation | 1.713209e-01 | 0.766 |
| R-HSA-202403 | TCR signaling | 2.486734e-01 | 0.604 |
| R-HSA-9759476 | Regulation of Homotypic Cell-Cell Adhesion | 1.440199e-01 | 0.842 |
| R-HSA-421270 | Cell-cell junction organization | 2.189304e-01 | 0.660 |
| R-HSA-418990 | Adherens junctions interactions | 2.145802e-01 | 0.668 |
| R-HSA-9755088 | Ribavirin ADME | 1.713209e-01 | 0.766 |
| R-HSA-112409 | RAF-independent MAPK1/3 activation | 1.811199e-01 | 0.742 |
| R-HSA-9022699 | MECP2 regulates neuronal receptors and channels | 2.210122e-01 | 0.656 |
| R-HSA-70326 | Glucose metabolism | 1.567510e-01 | 0.805 |
| R-HSA-1538133 | G0 and Early G1 | 2.818233e-01 | 0.550 |
| R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | 1.331346e-01 | 0.876 |
| R-HSA-450282 | MAPK targets/ Nuclear events mediated by MAP kinases | 2.513677e-01 | 0.600 |
| R-HSA-5339562 | Uptake and actions of bacterial toxins | 2.306082e-01 | 0.637 |
| R-HSA-9730414 | MITF-M-regulated melanocyte development | 1.981773e-01 | 0.703 |
| R-HSA-390471 | Association of TriC/CCT with target proteins during biosynthesis | 3.020792e-01 | 0.520 |
| R-HSA-5696394 | DNA Damage Recognition in GG-NER | 3.020792e-01 | 0.520 |
| R-HSA-180534 | Vpu mediated degradation of CD4 | 3.020792e-01 | 0.520 |
| R-HSA-9619665 | EGR2 and SOX10-mediated initiation of Schwann cell myelination | 3.020792e-01 | 0.520 |
| R-HSA-8964539 | Glutamate and glutamine metabolism | 3.020792e-01 | 0.520 |
| R-HSA-6784531 | tRNA processing in the nucleus | 3.043632e-01 | 0.517 |
| R-HSA-597592 | Post-translational protein modification | 3.054422e-01 | 0.515 |
| R-HSA-168255 | Influenza Infection | 3.070630e-01 | 0.513 |
| R-HSA-8848021 | Signaling by PTK6 | 3.118360e-01 | 0.506 |
| R-HSA-9006927 | Signaling by Non-Receptor Tyrosine Kinases | 3.118360e-01 | 0.506 |
| R-HSA-2426168 | Activation of gene expression by SREBF (SREBP) | 3.118360e-01 | 0.506 |
| R-HSA-6814122 | Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding | 3.121722e-01 | 0.506 |
| R-HSA-5205647 | Mitophagy | 3.121722e-01 | 0.506 |
| R-HSA-2142845 | Hyaluronan metabolism | 3.121722e-01 | 0.506 |
| R-HSA-75815 | Ubiquitin-dependent degradation of Cyclin D | 3.121722e-01 | 0.506 |
| R-HSA-349425 | Autodegradation of the E3 ubiquitin ligase COP1 | 3.121722e-01 | 0.506 |
| R-HSA-9768919 | NPAS4 regulates expression of target genes | 3.121722e-01 | 0.506 |
| R-HSA-9614399 | Regulation of localization of FOXO transcription factors | 3.203538e-01 | 0.494 |
| R-HSA-192814 | vRNA Synthesis | 3.203538e-01 | 0.494 |
| R-HSA-192905 | vRNP Assembly | 3.203538e-01 | 0.494 |
| R-HSA-9706019 | RHOBTB3 ATPase cycle | 3.203538e-01 | 0.494 |
| R-HSA-9635465 | Suppression of apoptosis | 3.203538e-01 | 0.494 |
| R-HSA-9662834 | CD163 mediating an anti-inflammatory response | 3.203538e-01 | 0.494 |
| R-HSA-75205 | Dissolution of Fibrin Clot | 3.203538e-01 | 0.494 |
| R-HSA-8854050 | FBXL7 down-regulates AURKA during mitotic entry and in early mitosis | 3.222338e-01 | 0.492 |
| R-HSA-174113 | SCF-beta-TrCP mediated degradation of Emi1 | 3.222338e-01 | 0.492 |
| R-HSA-5693616 | Presynaptic phase of homologous DNA pairing and strand exchange | 3.222338e-01 | 0.492 |
| R-HSA-2559585 | Oncogene Induced Senescence | 3.222338e-01 | 0.492 |
| R-HSA-169911 | Regulation of Apoptosis | 3.222338e-01 | 0.492 |
| R-HSA-917977 | Transferrin endocytosis and recycling | 3.222338e-01 | 0.492 |
| R-HSA-9755511 | KEAP1-NFE2L2 pathway | 3.242611e-01 | 0.489 |
| R-HSA-983169 | Class I MHC mediated antigen processing & presentation | 3.254134e-01 | 0.488 |
| R-HSA-3371511 | HSF1 activation | 3.322581e-01 | 0.479 |
| R-HSA-180585 | Vif-mediated degradation of APOBEC3G | 3.322581e-01 | 0.479 |
| R-HSA-450408 | AUF1 (hnRNP D0) binds and destabilizes mRNA | 3.322581e-01 | 0.479 |
| R-HSA-8941326 | RUNX2 regulates bone development | 3.322581e-01 | 0.479 |
| R-HSA-111461 | Cytochrome c-mediated apoptotic response | 3.388538e-01 | 0.470 |
| R-HSA-113501 | Inhibition of replication initiation of damaged DNA by RB1/E2F1 | 3.388538e-01 | 0.470 |
| R-HSA-9623433 | NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis | 3.388538e-01 | 0.470 |
| R-HSA-6802948 | Signaling by high-kinase activity BRAF mutants | 3.422398e-01 | 0.466 |
| R-HSA-4641258 | Degradation of DVL | 3.422398e-01 | 0.466 |
| R-HSA-4641257 | Degradation of AXIN | 3.422398e-01 | 0.466 |
| R-HSA-9762114 | GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 | 3.422398e-01 | 0.466 |
| R-HSA-168273 | Influenza Viral RNA Transcription and Replication | 3.435430e-01 | 0.464 |
| R-HSA-69206 | G1/S Transition | 3.437432e-01 | 0.464 |
| R-HSA-8868773 | rRNA processing in the nucleus and cytosol | 3.465254e-01 | 0.460 |
| R-HSA-5688426 | Deubiquitination | 3.488812e-01 | 0.457 |
| R-HSA-5213460 | RIPK1-mediated regulated necrosis | 3.521737e-01 | 0.453 |
| R-HSA-8957275 | Post-translational protein phosphorylation | 3.539818e-01 | 0.451 |
| R-HSA-9925563 | Developmental Lineage of Pancreatic Ductal Cells | 3.566768e-01 | 0.448 |
| R-HSA-8941856 | RUNX3 regulates NOTCH signaling | 3.568513e-01 | 0.448 |
| R-HSA-9634285 | Constitutive Signaling by Overexpressed ERBB2 | 3.568513e-01 | 0.448 |
| R-HSA-73943 | Reversal of alkylation damage by DNA dioxygenases | 3.568513e-01 | 0.448 |
| R-HSA-9617629 | Regulation of FOXO transcriptional activity by acetylation | 3.568513e-01 | 0.448 |
| R-HSA-1679131 | Trafficking and processing of endosomal TLR | 3.568513e-01 | 0.448 |
| R-HSA-69091 | Polymerase switching | 3.568513e-01 | 0.448 |
| R-HSA-69109 | Leading Strand Synthesis | 3.568513e-01 | 0.448 |
| R-HSA-446205 | Synthesis of GDP-mannose | 3.568513e-01 | 0.448 |
| R-HSA-877312 | Regulation of IFNG signaling | 3.568513e-01 | 0.448 |
| R-HSA-8983711 | OAS antiviral response | 3.568513e-01 | 0.448 |
| R-HSA-209543 | p75NTR recruits signalling complexes | 3.568513e-01 | 0.448 |
| R-HSA-9824446 | Viral Infection Pathways | 3.580071e-01 | 0.446 |
| R-HSA-983705 | Signaling by the B Cell Receptor (BCR) | 3.580787e-01 | 0.446 |
| R-HSA-193704 | p75 NTR receptor-mediated signalling | 3.601800e-01 | 0.443 |
| R-HSA-1236978 | Cross-presentation of soluble exogenous antigens (endosomes) | 3.620551e-01 | 0.441 |
| R-HSA-9929356 | GSK3B-mediated proteasomal degradation of PD-L1(CD274) | 3.620551e-01 | 0.441 |
| R-HSA-9820965 | Respiratory syncytial virus (RSV) genome replication, transcription and translat... | 3.620551e-01 | 0.441 |
| R-HSA-9764560 | Regulation of CDH1 Gene Transcription | 3.641254e-01 | 0.439 |
| R-HSA-453276 | Regulation of mitotic cell cycle | 3.715599e-01 | 0.430 |
| R-HSA-174143 | APC/C-mediated degradation of cell cycle proteins | 3.715599e-01 | 0.430 |
| R-HSA-5632684 | Hedgehog 'on' state | 3.715599e-01 | 0.430 |
| R-HSA-5696395 | Formation of Incision Complex in GG-NER | 3.718796e-01 | 0.430 |
| R-HSA-3371568 | Attenuation phase | 3.718796e-01 | 0.430 |
| R-HSA-9604323 | Negative regulation of NOTCH4 signaling | 3.718796e-01 | 0.430 |
| R-HSA-8982491 | Glycogen metabolism | 3.718796e-01 | 0.430 |
| R-HSA-9659787 | Aberrant regulation of mitotic G1/S transition in cancer due to RB1 defects | 3.743600e-01 | 0.427 |
| R-HSA-9661069 | Defective binding of RB1 mutants to E2F1,(E2F2, E2F3) | 3.743600e-01 | 0.427 |
| R-HSA-1482883 | Acyl chain remodeling of DAG and TAG | 3.743600e-01 | 0.427 |
| R-HSA-8949664 | Processing of SMDT1 | 3.743600e-01 | 0.427 |
| R-HSA-162658 | Golgi Cisternae Pericentriolar Stack Reorganization | 3.743600e-01 | 0.427 |
| R-HSA-9682706 | Replication of the SARS-CoV-1 genome | 3.743600e-01 | 0.427 |
| R-HSA-1474165 | Reproduction | 3.761829e-01 | 0.425 |
| R-HSA-5578749 | Transcriptional regulation by small RNAs | 3.789781e-01 | 0.421 |
| R-HSA-499943 | Interconversion of nucleotide di- and triphosphates | 3.789781e-01 | 0.421 |
| R-HSA-198725 | Nuclear Events (kinase and transcription factor activation) | 3.789781e-01 | 0.421 |
| R-HSA-5218920 | VEGFR2 mediated vascular permeability | 3.816427e-01 | 0.418 |
| R-HSA-5362768 | Hh mutants are degraded by ERAD | 3.816427e-01 | 0.418 |
| R-HSA-9929491 | SPOP-mediated proteasomal degradation of PD-L1(CD274) | 3.816427e-01 | 0.418 |
| R-HSA-110313 | Translesion synthesis by Y family DNA polymerases bypasses lesions on DNA templa... | 3.816427e-01 | 0.418 |
| R-HSA-159236 | Transport of Mature mRNA derived from an Intron-Containing Transcript | 3.863776e-01 | 0.413 |
| R-HSA-204998 | Cell death signalling via NRAGE, NRIF and NADE | 3.863776e-01 | 0.413 |
| R-HSA-5674135 | MAP2K and MAPK activation | 3.913408e-01 | 0.407 |
| R-HSA-9656223 | Signaling by RAF1 mutants | 3.913408e-01 | 0.407 |
| R-HSA-9932298 | Degradation of CRY and PER proteins | 3.913408e-01 | 0.407 |
| R-HSA-5610780 | Degradation of GLI1 by the proteasome | 3.913408e-01 | 0.407 |
| R-HSA-3000480 | Scavenging by Class A Receptors | 3.913408e-01 | 0.407 |
| R-HSA-5610783 | Degradation of GLI2 by the proteasome | 3.913408e-01 | 0.407 |
| R-HSA-5610785 | GLI3 is processed to GLI3R by the proteasome | 3.913408e-01 | 0.407 |
| R-HSA-69166 | Removal of the Flap Intermediate | 3.913931e-01 | 0.407 |
| R-HSA-1663150 | The activation of arylsulfatases | 3.913931e-01 | 0.407 |
| R-HSA-9933939 | Formation of the polybromo-BAF (pBAF) complex | 3.913931e-01 | 0.407 |
| R-HSA-975163 | IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation | 3.913931e-01 | 0.407 |
| R-HSA-9856872 | Malate-aspartate shuttle | 3.913931e-01 | 0.407 |
| R-HSA-9679514 | SARS-CoV-1 Genome Replication and Transcription | 3.913931e-01 | 0.407 |
| R-HSA-9013694 | Signaling by NOTCH4 | 3.937562e-01 | 0.405 |
| R-HSA-165159 | MTOR signalling | 4.009700e-01 | 0.397 |
| R-HSA-8852135 | Protein ubiquitination | 4.011117e-01 | 0.397 |
| R-HSA-917937 | Iron uptake and transport | 4.011117e-01 | 0.397 |
| R-HSA-937072 | TRAF6-mediated induction of TAK1 complex within TLR4 complex | 4.079634e-01 | 0.389 |
| R-HSA-8964315 | G beta:gamma signalling through BTK | 4.079634e-01 | 0.389 |
| R-HSA-69183 | Processive synthesis on the lagging strand | 4.079634e-01 | 0.389 |
| R-HSA-111447 | Activation of BAD and translocation to mitochondria | 4.079634e-01 | 0.389 |
| R-HSA-73942 | DNA Damage Reversal | 4.079634e-01 | 0.389 |
| R-HSA-9755779 | SARS-CoV-2 targets host intracellular signalling and regulatory pathways | 4.079634e-01 | 0.389 |
| R-HSA-9735871 | SARS-CoV-1 targets host intracellular signalling and regulatory pathways | 4.079634e-01 | 0.389 |
| R-HSA-8875360 | InlB-mediated entry of Listeria monocytogenes into host cell | 4.079634e-01 | 0.389 |
| R-HSA-446353 | Cell-extracellular matrix interactions | 4.079634e-01 | 0.389 |
| R-HSA-193639 | p75NTR signals via NF-kB | 4.079634e-01 | 0.389 |
| R-HSA-5387390 | Hh mutants abrogate ligand secretion | 4.105270e-01 | 0.387 |
| R-HSA-2173789 | TGF-beta receptor signaling activates SMADs | 4.105270e-01 | 0.387 |
| R-HSA-9018519 | Estrogen-dependent gene expression | 4.139880e-01 | 0.383 |
| R-HSA-211000 | Gene Silencing by RNA | 4.157194e-01 | 0.381 |
| R-HSA-9024446 | NR1H2 and NR1H3-mediated signaling | 4.157450e-01 | 0.381 |
| R-HSA-9820952 | Respiratory Syncytial Virus Infection Pathway | 4.193666e-01 | 0.377 |
| R-HSA-69231 | Cyclin D associated events in G1 | 4.200085e-01 | 0.377 |
| R-HSA-69236 | G1 Phase | 4.200085e-01 | 0.377 |
| R-HSA-3928662 | EPHB-mediated forward signaling | 4.200085e-01 | 0.377 |
| R-HSA-187577 | SCF(Skp2)-mediated degradation of p27/p21 | 4.200085e-01 | 0.377 |
| R-HSA-6791226 | Major pathway of rRNA processing in the nucleolus and cytosol | 4.212612e-01 | 0.375 |
| R-HSA-76002 | Platelet activation, signaling and aggregation | 4.224228e-01 | 0.374 |
| R-HSA-73864 | RNA Polymerase I Transcription | 4.230189e-01 | 0.374 |
| R-HSA-4086400 | PCP/CE pathway | 4.230189e-01 | 0.374 |
| R-HSA-354194 | GRB2:SOS provides linkage to MAPK signaling for Integrins | 4.240836e-01 | 0.373 |
| R-HSA-9687136 | Aberrant regulation of mitotic exit in cancer due to RB1 defects | 4.240836e-01 | 0.373 |
| R-HSA-210744 | Regulation of gene expression in late stage (branching morphogenesis) pancreatic... | 4.240836e-01 | 0.373 |
| R-HSA-388844 | Receptor-type tyrosine-protein phosphatases | 4.240836e-01 | 0.373 |
| R-HSA-140534 | Caspase activation via Death Receptors in the presence of ligand | 4.240836e-01 | 0.373 |
| R-HSA-5635838 | Activation of SMO | 4.240836e-01 | 0.373 |
| R-HSA-76009 | Platelet Aggregation (Plug Formation) | 4.294116e-01 | 0.367 |
| R-HSA-5678895 | Defective CFTR causes cystic fibrosis | 4.294116e-01 | 0.367 |
| R-HSA-9824272 | Somitogenesis | 4.294116e-01 | 0.367 |
| R-HSA-9664407 | Parasite infection | 4.354487e-01 | 0.361 |
| R-HSA-9664422 | FCGR3A-mediated phagocytosis | 4.354487e-01 | 0.361 |
| R-HSA-9664417 | Leishmania phagocytosis | 4.354487e-01 | 0.361 |
| R-HSA-5689880 | Ub-specific processing proteases | 4.357745e-01 | 0.361 |
| R-HSA-6806834 | Signaling by MET | 4.374718e-01 | 0.359 |
| R-HSA-6802946 | Signaling by moderate kinase activity BRAF mutants | 4.387335e-01 | 0.358 |
| R-HSA-6802955 | Paradoxical activation of RAF signaling by kinase inactive BRAF | 4.387335e-01 | 0.358 |
| R-HSA-9649948 | Signaling downstream of RAS mutants | 4.387335e-01 | 0.358 |
| R-HSA-174084 | Autodegradation of Cdh1 by Cdh1:APC/C | 4.387335e-01 | 0.358 |
| R-HSA-6802949 | Signaling by RAS mutants | 4.387335e-01 | 0.358 |
| R-HSA-9664424 | Cell recruitment (pro-inflammatory response) | 4.387335e-01 | 0.358 |
| R-HSA-9660826 | Purinergic signaling in leishmaniasis infection | 4.387335e-01 | 0.358 |
| R-HSA-8964616 | G beta:gamma signalling through CDC42 | 4.397658e-01 | 0.357 |
| R-HSA-1566977 | Fibronectin matrix formation | 4.397658e-01 | 0.357 |
| R-HSA-3134975 | Regulation of innate immune responses to cytosolic DNA | 4.397658e-01 | 0.357 |
| R-HSA-70370 | Galactose catabolism | 4.397658e-01 | 0.357 |
| R-HSA-5693607 | Processing of DNA double-strand break ends | 4.446472e-01 | 0.352 |
| R-HSA-9678108 | SARS-CoV-1 Infection | 4.454153e-01 | 0.351 |
| R-HSA-1483249 | Inositol phosphate metabolism | 4.461427e-01 | 0.351 |
| R-HSA-174154 | APC/C:Cdc20 mediated degradation of Securin | 4.479717e-01 | 0.349 |
| R-HSA-162599 | Late Phase of HIV Life Cycle | 4.514323e-01 | 0.345 |
| R-HSA-72202 | Transport of Mature Transcript to Cytoplasm | 4.517864e-01 | 0.345 |
| R-HSA-983168 | Antigen processing: Ubiquitination & Proteasome degradation | 4.534107e-01 | 0.344 |
| R-HSA-5637812 | Signaling by EGFRvIII in Cancer | 4.550220e-01 | 0.342 |
| R-HSA-5637810 | Constitutive Signaling by EGFRvIII | 4.550220e-01 | 0.342 |
| R-HSA-174437 | Removal of the Flap Intermediate from the C-strand | 4.550220e-01 | 0.342 |
| R-HSA-372708 | p130Cas linkage to MAPK signaling for integrins | 4.550220e-01 | 0.342 |
| R-HSA-139853 | Elevation of cytosolic Ca2+ levels | 4.550220e-01 | 0.342 |
| R-HSA-164938 | Nef-mediates down modulation of cell surface receptors by recruiting them to cla... | 4.550220e-01 | 0.342 |
| R-HSA-1660517 | Synthesis of PIPs at the late endosome membrane | 4.550220e-01 | 0.342 |
| R-HSA-5358565 | Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) | 4.550220e-01 | 0.342 |
| R-HSA-9694686 | Replication of the SARS-CoV-2 genome | 4.550220e-01 | 0.342 |
| R-HSA-5620924 | Intraflagellar transport | 4.571239e-01 | 0.340 |
| R-HSA-389356 | Co-stimulation by CD28 | 4.571239e-01 | 0.340 |
| R-HSA-112314 | Neurotransmitter receptors and postsynaptic signal transmission | 4.576225e-01 | 0.339 |
| R-HSA-109582 | Hemostasis | 4.606285e-01 | 0.337 |
| R-HSA-381426 | Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-l... | 4.641641e-01 | 0.333 |
| R-HSA-5696399 | Global Genome Nucleotide Excision Repair (GG-NER) | 4.659496e-01 | 0.332 |
| R-HSA-8939236 | RUNX1 regulates transcription of genes involved in differentiation of HSCs | 4.659496e-01 | 0.332 |
| R-HSA-73893 | DNA Damage Bypass | 4.661878e-01 | 0.331 |
| R-HSA-5651801 | PCNA-Dependent Long Patch Base Excision Repair | 4.698636e-01 | 0.328 |
| R-HSA-416993 | Trafficking of GluR2-containing AMPA receptors | 4.698636e-01 | 0.328 |
| R-HSA-418217 | G beta:gamma signalling through PLC beta | 4.698636e-01 | 0.328 |
| R-HSA-9614657 | FOXO-mediated transcription of cell death genes | 4.698636e-01 | 0.328 |
| R-HSA-500657 | Presynaptic function of Kainate receptors | 4.698636e-01 | 0.328 |
| R-HSA-111471 | Apoptotic factor-mediated response | 4.698636e-01 | 0.328 |
| R-HSA-1839117 | Signaling by cytosolic FGFR1 fusion mutants | 4.698636e-01 | 0.328 |
| R-HSA-2564830 | Cytosolic iron-sulfur cluster assembly | 4.698636e-01 | 0.328 |
| R-HSA-9665348 | Signaling by ERBB2 ECD mutants | 4.698636e-01 | 0.328 |
| R-HSA-8849932 | Synaptic adhesion-like molecules | 4.698636e-01 | 0.328 |
| R-HSA-9748787 | Azathioprine ADME | 4.751616e-01 | 0.323 |
| R-HSA-4420097 | VEGFA-VEGFR2 Pathway | 4.760631e-01 | 0.322 |
| R-HSA-9909615 | Regulation of PD-L1(CD274) Post-translational modification | 4.799494e-01 | 0.319 |
| R-HSA-912446 | Meiotic recombination | 4.840433e-01 | 0.315 |
| R-HSA-1234176 | Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha | 4.840433e-01 | 0.315 |
| R-HSA-5358346 | Hedgehog ligand biogenesis | 4.840433e-01 | 0.315 |
| R-HSA-392851 | Prostacyclin signalling through prostacyclin receptor | 4.843019e-01 | 0.315 |
| R-HSA-113510 | E2F mediated regulation of DNA replication | 4.843019e-01 | 0.315 |
| R-HSA-912631 | Regulation of signaling by CBL | 4.843019e-01 | 0.315 |
| R-HSA-1237112 | Methionine salvage pathway | 4.843019e-01 | 0.315 |
| R-HSA-9694682 | SARS-CoV-2 Genome Replication and Transcription | 4.843019e-01 | 0.315 |
| R-HSA-163841 | Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation | 4.868846e-01 | 0.313 |
| R-HSA-9007101 | Rab regulation of trafficking | 4.878604e-01 | 0.312 |
| R-HSA-73772 | RNA Polymerase I Promoter Escape | 4.928314e-01 | 0.307 |
| R-HSA-174184 | Cdc20:Phospho-APC/C mediated degradation of Cyclin A | 4.928314e-01 | 0.307 |
| R-HSA-8866654 | E3 ubiquitin ligases ubiquitinate target proteins | 4.928314e-01 | 0.307 |
| R-HSA-68949 | Orc1 removal from chromatin | 4.928314e-01 | 0.307 |
| R-HSA-9931269 | AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) | 4.928314e-01 | 0.307 |
| R-HSA-9634815 | Transcriptional Regulation by NPAS4 | 4.928314e-01 | 0.307 |
| R-HSA-390466 | Chaperonin-mediated protein folding | 4.937748e-01 | 0.306 |
| R-HSA-438064 | Post NMDA receptor activation events | 4.937748e-01 | 0.306 |
| R-HSA-163210 | Formation of ATP by chemiosmotic coupling | 4.983478e-01 | 0.302 |
| R-HSA-2022857 | Keratan sulfate degradation | 4.983478e-01 | 0.302 |
| R-HSA-5620922 | BBSome-mediated cargo-targeting to cilium | 4.983478e-01 | 0.302 |
| R-HSA-3322077 | Glycogen synthesis | 4.983478e-01 | 0.302 |
| R-HSA-8878166 | Transcriptional regulation by RUNX2 | 4.995487e-01 | 0.301 |
| R-HSA-179419 | APC:Cdc20 mediated degradation of cell cycle proteins prior to satisfation of th... | 5.015244e-01 | 0.300 |
| R-HSA-8948751 | Regulation of PTEN stability and activity | 5.015244e-01 | 0.300 |
| R-HSA-1483257 | Phospholipid metabolism | 5.031453e-01 | 0.298 |
| R-HSA-69017 | CDK-mediated phosphorylation and removal of Cdc6 | 5.101209e-01 | 0.292 |
| R-HSA-73886 | Chromosome Maintenance | 5.111207e-01 | 0.291 |
| R-HSA-9759194 | Nuclear events mediated by NFE2L2 | 5.111207e-01 | 0.291 |
| R-HSA-1236382 | Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants | 5.120120e-01 | 0.291 |
| R-HSA-5637815 | Signaling by Ligand-Responsive EGFR Variants in Cancer | 5.120120e-01 | 0.291 |
| R-HSA-202040 | G-protein activation | 5.120120e-01 | 0.291 |
| R-HSA-392170 | ADP signalling through P2Y purinoceptor 12 | 5.120120e-01 | 0.291 |
| R-HSA-69186 | Lagging Strand Synthesis | 5.120120e-01 | 0.291 |
| R-HSA-9931295 | PD-L1(CD274) glycosylation and translocation to plasma membrane | 5.120120e-01 | 0.291 |
| R-HSA-9013695 | NOTCH4 Intracellular Domain Regulates Transcription | 5.120120e-01 | 0.291 |
| R-HSA-8878171 | Transcriptional regulation by RUNX1 | 5.183799e-01 | 0.285 |
| R-HSA-176409 | APC/C:Cdc20 mediated degradation of mitotic proteins | 5.186197e-01 | 0.285 |
| R-HSA-442982 | Ras activation upon Ca2+ influx through NMDA receptor | 5.253048e-01 | 0.280 |
| R-HSA-5696397 | Gap-filling DNA repair synthesis and ligation in GG-NER | 5.253048e-01 | 0.280 |
| R-HSA-9617828 | FOXO-mediated transcription of cell cycle genes | 5.253048e-01 | 0.280 |
| R-HSA-76066 | RNA Polymerase III Transcription Initiation From Type 2 Promoter | 5.253048e-01 | 0.280 |
| R-HSA-9705462 | Inactivation of CSF3 (G-CSF) signaling | 5.253048e-01 | 0.280 |
| R-HSA-9617324 | Negative regulation of NMDA receptor-mediated neuronal transmission | 5.253048e-01 | 0.280 |
| R-HSA-8949215 | Mitochondrial calcium ion transport | 5.253048e-01 | 0.280 |
| R-HSA-8876384 | Listeria monocytogenes entry into host cells | 5.253048e-01 | 0.280 |
| R-HSA-109606 | Intrinsic Pathway for Apoptosis | 5.270199e-01 | 0.278 |
| R-HSA-176814 | Activation of APC/C and APC/C:Cdc20 mediated degradation of mitotic proteins | 5.270199e-01 | 0.278 |
| R-HSA-177929 | Signaling by EGFR | 5.270199e-01 | 0.278 |
| R-HSA-162587 | HIV Life Cycle | 5.291339e-01 | 0.276 |
| R-HSA-391251 | Protein folding | 5.341090e-01 | 0.272 |
| R-HSA-74752 | Signaling by Insulin receptor | 5.341090e-01 | 0.272 |
| R-HSA-6791312 | TP53 Regulates Transcription of Cell Cycle Genes | 5.353204e-01 | 0.271 |
| R-HSA-350054 | Notch-HLH transcription pathway | 5.382363e-01 | 0.269 |
| R-HSA-76071 | RNA Polymerase III Transcription Initiation From Type 3 Promoter | 5.382363e-01 | 0.269 |
| R-HSA-76061 | RNA Polymerase III Transcription Initiation From Type 1 Promoter | 5.382363e-01 | 0.269 |
| R-HSA-912694 | Regulation of IFNA/IFNB signaling | 5.382363e-01 | 0.269 |
| R-HSA-168799 | Neurotoxicity of clostridium toxins | 5.382363e-01 | 0.269 |
| R-HSA-2173788 | Downregulation of TGF-beta receptor signaling | 5.382363e-01 | 0.269 |
| R-HSA-194138 | Signaling by VEGF | 5.395007e-01 | 0.268 |
| R-HSA-73857 | RNA Polymerase II Transcription | 5.402410e-01 | 0.267 |
| R-HSA-72312 | rRNA processing | 5.436764e-01 | 0.265 |
| R-HSA-212436 | Generic Transcription Pathway | 5.470236e-01 | 0.262 |
| R-HSA-1474290 | Collagen formation | 5.471458e-01 | 0.262 |
| R-HSA-392451 | G beta:gamma signalling through PI3Kgamma | 5.508163e-01 | 0.259 |
| R-HSA-389957 | Prefoldin mediated transfer of substrate to CCT/TriC | 5.508163e-01 | 0.259 |
| R-HSA-9648895 | Response of EIF2AK1 (HRI) to heme deficiency | 5.508163e-01 | 0.259 |
| R-HSA-982772 | Growth hormone receptor signaling | 5.508163e-01 | 0.259 |
| R-HSA-3000170 | Syndecan interactions | 5.508163e-01 | 0.259 |
| R-HSA-180786 | Extension of Telomeres | 5.516195e-01 | 0.258 |
| R-HSA-186712 | Regulation of beta-cell development | 5.516195e-01 | 0.258 |
| R-HSA-2022090 | Assembly of collagen fibrils and other multimeric structures | 5.516195e-01 | 0.258 |
| R-HSA-1280218 | Adaptive Immune System | 5.590220e-01 | 0.253 |
| R-HSA-1227986 | Signaling by ERBB2 | 5.596167e-01 | 0.252 |
| R-HSA-351202 | Metabolism of polyamines | 5.596167e-01 | 0.252 |
| R-HSA-9954709 | Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide | 5.599671e-01 | 0.252 |
| R-HSA-389960 | Formation of tubulin folding intermediates by CCT/TriC | 5.630544e-01 | 0.249 |
| R-HSA-428930 | Thromboxane signalling through TP receptor | 5.630544e-01 | 0.249 |
| R-HSA-110314 | Recognition of DNA damage by PCNA-containing replication complex | 5.630544e-01 | 0.249 |
| R-HSA-418592 | ADP signalling through P2Y purinoceptor 1 | 5.630544e-01 | 0.249 |
| R-HSA-9665686 | Signaling by ERBB2 TMD/JMD mutants | 5.630544e-01 | 0.249 |
| R-HSA-1296071 | Potassium Channels | 5.662952e-01 | 0.247 |
| R-HSA-8939902 | Regulation of RUNX2 expression and activity | 5.675118e-01 | 0.246 |
| R-HSA-157579 | Telomere Maintenance | 5.725673e-01 | 0.242 |
| R-HSA-376176 | Signaling by ROBO receptors | 5.747944e-01 | 0.240 |
| R-HSA-3000157 | Laminin interactions | 5.749597e-01 | 0.240 |
| R-HSA-420029 | Tight junction interactions | 5.749597e-01 | 0.240 |
| R-HSA-174411 | Polymerase switching on the C-strand of the telomere | 5.749597e-01 | 0.240 |
| R-HSA-9932451 | SWI/SNF chromatin remodelers | 5.749597e-01 | 0.240 |
| R-HSA-9932444 | ATP-dependent chromatin remodelers | 5.749597e-01 | 0.240 |
| R-HSA-5218921 | VEGFR2 mediated cell proliferation | 5.749597e-01 | 0.240 |
| R-HSA-1660516 | Synthesis of PIPs at the early endosome membrane | 5.749597e-01 | 0.240 |
| R-HSA-5601884 | PIWI-interacting RNA (piRNA) biogenesis | 5.749597e-01 | 0.240 |
| R-HSA-375165 | NCAM signaling for neurite out-growth | 5.753044e-01 | 0.240 |
| R-HSA-1268020 | Mitochondrial protein import | 5.753044e-01 | 0.240 |
| R-HSA-176408 | Regulation of APC/C activators between G1/S and early anaphase | 5.753044e-01 | 0.240 |
| R-HSA-2559586 | DNA Damage/Telomere Stress Induced Senescence | 5.753044e-01 | 0.240 |
| R-HSA-72203 | Processing of Capped Intron-Containing Pre-mRNA | 5.821485e-01 | 0.235 |
| R-HSA-1643713 | Signaling by EGFR in Cancer | 5.865414e-01 | 0.232 |
| R-HSA-400042 | Adrenaline,noradrenaline inhibits insulin secretion | 5.865414e-01 | 0.232 |
| R-HSA-8874081 | MET activates PTK2 signaling | 5.865414e-01 | 0.232 |
| R-HSA-5689901 | Metalloprotease DUBs | 5.865414e-01 | 0.232 |
| R-HSA-1855183 | Synthesis of IP2, IP, and Ins in the cytosol | 5.865414e-01 | 0.232 |
| R-HSA-9638630 | Attachment of bacteria to epithelial cells | 5.865414e-01 | 0.232 |
| R-HSA-9658195 | Leishmania infection | 5.896265e-01 | 0.229 |
| R-HSA-9824443 | Parasitic Infection Pathways | 5.896265e-01 | 0.229 |
| R-HSA-5610787 | Hedgehog 'off' state | 5.910425e-01 | 0.228 |
| R-HSA-174414 | Processive synthesis on the C-strand of the telomere | 5.978082e-01 | 0.223 |
| R-HSA-167243 | Tat-mediated HIV elongation arrest and recovery | 5.978082e-01 | 0.223 |
| R-HSA-167238 | Pausing and recovery of Tat-mediated HIV elongation | 5.978082e-01 | 0.223 |
| R-HSA-73863 | RNA Polymerase I Transcription Termination | 5.978082e-01 | 0.223 |
| R-HSA-8949613 | Cristae formation | 5.978082e-01 | 0.223 |
| R-HSA-8866652 | Synthesis of active ubiquitin: roles of E1 and E2 enzymes | 5.978082e-01 | 0.223 |
| R-HSA-193807 | Synthesis of bile acids and bile salts via 27-hydroxycholesterol | 5.978082e-01 | 0.223 |
| R-HSA-264876 | Insulin processing | 5.978082e-01 | 0.223 |
| R-HSA-1234174 | Cellular response to hypoxia | 5.980645e-01 | 0.223 |
| R-HSA-5621481 | C-type lectin receptors (CLRs) | 6.015846e-01 | 0.221 |
| R-HSA-442755 | Activation of NMDA receptors and postsynaptic events | 6.030700e-01 | 0.220 |
| R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | 6.030700e-01 | 0.220 |
| R-HSA-112315 | Transmission across Chemical Synapses | 6.048571e-01 | 0.218 |
| R-HSA-167287 | HIV elongation arrest and recovery | 6.087686e-01 | 0.216 |
| R-HSA-167290 | Pausing and recovery of HIV elongation | 6.087686e-01 | 0.216 |
| R-HSA-171319 | Telomere Extension By Telomerase | 6.087686e-01 | 0.216 |
| R-HSA-5205685 | PINK1-PRKN Mediated Mitophagy | 6.087686e-01 | 0.216 |
| R-HSA-451326 | Activation of kainate receptors upon glutamate binding | 6.087686e-01 | 0.216 |
| R-HSA-163685 | Integration of energy metabolism | 6.091020e-01 | 0.215 |
| R-HSA-3858494 | Beta-catenin independent WNT signaling | 6.091020e-01 | 0.215 |
| R-HSA-9948299 | Ribosome-associated quality control | 6.192222e-01 | 0.208 |
| R-HSA-5358351 | Signaling by Hedgehog | 6.192222e-01 | 0.208 |
| R-HSA-9674555 | Signaling by CSF3 (G-CSF) | 6.194310e-01 | 0.208 |
| R-HSA-210745 | Regulation of gene expression in beta cells | 6.194310e-01 | 0.208 |
| R-HSA-418360 | Platelet calcium homeostasis | 6.194310e-01 | 0.208 |
| R-HSA-9664565 | Signaling by ERBB2 KD Mutants | 6.194310e-01 | 0.208 |
| R-HSA-420092 | Glucagon-type ligand receptors | 6.194310e-01 | 0.208 |
| R-HSA-5218859 | Regulated Necrosis | 6.198970e-01 | 0.208 |
| R-HSA-9833110 | RSV-host interactions | 6.206692e-01 | 0.207 |
| R-HSA-5696398 | Nucleotide Excision Repair | 6.264164e-01 | 0.203 |
| R-HSA-9687139 | Aberrant regulation of mitotic cell cycle due to RB1 defects | 6.298035e-01 | 0.201 |
| R-HSA-76046 | RNA Polymerase III Transcription Initiation | 6.298035e-01 | 0.201 |
| R-HSA-1227990 | Signaling by ERBB2 in Cancer | 6.298035e-01 | 0.201 |
| R-HSA-456926 | Thrombin signalling through proteinase activated receptors (PARs) | 6.298035e-01 | 0.201 |
| R-HSA-380972 | Energy dependent regulation of mTOR by LKB1-AMPK | 6.298035e-01 | 0.201 |
| R-HSA-888590 | GABA synthesis, release, reuptake and degradation | 6.298035e-01 | 0.201 |
| R-HSA-9013508 | NOTCH3 Intracellular Domain Regulates Transcription | 6.298035e-01 | 0.201 |
| R-HSA-1474151 | Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation | 6.298035e-01 | 0.201 |
| R-HSA-9933387 | RORA,B,C and NR1D1 (REV-ERBA) regulate gene expression | 6.298035e-01 | 0.201 |
| R-HSA-114452 | Activation of BH3-only proteins | 6.298035e-01 | 0.201 |
| R-HSA-195253 | Degradation of beta-catenin by the destruction complex | 6.339383e-01 | 0.198 |
| R-HSA-69239 | Synthesis of DNA | 6.377307e-01 | 0.195 |
| R-HSA-389958 | Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding | 6.398938e-01 | 0.194 |
| R-HSA-8963693 | Aspartate and asparagine metabolism | 6.398938e-01 | 0.194 |
| R-HSA-186763 | Downstream signal transduction | 6.398938e-01 | 0.194 |
| R-HSA-1257604 | PIP3 activates AKT signaling | 6.400731e-01 | 0.194 |
| R-HSA-450531 | Regulation of mRNA stability by proteins that bind AU-rich elements | 6.475711e-01 | 0.189 |
| R-HSA-69190 | DNA strand elongation | 6.497098e-01 | 0.187 |
| R-HSA-2871837 | FCERI mediated NF-kB activation | 6.533276e-01 | 0.185 |
| R-HSA-8951664 | Neddylation | 6.534197e-01 | 0.185 |
| R-HSA-69052 | Switching of origins to a post-replicative state | 6.542354e-01 | 0.184 |
| R-HSA-2022854 | Keratan sulfate biosynthesis | 6.592587e-01 | 0.181 |
| R-HSA-397795 | G-protein beta:gamma signalling | 6.592587e-01 | 0.181 |
| R-HSA-1839124 | FGFR1 mutant receptor activation | 6.592587e-01 | 0.181 |
| R-HSA-6804758 | Regulation of TP53 Activity through Acetylation | 6.592587e-01 | 0.181 |
| R-HSA-9930044 | Nuclear RNA decay | 6.592587e-01 | 0.181 |
| R-HSA-159418 | Recycling of bile acids and salts | 6.592587e-01 | 0.181 |
| R-HSA-5609975 | Diseases associated with glycosylation precursor biosynthesis | 6.592587e-01 | 0.181 |
| R-HSA-1222556 | ROS and RNS production in phagocytes | 6.607988e-01 | 0.180 |
| R-HSA-71387 | Metabolism of carbohydrates and carbohydrate derivatives | 6.625282e-01 | 0.179 |
| R-HSA-1482788 | Acyl chain remodelling of PC | 6.685480e-01 | 0.175 |
| R-HSA-9768727 | Regulation of CDH1 posttranslational processing and trafficking to plasma membra... | 6.685480e-01 | 0.175 |
| R-HSA-199220 | Vitamin B5 (pantothenate) metabolism | 6.685480e-01 | 0.175 |
| R-HSA-73854 | RNA Polymerase I Promoter Clearance | 6.736255e-01 | 0.172 |
| R-HSA-5689603 | UCH proteinases | 6.736255e-01 | 0.172 |
| R-HSA-9758941 | Gastrulation | 6.764064e-01 | 0.170 |
| R-HSA-9680350 | Signaling by CSF1 (M-CSF) in myeloid cells | 6.775845e-01 | 0.169 |
| R-HSA-392518 | Signal amplification | 6.775845e-01 | 0.169 |
| R-HSA-203615 | eNOS activation | 6.775845e-01 | 0.169 |
| R-HSA-110328 | Recognition and association of DNA glycosylase with site containing an affected ... | 6.775845e-01 | 0.169 |
| R-HSA-1368108 | BMAL1:CLOCK,NPAS2 activates circadian expression | 6.775845e-01 | 0.169 |
| R-HSA-446203 | Asparagine N-linked glycosylation | 6.779873e-01 | 0.169 |
| R-HSA-2173782 | Binding and Uptake of Ligands by Scavenger Receptors | 6.808921e-01 | 0.167 |
| R-HSA-9711123 | Cellular response to chemical stress | 6.815241e-01 | 0.167 |
| R-HSA-5628897 | TP53 Regulates Metabolic Genes | 6.856489e-01 | 0.164 |
| R-HSA-6783783 | Interleukin-10 signaling | 6.860561e-01 | 0.164 |
| R-HSA-5619084 | ABC transporter disorders | 6.860561e-01 | 0.164 |
| R-HSA-1482839 | Acyl chain remodelling of PE | 6.863752e-01 | 0.163 |
| R-HSA-9772755 | Formation of WDR5-containing histone-modifying complexes | 6.863752e-01 | 0.163 |
| R-HSA-749476 | RNA Polymerase III Abortive And Retractive Initiation | 6.949268e-01 | 0.158 |
| R-HSA-432720 | Lysosome Vesicle Biogenesis | 6.949268e-01 | 0.158 |
| R-HSA-74158 | RNA Polymerase III Transcription | 6.949268e-01 | 0.158 |
| R-HSA-163560 | Triglyceride catabolism | 6.949268e-01 | 0.158 |
| R-HSA-69205 | G1/S-Specific Transcription | 6.949268e-01 | 0.158 |
| R-HSA-72163 | mRNA Splicing - Major Pathway | 6.993166e-01 | 0.155 |
| R-HSA-549127 | SLC-mediated transport of organic cations | 7.032456e-01 | 0.153 |
| R-HSA-5663205 | Infectious disease | 7.110614e-01 | 0.148 |
| R-HSA-9610379 | HCMV Late Events | 7.110710e-01 | 0.148 |
| R-HSA-202131 | Metabolism of nitric oxide: NOS3 activation and regulation | 7.113382e-01 | 0.148 |
| R-HSA-9931953 | Biofilm formation | 7.113382e-01 | 0.148 |
| R-HSA-8875878 | MET promotes cell motility | 7.113382e-01 | 0.148 |
| R-HSA-8939211 | ESR-mediated signaling | 7.122476e-01 | 0.147 |
| R-HSA-9711097 | Cellular response to starvation | 7.152078e-01 | 0.146 |
| R-HSA-167200 | Formation of HIV-1 elongation complex containing HIV-1 Tat | 7.192105e-01 | 0.143 |
| R-HSA-9931509 | Expression of BMAL (ARNTL), CLOCK, and NPAS2 | 7.192105e-01 | 0.143 |
| R-HSA-71336 | Pentose phosphate pathway | 7.192105e-01 | 0.143 |
| R-HSA-6794362 | Protein-protein interactions at synapses | 7.265274e-01 | 0.139 |
| R-HSA-167246 | Tat-mediated elongation of the HIV-1 transcript | 7.268687e-01 | 0.139 |
| R-HSA-9670095 | Inhibition of DNA recombination at telomere | 7.268687e-01 | 0.139 |
| R-HSA-167152 | Formation of HIV elongation complex in the absence of HIV Tat | 7.268687e-01 | 0.139 |
| R-HSA-167169 | HIV Transcription Elongation | 7.268687e-01 | 0.139 |
| R-HSA-9844594 | Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 | 7.268687e-01 | 0.139 |
| R-HSA-9843743 | Transcriptional regulation of brown and beige adipocyte differentiation | 7.268687e-01 | 0.139 |
| R-HSA-9854311 | Maturation of TCA enzymes and regulation of TCA cycle | 7.268687e-01 | 0.139 |
| R-HSA-427389 | ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression | 7.268687e-01 | 0.139 |
| R-HSA-379726 | Mitochondrial tRNA aminoacylation | 7.268687e-01 | 0.139 |
| R-HSA-212165 | Epigenetic regulation of gene expression | 7.296660e-01 | 0.137 |
| R-HSA-8876198 | RAB GEFs exchange GTP for GDP on RABs | 7.319345e-01 | 0.136 |
| R-HSA-6809371 | Formation of the cornified envelope | 7.331619e-01 | 0.135 |
| R-HSA-9694548 | Maturation of spike protein | 7.343184e-01 | 0.134 |
| R-HSA-9607240 | FLT3 Signaling | 7.343184e-01 | 0.134 |
| R-HSA-72172 | mRNA Splicing | 7.397614e-01 | 0.131 |
| R-HSA-9615017 | FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes | 7.415653e-01 | 0.130 |
| R-HSA-174417 | Telomere C-strand (Lagging Strand) Synthesis | 7.415653e-01 | 0.130 |
| R-HSA-5655302 | Signaling by FGFR1 in disease | 7.415653e-01 | 0.130 |
| R-HSA-9609736 | Assembly and cell surface presentation of NMDA receptors | 7.415653e-01 | 0.130 |
| R-HSA-5619115 | Disorders of transmembrane transporters | 7.453644e-01 | 0.128 |
| R-HSA-420499 | Class C/3 (Metabotropic glutamate/pheromone receptors) | 7.476134e-01 | 0.126 |
| R-HSA-381676 | Glucagon-like Peptide-1 (GLP1) regulates insulin secretion | 7.486151e-01 | 0.126 |
| R-HSA-73762 | RNA Polymerase I Transcription Initiation | 7.486151e-01 | 0.126 |
| R-HSA-73928 | Depyrimidination | 7.486151e-01 | 0.126 |
| R-HSA-110329 | Cleavage of the damaged pyrimidine | 7.486151e-01 | 0.126 |
| R-HSA-512988 | Interleukin-3, Interleukin-5 and GM-CSF signaling | 7.486151e-01 | 0.126 |
| R-HSA-5619102 | SLC transporter disorders | 7.504893e-01 | 0.125 |
| R-HSA-1474244 | Extracellular matrix organization | 7.522765e-01 | 0.124 |
| R-HSA-187037 | Signaling by NTRK1 (TRKA) | 7.547106e-01 | 0.122 |
| R-HSA-9637690 | Response of Mtb to phagocytosis | 7.554729e-01 | 0.122 |
| R-HSA-112310 | Neurotransmitter release cycle | 7.576238e-01 | 0.121 |
| R-HSA-8986944 | Transcriptional Regulation by MECP2 | 7.624993e-01 | 0.118 |
| R-HSA-606279 | Deposition of new CENPA-containing nucleosomes at the centromere | 7.686336e-01 | 0.114 |
| R-HSA-774815 | Nucleosome assembly | 7.686336e-01 | 0.114 |
| R-HSA-9660821 | ADORA2B mediated anti-inflammatory cytokines production | 7.686336e-01 | 0.114 |
| R-HSA-3560782 | Diseases associated with glycosaminoglycan metabolism | 7.686336e-01 | 0.114 |
| R-HSA-432040 | Vasopressin regulates renal water homeostasis via Aquaporins | 7.686336e-01 | 0.114 |
| R-HSA-9909396 | Circadian clock | 7.748387e-01 | 0.111 |
| R-HSA-72165 | mRNA Splicing - Minor Pathway | 7.749465e-01 | 0.111 |
| R-HSA-2299718 | Condensation of Prophase Chromosomes | 7.749465e-01 | 0.111 |
| R-HSA-2514859 | Inactivation, recovery and regulation of the phototransduction cascade | 7.749465e-01 | 0.111 |
| R-HSA-68867 | Assembly of the pre-replicative complex | 7.766188e-01 | 0.110 |
| R-HSA-9006925 | Intracellular signaling by second messengers | 7.811527e-01 | 0.107 |
| R-HSA-9837999 | Mitochondrial protein degradation | 7.811598e-01 | 0.107 |
| R-HSA-9954716 | ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri... | 7.856197e-01 | 0.105 |
| R-HSA-9634597 | GPER1 signaling | 7.870613e-01 | 0.104 |
| R-HSA-9031628 | NGF-stimulated transcription | 7.870613e-01 | 0.104 |
| R-HSA-425410 | Metal ion SLC transporters | 7.870613e-01 | 0.104 |
| R-HSA-2122947 | NOTCH1 Intracellular Domain Regulates Transcription | 7.928725e-01 | 0.101 |
| R-HSA-1638074 | Keratan sulfate/keratin metabolism | 7.928725e-01 | 0.101 |
| R-HSA-157858 | Gap junction trafficking and regulation | 7.928725e-01 | 0.101 |
| R-HSA-381340 | Transcriptional regulation of white adipocyte differentiation | 7.943005e-01 | 0.100 |
| R-HSA-2559583 | Cellular Senescence | 7.985754e-01 | 0.098 |
| R-HSA-422356 | Regulation of insulin secretion | 8.026696e-01 | 0.095 |
| R-HSA-2514856 | The phototransduction cascade | 8.040244e-01 | 0.095 |
| R-HSA-6807070 | PTEN Regulation | 8.042119e-01 | 0.095 |
| R-HSA-3214847 | HATs acetylate histones | 8.067399e-01 | 0.093 |
| R-HSA-112382 | Formation of RNA Pol II elongation complex | 8.093736e-01 | 0.092 |
| R-HSA-382556 | ABC-family proteins mediated transport | 8.107354e-01 | 0.091 |
| R-HSA-75955 | RNA Polymerase II Transcription Elongation | 8.145771e-01 | 0.089 |
| R-HSA-9009391 | Extra-nuclear estrogen signaling | 8.146571e-01 | 0.089 |
| R-HSA-2559580 | Oxidative Stress Induced Senescence | 8.185061e-01 | 0.087 |
| R-HSA-73929 | Base-Excision Repair, AP Site Formation | 8.196389e-01 | 0.086 |
| R-HSA-418597 | G alpha (z) signalling events | 8.245629e-01 | 0.084 |
| R-HSA-6811436 | COPI-independent Golgi-to-ER retrograde traffic | 8.245629e-01 | 0.084 |
| R-HSA-9012852 | Signaling by NOTCH3 | 8.245629e-01 | 0.084 |
| R-HSA-8856825 | Cargo recognition for clathrin-mediated endocytosis | 8.259902e-01 | 0.083 |
| R-HSA-9006931 | Signaling by Nuclear Receptors | 8.292961e-01 | 0.081 |
| R-HSA-6782210 | Gap-filling DNA repair synthesis and ligation in TC-NER | 8.293527e-01 | 0.081 |
| R-HSA-5617472 | Activation of anterior HOX genes in hindbrain development during early embryogen... | 8.296274e-01 | 0.081 |
| R-HSA-5619507 | Activation of HOX genes during differentiation | 8.296274e-01 | 0.081 |
| R-HSA-1483166 | Synthesis of PA | 8.340120e-01 | 0.079 |
| R-HSA-9006934 | Signaling by Receptor Tyrosine Kinases | 8.342680e-01 | 0.079 |
| R-HSA-166520 | Signaling by NTRKs | 8.363388e-01 | 0.078 |
| R-HSA-1266738 | Developmental Biology | 8.363573e-01 | 0.078 |
| R-HSA-418346 | Platelet homeostasis | 8.366971e-01 | 0.077 |
| R-HSA-6782135 | Dual incision in TC-NER | 8.385443e-01 | 0.076 |
| R-HSA-9029569 | NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflu... | 8.385443e-01 | 0.076 |
| R-HSA-9772572 | Early SARS-CoV-2 Infection Events | 8.385443e-01 | 0.076 |
| R-HSA-1799339 | SRP-dependent cotranslational protein targeting to membrane | 8.401318e-01 | 0.076 |
| R-HSA-8979227 | Triglyceride metabolism | 8.429532e-01 | 0.074 |
| R-HSA-2672351 | Stimuli-sensing channels | 8.435009e-01 | 0.074 |
| R-HSA-9609690 | HCMV Early Events | 8.440782e-01 | 0.074 |
| R-HSA-69002 | DNA Replication Pre-Initiation | 8.468055e-01 | 0.072 |
| R-HSA-2644602 | Signaling by NOTCH1 PEST Domain Mutants in Cancer | 8.472420e-01 | 0.072 |
| R-HSA-2894858 | Signaling by NOTCH1 HD+PEST Domain Mutants in Cancer | 8.472420e-01 | 0.072 |
| R-HSA-2894862 | Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants | 8.472420e-01 | 0.072 |
| R-HSA-2644606 | Constitutive Signaling by NOTCH1 PEST Domain Mutants | 8.472420e-01 | 0.072 |
| R-HSA-2644603 | Signaling by NOTCH1 in Cancer | 8.472420e-01 | 0.072 |
| R-HSA-8943724 | Regulation of PTEN gene transcription | 8.472420e-01 | 0.072 |
| R-HSA-379724 | tRNA Aminoacylation | 8.472420e-01 | 0.072 |
| R-HSA-9820448 | Developmental Cell Lineages of the Exocrine Pancreas | 8.478615e-01 | 0.072 |
| R-HSA-9010553 | Regulation of expression of SLITs and ROBOs | 8.478615e-01 | 0.072 |
| R-HSA-69306 | DNA Replication | 8.506299e-01 | 0.070 |
| R-HSA-445717 | Aquaporin-mediated transport | 8.514138e-01 | 0.070 |
| R-HSA-211976 | Endogenous sterols | 8.514138e-01 | 0.070 |
| R-HSA-9707616 | Heme signaling | 8.554721e-01 | 0.068 |
| R-HSA-186797 | Signaling by PDGF | 8.554721e-01 | 0.068 |
| R-HSA-1483206 | Glycerophospholipid biosynthesis | 8.610924e-01 | 0.065 |
| R-HSA-2454202 | Fc epsilon receptor (FCERI) signaling | 8.610924e-01 | 0.065 |
| R-HSA-8953854 | Metabolism of RNA | 8.614062e-01 | 0.065 |
| R-HSA-9609646 | HCMV Infection | 8.660153e-01 | 0.062 |
| R-HSA-392499 | Metabolism of proteins | 8.711671e-01 | 0.060 |
| R-HSA-193368 | Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol | 8.741631e-01 | 0.058 |
| R-HSA-1592230 | Mitochondrial biogenesis | 8.765237e-01 | 0.057 |
| R-HSA-167172 | Transcription of the HIV genome | 8.776012e-01 | 0.057 |
| R-HSA-1650814 | Collagen biosynthesis and modifying enzymes | 8.776012e-01 | 0.057 |
| R-HSA-388841 | Regulation of T cell activation by CD28 family | 8.779077e-01 | 0.057 |
| R-HSA-75105 | Fatty acyl-CoA biosynthesis | 8.841988e-01 | 0.053 |
| R-HSA-9840310 | Glycosphingolipid catabolism | 8.841988e-01 | 0.053 |
| R-HSA-5250913 | Positive epigenetic regulation of rRNA expression | 8.873634e-01 | 0.052 |
| R-HSA-8978934 | Metabolism of cofactors | 8.873634e-01 | 0.052 |
| R-HSA-3000178 | ECM proteoglycans | 8.873634e-01 | 0.052 |
| R-HSA-5620920 | Cargo trafficking to the periciliary membrane | 8.873634e-01 | 0.052 |
| R-HSA-9856649 | Transcriptional and post-translational regulation of MITF-M expression and activ... | 8.873634e-01 | 0.052 |
| R-HSA-4086398 | Ca2+ pathway | 8.934359e-01 | 0.049 |
| R-HSA-72306 | tRNA processing | 8.934449e-01 | 0.049 |
| R-HSA-674695 | RNA Polymerase II Pre-transcription Events | 8.963485e-01 | 0.048 |
| R-HSA-1226099 | Signaling by FGFR in disease | 8.963485e-01 | 0.048 |
| R-HSA-9909648 | Regulation of PD-L1(CD274) expression | 8.974515e-01 | 0.047 |
| R-HSA-6781827 | Transcription-Coupled Nucleotide Excision Repair (TC-NER) | 8.991817e-01 | 0.046 |
| R-HSA-71403 | Citric acid cycle (TCA cycle) | 8.991817e-01 | 0.046 |
| R-HSA-9662851 | Anti-inflammatory response favouring Leishmania parasite infection | 8.994036e-01 | 0.046 |
| R-HSA-9664433 | Leishmania parasite growth and survival | 8.994036e-01 | 0.046 |
| R-HSA-1980143 | Signaling by NOTCH1 | 9.019377e-01 | 0.045 |
| R-HSA-9694635 | Translation of Structural Proteins | 9.046184e-01 | 0.044 |
| R-HSA-9843745 | Adipogenesis | 9.132214e-01 | 0.039 |
| R-HSA-2151201 | Transcriptional activation of mitochondrial biogenesis | 9.146299e-01 | 0.039 |
| R-HSA-9707564 | Cytoprotection by HMOX1 | 9.192352e-01 | 0.037 |
| R-HSA-112316 | Neuronal System | 9.235207e-01 | 0.035 |
| R-HSA-1614635 | Sulfur amino acid metabolism | 9.277154e-01 | 0.033 |
| R-HSA-173623 | Classical antibody-mediated complement activation | 9.316163e-01 | 0.031 |
| R-HSA-156902 | Peptide chain elongation | 9.316163e-01 | 0.031 |
| R-HSA-1630316 | Glycosaminoglycan metabolism | 9.320175e-01 | 0.031 |
| R-HSA-373080 | Class B/2 (Secretin family receptors) | 9.353071e-01 | 0.029 |
| R-HSA-8856828 | Clathrin-mediated endocytosis | 9.366878e-01 | 0.028 |
| R-HSA-9954714 | PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA | 9.370772e-01 | 0.028 |
| R-HSA-1912408 | Pre-NOTCH Transcription and Translation | 9.370772e-01 | 0.028 |
| R-HSA-975956 | Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) | 9.387991e-01 | 0.027 |
| R-HSA-156842 | Eukaryotic Translation Elongation | 9.404739e-01 | 0.027 |
| R-HSA-9772573 | Late SARS-CoV-2 Infection Events | 9.404739e-01 | 0.027 |
| R-HSA-389948 | Co-inhibition by PD-1 | 9.409161e-01 | 0.026 |
| R-HSA-983695 | Antigen activates B Cell Receptor (BCR) leading to generation of second messenge... | 9.421030e-01 | 0.026 |
| R-HSA-2029481 | FCGR activation | 9.421030e-01 | 0.026 |
| R-HSA-72764 | Eukaryotic Translation Termination | 9.467281e-01 | 0.024 |
| R-HSA-72689 | Formation of a pool of free 40S subunits | 9.467281e-01 | 0.024 |
| R-HSA-6805567 | Keratinization | 9.487269e-01 | 0.023 |
| R-HSA-9609507 | Protein localization | 9.496229e-01 | 0.022 |
| R-HSA-1989781 | PPARA activates gene expression | 9.518885e-01 | 0.021 |
| R-HSA-9614085 | FOXO-mediated transcription | 9.523266e-01 | 0.021 |
| R-HSA-192105 | Synthesis of bile acids and bile salts | 9.523266e-01 | 0.021 |
| R-HSA-400206 | Regulation of lipid metabolism by PPARalpha | 9.540567e-01 | 0.020 |
| R-HSA-2408557 | Selenocysteine synthesis | 9.549016e-01 | 0.020 |
| R-HSA-192823 | Viral mRNA Translation | 9.573379e-01 | 0.019 |
| R-HSA-9633012 | Response of EIF2AK4 (GCN2) to amino acid deficiency | 9.585063e-01 | 0.018 |
| R-HSA-111885 | Opioid Signalling | 9.585063e-01 | 0.018 |
| R-HSA-166786 | Creation of C4 and C2 activators | 9.618235e-01 | 0.017 |
| R-HSA-72706 | GTP hydrolysis and joining of the 60S ribosomal subunit | 9.638866e-01 | 0.016 |
| R-HSA-156827 | L13a-mediated translational silencing of Ceruloplasmin expression | 9.638866e-01 | 0.016 |
| R-HSA-194068 | Bile acid and bile salt metabolism | 9.658384e-01 | 0.015 |
| R-HSA-6803157 | Antimicrobial peptides | 9.667745e-01 | 0.015 |
| R-HSA-927802 | Nonsense-Mediated Decay (NMD) | 9.676849e-01 | 0.014 |
| R-HSA-975957 | Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) | 9.676849e-01 | 0.014 |
| R-HSA-198933 | Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell | 9.681337e-01 | 0.014 |
| R-HSA-1912422 | Pre-NOTCH Expression and Processing | 9.685705e-01 | 0.014 |
| R-HSA-166663 | Initial triggering of complement | 9.702697e-01 | 0.013 |
| R-HSA-9824439 | Bacterial Infection Pathways | 9.707879e-01 | 0.013 |
| R-HSA-611105 | Respiratory electron transport | 9.725015e-01 | 0.012 |
| R-HSA-15869 | Metabolism of nucleotides | 9.725035e-01 | 0.012 |
| R-HSA-72613 | Eukaryotic Translation Initiation | 9.726482e-01 | 0.012 |
| R-HSA-72737 | Cap-dependent Translation Initiation | 9.726482e-01 | 0.012 |
| R-HSA-202733 | Cell surface interactions at the vascular wall | 9.730794e-01 | 0.012 |
| R-HSA-2980736 | Peptide hormone metabolism | 9.733980e-01 | 0.012 |
| R-HSA-157118 | Signaling by NOTCH | 9.747393e-01 | 0.011 |
| R-HSA-201681 | TCF dependent signaling in response to WNT | 9.755641e-01 | 0.011 |
| R-HSA-195721 | Signaling by WNT | 9.760042e-01 | 0.011 |
| R-HSA-3781865 | Diseases of glycosylation | 9.761358e-01 | 0.010 |
| R-HSA-9635486 | Infection with Mycobacterium tuberculosis | 9.761978e-01 | 0.010 |
| R-HSA-1660662 | Glycosphingolipid metabolism | 9.774854e-01 | 0.010 |
| R-HSA-977606 | Regulation of Complement cascade | 9.787035e-01 | 0.009 |
| R-HSA-4839726 | Chromatin organization | 9.791562e-01 | 0.009 |
| R-HSA-9664323 | FCGR3A-mediated IL10 synthesis | 9.798559e-01 | 0.009 |
| R-HSA-199418 | Negative regulation of the PI3K/AKT network | 9.819773e-01 | 0.008 |
| R-HSA-446219 | Synthesis of substrates in N-glycan biosythesis | 9.829528e-01 | 0.007 |
| R-HSA-1474228 | Degradation of the extracellular matrix | 9.834207e-01 | 0.007 |
| R-HSA-72766 | Translation | 9.853015e-01 | 0.006 |
| R-HSA-8957322 | Metabolism of steroids | 9.857201e-01 | 0.006 |
| R-HSA-166658 | Complement cascade | 9.890807e-01 | 0.005 |
| R-HSA-2187338 | Visual phototransduction | 9.896724e-01 | 0.005 |
| R-HSA-9748784 | Drug ADME | 9.896950e-01 | 0.004 |
| R-HSA-446193 | Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, L... | 9.921841e-01 | 0.003 |
| R-HSA-3247509 | Chromatin modifying enzymes | 9.930251e-01 | 0.003 |
| R-HSA-2408522 | Selenoamino acid metabolism | 9.935699e-01 | 0.003 |
| R-HSA-211897 | Cytochrome P450 - arranged by substrate type | 9.940860e-01 | 0.003 |
| R-HSA-418555 | G alpha (s) signalling events | 9.948560e-01 | 0.002 |
| R-HSA-375276 | Peptide ligand-binding receptors | 9.966158e-01 | 0.001 |
| R-HSA-1428517 | Aerobic respiration and respiratory electron transport | 9.973292e-01 | 0.001 |
| R-HSA-382551 | Transport of small molecules | 9.973706e-01 | 0.001 |
| R-HSA-418594 | G alpha (i) signalling events | 9.975626e-01 | 0.001 |
| R-HSA-211945 | Phase I - Functionalization of compounds | 9.976560e-01 | 0.001 |
| R-HSA-428157 | Sphingolipid metabolism | 9.977745e-01 | 0.001 |
| R-HSA-9640148 | Infection with Enterobacteria | 9.978955e-01 | 0.001 |
| R-HSA-71291 | Metabolism of amino acids and derivatives | 9.988477e-01 | 0.001 |
| R-HSA-196849 | Metabolism of water-soluble vitamins and cofactors | 9.990387e-01 | 0.000 |
| R-HSA-416476 | G alpha (q) signalling events | 9.996294e-01 | 0.000 |
| R-HSA-196854 | Metabolism of vitamins and cofactors | 9.997372e-01 | 0.000 |
| R-HSA-388396 | GPCR downstream signalling | 9.998404e-01 | 0.000 |
| R-HSA-425407 | SLC-mediated transmembrane transport | 9.998912e-01 | 0.000 |
| R-HSA-5668914 | Diseases of metabolism | 9.999503e-01 | 0.000 |
| R-HSA-500792 | GPCR ligand binding | 9.999622e-01 | 0.000 |
| R-HSA-372790 | Signaling by GPCR | 9.999714e-01 | 0.000 |
| R-HSA-373076 | Class A/1 (Rhodopsin-like receptors) | 9.999908e-01 | 0.000 |
| R-HSA-8978868 | Fatty acid metabolism | 9.999936e-01 | 0.000 |
| R-HSA-211859 | Biological oxidations | 9.999961e-01 | 0.000 |
| R-HSA-556833 | Metabolism of lipids | 9.999992e-01 | 0.000 |
| R-HSA-9709957 | Sensory Perception | 1.000000e+00 | 0.000 |
| R-HSA-1430728 | Metabolism | 1.000000e+00 | 0.000 |
Download
| kinase | JSD_mean | pearson_surrounding | kinase_max_IC_position | max_position_JSD |
|---|---|---|---|---|
COT |
0.882 | 0.144 | 2 | 0.875 |
RSK2 |
0.877 | 0.286 | -3 | 0.861 |
PIM3 |
0.877 | 0.231 | -3 | 0.876 |
PRKD2 |
0.877 | 0.289 | -3 | 0.842 |
PRKD1 |
0.875 | 0.236 | -3 | 0.861 |
CAMK1B |
0.874 | 0.242 | -3 | 0.907 |
PIM1 |
0.874 | 0.296 | -3 | 0.856 |
CLK3 |
0.872 | 0.210 | 1 | 0.835 |
P90RSK |
0.871 | 0.253 | -3 | 0.859 |
CDC7 |
0.871 | 0.061 | 1 | 0.857 |
PKN3 |
0.871 | 0.191 | -3 | 0.870 |
CDKL1 |
0.871 | 0.233 | -3 | 0.877 |
RAF1 |
0.870 | 0.102 | 1 | 0.859 |
MAPKAPK3 |
0.869 | 0.228 | -3 | 0.842 |
TSSK2 |
0.869 | 0.231 | -5 | 0.892 |
MAPKAPK2 |
0.869 | 0.256 | -3 | 0.814 |
P70S6KB |
0.867 | 0.235 | -3 | 0.872 |
RSK3 |
0.867 | 0.226 | -3 | 0.856 |
NDR2 |
0.866 | 0.097 | -3 | 0.853 |
SRPK1 |
0.865 | 0.224 | -3 | 0.844 |
NUAK2 |
0.865 | 0.168 | -3 | 0.892 |
TSSK1 |
0.865 | 0.220 | -3 | 0.893 |
WNK1 |
0.865 | 0.130 | -2 | 0.882 |
IKKB |
0.865 | 0.007 | -2 | 0.786 |
PRPK |
0.865 | -0.105 | -1 | 0.870 |
PKN2 |
0.864 | 0.166 | -3 | 0.874 |
AMPKA1 |
0.864 | 0.178 | -3 | 0.882 |
NLK |
0.864 | 0.078 | 1 | 0.814 |
ATR |
0.864 | 0.112 | 1 | 0.877 |
CDKL5 |
0.864 | 0.185 | -3 | 0.873 |
NDR1 |
0.864 | 0.137 | -3 | 0.869 |
PRKD3 |
0.863 | 0.258 | -3 | 0.838 |
CAMLCK |
0.863 | 0.169 | -2 | 0.872 |
DSTYK |
0.863 | 0.020 | 2 | 0.860 |
NIK |
0.862 | 0.152 | -3 | 0.891 |
MOS |
0.862 | 0.004 | 1 | 0.871 |
TBK1 |
0.862 | -0.004 | 1 | 0.761 |
PKCD |
0.862 | 0.165 | 2 | 0.781 |
CAMK2G |
0.862 | -0.004 | 2 | 0.805 |
SKMLCK |
0.862 | 0.157 | -2 | 0.858 |
PKACG |
0.862 | 0.181 | -2 | 0.784 |
ULK2 |
0.861 | -0.083 | 2 | 0.793 |
RSK4 |
0.861 | 0.266 | -3 | 0.825 |
CAMK2D |
0.861 | 0.115 | -3 | 0.877 |
DAPK2 |
0.861 | 0.182 | -3 | 0.900 |
AMPKA2 |
0.860 | 0.187 | -3 | 0.867 |
SRPK2 |
0.860 | 0.231 | -3 | 0.793 |
MARK4 |
0.860 | 0.068 | 4 | 0.820 |
MELK |
0.860 | 0.214 | -3 | 0.862 |
LATS2 |
0.859 | 0.098 | -5 | 0.775 |
PDHK4 |
0.859 | -0.202 | 1 | 0.858 |
MSK2 |
0.858 | 0.191 | -3 | 0.831 |
ERK5 |
0.858 | 0.051 | 1 | 0.759 |
MTOR |
0.858 | -0.113 | 1 | 0.781 |
CAMK2B |
0.858 | 0.176 | 2 | 0.772 |
IKKE |
0.857 | -0.018 | 1 | 0.761 |
ICK |
0.857 | 0.155 | -3 | 0.890 |
CAMK4 |
0.857 | 0.124 | -3 | 0.866 |
GRK6 |
0.856 | 0.095 | 1 | 0.837 |
MSK1 |
0.856 | 0.217 | -3 | 0.835 |
MST4 |
0.856 | 0.049 | 2 | 0.796 |
AURC |
0.856 | 0.150 | -2 | 0.698 |
PAK1 |
0.856 | 0.137 | -2 | 0.812 |
BMPR2 |
0.856 | -0.204 | -2 | 0.866 |
GCN2 |
0.856 | -0.207 | 2 | 0.785 |
PKACB |
0.856 | 0.227 | -2 | 0.717 |
NIM1 |
0.855 | 0.077 | 3 | 0.764 |
NUAK1 |
0.855 | 0.149 | -3 | 0.858 |
WNK3 |
0.855 | -0.038 | 1 | 0.828 |
PDHK1 |
0.855 | -0.149 | 1 | 0.858 |
RIPK3 |
0.855 | -0.021 | 3 | 0.716 |
CAMK2A |
0.854 | 0.163 | 2 | 0.770 |
HIPK4 |
0.854 | 0.093 | 1 | 0.780 |
HUNK |
0.854 | -0.037 | 2 | 0.805 |
PRKX |
0.854 | 0.267 | -3 | 0.769 |
AKT2 |
0.854 | 0.257 | -3 | 0.807 |
SGK3 |
0.854 | 0.246 | -3 | 0.835 |
MNK2 |
0.854 | 0.123 | -2 | 0.821 |
PAK3 |
0.853 | 0.094 | -2 | 0.821 |
CHAK2 |
0.853 | 0.002 | -1 | 0.890 |
PIM2 |
0.853 | 0.246 | -3 | 0.845 |
LATS1 |
0.853 | 0.177 | -3 | 0.858 |
CHK1 |
0.853 | 0.166 | -3 | 0.852 |
IKKA |
0.853 | 0.015 | -2 | 0.760 |
PAK6 |
0.852 | 0.131 | -2 | 0.769 |
CLK1 |
0.852 | 0.219 | -3 | 0.843 |
ULK1 |
0.852 | -0.121 | -3 | 0.784 |
CLK4 |
0.852 | 0.203 | -3 | 0.858 |
ATM |
0.851 | 0.114 | 1 | 0.838 |
SIK |
0.851 | 0.151 | -3 | 0.839 |
MYLK4 |
0.851 | 0.170 | -2 | 0.802 |
FAM20C |
0.851 | 0.117 | 2 | 0.641 |
PKG2 |
0.851 | 0.180 | -2 | 0.732 |
QSK |
0.851 | 0.107 | 4 | 0.794 |
AURB |
0.850 | 0.135 | -2 | 0.695 |
GRK5 |
0.850 | -0.134 | -3 | 0.819 |
SRPK3 |
0.849 | 0.171 | -3 | 0.823 |
QIK |
0.849 | 0.054 | -3 | 0.871 |
NEK7 |
0.849 | -0.150 | -3 | 0.812 |
MNK1 |
0.849 | 0.132 | -2 | 0.834 |
PKCB |
0.849 | 0.113 | 2 | 0.727 |
GRK1 |
0.849 | 0.025 | -2 | 0.772 |
NEK6 |
0.848 | -0.104 | -2 | 0.822 |
DYRK2 |
0.848 | 0.108 | 1 | 0.673 |
MLK1 |
0.847 | -0.126 | 2 | 0.795 |
CAMK1G |
0.847 | 0.176 | -3 | 0.855 |
TGFBR2 |
0.847 | -0.098 | -2 | 0.741 |
AKT1 |
0.847 | 0.251 | -3 | 0.812 |
RIPK1 |
0.847 | -0.069 | 1 | 0.814 |
CLK2 |
0.846 | 0.243 | -3 | 0.843 |
BCKDK |
0.846 | -0.122 | -1 | 0.833 |
BRSK1 |
0.846 | 0.099 | -3 | 0.856 |
NEK9 |
0.846 | -0.105 | 2 | 0.815 |
IRE1 |
0.845 | -0.030 | 1 | 0.799 |
DNAPK |
0.845 | 0.156 | 1 | 0.794 |
PAK2 |
0.845 | 0.078 | -2 | 0.801 |
CAMK1D |
0.845 | 0.249 | -3 | 0.790 |
SSTK |
0.845 | 0.155 | 4 | 0.783 |
PKR |
0.845 | 0.062 | 1 | 0.852 |
IRE2 |
0.845 | 0.012 | 2 | 0.789 |
PKCG |
0.845 | 0.071 | 2 | 0.729 |
DLK |
0.845 | -0.093 | 1 | 0.828 |
P70S6K |
0.845 | 0.207 | -3 | 0.817 |
PKACA |
0.844 | 0.220 | -2 | 0.678 |
PKCH |
0.844 | 0.084 | 2 | 0.724 |
JNK2 |
0.844 | 0.094 | 1 | 0.596 |
PKCA |
0.844 | 0.073 | 2 | 0.718 |
MARK3 |
0.844 | 0.068 | 4 | 0.750 |
MASTL |
0.843 | -0.244 | -2 | 0.818 |
MARK2 |
0.843 | 0.060 | 4 | 0.716 |
DCAMKL1 |
0.843 | 0.176 | -3 | 0.848 |
PLK1 |
0.843 | -0.008 | -2 | 0.772 |
MAPKAPK5 |
0.842 | 0.104 | -3 | 0.820 |
ANKRD3 |
0.842 | -0.129 | 1 | 0.855 |
MLK2 |
0.841 | -0.141 | 2 | 0.793 |
BRSK2 |
0.840 | 0.027 | -3 | 0.862 |
NEK2 |
0.840 | -0.020 | 2 | 0.790 |
MARK1 |
0.840 | 0.056 | 4 | 0.777 |
AURA |
0.840 | 0.099 | -2 | 0.650 |
ALK4 |
0.840 | -0.028 | -2 | 0.791 |
PKCZ |
0.840 | 0.037 | 2 | 0.774 |
BRAF |
0.840 | 0.068 | -4 | 0.808 |
CDK8 |
0.839 | -0.028 | 1 | 0.646 |
DYRK1A |
0.839 | 0.150 | 1 | 0.717 |
BMPR1B |
0.839 | 0.050 | 1 | 0.788 |
SNRK |
0.839 | -0.027 | 2 | 0.720 |
PHKG1 |
0.839 | 0.023 | -3 | 0.867 |
SMMLCK |
0.839 | 0.160 | -3 | 0.882 |
JNK3 |
0.839 | 0.059 | 1 | 0.629 |
TTBK2 |
0.838 | -0.161 | 2 | 0.707 |
SMG1 |
0.837 | 0.031 | 1 | 0.843 |
DCAMKL2 |
0.837 | 0.118 | -3 | 0.872 |
KIS |
0.837 | -0.034 | 1 | 0.671 |
TGFBR1 |
0.836 | -0.019 | -2 | 0.753 |
MEK1 |
0.836 | -0.148 | 2 | 0.817 |
MLK3 |
0.836 | -0.078 | 2 | 0.725 |
HIPK1 |
0.836 | 0.124 | 1 | 0.691 |
SGK1 |
0.836 | 0.268 | -3 | 0.740 |
CDK7 |
0.835 | -0.024 | 1 | 0.653 |
AKT3 |
0.835 | 0.251 | -3 | 0.752 |
PLK3 |
0.835 | -0.024 | 2 | 0.778 |
CHAK1 |
0.835 | -0.079 | 2 | 0.738 |
VRK2 |
0.835 | -0.163 | 1 | 0.865 |
GRK4 |
0.835 | -0.171 | -2 | 0.779 |
PHKG2 |
0.835 | 0.089 | -3 | 0.862 |
WNK4 |
0.835 | 0.016 | -2 | 0.872 |
PKCT |
0.834 | 0.091 | 2 | 0.732 |
CAMK1A |
0.834 | 0.237 | -3 | 0.769 |
YSK4 |
0.834 | -0.113 | 1 | 0.785 |
CDK19 |
0.833 | -0.025 | 1 | 0.607 |
CDK5 |
0.833 | 0.009 | 1 | 0.670 |
GRK7 |
0.833 | 0.030 | 1 | 0.759 |
DAPK3 |
0.833 | 0.205 | -3 | 0.867 |
PKN1 |
0.833 | 0.175 | -3 | 0.831 |
ALK2 |
0.832 | 0.008 | -2 | 0.766 |
DYRK3 |
0.832 | 0.149 | 1 | 0.695 |
P38A |
0.832 | 0.016 | 1 | 0.667 |
IRAK4 |
0.832 | 0.003 | 1 | 0.812 |
CHK2 |
0.832 | 0.226 | -3 | 0.766 |
SBK |
0.832 | 0.259 | -3 | 0.718 |
MRCKA |
0.831 | 0.239 | -3 | 0.834 |
HIPK2 |
0.831 | 0.095 | 1 | 0.584 |
CDK2 |
0.831 | -0.009 | 1 | 0.688 |
MLK4 |
0.831 | -0.101 | 2 | 0.718 |
DRAK1 |
0.830 | -0.040 | 1 | 0.747 |
HIPK3 |
0.830 | 0.090 | 1 | 0.683 |
CDK13 |
0.830 | -0.033 | 1 | 0.625 |
PASK |
0.830 | 0.103 | -3 | 0.875 |
MRCKB |
0.829 | 0.227 | -3 | 0.828 |
CDK18 |
0.829 | 0.002 | 1 | 0.580 |
DYRK4 |
0.829 | 0.088 | 1 | 0.597 |
PKCI |
0.829 | 0.074 | 2 | 0.741 |
CDK1 |
0.829 | -0.000 | 1 | 0.607 |
DYRK1B |
0.829 | 0.090 | 1 | 0.625 |
ACVR2A |
0.828 | -0.067 | -2 | 0.741 |
PAK5 |
0.828 | 0.075 | -2 | 0.690 |
CDK14 |
0.828 | 0.046 | 1 | 0.627 |
P38B |
0.827 | 0.019 | 1 | 0.597 |
PKCE |
0.827 | 0.132 | 2 | 0.712 |
ACVR2B |
0.827 | -0.065 | -2 | 0.756 |
CAMKK1 |
0.827 | 0.044 | -2 | 0.839 |
ERK2 |
0.827 | -0.007 | 1 | 0.640 |
DAPK1 |
0.827 | 0.186 | -3 | 0.859 |
PINK1 |
0.827 | -0.126 | 1 | 0.818 |
ROCK2 |
0.826 | 0.234 | -3 | 0.846 |
P38G |
0.825 | 0.013 | 1 | 0.518 |
CDK9 |
0.825 | -0.037 | 1 | 0.633 |
NEK5 |
0.825 | -0.066 | 1 | 0.836 |
TLK2 |
0.825 | -0.119 | 1 | 0.828 |
HRI |
0.825 | -0.195 | -2 | 0.822 |
PLK4 |
0.824 | -0.125 | 2 | 0.673 |
PRP4 |
0.824 | -0.030 | -3 | 0.711 |
MST3 |
0.824 | -0.017 | 2 | 0.795 |
CDK10 |
0.824 | 0.071 | 1 | 0.612 |
ERK1 |
0.824 | -0.008 | 1 | 0.589 |
PERK |
0.823 | -0.178 | -2 | 0.808 |
ZAK |
0.823 | -0.136 | 1 | 0.785 |
P38D |
0.823 | 0.055 | 1 | 0.552 |
MEK5 |
0.823 | -0.242 | 2 | 0.806 |
CDK12 |
0.823 | -0.030 | 1 | 0.598 |
PAK4 |
0.823 | 0.064 | -2 | 0.685 |
CDK17 |
0.823 | -0.016 | 1 | 0.527 |
MEKK1 |
0.822 | -0.174 | 1 | 0.819 |
GRK2 |
0.822 | -0.099 | -2 | 0.683 |
BMPR1A |
0.822 | 0.023 | 1 | 0.777 |
MEKK3 |
0.822 | -0.175 | 1 | 0.799 |
CAMKK2 |
0.822 | 0.017 | -2 | 0.839 |
MEKK2 |
0.821 | -0.136 | 2 | 0.793 |
GAK |
0.821 | 0.033 | 1 | 0.828 |
IRAK1 |
0.820 | -0.145 | -1 | 0.783 |
DMPK1 |
0.820 | 0.241 | -3 | 0.845 |
CDK16 |
0.820 | 0.025 | 1 | 0.546 |
CDK3 |
0.820 | 0.026 | 1 | 0.545 |
TLK1 |
0.820 | -0.125 | -2 | 0.767 |
TAO3 |
0.819 | -0.065 | 1 | 0.799 |
LKB1 |
0.819 | -0.001 | -3 | 0.800 |
BUB1 |
0.819 | 0.130 | -5 | 0.837 |
NEK8 |
0.818 | -0.083 | 2 | 0.811 |
MPSK1 |
0.818 | -0.043 | 1 | 0.772 |
TAO2 |
0.818 | -0.063 | 2 | 0.830 |
CK2A2 |
0.817 | 0.108 | 1 | 0.703 |
NEK4 |
0.817 | -0.020 | 1 | 0.814 |
PDK1 |
0.817 | -0.011 | 1 | 0.792 |
PKG1 |
0.816 | 0.150 | -2 | 0.664 |
CK1E |
0.816 | -0.085 | -3 | 0.517 |
ROCK1 |
0.816 | 0.219 | -3 | 0.833 |
GSK3B |
0.816 | -0.039 | 4 | 0.416 |
MAK |
0.815 | 0.157 | -2 | 0.745 |
CRIK |
0.815 | 0.230 | -3 | 0.806 |
MOK |
0.815 | 0.155 | 1 | 0.694 |
TNIK |
0.814 | 0.030 | 3 | 0.851 |
TAK1 |
0.814 | -0.011 | 1 | 0.842 |
TTBK1 |
0.814 | -0.156 | 2 | 0.637 |
HGK |
0.814 | -0.015 | 3 | 0.850 |
LRRK2 |
0.814 | -0.045 | 2 | 0.834 |
LOK |
0.813 | 0.014 | -2 | 0.815 |
ERK7 |
0.813 | 0.013 | 2 | 0.551 |
CDK4 |
0.813 | 0.027 | 1 | 0.589 |
EEF2K |
0.813 | -0.030 | 3 | 0.836 |
JNK1 |
0.813 | 0.020 | 1 | 0.582 |
GCK |
0.812 | -0.017 | 1 | 0.814 |
MINK |
0.812 | -0.018 | 1 | 0.814 |
CDK6 |
0.811 | 0.013 | 1 | 0.605 |
NEK11 |
0.811 | -0.189 | 1 | 0.796 |
GSK3A |
0.811 | -0.025 | 4 | 0.428 |
NEK1 |
0.811 | -0.016 | 1 | 0.809 |
MEKK6 |
0.811 | -0.088 | 1 | 0.789 |
MST2 |
0.811 | -0.079 | 1 | 0.821 |
PLK2 |
0.810 | 0.015 | -3 | 0.777 |
HPK1 |
0.810 | 0.010 | 1 | 0.806 |
PBK |
0.808 | 0.030 | 1 | 0.747 |
VRK1 |
0.808 | -0.104 | 2 | 0.862 |
KHS1 |
0.808 | 0.049 | 1 | 0.809 |
KHS2 |
0.808 | 0.076 | 1 | 0.821 |
CK2A1 |
0.806 | 0.076 | 1 | 0.680 |
MAP3K15 |
0.805 | -0.139 | 1 | 0.767 |
CK1D |
0.805 | -0.093 | -3 | 0.463 |
SLK |
0.805 | -0.043 | -2 | 0.744 |
STK33 |
0.805 | -0.120 | 2 | 0.622 |
GRK3 |
0.805 | -0.109 | -2 | 0.626 |
MST1 |
0.805 | -0.072 | 1 | 0.809 |
PDHK3_TYR |
0.804 | 0.157 | 4 | 0.898 |
CK1A2 |
0.804 | -0.089 | -3 | 0.471 |
CK1G1 |
0.803 | -0.117 | -3 | 0.500 |
RIPK2 |
0.803 | -0.183 | 1 | 0.745 |
YSK1 |
0.802 | -0.074 | 2 | 0.777 |
MEK2 |
0.800 | -0.226 | 2 | 0.794 |
HASPIN |
0.798 | 0.046 | -1 | 0.738 |
NEK3 |
0.797 | -0.135 | 1 | 0.760 |
TESK1_TYR |
0.796 | -0.043 | 3 | 0.874 |
BIKE |
0.795 | 0.021 | 1 | 0.705 |
PDHK4_TYR |
0.792 | -0.014 | 2 | 0.854 |
LIMK2_TYR |
0.792 | 0.017 | -3 | 0.872 |
MYO3B |
0.791 | -0.038 | 2 | 0.795 |
TTK |
0.791 | -0.075 | -2 | 0.759 |
MAP2K4_TYR |
0.790 | -0.128 | -1 | 0.891 |
PINK1_TYR |
0.790 | -0.102 | 1 | 0.826 |
MAP2K7_TYR |
0.790 | -0.210 | 2 | 0.842 |
MAP2K6_TYR |
0.789 | -0.086 | -1 | 0.899 |
PKMYT1_TYR |
0.789 | -0.163 | 3 | 0.828 |
EPHA6 |
0.789 | 0.037 | -1 | 0.877 |
BMPR2_TYR |
0.788 | -0.064 | -1 | 0.874 |
MYO3A |
0.787 | -0.071 | 1 | 0.808 |
OSR1 |
0.786 | -0.135 | 2 | 0.769 |
RET |
0.786 | -0.051 | 1 | 0.806 |
ALPHAK3 |
0.786 | -0.046 | -1 | 0.793 |
PDHK1_TYR |
0.785 | -0.124 | -1 | 0.908 |
ASK1 |
0.784 | -0.161 | 1 | 0.756 |
TAO1 |
0.784 | -0.100 | 1 | 0.735 |
YANK3 |
0.784 | -0.074 | 2 | 0.419 |
EPHB4 |
0.782 | -0.028 | -1 | 0.865 |
LIMK1_TYR |
0.782 | -0.177 | 2 | 0.841 |
DDR1 |
0.781 | -0.082 | 4 | 0.805 |
TYK2 |
0.781 | -0.135 | 1 | 0.807 |
ROS1 |
0.781 | -0.081 | 3 | 0.742 |
TYRO3 |
0.780 | -0.119 | 3 | 0.768 |
AAK1 |
0.778 | 0.051 | 1 | 0.599 |
MST1R |
0.778 | -0.158 | 3 | 0.766 |
JAK2 |
0.777 | -0.146 | 1 | 0.801 |
CSF1R |
0.775 | -0.129 | 3 | 0.748 |
INSRR |
0.774 | -0.070 | 3 | 0.717 |
ABL2 |
0.774 | -0.077 | -1 | 0.833 |
FER |
0.774 | -0.117 | 1 | 0.860 |
EPHA4 |
0.774 | -0.045 | 2 | 0.772 |
TNK1 |
0.773 | -0.053 | 3 | 0.744 |
TNNI3K_TYR |
0.773 | -0.038 | 1 | 0.810 |
JAK3 |
0.773 | -0.128 | 1 | 0.776 |
EPHB1 |
0.772 | -0.073 | 1 | 0.833 |
STLK3 |
0.772 | -0.201 | 1 | 0.759 |
TNK2 |
0.771 | -0.097 | 3 | 0.707 |
PDGFRB |
0.771 | -0.146 | 3 | 0.769 |
YES1 |
0.771 | -0.111 | -1 | 0.849 |
NEK10_TYR |
0.771 | -0.081 | 1 | 0.687 |
EPHB3 |
0.770 | -0.069 | -1 | 0.850 |
TXK |
0.770 | -0.043 | 1 | 0.813 |
FLT3 |
0.770 | -0.115 | 3 | 0.756 |
FGFR2 |
0.770 | -0.140 | 3 | 0.762 |
ABL1 |
0.769 | -0.106 | -1 | 0.824 |
EPHB2 |
0.769 | -0.057 | -1 | 0.843 |
SRMS |
0.769 | -0.103 | 1 | 0.840 |
TEK |
0.768 | -0.132 | 3 | 0.700 |
AXL |
0.768 | -0.112 | 3 | 0.738 |
FGR |
0.768 | -0.193 | 1 | 0.824 |
ITK |
0.768 | -0.108 | -1 | 0.801 |
KDR |
0.766 | -0.124 | 3 | 0.714 |
HCK |
0.765 | -0.164 | -1 | 0.821 |
FGFR1 |
0.765 | -0.171 | 3 | 0.730 |
PDGFRA |
0.764 | -0.190 | 3 | 0.759 |
KIT |
0.764 | -0.178 | 3 | 0.752 |
MERTK |
0.764 | -0.118 | 3 | 0.730 |
JAK1 |
0.763 | -0.123 | 1 | 0.751 |
ALK |
0.763 | -0.127 | 3 | 0.674 |
LTK |
0.762 | -0.116 | 3 | 0.695 |
DDR2 |
0.762 | -0.023 | 3 | 0.698 |
TEC |
0.761 | -0.106 | -1 | 0.745 |
EPHA7 |
0.761 | -0.093 | 2 | 0.784 |
WEE1_TYR |
0.761 | -0.133 | -1 | 0.753 |
LCK |
0.761 | -0.129 | -1 | 0.819 |
BTK |
0.761 | -0.187 | -1 | 0.766 |
BMX |
0.761 | -0.097 | -1 | 0.719 |
CK1A |
0.760 | -0.142 | -3 | 0.370 |
BLK |
0.759 | -0.093 | -1 | 0.832 |
EPHA3 |
0.759 | -0.133 | 2 | 0.755 |
PTK6 |
0.759 | -0.197 | -1 | 0.741 |
NTRK1 |
0.758 | -0.198 | -1 | 0.841 |
EPHA1 |
0.757 | -0.144 | 3 | 0.712 |
FLT4 |
0.756 | -0.172 | 3 | 0.712 |
FGFR3 |
0.756 | -0.164 | 3 | 0.733 |
INSR |
0.756 | -0.163 | 3 | 0.692 |
FRK |
0.755 | -0.128 | -1 | 0.845 |
EPHA5 |
0.755 | -0.076 | 2 | 0.771 |
MET |
0.755 | -0.211 | 3 | 0.736 |
ERBB2 |
0.754 | -0.209 | 1 | 0.760 |
FLT1 |
0.753 | -0.185 | -1 | 0.856 |
NTRK2 |
0.753 | -0.236 | 3 | 0.707 |
FYN |
0.752 | -0.106 | -1 | 0.784 |
PTK2B |
0.752 | -0.114 | -1 | 0.789 |
MATK |
0.750 | -0.154 | -1 | 0.766 |
LYN |
0.748 | -0.176 | 3 | 0.672 |
CSK |
0.748 | -0.155 | 2 | 0.782 |
EGFR |
0.746 | -0.124 | 1 | 0.663 |
EPHA8 |
0.746 | -0.141 | -1 | 0.820 |
NTRK3 |
0.746 | -0.216 | -1 | 0.793 |
CK1G3 |
0.746 | -0.121 | -3 | 0.322 |
YANK2 |
0.745 | -0.126 | 2 | 0.433 |
PTK2 |
0.742 | -0.073 | -1 | 0.785 |
FGFR4 |
0.741 | -0.154 | -1 | 0.792 |
SRC |
0.740 | -0.182 | -1 | 0.792 |
IGF1R |
0.739 | -0.160 | 3 | 0.630 |
SYK |
0.738 | -0.093 | -1 | 0.776 |
EPHA2 |
0.737 | -0.141 | -1 | 0.786 |
MUSK |
0.736 | -0.196 | 1 | 0.643 |
ERBB4 |
0.731 | -0.135 | 1 | 0.685 |
FES |
0.722 | -0.200 | -1 | 0.696 |
CK1G2 |
0.716 | -0.162 | -3 | 0.416 |
ZAP70 |
0.708 | -0.158 | -1 | 0.694 |