Motif 979 (n=116)
Position-wise Probabilities
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| uniprot | genes | site | source | protein | function |
|---|---|---|---|---|---|
| E9PCH4 | None | S751 | ochoa | Rap guanine nucleotide exchange factor 6 | None |
| F6TDL0 | P3R3URF-PIK3R3 | Y230 | ochoa | Phosphatidylinositol 3-kinase regulatory subunit gamma (Phosphatidylinositol 3-kinase 55 kDa regulatory subunit gamma) (p55PIK) | Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1. {ECO:0000256|ARBA:ARBA00057933}. |
| H0YIS7 | RNASEK-C17orf49 | S77 | ochoa | BPTF-associated chromatin complex component 1 (BPTF-associated protein of 18 kDa) (Chromatin complexes subunit BAP18) | Component of chromatin complexes such as the MLL1/MLL and NURF complexes. {ECO:0000256|ARBA:ARBA00059556}. |
| O15554 | KCNN4 | S334 | psp | Intermediate conductance calcium-activated potassium channel protein 4 (SKCa 4) (SKCa4) (hSK4) (Gardos channel) (IKCa1) (hIK1) (KCa3.1) (Putative Gardos channel) (hKCa4) | Intermediate conductance calcium-activated potassium channel that mediates the voltage-independent transmembrane transfer of potassium across the cell membrane through a constitutive interaction with calmodulin which binds the intracellular calcium allowing its opening (PubMed:10026195, PubMed:10961988, PubMed:11425865, PubMed:15831468, PubMed:17157250, PubMed:18796614, PubMed:26148990, PubMed:9326665, PubMed:9380751, PubMed:9407042). The current is characterized by a voltage-independent activation, an intracellular calcium concentration increase-dependent activation and a single-channel conductance of about 25 picosiemens (PubMed:9326665, PubMed:9380751, PubMed:9407042). Also presents an inwardly rectifying current, thus reducing its already small outward conductance of potassium ions, which is particularly the case when the membrane potential displays positive values, above + 20 mV (PubMed:9326665, PubMed:9380751, PubMed:9407042). Controls calcium influx during vascular contractility by being responsible of membrane hyperpolarization induced by vasoactive factors in proliferative vascular smooth muscle cell types (By similarity). Following calcium influx, the consecutive activation of KCNN4 channel leads to a hyperpolarization of the cell membrane potential and hence an increase of the electrical driving force for further calcium influx promoting sustained calcium entry in response to stimulation with chemotactic peptides (PubMed:26418693). Required for maximal calcium influx and proliferation during the reactivation of naive T-cells (PubMed:17157250, PubMed:18796614). Plays a role in the late stages of EGF-induced macropinocytosis through activation by PI(3)P (PubMed:24591580). {ECO:0000250|UniProtKB:Q9QYW1, ECO:0000269|PubMed:10026195, ECO:0000269|PubMed:10961988, ECO:0000269|PubMed:11425865, ECO:0000269|PubMed:15831468, ECO:0000269|PubMed:17157250, ECO:0000269|PubMed:18796614, ECO:0000269|PubMed:24591580, ECO:0000269|PubMed:26148990, ECO:0000269|PubMed:26418693, ECO:0000269|PubMed:9326665, ECO:0000269|PubMed:9380751, ECO:0000269|PubMed:9407042}. |
| O60271 | SPAG9 | S705 | 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}. |
| O60506 | SYNCRIP | S159 | ochoa | Heterogeneous nuclear ribonucleoprotein Q (hnRNP Q) (Glycine- and tyrosine-rich RNA-binding protein) (GRY-RBP) (NS1-associated protein 1) (Synaptotagmin-binding, cytoplasmic RNA-interacting protein) | Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:11134005, ECO:0000269|PubMed:11352648, ECO:0000269|PubMed:11574476, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:23071094}. |
| O75052 | NOS1AP | S249 | ochoa | Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (C-terminal PDZ ligand of neuronal nitric oxide synthase protein) (Nitric oxide synthase 1 adaptor protein) | Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4 (By similarity). In kidney podocytes, plays a role in podosomes and filopodia formation through CDC42 activation (PubMed:33523862). {ECO:0000250|UniProtKB:O54960, ECO:0000269|PubMed:33523862}. |
| O75083 | WDR1 | S189 | ochoa | WD repeat-containing protein 1 (Actin-interacting protein 1) (AIP1) (NORI-1) | Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins (PubMed:15629458, PubMed:27557945, PubMed:29751004). Enhances cofilin-mediated actin severing (By similarity). Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions (PubMed:18494608). Involved in myocardium sarcomere organization. Required for cardiomyocyte growth and maintenance (By similarity). Involved in megakaryocyte maturation and platelet shedding. Required for the establishment of planar cell polarity (PCP) during follicular epithelium development and for cell shape changes during PCP; the function seems to implicate cooperation with CFL1 and/or DSTN/ADF. Involved in the generation/maintenance of cortical tension (By similarity). Involved in assembly and maintenance of epithelial apical cell junctions and plays a role in the organization of the perijunctional actomyosin belt (PubMed:25792565). {ECO:0000250|UniProtKB:O88342, ECO:0000250|UniProtKB:Q9W7F2, ECO:0000269|PubMed:15629458, ECO:0000269|PubMed:18494608, ECO:0000269|PubMed:25792565, ECO:0000269|PubMed:27557945, ECO:0000269|PubMed:29751004}. |
| O75955 | FLOT1 | S383 | ochoa | Flotillin-1 | May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. |
| O75970 | MPDZ | S1194 | ochoa | Multiple PDZ domain protein (Multi-PDZ domain protein 1) | Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses (PubMed:11150294, PubMed:15312654). Promotes clustering of HT2RC at the cell surface (By similarity). {ECO:0000250|UniProtKB:O55164, ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:15312654}. |
| O94808 | GFPT2 | S245 | ochoa | Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2 (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase 2) (Glutamine:fructose-6-phosphate amidotransferase 2) (GFAT 2) (GFAT2) (Hexosephosphate aminotransferase 2) | Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. |
| P07900 | HSP90AA1 | S623 | ochoa | Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Heat shock protein family C member 1) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38) | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812). {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:12526792, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123, ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155, ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.; FUNCTION: (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion. {ECO:0000305|PubMed:22066472}. |
| P08238 | HSP90AB1 | S615 | ochoa | 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}. |
| P09429 | HMGB1 | S35 | ochoa|psp | High mobility group protein B1 (High mobility group protein 1) (HMG-1) | Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability (PubMed:33147444). Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as a sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as a danger-associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury (PubMed:27362237). Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors (PubMed:34743181). In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance (PubMed:23446148, PubMed:23519706, PubMed:23994764, PubMed:25048472). Has proangiogdenic activity (By similarity). May be involved in platelet activation (By similarity). Binds to phosphatidylserine and phosphatidylethanolamide (By similarity). Bound to RAGE mediates signaling for neuronal outgrowth (By similarity). May play a role in accumulation of expanded polyglutamine (polyQ) proteins such as huntingtin (HTT) or TBP (PubMed:23303669, PubMed:25549101). {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P12682, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:23303669, ECO:0000269|PubMed:25549101, ECO:0000269|PubMed:27362237, ECO:0000269|PubMed:33147444, ECO:0000269|PubMed:34743181, ECO:0000305|PubMed:23446148, ECO:0000305|PubMed:23519706, ECO:0000305|PubMed:23994764, ECO:0000305|PubMed:25048472}.; FUNCTION: Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity (PubMed:20123072). May have an enhancing role in nucleotide excision repair (NER) (By similarity). However, effects in NER using in vitro systems have been reported conflictingly (PubMed:19360789, PubMed:19446504). May be involved in mismatch repair (MMR) and base excision repair (BER) pathways (PubMed:15014079, PubMed:16143102, PubMed:17803946). May be involved in double strand break repair such as non-homologous end joining (NHEJ) (By similarity). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS) (By similarity). In vitro can displace histone H1 from highly bent DNA (By similarity). Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding (By similarity). Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities (By similarity). Facilitates binding of TP53 to DNA (PubMed:23063560). Proposed to be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1; however, this function has been questioned (By similarity). Can modulate the activity of the telomerase complex and may be involved in telomere maintenance (By similarity). {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:15014079, ECO:0000269|PubMed:16143102, ECO:0000269|PubMed:17803946, ECO:0000269|PubMed:19446504, ECO:0000269|PubMed:23063560, ECO:0000305|PubMed:19360789, ECO:0000305|PubMed:20123072}.; FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2 complex via competitive interaction with BECN1 leading to autophagy activation (PubMed:20819940). Involved in oxidative stress-mediated autophagy (PubMed:21395369). Can protect BECN1 and ATG5 from calpain-mediated cleavage and thus proposed to control their proautophagic and proapoptotic functions and to regulate the extent and severity of inflammation-associated cellular injury (By similarity). In myeloid cells has a protective role against endotoxemia and bacterial infection by promoting autophagy (By similarity). Involved in endosomal translocation and activation of TLR9 in response to CpG-DNA in macrophages (By similarity). {ECO:0000250|UniProtKB:P63158, ECO:0000269|PubMed:20819940, ECO:0000269|PubMed:21395369}.; FUNCTION: In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury; the CXCL12:HMGB1 complex triggers CXCR4 homodimerization (PubMed:22370717). Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER/RAGE and ITGAM (By similarity). Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors (By similarity). Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER/RAGE (PubMed:24971542). Disulfide HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways. Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10 (PubMed:12765338, PubMed:18354232, PubMed:19264983, PubMed:20547845, PubMed:24474694). Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12 (PubMed:15607795). TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96/MD-2 (PubMed:20547845). In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes (PubMed:18354232, PubMed:21660935, PubMed:25660311). Contributes to tumor proliferation by association with ACER/RAGE (By similarity). Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex (PubMed:18250463). Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism (By similarity). Inhibits phagocytosis of apoptotic cells by macrophages; the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells (By similarity). In adaptive immunity may be involved in enhancing immunity through activation of effector T cells and suppression of regulatory T (TReg) cells (PubMed:15944249, PubMed:22473704). In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression (By similarity). Also reported to limit proliferation of T-cells (By similarity). Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production (PubMed:19064698). Involved in induction of immunological tolerance by apoptotic cells; its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106 (PubMed:18631454). During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes (By similarity). {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:12765338, ECO:0000269|PubMed:15607795, ECO:0000269|PubMed:15944249, ECO:0000269|PubMed:18250463, ECO:0000269|PubMed:18354232, ECO:0000269|PubMed:18631454, ECO:0000269|PubMed:19064698, ECO:0000269|PubMed:19264983, ECO:0000269|PubMed:20547845, ECO:0000269|PubMed:21660935, ECO:0000269|PubMed:22370717, ECO:0000269|PubMed:22473704, ECO:0000269|PubMed:24474694, ECO:0000269|PubMed:24971542, ECO:0000269|PubMed:25660311, ECO:0000269|Ref.8}.; FUNCTION: (Microbial infection) Critical for entry of human coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus NL63/HCoV-NL63 (PubMed:33147444). Regulates the expression of the pro-viral genes ACE2 and CTSL through chromatin modulation (PubMed:33147444). Required for SARS-CoV-2 ORF3A-induced reticulophagy which induces endoplasmic reticulum stress and inflammatory responses and facilitates viral infection (PubMed:35239449). {ECO:0000269|PubMed:33147444, ECO:0000269|PubMed:35239449}.; FUNCTION: (Microbial infection) Associates with the influenza A viral protein NP in the nucleus of infected cells, promoting viral growth and enhancing the activity of the viral polymerase. {ECO:0000269|PubMed:22696656}.; FUNCTION: (Microbial infection) Promotes Epstein-Barr virus (EBV) latent-to-lytic switch by sustaining the expression of the viral transcription factor BZLF1 that acts as a molecular switch to induce the transition from the latent to the lytic or productive phase of the virus cycle. Mechanistically, participates in EBV reactivation through the NLRP3 inflammasome. {ECO:0000269|PubMed:34922257}.; FUNCTION: (Microbial infection) Facilitates dengue virus propagation via interaction with the untranslated regions of viral genome. In turn, this interaction with viral RNA may regulate secondary structure of dengue RNA thus facilitating its recognition by the replication complex. {ECO:0000269|PubMed:34971702}. |
| P0DPH7 | TUBA3C | Y103 | ochoa | Tubulin alpha-3C chain (EC 3.6.5.-) (Alpha-tubulin 2) (Alpha-tubulin 3C) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-3C chain] | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
| P0DPH8 | TUBA3D | Y103 | ochoa | Tubulin alpha-3D chain (EC 3.6.5.-) (Alpha-tubulin 3D) [Cleaved into: Detyrosinated tubulin alpha-3D chain] | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
| P10636 | MAPT | S602 | ochoa | Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau) | Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. {ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:32961270}. |
| P11055 | MYH3 | S181 | ochoa | Myosin-3 (Muscle embryonic myosin heavy chain) (Myosin heavy chain 3) (Myosin heavy chain, fast skeletal muscle, embryonic) (SMHCE) | Muscle contraction. |
| P12814 | ACTN1 | S763 | 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}. |
| P12882 | MYH1 | S181 | 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 | S180 | 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}. |
| P12931 | SRC | S97 | psp | Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src) | Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors (PubMed:34234773). Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (PubMed:21411625). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Phosphorylates PKP3 at 'Tyr-195' in response to reactive oxygen species, which may cause the release of PKP3 from desmosome cell junctions into the cytoplasm (PubMed:25501895). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1 (PubMed:11389730). Plays a role in EGF-mediated calcium-activated chloride channel activation (PubMed:18586953). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (PubMed:7853507). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14585963, PubMed:8755529). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750). Enhances RIGI-elicited antiviral signaling (PubMed:19419966). Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates BCAR1 at 'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity (PubMed:20525694). Phosphorylates synaptic vesicle protein synaptophysin (SYP) (By similarity). Involved in anchorage-independent cell growth (PubMed:19307596). Required for podosome formation (By similarity). Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration (PubMed:25731159). Phosphorylates OTUB1, promoting deubiquitination of RPTOR (PubMed:35927303). Phosphorylates caspase CASP8 at 'Tyr-380' which negatively regulates CASP8 processing and activation, down-regulating CASP8 proapoptotic function (PubMed:16619028). {ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:Q9WUD9, ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:16619028, ECO:0000269|PubMed:18586953, ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:21309750, ECO:0000269|PubMed:21411625, ECO:0000269|PubMed:22710723, ECO:0000269|PubMed:25501895, ECO:0000269|PubMed:25731159, ECO:0000269|PubMed:34234773, ECO:0000269|PubMed:35927303, ECO:0000269|PubMed:7853507, ECO:0000269|PubMed:8755529, ECO:0000269|PubMed:8759729, ECO:0000305|PubMed:11964124, ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}.; FUNCTION: [Isoform 1]: Non-receptor protein tyrosine kinase which phosphorylates synaptophysin with high affinity. {ECO:0000250|UniProtKB:Q9WUD9}.; FUNCTION: [Isoform 2]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in L1CAM-mediated neurite elongation, possibly by acting downstream of L1CAM to drive cytoskeletal rearrangements involved in neurite outgrowth (By similarity). {ECO:0000250|UniProtKB:Q9WUD9}.; FUNCTION: [Isoform 3]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in neurite elongation (By similarity). {ECO:0000250|UniProtKB:Q9WUD9}. |
| P13533 | MYH6 | S180 | ochoa | Myosin-6 (Myosin heavy chain 6) (Myosin heavy chain, cardiac muscle alpha isoform) (MyHC-alpha) | Muscle contraction. |
| P13535 | MYH8 | S183 | ochoa | Myosin-8 (Myosin heavy chain 8) (Myosin heavy chain, skeletal muscle, perinatal) (MyHC-perinatal) | Muscle contraction. |
| P16070 | CD44 | S686 | ochoa | CD44 antigen (CDw44) (Epican) (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Heparan sulfate proteoglycan) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44) | Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment (PubMed:16541107, PubMed:19703720, PubMed:22726066). Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection (PubMed:7528188). Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases (PubMed:18757307, PubMed:23589287). Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion (PubMed:15123640). {ECO:0000269|PubMed:15123640, ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:18757307, ECO:0000269|PubMed:19703720, ECO:0000269|PubMed:22726066, ECO:0000269|PubMed:23589287, ECO:0000269|PubMed:7528188}. |
| P20073 | ANXA7 | S437 | ochoa | Annexin A7 (Annexin VII) (Annexin-7) (Synexin) | Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. |
| P21796 | VDAC1 | T165 | ochoa | Non-selective voltage-gated ion channel VDAC1 (Outer mitochondrial membrane protein porin 1) (Plasmalemmal porin) (Porin 31HL) (Porin 31HM) (Voltage-dependent anion-selective channel protein 1) (VDAC-1) (hVDAC1) | Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:30061676, PubMed:8420959). The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:8420959). It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (PubMed:10661876, PubMed:18755977, PubMed:8420959). The open state has a weak anion selectivity whereas the closed state is cation-selective (PubMed:18755977, PubMed:8420959). Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:18755977, PubMed:31015432). In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:32047033). May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis (PubMed:15033708, PubMed:25296756). May mediate ATP export from cells (PubMed:30061676). Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity). Mediates cytochrome c efflux (PubMed:20230784). {ECO:0000250|UniProtKB:Q60932, ECO:0000269|PubMed:10661876, ECO:0000269|PubMed:11845315, ECO:0000269|PubMed:15033708, ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:20230784, ECO:0000269|PubMed:25296756, ECO:0000269|PubMed:30061676, ECO:0000269|PubMed:31015432, ECO:0000269|PubMed:32047033, ECO:0000269|PubMed:8420959}.; FUNCTION: Catalyzes the scrambling of phospholipids across the outer mitochondrial membrane; the mechanism is unrelated to channel activity and is capable of translocating both anionic and zwitterionic phospholipids. {ECO:0000269|PubMed:38065946}. |
| P22626 | HNRNPA2B1 | S85 | ochoa | Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1) | Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Also plays a role in the activation of the innate immune response (PubMed:31320558). Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10567417, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24356509, ECO:0000269|PubMed:26321680, ECO:0000303|PubMed:19099192}.; FUNCTION: (Microbial infection) Involved in the transport of HIV-1 genomic RNA out of the nucleus, to the microtubule organizing center (MTOC), and then from the MTOC to the cytoplasm: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) sequence motifs present on HIV-1 genomic RNA, and promotes its transport. {ECO:0000269|PubMed:15294897, ECO:0000269|PubMed:17004321}. |
| P25189 | MPZ | S226 | ochoa | Myelin protein P0 (Myelin peripheral protein) (MPP) (Myelin protein zero) | Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction. {ECO:0000269|PubMed:10545037, ECO:0000269|PubMed:18337304}. |
| P26583 | HMGB2 | S35 | ochoa | High mobility group protein B2 (High mobility group protein 2) (HMG-2) | Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity (PubMed:11909973, PubMed:18413230, PubMed:19522541, PubMed:19965638, PubMed:20123072, PubMed:7797075). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS) (By similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors (By similarity). In the extracellular compartment acts as a chemokine. Promotes proliferation and migration of endothelial cells implicating AGER/RAGE (PubMed:19811285). Has antimicrobial activity in gastrointestinal epithelial tissues (PubMed:23877675). Involved in inflammatory response to antigenic stimulus coupled with pro-inflammatory activity (By similarity). Involved in modulation of neurogenesis probably by regulation of neural stem proliferation (By similarity). Involved in articular cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin pathway (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P30681, ECO:0000269|PubMed:11909973, ECO:0000269|PubMed:18413230, ECO:0000269|PubMed:19522541, ECO:0000269|PubMed:19811285, ECO:0000269|PubMed:19965638, ECO:0000269|PubMed:23877675, ECO:0000269|PubMed:7797075, ECO:0000305|PubMed:20123072}. |
| P26639 | TARS1 | S534 | ochoa | Threonine--tRNA ligase 1, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase 1) | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (PubMed:25824639, PubMed:31374204). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage (By similarity). {ECO:0000250|UniProtKB:Q9D0R2, ECO:0000269|PubMed:25824639, ECO:0000269|PubMed:31374204}. |
| P28715 | ERCC5 | S428 | ochoa | DNA excision repair protein ERCC-5 (EC 3.1.-.-) (DNA repair protein complementing XP-G cells) (XPG) (Xeroderma pigmentosum group G-complementing protein) | Single-stranded structure-specific DNA endonuclease involved in DNA excision repair (PubMed:32522879, PubMed:32821917, PubMed:7651464, PubMed:8078765, PubMed:8090225, PubMed:8206890). Makes the 3'incision in DNA nucleotide excision repair (NER) (PubMed:32522879, PubMed:32821917, PubMed:8078765, PubMed:8090225). Binds and bends DNA repair bubble substrate and breaks base stacking at the single-strand/double-strand DNA junction of the DNA bubble (PubMed:32522879). Plays a role in base excision repair (BER) by promoting the binding of DNA glycosylase NTHL1 to its substrate and increasing NTHL1 catalytic activity that removes oxidized pyrimidines from DNA (PubMed:9927729). Involved in transcription-coupled nucleotide excision repair (TCR) which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (PubMed:16246722). Functions during the initial step of TCR in cooperation with ERCC6/CSB to recognized stalled RNA polymerase II (PubMed:16246722). Also, stimulates ERCC6/CSB binding to the DNA repair bubble and ERCC6/CSB ATPase activity (PubMed:16246722). Required for DNA replication fork maintenance and preservation of genomic stability (PubMed:26833090, PubMed:32522879). Involved in homologous recombination repair (HRR) induced by DNA replication stress by recruiting RAD51, BRCA2, and PALB2 to the damaged DNA site (PubMed:26833090). In TFIIH stimulates the 5'-3' helicase activity of XPD/ERCC2 and the DNA translocase activity of XPB/ERCC3 (PubMed:31253769). During HRR, binds to the replication fork with high specificity and stabilizes it (PubMed:32522879). Also, acts upstream of HRR, to promote the release of BRCA1 from DNA (PubMed:26833090). {ECO:0000269|PubMed:16246722, ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:31253769, ECO:0000269|PubMed:32522879, ECO:0000269|PubMed:32821917, ECO:0000269|PubMed:7651464, ECO:0000269|PubMed:8078765, ECO:0000269|PubMed:8090225, ECO:0000269|PubMed:8206890, ECO:0000269|PubMed:9927729}. |
| P30530 | AXL | S635 | ochoa | Tyrosine-protein kinase receptor UFO (EC 2.7.10.1) (AXL oncogene) | Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, AXL binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response. {ECO:0000269|PubMed:10403904, ECO:0000269|PubMed:11484958, ECO:0000269|PubMed:12364394, ECO:0000269|PubMed:12490074, ECO:0000269|PubMed:15507525, ECO:0000269|PubMed:15733062, ECO:0000269|PubMed:1656220, ECO:0000269|PubMed:18840707}.; FUNCTION: (Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope. {ECO:0000269|PubMed:17005688, ECO:0000269|PubMed:21501828, ECO:0000269|PubMed:22156524, ECO:0000269|PubMed:25277499}.; FUNCTION: (Microbial infection) Acts as a receptor for Ebolavirus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope. {ECO:0000269|PubMed:22673088}.; FUNCTION: (Microbial infection) Promotes Zika virus entry in glial cells, Sertoli cells and astrocytes (PubMed:28076778, PubMed:29379210, PubMed:31311882). Additionally, Zika virus potentiates AXL kinase activity to antagonize type I interferon signaling and thereby promotes infection (PubMed:28076778). Interferon signaling inhibition occurs via an SOCS1-dependent mechanism (PubMed:29379210). {ECO:0000269|PubMed:28076778, ECO:0000269|PubMed:29379210, ECO:0000269|PubMed:31311882}. |
| P39748 | FEN1 | S331 | ochoa | Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (DNase IV) (Flap structure-specific endonuclease 1) (Maturation factor 1) (MF1) (hFEN-1) | Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA. {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:10744741, ECO:0000269|PubMed:11986308, ECO:0000269|PubMed:18443037, ECO:0000269|PubMed:20729856, ECO:0000269|PubMed:26751069, ECO:0000269|PubMed:7961795, ECO:0000269|PubMed:8621570}. |
| P49790 | NUP153 | S709 | ochoa | Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153) | 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. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269|PubMed:23523133, ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:31913756}. |
| P50991 | CCT4 | S234 | ochoa | T-complex protein 1 subunit delta (TCP-1-delta) (EC 3.6.1.-) (CCT-delta) (Chaperonin containing T-complex polypeptide 1 subunit 4) (Stimulator of TAR RNA-binding) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
| P52272 | HNRNPM | S136 | ochoa | Heterogeneous nuclear ribonucleoprotein M (hnRNP M) | Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines. |
| P53621 | COPA | S402 | ochoa | Coatomer subunit alpha (Alpha-coat protein) (Alpha-COP) (HEP-COP) (HEPCOP) [Cleaved into: Xenin (Xenopsin-related peptide); Proxenin] | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; FUNCTION: Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor. |
| P54296 | MYOM2 | S627 | ochoa | Myomesin-2 (165 kDa connectin-associated protein) (165 kDa titin-associated protein) (M-protein) (Myomesin family member 2) | Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent. |
| P54578 | USP14 | S229 | ochoa | Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) (Deubiquitinating enzyme 14) (Ubiquitin thioesterase 14) (Ubiquitin-specific-processing protease 14) | Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins (PubMed:35145029). Ensures the regeneration of ubiquitin at the proteasome (PubMed:18162577, PubMed:28396413). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell (PubMed:18162577). Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (PubMed:19106094). Also serves as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1 (PubMed:19135427). Indispensable for synaptic development and function at neuromuscular junctions (NMJs) (By similarity). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation (PubMed:27666593). Inhibits OPTN-mediated selective autophagic degradation of KDM4D and thereby negatively regulates H3K9me2 and H3K9me3 (PubMed:35145029). {ECO:0000250|UniProtKB:Q9JMA1, ECO:0000269|PubMed:18162577, ECO:0000269|PubMed:19106094, ECO:0000269|PubMed:19135427, ECO:0000269|PubMed:27666593, ECO:0000269|PubMed:28396413, ECO:0000269|PubMed:35145029}. |
| P62913 | RPL11 | S29 | ochoa | Large ribosomal subunit protein uL5 (60S ribosomal protein L11) (CLL-associated antigen KW-12) | Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:19191325, PubMed:32669547). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (PubMed:19191325, PubMed:32669547). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (PubMed:19191325, PubMed:32669547). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:19191325, PubMed:32669547). As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs (PubMed:12962325, PubMed:19061985, PubMed:24120868). It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53 (PubMed:24120868). Promotes nucleolar location of PML (By similarity). {ECO:0000250|UniProtKB:Q9CXW4, ECO:0000269|PubMed:12962325, ECO:0000269|PubMed:19061985, ECO:0000269|PubMed:19191325, ECO:0000269|PubMed:24120868, ECO:0000269|PubMed:32669547}. |
| P68363 | TUBA1B | Y103 | ochoa | Tubulin alpha-1B chain (EC 3.6.5.-) (Alpha-tubulin ubiquitous) (Tubulin K-alpha-1) (Tubulin alpha-ubiquitous chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain] | Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (PubMed:38305685, PubMed:34996871, PubMed:38609661). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:38305685, PubMed:34996871, PubMed:38609661). Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:34996871, PubMed:38609661). {ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:38305685, ECO:0000269|PubMed:38609661}. |
| P68366 | TUBA4A | Y103 | ochoa | Tubulin alpha-4A chain (EC 3.6.5.-) (Alpha-tubulin 1) (Testis-specific alpha-tubulin) (Tubulin H2-alpha) (Tubulin alpha-1 chain) | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
| Q01813 | PFKP | S386 | ochoa|psp | ATP-dependent 6-phosphofructokinase, platelet type (ATP-PFK) (PFK-P) (EC 2.7.1.11) (6-phosphofructokinase type C) (Phosphofructo-1-kinase isozyme C) (PFK-C) (Phosphohexokinase) | Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. |
| Q02543 | RPL18A | S86 | ochoa | Large ribosomal subunit protein eL20 (60S ribosomal protein L18a) | Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}. |
| Q09666 | AHNAK | S5651 | ochoa | Neuroblast differentiation-associated protein AHNAK (Desmoyokin) | May be required for neuronal cell differentiation. |
| Q0IIM8 | TBC1D8B | S949 | ochoa | TBC1 domain family member 8B | Involved in vesicular recycling, probably as a RAB11B GTPase-activating protein. {ECO:0000269|PubMed:30661770}. |
| Q12923 | PTPN13 | S897 | ochoa | Tyrosine-protein phosphatase non-receptor type 13 (EC 3.1.3.48) (Fas-associated protein-tyrosine phosphatase 1) (FAP-1) (PTP-BAS) (Protein-tyrosine phosphatase 1E) (PTP-E1) (hPTPE1) (Protein-tyrosine phosphatase PTPL1) | Tyrosine phosphatase which negatively regulates FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling (PubMed:15611135). May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2 (PubMed:23604317). {ECO:0000269|PubMed:15611135, ECO:0000269|PubMed:23604317}. |
| Q13433 | SLC39A6 | S220 | ochoa | Zinc transporter ZIP6 (Estrogen-regulated protein LIV-1) (Solute carrier family 39 member 6) (Zrt- and Irt-like protein 6) (ZIP-6) | Zinc-influx transporter which plays a role in zinc homeostasis and in the induction of epithelial-to-mesenchymal transition (EMT) (PubMed:12839489, PubMed:18272141, PubMed:21422171, PubMed:23919497, PubMed:27274087, PubMed:34394081). When associated with SLC39A10, the heterodimer formed by SLC39A10 and SLC39A6 mediates cellular zinc uptake to trigger cells to undergo epithelial- to-mesenchymal transition (EMT) (PubMed:27274087). The SLC39A10-SLC39A6 heterodimer also controls NCAM1 phosphorylation and its integration into focal adhesion complexes during EMT (By similarity). Zinc influx inactivates GSK3B, enabling unphosphorylated SNAI1 in the nucleus to down-regulate adherence genes such as CDH1, causing loss of cell adherence (PubMed:23919497). In addition, the SLC39A10-SLC39A6 heterodimer plays an essentiel role in initiating mitosis by importing zinc into cells to initiate a pathway resulting in the onset of mitosis (PubMed:32797246). Participates in the T-cell receptor signaling regulation by mediating cellular zinc uptake into activated lymphocytes (PubMed:21422171, PubMed:30552163, PubMed:34394081). Regulates the zinc influx necessary for proper meiotic progression to metaphase II (MII) that allows the oocyte-to-egg transition (PubMed:25143461). {ECO:0000250|UniProtKB:Q8C145, ECO:0000269|PubMed:12839489, ECO:0000269|PubMed:18272141, ECO:0000269|PubMed:21422171, ECO:0000269|PubMed:23919497, ECO:0000269|PubMed:25143461, ECO:0000269|PubMed:27274087, ECO:0000269|PubMed:30552163, ECO:0000269|PubMed:32797246, ECO:0000269|PubMed:34394081}. |
| Q14980 | NUMA1 | S1721 | 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}. |
| Q15185 | PTGES3 | S39 | ochoa | Prostaglandin E synthase 3 (EC 5.3.99.3) (Cytosolic prostaglandin E2 synthase) (cPGES) (Hsp90 co-chaperone) (Progesterone receptor complex p23) (Telomerase-binding protein p23) | Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) (PubMed:10922363). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes (PubMed:11274138, PubMed:12077419). Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (PubMed:24711448). {ECO:0000269|PubMed:10922363, ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:12077419, ECO:0000269|PubMed:24711448}. |
| Q15365 | PCBP1 | S323 | ochoa | Poly(rC)-binding protein 1 (Alpha-CP1) (Heterogeneous nuclear ribonucleoprotein E1) (hnRNP E1) (Nucleic acid-binding protein SUB2.3) | Single-stranded nucleic acid binding protein that binds preferentially to oligo dC (PubMed:15731341, PubMed:7556077, PubMed:7607214, PubMed:8152927). Together with PCBP2, required for erythropoiesis, possibly by regulating mRNA splicing (By similarity). {ECO:0000250|UniProtKB:P60335, ECO:0000269|PubMed:15731341, ECO:0000269|PubMed:7556077, ECO:0000269|PubMed:7607214, ECO:0000269|PubMed:8152927}.; FUNCTION: (Microbial infection) In case of infection by poliovirus, plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. {ECO:0000269|PubMed:12414943}. |
| Q16143 | SNCB | S64 | ochoa | Beta-synuclein | Non-amyloid component of senile plaques found in Alzheimer disease. Could act as a regulator of SNCA aggregation process. Protects neurons from staurosporine and 6-hydroxy dopamine (6OHDA)-stimulated caspase activation in a p53/TP53-dependent manner. Contributes to restore the SNCA anti-apoptotic function abolished by 6OHDA. Not found in the Lewy bodies associated with Parkinson disease. |
| Q58FF7 | HSP90AB3P | S488 | ochoa | Putative heat shock protein HSP 90-beta-3 (Heat shock protein 90-beta c) (Heat shock protein 90Bc) | Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}. |
| Q5S007 | LRRK2 | T1503 | psp | Leucine-rich repeat serine/threonine-protein kinase 2 (EC 2.7.11.1) (EC 3.6.5.-) (Dardarin) | Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, innate immunity, autophagy, and vesicle trafficking (PubMed:17114044, PubMed:20949042, PubMed:21850687, PubMed:22012985, PubMed:23395371, PubMed:24687852, PubMed:25201882, PubMed:26014385, PubMed:26824392, PubMed:27830463, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421). Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation (PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421). Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB29, RAB35, and RAB43 (PubMed:23395371, PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421, PubMed:38127736). Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A (PubMed:26824392). Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A (PubMed:26824392). Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain (PubMed:29125462, PubMed:30398148). Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose-6-phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:23395371). Regulates neuronal process morphology in the intact central nervous system (CNS) (PubMed:17114044). Plays a role in synaptic vesicle trafficking (PubMed:24687852). Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization (PubMed:25201882). Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway (PubMed:22012985). The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes (PubMed:22012985). Phosphorylates PRDX3 (PubMed:21850687). By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis (PubMed:28720718). Acts as a positive regulator of innate immunity by mediating phosphorylation of RIPK2 downstream of NOD1 and NOD2, thereby enhancing RIPK2 activation (PubMed:27830463). Independent of its kinase activity, inhibits the proteasomal degradation of MAPT, thus promoting MAPT oligomerization and secretion (PubMed:26014385). In addition, has GTPase activity via its Roc domain which regulates LRRK2 kinase activity (PubMed:18230735, PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29212815). Recruited by RAB29/RAB7L1 to overloaded lysosomes where it phosphorylates and stabilizes RAB8A and RAB10 which promote lysosomal content release and suppress lysosomal enlargement through the EHBP1 and EHBP1L1 effector proteins (PubMed:30209220, PubMed:38227290). {ECO:0000269|PubMed:17114044, ECO:0000269|PubMed:18230735, ECO:0000269|PubMed:20949042, ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:22012985, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24687852, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:26014385, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:27830463, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:30635421, ECO:0000269|PubMed:38127736, ECO:0000269|PubMed:38227290}. |
| Q5T5X7 | BEND3 | S68 | ochoa | BEN domain-containing protein 3 | Transcriptional repressor which associates with the NoRC (nucleolar remodeling complex) complex and plays a key role in repressing rDNA transcription. The sumoylated form modulates the stability of the NoRC complex component BAZ2A/TIP5 by controlling its USP21-mediated deubiquitination (PubMed:21914818, PubMed:26100909). Binds to unmethylated major satellite DNA and is involved in the recruitment of the Polycomb repressive complex 2 (PRC2) to major satellites (By similarity). Stimulates the ERCC6L translocase and ATPase activities (PubMed:28977671). {ECO:0000250|UniProtKB:Q6PAL0, ECO:0000269|PubMed:21914818, ECO:0000269|PubMed:26100909, ECO:0000269|PubMed:28977671}. |
| Q6IQ49 | SDE2 | S373 | ochoa | Splicing regulator SDE2 (Replication stress response regulator SDE2) | Inhibits translesion DNA synthesis by preventing monoubiquitination of PCNA, this is necessary to counteract damage due to ultraviolet light-induced replication stress (PubMed:27906959). SDE2 is cleaved following PCNA binding, and its complete degradation is necessary to allow S-phase progression following DNA damage (PubMed:27906959). {ECO:0000269|PubMed:27906959}.; FUNCTION: Plays a role in pre-mRNA splicing by facilitating excision of relatively short introns featuring weak 3'-splice sites (ss) and high GC content (PubMed:34365507). May recruit CACTIN to the spliceosome (By similarity). {ECO:0000250|UniProtKB:O14113, ECO:0000269|PubMed:34365507}.; FUNCTION: Plays a role in ribosome biogenesis by enabling SNORD3- and SNORD118-dependent cleavage of the 47S rRNA precursor (PubMed:34365507). Binds ncRNA (non-coding RNA) including the snoRNAs SNORD3 and SNORD118 (PubMed:34365507). {ECO:0000269|PubMed:34365507}. |
| Q6R327 | RICTOR | S1581 | ochoa | Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3) | Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, 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:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). 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:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts 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). {ECO:0000250|UniProtKB:Q6QI06, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:19720745, ECO:0000269|PubMed:19935711, ECO:0000269|PubMed:19995915, ECO:0000269|PubMed:21343617, ECO:0000269|PubMed:33158864, ECO:0000269|PubMed:35904232, ECO:0000269|PubMed:35926713}. |
| Q71U36 | TUBA1A | Y103 | ochoa | Tubulin alpha-1A chain (EC 3.6.5.-) (Alpha-tubulin 3) (Tubulin B-alpha-1) (Tubulin alpha-3 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain] | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
| Q7Z6I8 | C5orf24 | S40 | ochoa | UPF0461 protein C5orf24 | None |
| Q7Z739 | YTHDF3 | S186 | ochoa | YTH domain-containing family protein 3 (DF3) | Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates their stability (PubMed:28106072, PubMed:28106076, PubMed:28281539, PubMed:32492408). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (PubMed:22575960, PubMed:24284625, PubMed:28106072, PubMed:28281539, PubMed:32492408). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex or PAN3 (PubMed:32492408). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (PubMed:28106072, PubMed:28106076, PubMed:32492408). Acts as a negative regulator of type I interferon response by down-regulating interferon-stimulated genes (ISGs) expression: acts by binding to FOXO3 mRNAs (By similarity). Binds to FOXO3 mRNAs independently of METTL3-mediated m6A modification (By similarity). Can also act as a regulator of mRNA stability in cooperation with YTHDF2 by binding to m6A-containing mRNA and promoting their degradation (PubMed:28106072). Recognizes and binds m6A-containing circular RNAs (circRNAs); circRNAs are generated through back-splicing of pre-mRNAs, a non-canonical splicing process promoted by dsRNA structures across circularizing exons (PubMed:28281539). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (PubMed:31292544, PubMed:31388144, PubMed:32451507). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (PubMed:31292544). May also recognize and bind N1-methyladenosine (m1A)-containing mRNAs: inhibits trophoblast invasion by binding to m1A-methylated transcripts of IGF1R, promoting their degradation (PubMed:32194978). {ECO:0000250|UniProtKB:Q8BYK6, ECO:0000269|PubMed:22575960, ECO:0000269|PubMed:24284625, ECO:0000269|PubMed:28106072, ECO:0000269|PubMed:28106076, ECO:0000269|PubMed:28281539, ECO:0000269|PubMed:31292544, ECO:0000269|PubMed:31388144, ECO:0000269|PubMed:32194978, ECO:0000269|PubMed:32451507, ECO:0000269|PubMed:32492408}.; FUNCTION: Has some antiviral activity against HIV-1 virus: incorporated into HIV-1 particles in a nucleocapsid-dependent manner and reduces viral infectivity in the next cycle of infection (PubMed:32053707). May interfere with this early step of the viral life cycle by binding to N6-methyladenosine (m6A) modified sites on the HIV-1 RNA genome (PubMed:32053707). {ECO:0000269|PubMed:32053707}. |
| Q86UX7 | FERMT3 | S60 | ochoa | Fermitin family homolog 3 (Kindlin-3) (MIG2-like protein) (Unc-112-related protein 2) | Plays a central role in cell adhesion in hematopoietic cells (PubMed:19234463, PubMed:26359933). Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3) (By similarity). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells (PubMed:19234460). Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By similarity). {ECO:0000250|UniProtKB:Q8K1B8, ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463, ECO:0000269|PubMed:26359933}.; FUNCTION: Isoform 2 may act as a repressor of NF-kappa-B and apoptosis. {ECO:0000269|PubMed:19064721, ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463}. |
| Q8IVF2 | AHNAK2 | S447 | ochoa | Protein AHNAK2 | None |
| Q8IXM2 | BACC1 | S36 | ochoa | BPTF-associated chromatin complex component 1 (BPTF-associated protein of 18 kDa) (Chromatin complexes subunit BAP18) | Component of chromatin complexes such as the MLL1/MLL and NURF complexes. |
| Q8IYT2 | CMTR2 | S423 | ochoa | Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296) (Cap methyltransferase 2) (Cap2 2'O-ribose methyltransferase 2) (HMTr2) (MTr2) (FtsJ methyltransferase domain-containing protein 1) (Protein adrift homolog) | S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N(7) methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs. {ECO:0000269|PubMed:21310715}. |
| Q8IZD0 | SAMD14 | S373 | ochoa | Sterile alpha motif domain-containing protein 14 (SAM domain-containing protein 14) | None |
| Q8N1S5 | SLC39A11 | S153 | ochoa | Zinc transporter ZIP11 (Solute carrier family 39 member 11) (Zrt- and Irt-like protein 11) (ZIP-11) | Zinc importer that regulates cytosolic zinc concentrations either via zinc influx from the extracellular compartment or efflux from intracellular organelles such as Golgi apparatus. May transport copper ions as well. The transport mechanism remains to be elucidated. {ECO:0000250|UniProtKB:Q8BWY7}. |
| Q8NFT8 | DNER | S696 | ochoa | Delta and Notch-like epidermal growth factor-related receptor | Activator of the NOTCH1 pathway. May mediate neuron-glia interaction during astrocytogenesis (By similarity). {ECO:0000250}. |
| Q8TEU7 | RAPGEF6 | S701 | ochoa | Rap guanine nucleotide exchange factor 6 (PDZ domain-containing guanine nucleotide exchange factor 2) (PDZ-GEF2) (RA-GEF-2) | Guanine nucleotide exchange factor (GEF) for Rap1A, Rap2A and M-Ras GTPases. Does not interact with cAMP. {ECO:0000269|PubMed:11524421, ECO:0000269|PubMed:12581858}. |
| Q8TEV9 | SMCR8 | S643 | 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}. |
| Q8WWI1 | LMO7 | Y185 | ochoa | LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP) | None |
| Q92569 | PIK3R3 | Y184 | ochoa | Phosphatidylinositol 3-kinase regulatory subunit gamma (PI3-kinase regulatory subunit gamma) (PI3K regulatory subunit gamma) (PtdIns-3-kinase regulatory subunit gamma) (Phosphatidylinositol 3-kinase 55 kDa regulatory subunit gamma) (PI3-kinase subunit p55-gamma) (PtdIns-3-kinase regulatory subunit p55-gamma) (p55PIK) | Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1. |
| Q92630 | DYRK2 | S449 | psp | Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC 2.7.12.1) | Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser-641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX and DPYSL2. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro). {ECO:0000269|PubMed:11311121, ECO:0000269|PubMed:12588975, ECO:0000269|PubMed:14593110, ECO:0000269|PubMed:15910284, ECO:0000269|PubMed:16511445, ECO:0000269|PubMed:16611631, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:18455992, ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19287380, ECO:0000269|PubMed:22307329, ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:23362280, ECO:0000269|PubMed:9748265}. |
| Q96D71 | REPS1 | S736 | ochoa | RalBP1-associated Eps domain-containing protein 1 (RalBP1-interacting protein 1) | May coordinate the cellular actions of activated EGF receptors and Ral-GTPases. {ECO:0000250}. |
| Q96EH3 | MALSU1 | S82 | ochoa | Mitochondrial assembly of ribosomal large subunit protein 1 | Required for normal mitochondrial ribosome function and mitochondrial translation (PubMed:22238375, PubMed:23171548). May play a role in ribosome biogenesis by preventing premature association of the 28S and 39S ribosomal subunits (Probable). Interacts with mitochondrial ribosomal protein uL14m (MRPL14), probably blocking formation of intersubunit bridge B8, preventing association of the 28S and 39S ribosomal subunits (Probable). Addition to isolated mitochondrial ribosomal subunits partially inhibits translation, probably by interfering with the association of the 28S and 39S ribosomal subunits and the formation of functional ribosomes (Probable). May also participate in the assembly and/or regulation of the stability of the large subunit of the mitochondrial ribosome (PubMed:22238376, PubMed:23171548). May function as a ribosomal silencing factor (Probable). {ECO:0000269|PubMed:22238375, ECO:0000269|PubMed:22238376, ECO:0000269|PubMed:23171548, ECO:0000305|PubMed:22829778, ECO:0000305|PubMed:28892042}. |
| Q96GE4 | CEP95 | S243 | ochoa | Centrosomal protein of 95 kDa (Cep95) (Coiled-coil domain-containing protein 45) | None |
| Q96QE3 | ATAD5 | S311 | ochoa | ATPase family AAA domain-containing protein 5 (Chromosome fragility-associated gene 1 protein) | Has an important role in DNA replication and in maintaining genome integrity during replication stress (PubMed:15983387, PubMed:19755857). Involved in a RAD9A-related damage checkpoint, a pathway that is important in determining whether DNA damage is compatible with cell survival or whether it requires cell elimination by apoptosis (PubMed:15983387). Modulates the RAD9A interaction with BCL2 and thereby induces DNA damage-induced apoptosis (PubMed:15983387). Promotes PCNA deubiquitination by recruiting the ubiquitin-specific protease 1 (USP1) and WDR48 thereby down-regulating the error-prone damage bypass pathway (PubMed:20147293). As component of the ATAD5 RFC-like complex, regulates the function of the DNA polymerase processivity factor PCNA by unloading the ring-shaped PCNA homotrimer from DNA after replication during the S phase of the cell cycle (PubMed:23277426, PubMed:23937667). This seems to be dependent on its ATPase activity (PubMed:23277426). Plays important roles in restarting stalled replication forks under replication stress, by unloading the PCNA homotrimer from DNA and recruiting RAD51 possibly through an ATR-dependent manner (PubMed:31844045). Ultimately this enables replication fork regression, breakage, and eventual fork restart (PubMed:31844045). Both the PCNA unloading activity and the interaction with WDR48 are required to efficiently recruit RAD51 to stalled replication forks (PubMed:31844045). Promotes the generation of MUS81-mediated single-stranded DNA-associated breaks in response to replication stress, which is an alternative pathway to restart stalled/regressed replication forks (PubMed:31844045). {ECO:0000269|PubMed:15983387, ECO:0000269|PubMed:19755857, ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:23277426, ECO:0000269|PubMed:23937667, ECO:0000269|PubMed:31844045}. |
| Q9BQE3 | TUBA1C | Y103 | ochoa | Tubulin alpha-1C chain (EC 3.6.5.-) (Alpha-tubulin 6) (Tubulin alpha-6 chain) [Cleaved into: Detyrosinated tubulin alpha-1C chain] | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
| Q9BT25 | HAUS8 | S105 | ochoa | HAUS augmin-like complex subunit 8 (HEC1/NDC80-interacting centrosome-associated protein 1) (Sarcoma antigen NY-SAR-48) | Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:18362163, ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}. |
| Q9BYF1 | ACE2 | S680 | psp | Angiotensin-converting enzyme 2 (EC 3.4.17.23) (Angiotensin-converting enzyme homolog) (ACEH) (Angiotensin-converting enzyme-related carboxypeptidase) (ACE-related carboxypeptidase) (EC 3.4.17.-) (Metalloprotease MPROT15) [Cleaved into: Processed angiotensin-converting enzyme 2] | Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis (PubMed:27217402). Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II (PubMed:10924499, PubMed:10969042, PubMed:11815627, PubMed:14504186, PubMed:19021774). Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin (PubMed:10969042, PubMed:11815627). Also cleaves other biological peptides, such as apelins (apelin-13, [Pyr1]apelin-13, apelin-17, apelin-36), casomorphins (beta-casomorphin-7, neocasomorphin) and dynorphin A with high efficiency (PubMed:11815627, PubMed:27217402, PubMed:28293165). In addition, ACE2 C-terminus is homologous to collectrin and is responsible for the trafficking of the neutral amino acid transporter SL6A19 to the plasma membrane of gut epithelial cells via direct interaction, regulating its expression on the cell surface and its catalytic activity (PubMed:18424768, PubMed:19185582). {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:11815627, ECO:0000269|PubMed:14504186, ECO:0000269|PubMed:18424768, ECO:0000269|PubMed:19021774, ECO:0000269|PubMed:19185582, ECO:0000269|PubMed:27217402}.; FUNCTION: (Microbial infection) Acts as a receptor for human coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus NL63/HCoV-NL63. {ECO:0000269|PubMed:14647384, ECO:0000269|PubMed:15452268, ECO:0000269|PubMed:15791205, ECO:0000269|PubMed:15897467, ECO:0000269|PubMed:19901337, ECO:0000269|PubMed:24227843, ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32221306, ECO:0000269|PubMed:32225175, ECO:0000269|PubMed:33000221, ECO:0000269|PubMed:33082294, ECO:0000269|PubMed:33432067}.; FUNCTION: [Isoform 2]: Non-functional as a carboxypeptidase. {ECO:0000269|PubMed:33077916}.; FUNCTION: [Isoform 2]: (Microbial infection) Non-functional as a receptor for human coronavirus SARS-CoV-2. {ECO:0000269|PubMed:33077916, ECO:0000269|PubMed:33432184}. |
| Q9H8V3 | ECT2 | S20 | ochoa | Protein ECT2 (Epithelial cell-transforming sequence 2 oncogene) | Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. 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. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. {ECO:0000269|PubMed:10579713, ECO:0000269|PubMed:14645260, ECO:0000269|PubMed:15254234, ECO:0000269|PubMed:15545273, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16170345, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:16495035, ECO:0000269|PubMed:19129481, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19617897, ECO:0000269|PubMed:21189248, ECO:0000269|PubMed:21373644, ECO:0000269|PubMed:25068414, ECO:0000269|PubMed:31888991}. |
| Q9H902 | REEP1 | S114 | ochoa | Receptor expression-enhancing protein 1 (Spastic paraplegia 31 protein) | Required for endoplasmic reticulum (ER) network formation, shaping and remodeling; it links ER tubules to the cytoskeleton. May also enhance the cell surface expression of odorant receptors (PubMed:20200447). May play a role in long-term axonal maintenance (PubMed:24478229). {ECO:0000269|PubMed:20200447, ECO:0000269|PubMed:24478229}. |
| Q9NR09 | BIRC6 | S3937 | ochoa | Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6 (EC 2.3.2.24) (BIR repeat-containing ubiquitin-conjugating enzyme) (BRUCE) (Baculoviral IAP repeat-containing protein 6) (Ubiquitin-conjugating BIR domain enzyme apollon) (APOLLON) | Anti-apoptotic protein known as inhibitor of apoptosis (IAP) which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase (PubMed:14765125, PubMed:15200957, PubMed:18329369). Unlike most IAPs, does not contain a RING domain and it is not a RING-type E3 ligase (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). Instead acts as a dual E2/E3 enzyme that combines ubiquitin conjugating (E2) and ubiquitin ligase (E3) activities in a single polypeptide (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). Ubiquitination is mediated by a non-canonical E1 ubiquitin activating enzyme UBA6 (PubMed:36758104, PubMed:36758105, PubMed:36758106). Ubiquitinates CASP3, CASP7 and CASP9 and inhibits their caspase activity; also ubiquitinates their procaspases but to a weaker extent (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). Ubiquitinates pro-apoptotic factors DIABLO/SMAC and HTRA2 (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). DIABLO/SMAC antagonizes the caspase inhibition activity of BIRC6 by competing for the same binding sites as the caspases (PubMed:18329369, PubMed:36758106). Ubiquitinates the autophagy protein MAP1LC3B; this activity is also inhibited by DIABLO/SMAC (PubMed:36758105). Important regulator for the final stages of cytokinesis (PubMed:18329369). Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification (PubMed:18329369). {ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:18329369, ECO:0000269|PubMed:36758104, ECO:0000269|PubMed:36758105, ECO:0000269|PubMed:36758106}. |
| Q9NV92 | NDFIP2 | S220 | ochoa | NEDD4 family-interacting protein 2 (NEDD4 WW domain-binding protein 5A) (Putative MAPK-activating protein PM04/PM05/PM06/PM07) (Putative NF-kappa-B-activating protein 413) | Activates HECT domain-containing E3 ubiquitin-protein ligases, including ITCH, NEDD4, NEDD4L, SMURF2, WWP1 and WWP2, and consequently modulates the stability of their targets. As a result, may control many cellular processes. Recruits ITCH, NEDD4 and SMURF2 to endosomal membranes. Negatively regulates KCNH2 potassium channel activity by decreasing its cell-surface expression and interfering with channel maturation through recruitment of NEDD4L to the Golgi apparatus and multivesicular body where it mediates KCNH2 degradation (PubMed:26363003). May modulate EGFR signaling. Together with NDFIP1, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination (By similarity). {ECO:0000250|UniProtKB:Q91ZP6, ECO:0000269|PubMed:12761501, ECO:0000269|PubMed:19343052, ECO:0000269|PubMed:20534535, ECO:0000269|PubMed:26363003}. |
| Q9NY65 | TUBA8 | Y103 | ochoa | Tubulin alpha-8 chain (EC 3.6.5.-) (Alpha-tubulin 8) (Tubulin alpha chain-like 2) [Cleaved into: Dephenylalaninated tubulin alpha-8 chain] | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
| Q9P2Y5 | UVRAG | S554 | ochoa | UV radiation resistance-associated gene protein (p63) | Versatile protein that is involved in regulation of different cellular pathways implicated in membrane trafficking. Involved in regulation of the COPI-dependent retrograde transport from Golgi and the endoplasmic reticulum by associating with the NRZ complex; the function is dependent on its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P) (PubMed:16799551, PubMed:18552835, PubMed:20643123, PubMed:24056303, PubMed:28306502). During autophagy acts as a regulatory subunit of the alternative PI3K complex II (PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate and is believed to be involved in maturation of autophagosomes and endocytosis. Activates lipid kinase activity of PIK3C3 (PubMed:16799551, PubMed:20643123, PubMed:24056303, PubMed:28306502). Involved in the regulation of degradative endocytic trafficking and cytokinesis, and in regulation of ATG9A transport from the Golgi to the autophagosome; the functions seems to implicate its association with PI3KC3-C2 (PubMed:16799551, PubMed:20643123, PubMed:24056303). Involved in maturation of autophagosomes and degradative endocytic trafficking independently of BECN1 but depending on its association with a class C Vps complex (possibly the HOPS complex); the association is also proposed to promote autophagosome recruitment and activation of Rab7 and endosome-endosome fusion events (PubMed:18552835, PubMed:28306502). Enhances class C Vps complex (possibly HOPS complex) association with a SNARE complex and promotes fusogenic SNARE complex formation during late endocytic membrane fusion (PubMed:24550300). In case of negative-strand RNA virus infection is required for efficient virus entry, promotes endocytic transport of virions and is implicated in a VAMP8-specific fusogenic SNARE complex assembly (PubMed:24550300). {ECO:0000269|PubMed:18552835, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:24056303, ECO:0000269|PubMed:28306502, ECO:0000305}.; FUNCTION: Involved in maintaining chromosomal stability. Promotes DNA double-strand break (DSB) repair by association with DNA-dependent protein kinase complex DNA-PK and activating it in non-homologous end joining (NHEJ) (PubMed:22542840). Required for centrosome stability and proper chromosome segregation (PubMed:22542840). {ECO:0000269|PubMed:22542840}. |
| Q9UJM8 | HAO1 | S65 | ochoa | 2-Hydroxyacid oxidase 1 (HAOX1) (EC 1.1.3.15) (Glycolate oxidase) (GO) (GOX) (Glyoxylate oxidase) (EC 1.2.3.5) | Broad substrate specificity (S)-2-hydroxy-acid oxidase that preferentially oxidizes glycolate (PubMed:10777549, PubMed:10978532, PubMed:17669354, PubMed:18215067). The glyoxylate produced by the oxidation of glycolate can then be utilized by alanine-glyoxylate aminotransferase for the peroxisomal synthesis of glycine; this pathway appears to be an important step for the detoxification of glyoxylate which, if allowed to accumulate, may be metabolized to oxalate with formation of kidney stones (PubMed:10978532, PubMed:17669354). Can also catalyze the oxidation of glyoxylate, and long chain hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, albeit with much lower catalytic efficiency (PubMed:10777549, PubMed:17669354, PubMed:18215067). Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the physiological electron acceptor, leading to the production of H2O2 (PubMed:10777549, PubMed:10978532, PubMed:17669354, PubMed:18215067). Is not active on L-lactate and 2-hydroxybutanoate (PubMed:10777549). {ECO:0000269|PubMed:10777549, ECO:0000269|PubMed:10978532, ECO:0000269|PubMed:17669354, ECO:0000269|PubMed:18215067, ECO:0000303|PubMed:10978532, ECO:0000303|PubMed:17669354}. |
| Q9UKF6 | CPSF3 | S633 | ochoa | Cleavage and polyadenylation specificity factor subunit 3 (EC 3.1.27.-) (Cleavage and polyadenylation specificity factor 73 kDa subunit) (CPSF 73 kDa subunit) (mRNA 3'-end-processing endonuclease CPSF-73) | Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as an mRNA 3'-end-processing endonuclease (PubMed:30507380). Also involved in the histone 3'-end pre-mRNA processing (PubMed:30507380). U7 snRNP-dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. Required for entering/progressing through S-phase of the cell cycle (PubMed:30507380). Required for the selective processing of microRNAs (miRNAs) during embryonic stem cell differentiation via its interaction with ISY1 (By similarity). Required for the biogenesis of all miRNAs from the pri-miR-17-92 primary transcript except miR-92a (By similarity). Only required for the biogenesis of miR-290 and miR-96 from the pri-miR-290-295 and pri-miR-96-183 primary transcripts, respectively (By similarity). {ECO:0000250|UniProtKB:Q9QXK7, ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:15037765, ECO:0000269|PubMed:17128255, ECO:0000269|PubMed:18688255, ECO:0000269|PubMed:30507380}. |
| Q9UKX2 | MYH2 | S54 | 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 | S181 | 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}. |
| Q9UPM8 | AP4E1 | S751 | ochoa | AP-4 complex subunit epsilon-1 (AP-4 adaptor complex subunit epsilon) (Adaptor-related protein complex 4 subunit epsilon-1) (Epsilon subunit of AP-4) (Epsilon-adaptin) | Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways (PubMed:10066790, PubMed:10436028). AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal (Probable). {ECO:0000269|PubMed:10066790, ECO:0000269|PubMed:10436028, ECO:0000305|PubMed:10066790, ECO:0000305|PubMed:10436028}. |
| Q9UQ84 | EXO1 | S510 | ochoa | Exonuclease 1 (hExo1) (EC 3.1.-.-) (Exonuclease I) (hExoI) | 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch-containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. Essential for male and female meiosis. {ECO:0000269|PubMed:10364235, ECO:0000269|PubMed:10608837, ECO:0000269|PubMed:11809771, ECO:0000269|PubMed:11842105, ECO:0000269|PubMed:12414623, ECO:0000269|PubMed:12704184, ECO:0000269|PubMed:14636568, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:15225546, ECO:0000269|PubMed:15886194, ECO:0000269|PubMed:16143102, ECO:0000269|PubMed:9685493}. |
| Q9Y277 | VDAC3 | S165 | ochoa | Non-selective voltage-gated ion channel VDAC3 (VDAC-3) (hVDAC3) (Outer mitochondrial membrane protein porin 3) | Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:31935282). Forms a high-conducting channel with a stable open state and a voltage-induced closure with a mild preference for anions over cations (PubMed:31935282). Involved in male fertility and sperm mitochondrial sheath formation (By similarity). {ECO:0000250|UniProtKB:Q60931, ECO:0000269|PubMed:31935282}. |
| Q9Y5Z4 | HEBP2 | S141 | ochoa | Heme-binding protein 2 (Placental protein 23) (PP23) (Protein SOUL) | Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. {ECO:0000269|PubMed:17098234}. |
| Q9Y623 | MYH4 | S181 | 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. |
| Q9Y6D9 | MAD1L1 | S62 | psp | Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1) (Mitotic checkpoint MAD1 protein homolog) (HsMAD1) (hMAD1) (Tax-binding protein 181) | Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (PubMed:10049595, PubMed:20133940, PubMed:29162720). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (PubMed:29162720). {ECO:0000269|PubMed:10049595, ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:36322655}.; FUNCTION: [Isoform 3]: Sequesters MAD2L1 in the cytoplasm preventing its function as an activator of the mitotic spindle assembly checkpoint (SAC) resulting in SAC impairment and chromosomal instability in hepatocellular carcinomas. {ECO:0000269|PubMed:19010891}. |
| Q9Y6Q9 | NCOA3 | S101 | 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. |
| R4GMW8 | BIVM-ERCC5 | S882 | ochoa | DNA excision repair protein ERCC-5 | None |
| Q9BY77 | POLDIP3 | S63 | EPSD|PSP | Polymerase delta-interacting protein 3 (46 kDa DNA polymerase delta interaction protein) (p46) (S6K1 Aly/REF-like target) (SKAR) | Is involved in regulation of translation. Is preferentially associated with CBC-bound spliced mRNA-protein complexes during the pioneer round of mRNA translation. Contributes to enhanced translational efficiency of spliced over nonspliced mRNAs. Recruits activated ribosomal protein S6 kinase beta-1 I/RPS6KB1 to newly synthesized mRNA. Involved in nuclear mRNA export; probably mediated by association with the TREX complex. {ECO:0000269|PubMed:18423201, ECO:0000269|PubMed:22928037}. |
| P13639 | EEF2 | S732 | Sugiyama | Elongation factor 2 (EF-2) (EC 3.6.5.-) | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:26593721). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (PubMed:26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:26593721). {ECO:0000269|PubMed:26593721}. |
| P61313 | RPL15 | Y119 | Sugiyama | Large ribosomal subunit protein eL15 (60S ribosomal protein L15) | Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}. |
| P33992 | MCM5 | S490 | Sugiyama | DNA replication licensing factor MCM5 (EC 3.6.4.12) (CDC46 homolog) (P1-CDC46) | Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:16899510, PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:32453425). {ECO:0000269|PubMed:16899510, ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232}. |
| P43490 | NAMPT | S180 | Sugiyama | Nicotinamide phosphoribosyltransferase (NAmPRTase) (Nampt) (EC 2.4.2.12) (Pre-B-cell colony-enhancing factor 1) (Pre-B cell-enhancing factor) (Visfatin) | Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression (By similarity). {ECO:0000250|UniProtKB:Q99KQ4, ECO:0000269|PubMed:24130902}. |
| P40227 | CCT6A | S49 | Sugiyama | T-complex protein 1 subunit zeta (TCP-1-zeta) (EC 3.6.1.-) (Acute morphine dependence-related protein 2) (CCT-zeta-1) (Chaperonin containing T-complex polypeptide 1 subunit 6A) (HTR3) (Tcp20) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). {ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
| P11137 | MAP2 | S1675 | EPSD | Microtubule-associated protein 2 (MAP-2) | The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules. |
| P21802 | FGFR2 | S410 | Sugiyama | Fibroblast growth factor receptor 2 (FGFR-2) (EC 2.7.10.1) (K-sam) (KGFR) (Keratinocyte growth factor receptor) (CD antigen CD332) | Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1. {ECO:0000269|PubMed:12529371, ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:16384934, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18374639, ECO:0000269|PubMed:19103595, ECO:0000269|PubMed:19387476, ECO:0000269|PubMed:19410646, ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:8663044}. |
| P36897 | TGFBR1 | S387 | Sugiyama | TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I) | Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis (PubMed:33914044). The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation. {ECO:0000269|PubMed:15761148, ECO:0000269|PubMed:16754747, ECO:0000269|PubMed:18758450, ECO:0000269|PubMed:33914044, ECO:0000269|PubMed:7774578, ECO:0000269|PubMed:8752209, ECO:0000269|PubMed:8980228, ECO:0000269|PubMed:9346908}. |
| P09960 | LTA4H | S486 | Sugiyama | Leukotriene A-4 hydrolase (LTA-4 hydrolase) (EC 3.3.2.6) (Leukotriene A(4) hydrolase) (Tripeptide aminopeptidase LTA4H) (EC 3.4.11.4) | Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities. Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4) (PubMed:11917124, PubMed:12207002, PubMed:15078870, PubMed:18804029, PubMed:1897988, PubMed:1975494, PubMed:2244921). Also has aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides (PubMed:18804029, PubMed:20813919). In addition to its pro-inflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL) (PubMed:20813919, PubMed:24591641). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions (PubMed:21206090). {ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029, ECO:0000269|PubMed:1897988, ECO:0000269|PubMed:1975494, ECO:0000269|PubMed:20813919, ECO:0000269|PubMed:21206090, ECO:0000269|PubMed:2244921, ECO:0000269|PubMed:24591641}. |
| Q13310 | PABPC4 | S212 | Sugiyama | Polyadenylate-binding protein 4 (PABP-4) (Poly(A)-binding protein 4) (Activated-platelet protein 1) (APP-1) (Inducible poly(A)-binding protein) (iPABP) | Binds the poly(A) tail of mRNA (PubMed:8524242). Binds to SMIM26 mRNA and plays a role in its post-transcriptional regulation (PubMed:37009826). May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo (By similarity). {ECO:0000250|UniProtKB:P11940, ECO:0000269|PubMed:37009826, ECO:0000269|PubMed:8524242}. |
| Q9Y262 | EIF3L | S255 | Sugiyama | Eukaryotic translation initiation factor 3 subunit L (eIF3l) (Eukaryotic translation initiation factor 3 subunit 6-interacting protein) (Eukaryotic translation initiation factor 3 subunit E-interacting protein) | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03011, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.; FUNCTION: (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}. |
| Q969G3 | SMARCE1 | S262 | Sugiyama | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 (BRG1-associated factor 57) (BAF57) | Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Required for the coactivation of estrogen responsive promoters by SWI/SNF complexes and the SRC/p160 family of histone acetyltransferases (HATs). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells. {ECO:0000250|UniProtKB:O54941, ECO:0000303|PubMed:12672490, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
| Q9BUP3 | HTATIP2 | S177 | Sugiyama | Protein HTATIP2 (30 kDa HIV-1 TAT-interacting protein) (HIV-1 TAT-interactive protein 2) | Represses translation by preventing reactivation of elongation factor eEF1A (By similarity). May also inhibit nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors (PubMed:15282309). Has additionally been proposed to act as a redox sensor involved in cellular oxidative stress surveillance (PubMed:18519672). {ECO:0000250|UniProtKB:B0BNF8, ECO:0000269|PubMed:15282309, ECO:0000269|PubMed:18519672}. |
| O14979 | HNRNPDL | S293 | Sugiyama | Heterogeneous nuclear ribonucleoprotein D-like (hnRNP D-like) (hnRNP DL) (AU-rich element RNA-binding factor) (JKT41-binding protein) (Protein laAUF1) | Acts as a transcriptional regulator. Promotes transcription repression. Promotes transcription activation in differentiated myotubes (By similarity). Binds to double- and single-stranded DNA sequences. Binds to the transcription suppressor CATR sequence of the COX5B promoter (By similarity). Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Binds both to nuclear and cytoplasmic poly(A) mRNAs. Binds to poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA consensus sequence. {ECO:0000250, ECO:0000269|PubMed:9538234}. |
| Q8IW41 | MAPKAPK5 | S440 | Sugiyama | MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAP-K5) (MAPKAPK-5) (MK-5) (MK5) (EC 2.7.11.1) (p38-regulated/activated protein kinase) (PRAK) | Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement. {ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:17728103, ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:9628874}. |
| P60520 | GABARAPL2 | S39 | Sugiyama | Gamma-aminobutyric acid receptor-associated protein-like 2 (GABA(A) receptor-associated protein-like 2) (Ganglioside expression factor 2) (GEF-2) (General protein transport factor p16) (Golgi-associated ATPase enhancer of 16 kDa) (GATE-16) (MAP1 light chain 3-related protein) | Ubiquitin-like modifier involved in intra-Golgi traffic (By similarity). Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation (By similarity). It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy (PubMed:20418806, PubMed:23209295). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (PubMed:20418806, PubMed:23209295). Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20418806, PubMed:23209295). {ECO:0000250|UniProtKB:P60519, ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:23209295}. |
| P78371 | CCT2 | S438 | Sugiyama | T-complex protein 1 subunit beta (TCP-1-beta) (EC 3.6.1.-) (CCT-beta) (Chaperonin containing T-complex polypeptide 1 subunit 2) | 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}. |
Download
| reactome_id | name | p | -log10_p |
|---|---|---|---|
| R-HSA-389960 | Formation of tubulin folding intermediates by CCT/TriC | 5.551115e-15 | 14.256 |
| R-HSA-389958 | Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding | 5.273559e-14 | 13.278 |
| R-HSA-389957 | Prefoldin mediated transfer of substrate to CCT/TriC | 7.525869e-12 | 11.123 |
| R-HSA-9612973 | Autophagy | 5.923559e-10 | 9.227 |
| R-HSA-3371497 | HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig... | 1.930326e-09 | 8.714 |
| R-HSA-390466 | Chaperonin-mediated protein folding | 1.221523e-09 | 8.913 |
| R-HSA-9619483 | Activation of AMPK downstream of NMDARs | 9.742218e-10 | 9.011 |
| R-HSA-190840 | Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane | 1.430519e-09 | 8.845 |
| R-HSA-9663891 | Selective autophagy | 1.358915e-09 | 8.867 |
| R-HSA-190872 | Transport of connexons to the plasma membrane | 1.938527e-09 | 8.713 |
| R-HSA-1632852 | Macroautophagy | 1.920638e-09 | 8.717 |
| R-HSA-391251 | Protein folding | 2.276312e-09 | 8.643 |
| R-HSA-389977 | Post-chaperonin tubulin folding pathway | 3.424855e-09 | 8.465 |
| R-HSA-9646399 | Aggrephagy | 1.180931e-08 | 7.928 |
| R-HSA-8852276 | The role of GTSE1 in G2/M progression after G2 checkpoint | 1.547492e-08 | 7.810 |
| R-HSA-380320 | Recruitment of NuMA to mitotic centrosomes | 1.895879e-08 | 7.722 |
| R-HSA-437239 | Recycling pathway of L1 | 3.916398e-08 | 7.407 |
| R-HSA-5620920 | Cargo trafficking to the periciliary membrane | 4.301311e-08 | 7.366 |
| R-HSA-157858 | Gap junction trafficking and regulation | 5.135958e-08 | 7.289 |
| R-HSA-9668328 | Sealing of the nuclear envelope (NE) by ESCRT-III | 6.955575e-08 | 7.158 |
| R-HSA-190861 | Gap junction assembly | 9.728805e-08 | 7.012 |
| R-HSA-428359 | Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RN... | 1.352902e-07 | 6.869 |
| R-HSA-438064 | Post NMDA receptor activation events | 2.192994e-07 | 6.659 |
| R-HSA-9609736 | Assembly and cell surface presentation of NMDA receptors | 3.196838e-07 | 6.495 |
| R-HSA-190828 | Gap junction trafficking | 4.741503e-07 | 6.324 |
| R-HSA-8955332 | Carboxyterminal post-translational modifications of tubulin | 6.870334e-07 | 6.163 |
| R-HSA-442755 | Activation of NMDA receptors and postsynaptic events | 8.393982e-07 | 6.076 |
| R-HSA-9833482 | PKR-mediated signaling | 1.321099e-06 | 5.879 |
| R-HSA-6811436 | COPI-independent Golgi-to-ER retrograde traffic | 1.677348e-06 | 5.775 |
| R-HSA-8851708 | Signaling by FGFR2 IIIa TM | 2.685822e-06 | 5.571 |
| R-HSA-1839126 | FGFR2 mutant receptor activation | 2.609932e-06 | 5.583 |
| R-HSA-5617833 | Cilium Assembly | 2.756356e-06 | 5.560 |
| R-HSA-983189 | Kinesins | 2.760955e-06 | 5.559 |
| R-HSA-68877 | Mitotic Prometaphase | 3.153421e-06 | 5.501 |
| R-HSA-6807878 | COPI-mediated anterograde transport | 5.493070e-06 | 5.260 |
| R-HSA-6811434 | COPI-dependent Golgi-to-ER retrograde traffic | 5.493070e-06 | 5.260 |
| R-HSA-390450 | Folding of actin by CCT/TriC | 6.134906e-06 | 5.212 |
| R-HSA-1445148 | Translocation of SLC2A4 (GLUT4) to the plasma membrane | 8.550446e-06 | 5.068 |
| R-HSA-5620924 | Intraflagellar transport | 1.160326e-05 | 4.935 |
| R-HSA-9648025 | EML4 and NUDC in mitotic spindle formation | 1.326210e-05 | 4.877 |
| R-HSA-5655253 | Signaling by FGFR2 in disease | 1.411935e-05 | 4.850 |
| R-HSA-2995410 | Nuclear Envelope (NE) Reassembly | 1.451992e-05 | 4.838 |
| R-HSA-69275 | G2/M Transition | 1.518238e-05 | 4.819 |
| R-HSA-453274 | Mitotic G2-G2/M phases | 1.648537e-05 | 4.783 |
| R-HSA-373760 | L1CAM interactions | 2.204655e-05 | 4.657 |
| R-HSA-9675108 | Nervous system development | 2.367766e-05 | 4.626 |
| R-HSA-1169410 | Antiviral mechanism by IFN-stimulated genes | 2.386024e-05 | 4.622 |
| R-HSA-2500257 | Resolution of Sister Chromatid Cohesion | 2.874862e-05 | 4.541 |
| R-HSA-5654727 | Negative regulation of FGFR2 signaling | 3.469268e-05 | 4.460 |
| R-HSA-8856688 | Golgi-to-ER retrograde transport | 5.455810e-05 | 4.263 |
| R-HSA-69278 | Cell Cycle, Mitotic | 6.203440e-05 | 4.207 |
| R-HSA-5654221 | Phospholipase C-mediated cascade; FGFR2 | 7.735410e-05 | 4.112 |
| R-HSA-1280215 | Cytokine Signaling in Immune system | 8.337804e-05 | 4.079 |
| R-HSA-190241 | FGFR2 ligand binding and activation | 8.988325e-05 | 4.046 |
| R-HSA-1226099 | Signaling by FGFR in disease | 9.501153e-05 | 4.022 |
| R-HSA-5336415 | Uptake and function of diphtheria toxin | 1.027140e-04 | 3.988 |
| R-HSA-199977 | ER to Golgi Anterograde Transport | 1.150354e-04 | 3.939 |
| R-HSA-5654738 | Signaling by FGFR2 | 1.390699e-04 | 3.857 |
| R-HSA-422475 | Axon guidance | 1.445386e-04 | 3.840 |
| R-HSA-5654695 | PI-3K cascade:FGFR2 | 1.756116e-04 | 3.755 |
| R-HSA-2219528 | PI3K/AKT Signaling in Cancer | 1.805287e-04 | 3.743 |
| R-HSA-5654699 | SHC-mediated cascade:FGFR2 | 2.224825e-04 | 3.653 |
| R-HSA-1852241 | Organelle biogenesis and maintenance | 2.210305e-04 | 3.656 |
| R-HSA-2467813 | Separation of Sister Chromatids | 2.227310e-04 | 3.652 |
| R-HSA-5654700 | FRS-mediated FGFR2 signaling | 2.490139e-04 | 3.604 |
| R-HSA-6811558 | PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling | 2.259002e-04 | 3.646 |
| R-HSA-68886 | M Phase | 2.433231e-04 | 3.614 |
| R-HSA-1640170 | Cell Cycle | 2.343025e-04 | 3.630 |
| R-HSA-112314 | Neurotransmitter receptors and postsynaptic signal transmission | 2.270937e-04 | 3.644 |
| R-HSA-2132295 | MHC class II antigen presentation | 2.259002e-04 | 3.646 |
| R-HSA-5663202 | Diseases of signal transduction by growth factor receptors and second messengers | 2.808905e-04 | 3.551 |
| R-HSA-199418 | Negative regulation of the PI3K/AKT network | 3.172584e-04 | 3.499 |
| R-HSA-2219530 | Constitutive Signaling by Aberrant PI3K in Cancer | 3.381574e-04 | 3.471 |
| R-HSA-190236 | Signaling by FGFR | 4.325682e-04 | 3.364 |
| R-HSA-390471 | Association of TriC/CCT with target proteins during biosynthesis | 4.581110e-04 | 3.339 |
| R-HSA-5610787 | Hedgehog 'off' state | 4.756273e-04 | 3.323 |
| R-HSA-6814122 | Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding | 5.022723e-04 | 3.299 |
| R-HSA-5654696 | Downstream signaling of activated FGFR2 | 5.493824e-04 | 3.260 |
| R-HSA-9609690 | HCMV Early Events | 6.645795e-04 | 3.177 |
| R-HSA-6811442 | Intra-Golgi and retrograde Golgi-to-ER traffic | 7.481374e-04 | 3.126 |
| R-HSA-948021 | Transport to the Golgi and subsequent modification | 7.929805e-04 | 3.101 |
| R-HSA-913531 | Interferon Signaling | 9.189763e-04 | 3.037 |
| R-HSA-2023837 | Signaling by FGFR2 amplification mutants | 9.246314e-04 | 3.034 |
| R-HSA-2033519 | Activated point mutants of FGFR2 | 1.150154e-03 | 2.939 |
| R-HSA-68882 | Mitotic Anaphase | 1.202730e-03 | 2.920 |
| R-HSA-2555396 | Mitotic Metaphase and Anaphase | 1.235125e-03 | 2.908 |
| R-HSA-5660489 | MTF1 activates gene expression | 1.323857e-03 | 2.878 |
| R-HSA-109704 | PI3K Cascade | 1.794209e-03 | 2.746 |
| R-HSA-983231 | Factors involved in megakaryocyte development and platelet production | 1.712029e-03 | 2.766 |
| R-HSA-8937144 | Aryl hydrocarbon receptor signalling | 2.326719e-03 | 2.633 |
| R-HSA-5358351 | Signaling by Hedgehog | 2.582601e-03 | 2.588 |
| R-HSA-112399 | IRS-mediated signalling | 2.700459e-03 | 2.569 |
| R-HSA-9609646 | HCMV Infection | 2.759778e-03 | 2.559 |
| R-HSA-380284 | Loss of proteins required for interphase microtubule organization from the centr... | 3.693025e-03 | 2.433 |
| R-HSA-380259 | Loss of Nlp from mitotic centrosomes | 3.693025e-03 | 2.433 |
| R-HSA-2428928 | IRS-related events triggered by IGF1R | 3.338519e-03 | 2.476 |
| R-HSA-2428924 | IGF1R signaling cascade | 3.879500e-03 | 2.411 |
| R-HSA-74751 | Insulin receptor signalling cascade | 3.879500e-03 | 2.411 |
| R-HSA-112315 | Transmission across Chemical Synapses | 3.407044e-03 | 2.468 |
| R-HSA-112316 | Neuronal System | 4.015365e-03 | 2.396 |
| R-HSA-8950505 | Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulati... | 4.072254e-03 | 2.390 |
| R-HSA-2404192 | Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) | 4.072254e-03 | 2.390 |
| R-HSA-8854518 | AURKA Activation by TPX2 | 4.271385e-03 | 2.369 |
| R-HSA-9825895 | Regulation of MITF-M-dependent genes involved in DNA replication, damage repair ... | 4.324143e-03 | 2.364 |
| R-HSA-9834752 | Respiratory syncytial virus genome replication | 5.116788e-03 | 2.291 |
| R-HSA-390522 | Striated Muscle Contraction | 5.431035e-03 | 2.265 |
| R-HSA-5205647 | Mitophagy | 5.811755e-03 | 2.236 |
| R-HSA-380270 | Recruitment of mitotic centrosome proteins and complexes | 5.851853e-03 | 2.233 |
| R-HSA-9820962 | Assembly and release of respiratory syncytial virus (RSV) virions | 5.970953e-03 | 2.224 |
| R-HSA-140342 | Apoptosis induced DNA fragmentation | 5.970953e-03 | 2.224 |
| R-HSA-199991 | Membrane Trafficking | 6.132666e-03 | 2.212 |
| R-HSA-380287 | Centrosome maturation | 6.366141e-03 | 2.196 |
| R-HSA-3371511 | HSF1 activation | 6.620194e-03 | 2.179 |
| R-HSA-9020591 | Interleukin-12 signaling | 6.634184e-03 | 2.178 |
| R-HSA-1257604 | PIP3 activates AKT signaling | 6.845500e-03 | 2.165 |
| R-HSA-190377 | FGFR2b ligand binding and activation | 6.885520e-03 | 2.162 |
| R-HSA-3371568 | Attenuation phase | 8.429308e-03 | 2.074 |
| R-HSA-8953854 | Metabolism of RNA | 8.320415e-03 | 2.080 |
| R-HSA-2565942 | Regulation of PLK1 Activity at G2/M Transition | 9.051130e-03 | 2.043 |
| R-HSA-190375 | FGFR2c ligand binding and activation | 9.980676e-03 | 2.001 |
| R-HSA-447115 | Interleukin-12 family signaling | 1.044953e-02 | 1.981 |
| R-HSA-156902 | Peptide chain elongation | 1.081972e-02 | 1.966 |
| R-HSA-109582 | Hemostasis | 1.136285e-02 | 1.945 |
| R-HSA-5620912 | Anchoring of the basal body to the plasma membrane | 1.158528e-02 | 1.936 |
| R-HSA-9824446 | Viral Infection Pathways | 1.176917e-02 | 1.929 |
| R-HSA-75153 | Apoptotic execution phase | 1.223296e-02 | 1.912 |
| R-HSA-399954 | Sema3A PAK dependent Axon repulsion | 1.232629e-02 | 1.909 |
| R-HSA-156842 | Eukaryotic Translation Elongation | 1.279758e-02 | 1.893 |
| R-HSA-74752 | Signaling by Insulin receptor | 1.279758e-02 | 1.893 |
| R-HSA-389356 | Co-stimulation by CD28 | 1.347269e-02 | 1.871 |
| R-HSA-8953897 | Cellular responses to stimuli | 1.362115e-02 | 1.866 |
| R-HSA-5653656 | Vesicle-mediated transport | 1.435548e-02 | 1.843 |
| R-HSA-72689 | Formation of a pool of free 40S subunits | 1.453598e-02 | 1.838 |
| R-HSA-9006925 | Intracellular signaling by second messengers | 1.485549e-02 | 1.828 |
| R-HSA-5660526 | Response to metal ions | 1.488790e-02 | 1.827 |
| R-HSA-76002 | Platelet activation, signaling and aggregation | 1.540469e-02 | 1.812 |
| R-HSA-3371571 | HSF1-dependent transactivation | 1.546195e-02 | 1.811 |
| R-HSA-5683057 | MAPK family signaling cascades | 1.599484e-02 | 1.796 |
| R-HSA-5339562 | Uptake and actions of bacterial toxins | 1.615984e-02 | 1.792 |
| R-HSA-446203 | Asparagine N-linked glycosylation | 1.649204e-02 | 1.783 |
| R-HSA-72203 | Processing of Capped Intron-Containing Pre-mRNA | 1.673141e-02 | 1.776 |
| R-HSA-9613829 | Chaperone Mediated Autophagy | 1.765742e-02 | 1.753 |
| R-HSA-168273 | Influenza Viral RNA Transcription and Replication | 1.863750e-02 | 1.730 |
| R-HSA-5620922 | BBSome-mediated cargo-targeting to cilium | 2.062697e-02 | 1.686 |
| R-HSA-1643685 | Disease | 2.118066e-02 | 1.674 |
| R-HSA-72706 | GTP hydrolysis and joining of the 60S ribosomal subunit | 2.176611e-02 | 1.662 |
| R-HSA-156827 | L13a-mediated translational silencing of Ceruloplasmin expression | 2.176611e-02 | 1.662 |
| R-HSA-8949215 | Mitochondrial calcium ion transport | 2.378885e-02 | 1.624 |
| R-HSA-9006934 | Signaling by Receptor Tyrosine Kinases | 2.414643e-02 | 1.617 |
| R-HSA-9938206 | Developmental Lineage of Mammary Stem Cells | 2.543958e-02 | 1.594 |
| R-HSA-9670439 | Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT m... | 2.543958e-02 | 1.594 |
| R-HSA-9669938 | Signaling by KIT in disease | 2.543958e-02 | 1.594 |
| R-HSA-8853333 | Signaling by FGFR2 fusions | 2.592877e-02 | 1.586 |
| R-HSA-8939211 | ESR-mediated signaling | 2.626760e-02 | 1.581 |
| R-HSA-449147 | Signaling by Interleukins | 2.718911e-02 | 1.566 |
| R-HSA-4420097 | VEGFA-VEGFR2 Pathway | 2.739580e-02 | 1.562 |
| R-HSA-72613 | Eukaryotic Translation Initiation | 2.807010e-02 | 1.552 |
| R-HSA-72737 | Cap-dependent Translation Initiation | 2.807010e-02 | 1.552 |
| R-HSA-5218859 | Regulated Necrosis | 2.971579e-02 | 1.527 |
| R-HSA-168255 | Influenza Infection | 3.087759e-02 | 1.510 |
| R-HSA-3371556 | Cellular response to heat stress | 3.158974e-02 | 1.500 |
| R-HSA-9665230 | Drug resistance in ERBB2 KD mutants | 3.442247e-02 | 1.463 |
| R-HSA-9652282 | Drug-mediated inhibition of ERBB2 signaling | 3.442247e-02 | 1.463 |
| R-HSA-3645790 | TGFBR2 Kinase Domain Mutants in Cancer | 3.442247e-02 | 1.463 |
| R-HSA-9665245 | Resistance of ERBB2 KD mutants to tesevatinib | 3.442247e-02 | 1.463 |
| R-HSA-9665249 | Resistance of ERBB2 KD mutants to afatinib | 3.442247e-02 | 1.463 |
| R-HSA-9665250 | Resistance of ERBB2 KD mutants to AEE788 | 3.442247e-02 | 1.463 |
| R-HSA-9665737 | Drug resistance in ERBB2 TMD/JMD mutants | 3.442247e-02 | 1.463 |
| R-HSA-9665233 | Resistance of ERBB2 KD mutants to trastuzumab | 3.442247e-02 | 1.463 |
| R-HSA-9665246 | Resistance of ERBB2 KD mutants to neratinib | 3.442247e-02 | 1.463 |
| R-HSA-9665251 | Resistance of ERBB2 KD mutants to lapatinib | 3.442247e-02 | 1.463 |
| R-HSA-9665244 | Resistance of ERBB2 KD mutants to sapitinib | 3.442247e-02 | 1.463 |
| R-HSA-9665247 | Resistance of ERBB2 KD mutants to osimertinib | 3.442247e-02 | 1.463 |
| R-HSA-3656535 | TGFBR1 LBD Mutants in Cancer | 3.442247e-02 | 1.463 |
| R-HSA-5205685 | PINK1-PRKN Mediated Mitophagy | 3.626405e-02 | 1.441 |
| R-HSA-3642278 | Loss of Function of TGFBR2 in Cancer | 3.442247e-02 | 1.463 |
| R-HSA-9927432 | Developmental Lineage of Mammary Gland Myoepithelial Cells | 3.821332e-02 | 1.418 |
| R-HSA-194138 | Signaling by VEGF | 3.535784e-02 | 1.452 |
| R-HSA-389357 | CD28 dependent PI3K/Akt signaling | 3.435483e-02 | 1.464 |
| R-HSA-114608 | Platelet degranulation | 3.693502e-02 | 1.433 |
| R-HSA-76005 | Response to elevated platelet cytosolic Ca2+ | 4.277090e-02 | 1.369 |
| R-HSA-9008059 | Interleukin-37 signaling | 4.020182e-02 | 1.396 |
| R-HSA-2262752 | Cellular responses to stress | 3.925137e-02 | 1.406 |
| R-HSA-5663205 | Infectious disease | 4.311617e-02 | 1.365 |
| R-HSA-69190 | DNA strand elongation | 4.429322e-02 | 1.354 |
| R-HSA-72202 | Transport of Mature Transcript to Cytoplasm | 4.523981e-02 | 1.344 |
| R-HSA-9018519 | Estrogen-dependent gene expression | 4.632636e-02 | 1.334 |
| R-HSA-354192 | Integrin signaling | 4.639451e-02 | 1.334 |
| R-HSA-5675482 | Regulation of necroptotic cell death | 4.639451e-02 | 1.334 |
| R-HSA-9619665 | EGR2 and SOX10-mediated initiation of Schwann cell myelination | 4.853180e-02 | 1.314 |
| R-HSA-5357801 | Programmed Cell Death | 4.874867e-02 | 1.312 |
| R-HSA-5687128 | MAPK6/MAPK4 signaling | 4.899858e-02 | 1.310 |
| R-HSA-1368108 | BMAL1:CLOCK,NPAS2 activates circadian expression | 5.070432e-02 | 1.295 |
| R-HSA-9768919 | NPAS4 regulates expression of target genes | 5.070432e-02 | 1.295 |
| R-HSA-3656532 | TGFBR1 KD Mutants in Cancer | 5.118988e-02 | 1.291 |
| R-HSA-191650 | Regulation of gap junction activity | 5.118988e-02 | 1.291 |
| R-HSA-6804756 | Regulation of TP53 Activity through Phosphorylation | 5.158689e-02 | 1.287 |
| R-HSA-8853659 | RET signaling | 5.515200e-02 | 1.258 |
| R-HSA-1266738 | Developmental Biology | 5.832592e-02 | 1.234 |
| R-HSA-9954714 | PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA | 5.834115e-02 | 1.234 |
| R-HSA-3656534 | Loss of Function of TGFBR1 in Cancer | 5.946485e-02 | 1.226 |
| R-HSA-3304356 | SMAD2/3 Phosphorylation Motif Mutants in Cancer | 5.946485e-02 | 1.226 |
| R-HSA-5213460 | RIPK1-mediated regulated necrosis | 5.973152e-02 | 1.224 |
| R-HSA-975956 | Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) | 5.973985e-02 | 1.224 |
| R-HSA-6798695 | Neutrophil degranulation | 6.007484e-02 | 1.221 |
| R-HSA-159231 | Transport of Mature mRNA Derived from an Intronless Transcript | 6.206889e-02 | 1.207 |
| R-HSA-159234 | Transport of Mature mRNAs Derived from Intronless Transcripts | 6.443705e-02 | 1.191 |
| R-HSA-9954716 | ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri... | 6.549088e-02 | 1.184 |
| R-HSA-192823 | Viral mRNA Translation | 7.931510e-02 | 1.101 |
| R-HSA-1799339 | SRP-dependent cotranslational protein targeting to membrane | 8.750032e-02 | 1.058 |
| R-HSA-9603381 | Activated NTRK3 signals through PI3K | 8.386223e-02 | 1.076 |
| R-HSA-76009 | Platelet Aggregation (Plug Formation) | 7.925356e-02 | 1.101 |
| R-HSA-9954709 | Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide | 6.696716e-02 | 1.174 |
| R-HSA-8857538 | PTK6 promotes HIF1A stabilization | 7.580041e-02 | 1.120 |
| R-HSA-9927418 | Developmental Lineage of Mammary Gland Luminal Epithelial Cells | 7.171919e-02 | 1.144 |
| R-HSA-72764 | Eukaryotic Translation Termination | 6.696716e-02 | 1.174 |
| R-HSA-3304351 | Signaling by TGF-beta Receptor Complex in Cancer | 7.580041e-02 | 1.120 |
| R-HSA-1433557 | Signaling by SCF-KIT | 7.420351e-02 | 1.130 |
| R-HSA-3304349 | Loss of Function of SMAD2/3 in Cancer | 6.766815e-02 | 1.170 |
| R-HSA-5218920 | VEGFR2 mediated vascular permeability | 6.683528e-02 | 1.175 |
| R-HSA-1296052 | Ca2+ activated K+ channels | 8.386223e-02 | 1.076 |
| R-HSA-2408557 | Selenocysteine synthesis | 7.614010e-02 | 1.118 |
| R-HSA-418886 | Netrin mediated repulsion signals | 8.386223e-02 | 1.076 |
| R-HSA-9633012 | Response of EIF2AK4 (GCN2) to amino acid deficiency | 8.092408e-02 | 1.092 |
| R-HSA-446388 | Regulation of cytoskeletal remodeling and cell spreading by IPP complex componen... | 6.766815e-02 | 1.170 |
| R-HSA-445989 | TAK1-dependent IKK and NF-kappa-B activation | 8.440779e-02 | 1.074 |
| R-HSA-9009391 | Extra-nuclear estrogen signaling | 7.614010e-02 | 1.118 |
| R-HSA-9839389 | TGFBR3 regulates TGF-beta signaling | 8.386223e-02 | 1.076 |
| R-HSA-2029480 | Fcgamma receptor (FCGR) dependent phagocytosis | 9.051304e-02 | 1.043 |
| R-HSA-5689880 | Ub-specific processing proteases | 8.922417e-02 | 1.050 |
| R-HSA-5633007 | Regulation of TP53 Activity | 7.214399e-02 | 1.142 |
| R-HSA-168928 | DDX58/IFIH1-mediated induction of interferon-alpha/beta | 6.549088e-02 | 1.184 |
| R-HSA-9679191 | Potential therapeutics for SARS | 6.108062e-02 | 1.214 |
| R-HSA-168256 | Immune System | 6.216978e-02 | 1.206 |
| R-HSA-446652 | Interleukin-1 family signaling | 6.321573e-02 | 1.199 |
| R-HSA-9820965 | Respiratory syncytial virus (RSV) genome replication, transcription and translat... | 6.206889e-02 | 1.207 |
| R-HSA-9927354 | Co-stimulation by ICOS | 9.185423e-02 | 1.037 |
| R-HSA-1253288 | Downregulation of ERBB4 signaling | 9.185423e-02 | 1.037 |
| R-HSA-9032500 | Activated NTRK2 signals through FYN | 9.185423e-02 | 1.037 |
| R-HSA-927802 | Nonsense-Mediated Decay (NMD) | 9.602706e-02 | 1.018 |
| R-HSA-975957 | Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) | 9.602706e-02 | 1.018 |
| R-HSA-72187 | mRNA 3'-end processing | 9.771623e-02 | 1.010 |
| R-HSA-9634815 | Transcriptional Regulation by NPAS4 | 9.771623e-02 | 1.010 |
| R-HSA-9700645 | ALK mutants bind TKIs | 9.977699e-02 | 1.001 |
| R-HSA-176974 | Unwinding of DNA | 9.977699e-02 | 1.001 |
| R-HSA-430116 | GP1b-IX-V activation signalling | 9.977699e-02 | 1.001 |
| R-HSA-428542 | Regulation of commissural axon pathfinding by SLIT and ROBO | 9.977699e-02 | 1.001 |
| R-HSA-442380 | Zinc influx into cells by the SLC39 gene family | 9.977699e-02 | 1.001 |
| R-HSA-264870 | Caspase-mediated cleavage of cytoskeletal proteins | 9.977699e-02 | 1.001 |
| R-HSA-432722 | Golgi Associated Vesicle Biogenesis | 1.004456e-01 | 0.998 |
| R-HSA-72766 | Translation | 1.015807e-01 | 0.993 |
| R-HSA-5358493 | Synthesis of diphthamide-EEF2 | 1.231358e-01 | 0.910 |
| R-HSA-3000484 | Scavenging by Class F Receptors | 1.307876e-01 | 0.883 |
| R-HSA-2173791 | TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) | 1.533473e-01 | 0.814 |
| R-HSA-354194 | GRB2:SOS provides linkage to MAPK signaling for Integrins | 1.607373e-01 | 0.794 |
| R-HSA-77595 | Processing of Intronless Pre-mRNAs | 1.680632e-01 | 0.775 |
| R-HSA-5637810 | Constitutive Signaling by EGFRvIII | 1.753256e-01 | 0.756 |
| R-HSA-5637812 | Signaling by EGFRvIII in Cancer | 1.753256e-01 | 0.756 |
| R-HSA-372708 | p130Cas linkage to MAPK signaling for integrins | 1.753256e-01 | 0.756 |
| R-HSA-9709603 | Impaired BRCA2 binding to PALB2 | 1.896621e-01 | 0.722 |
| R-HSA-9934037 | Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) | 1.967373e-01 | 0.706 |
| R-HSA-9701193 | Defective homologous recombination repair (HRR) due to PALB2 loss of function | 1.967373e-01 | 0.706 |
| R-HSA-9704646 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 1.967373e-01 | 0.706 |
| R-HSA-9701192 | Defective homologous recombination repair (HRR) due to BRCA1 loss of function | 1.967373e-01 | 0.706 |
| R-HSA-9704331 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 1.967373e-01 | 0.706 |
| R-HSA-5637815 | Signaling by Ligand-Responsive EGFR Variants in Cancer | 2.037511e-01 | 0.691 |
| R-HSA-1236382 | Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants | 2.037511e-01 | 0.691 |
| R-HSA-5602498 | MyD88 deficiency (TLR2/4) | 2.037511e-01 | 0.691 |
| R-HSA-5603041 | IRAK4 deficiency (TLR2/4) | 2.107041e-01 | 0.676 |
| R-HSA-159236 | Transport of Mature mRNA derived from an Intron-Containing Transcript | 1.587683e-01 | 0.799 |
| R-HSA-3928664 | Ephrin signaling | 1.825250e-01 | 0.739 |
| R-HSA-72163 | mRNA Splicing - Major Pathway | 1.181125e-01 | 0.928 |
| R-HSA-9933939 | Formation of the polybromo-BAF (pBAF) complex | 1.458928e-01 | 0.836 |
| R-HSA-9933937 | Formation of the canonical BAF (cBAF) complex | 1.458928e-01 | 0.836 |
| R-HSA-9933946 | Formation of the embryonic stem cell BAF (esBAF) complex | 1.533473e-01 | 0.814 |
| R-HSA-9948299 | Ribosome-associated quality control | 1.555155e-01 | 0.808 |
| R-HSA-418885 | DCC mediated attractive signaling | 1.533473e-01 | 0.814 |
| R-HSA-72172 | mRNA Splicing | 1.346806e-01 | 0.871 |
| R-HSA-9733458 | Induction of Cell-Cell Fusion | 1.607373e-01 | 0.794 |
| R-HSA-9694614 | Attachment and Entry | 2.107041e-01 | 0.676 |
| R-HSA-192905 | vRNP Assembly | 1.154172e-01 | 0.938 |
| R-HSA-110362 | POLB-Dependent Long Patch Base Excision Repair | 1.231358e-01 | 0.910 |
| R-HSA-9634285 | Constitutive Signaling by Overexpressed ERBB2 | 1.307876e-01 | 0.883 |
| R-HSA-879415 | Advanced glycosylation endproduct receptor signaling | 1.307876e-01 | 0.883 |
| R-HSA-5685939 | HDR through MMEJ (alt-NHEJ) | 1.383731e-01 | 0.859 |
| R-HSA-9678110 | Attachment and Entry | 1.607373e-01 | 0.794 |
| R-HSA-5651801 | PCNA-Dependent Long Patch Base Excision Repair | 1.825250e-01 | 0.739 |
| R-HSA-73856 | RNA Polymerase II Transcription Termination | 1.229957e-01 | 0.910 |
| R-HSA-9924644 | Developmental Lineages of the Mammary Gland | 1.557149e-01 | 0.808 |
| R-HSA-912631 | Regulation of signaling by CBL | 1.896621e-01 | 0.722 |
| R-HSA-8876493 | InlA-mediated entry of Listeria monocytogenes into host cells | 1.154172e-01 | 0.938 |
| R-HSA-171007 | p38MAPK events | 1.533473e-01 | 0.814 |
| R-HSA-389513 | Co-inhibition by CTLA4 | 1.967373e-01 | 0.706 |
| R-HSA-1433559 | Regulation of KIT signaling | 1.458928e-01 | 0.836 |
| R-HSA-9018681 | Biosynthesis of protectins | 1.458928e-01 | 0.836 |
| R-HSA-199992 | trans-Golgi Network Vesicle Budding | 1.557149e-01 | 0.808 |
| R-HSA-9665348 | Signaling by ERBB2 ECD mutants | 1.825250e-01 | 0.739 |
| R-HSA-69166 | Removal of the Flap Intermediate | 1.458928e-01 | 0.836 |
| R-HSA-174437 | Removal of the Flap Intermediate from the C-strand | 1.753256e-01 | 0.756 |
| R-HSA-5358508 | Mismatch Repair | 1.825250e-01 | 0.739 |
| R-HSA-5358606 | Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) | 1.753256e-01 | 0.756 |
| R-HSA-844456 | The NLRP3 inflammasome | 1.896621e-01 | 0.722 |
| R-HSA-9034015 | Signaling by NTRK3 (TRKC) | 2.107041e-01 | 0.676 |
| R-HSA-9754560 | SARS-CoV-2 modulates autophagy | 1.154172e-01 | 0.938 |
| R-HSA-5358565 | Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) | 1.753256e-01 | 0.756 |
| R-HSA-9020265 | Biosynthesis of aspirin-triggered D-series resolvins | 1.753256e-01 | 0.756 |
| R-HSA-167044 | Signalling to RAS | 2.037511e-01 | 0.691 |
| R-HSA-9758274 | Regulation of NF-kappa B signaling | 1.607373e-01 | 0.794 |
| R-HSA-1227986 | Signaling by ERBB2 | 1.201125e-01 | 0.920 |
| R-HSA-8876384 | Listeria monocytogenes entry into host cells | 2.107041e-01 | 0.676 |
| R-HSA-162587 | HIV Life Cycle | 1.986565e-01 | 0.702 |
| R-HSA-8934903 | Receptor Mediated Mitophagy | 1.076311e-01 | 0.968 |
| R-HSA-210990 | PECAM1 interactions | 1.154172e-01 | 0.938 |
| R-HSA-9023661 | Biosynthesis of E-series 18(R)-resolvins | 1.458928e-01 | 0.836 |
| R-HSA-69183 | Processive synthesis on the lagging strand | 1.533473e-01 | 0.814 |
| R-HSA-9711097 | Cellular response to starvation | 2.008870e-01 | 0.697 |
| R-HSA-2022377 | Metabolism of Angiotensinogen to Angiotensins | 2.107041e-01 | 0.676 |
| R-HSA-5673001 | RAF/MAP kinase cascade | 1.360504e-01 | 0.866 |
| R-HSA-8849932 | Synaptic adhesion-like molecules | 1.825250e-01 | 0.739 |
| R-HSA-2029482 | Regulation of actin dynamics for phagocytic cup formation | 1.617879e-01 | 0.791 |
| R-HSA-5684996 | MAPK1/MAPK3 signaling | 1.453232e-01 | 0.838 |
| R-HSA-392499 | Metabolism of proteins | 1.117239e-01 | 0.952 |
| R-HSA-9006931 | Signaling by Nuclear Receptors | 1.211960e-01 | 0.917 |
| R-HSA-8876725 | Protein methylation | 1.533473e-01 | 0.814 |
| R-HSA-9018896 | Biosynthesis of E-series 18(S)-resolvins | 2.037511e-01 | 0.691 |
| R-HSA-391160 | Signal regulatory protein family interactions | 1.458928e-01 | 0.836 |
| R-HSA-446353 | Cell-extracellular matrix interactions | 1.533473e-01 | 0.814 |
| R-HSA-9010553 | Regulation of expression of SLITs and ROBOs | 1.875991e-01 | 0.727 |
| R-HSA-162582 | Signal Transduction | 1.080570e-01 | 0.966 |
| R-HSA-9772572 | Early SARS-CoV-2 Infection Events | 1.143986e-01 | 0.942 |
| R-HSA-1295596 | Spry regulation of FGF signaling | 1.533473e-01 | 0.814 |
| R-HSA-180292 | GAB1 signalosome | 1.825250e-01 | 0.739 |
| R-HSA-69186 | Lagging Strand Synthesis | 2.037511e-01 | 0.691 |
| R-HSA-1660499 | Synthesis of PIPs at the plasma membrane | 1.258958e-01 | 0.900 |
| R-HSA-435354 | Zinc transporters | 1.458928e-01 | 0.836 |
| R-HSA-373753 | Nephrin family interactions | 1.967373e-01 | 0.706 |
| R-HSA-9705671 | SARS-CoV-2 activates/modulates innate and adaptive immune responses | 1.660119e-01 | 0.780 |
| R-HSA-2408522 | Selenoamino acid metabolism | 2.143920e-01 | 0.669 |
| R-HSA-9705683 | SARS-CoV-2-host interactions | 1.738166e-01 | 0.760 |
| R-HSA-9856651 | MITF-M-dependent gene expression | 1.832229e-01 | 0.737 |
| R-HSA-376176 | Signaling by ROBO receptors | 1.315996e-01 | 0.881 |
| R-HSA-373755 | Semaphorin interactions | 1.288122e-01 | 0.890 |
| R-HSA-177929 | Signaling by EGFR | 1.087583e-01 | 0.964 |
| R-HSA-9679504 | Translation of Replicase and Assembly of the Replication Transcription Complex | 1.825250e-01 | 0.739 |
| R-HSA-162594 | Early Phase of HIV Life Cycle | 2.037511e-01 | 0.691 |
| R-HSA-109581 | Apoptosis | 2.098679e-01 | 0.678 |
| R-HSA-6803529 | FGFR2 alternative splicing | 2.175968e-01 | 0.662 |
| R-HSA-2173788 | Downregulation of TGF-beta receptor signaling | 2.175968e-01 | 0.662 |
| R-HSA-9018676 | Biosynthesis of D-series resolvins | 2.175968e-01 | 0.662 |
| R-HSA-9694676 | Translation of Replicase and Assembly of the Replication Transcription Complex | 2.175968e-01 | 0.662 |
| R-HSA-5688426 | Deubiquitination | 2.218589e-01 | 0.654 |
| R-HSA-9694516 | SARS-CoV-2 Infection | 2.233141e-01 | 0.651 |
| R-HSA-912526 | Interleukin receptor SHC signaling | 2.244298e-01 | 0.649 |
| R-HSA-446210 | Synthesis of UDP-N-acetyl-glucosamine | 2.244298e-01 | 0.649 |
| R-HSA-3000170 | Syndecan interactions | 2.244298e-01 | 0.649 |
| R-HSA-5674400 | Constitutive Signaling by AKT1 E17K in Cancer | 2.244298e-01 | 0.649 |
| R-HSA-1280218 | Adaptive Immune System | 2.254303e-01 | 0.647 |
| R-HSA-6791226 | Major pathway of rRNA processing in the nucleolus and cytosol | 2.303855e-01 | 0.638 |
| R-HSA-75067 | Processing of Capped Intronless Pre-mRNA | 2.312035e-01 | 0.636 |
| R-HSA-9665686 | Signaling by ERBB2 TMD/JMD mutants | 2.312035e-01 | 0.636 |
| R-HSA-933542 | TRAF6 mediated NF-kB activation | 2.312035e-01 | 0.636 |
| R-HSA-418592 | ADP signalling through P2Y purinoceptor 1 | 2.312035e-01 | 0.636 |
| R-HSA-5693554 | Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD... | 2.379185e-01 | 0.624 |
| R-HSA-9932451 | SWI/SNF chromatin remodelers | 2.379185e-01 | 0.624 |
| R-HSA-9932444 | ATP-dependent chromatin remodelers | 2.379185e-01 | 0.624 |
| R-HSA-2160916 | Hyaluronan degradation | 2.379185e-01 | 0.624 |
| R-HSA-9620244 | Long-term potentiation | 2.379185e-01 | 0.624 |
| R-HSA-5218921 | VEGFR2 mediated cell proliferation | 2.379185e-01 | 0.624 |
| R-HSA-1266695 | Interleukin-7 signaling | 2.379185e-01 | 0.624 |
| R-HSA-5601884 | PIWI-interacting RNA (piRNA) biogenesis | 2.379185e-01 | 0.624 |
| R-HSA-1643713 | Signaling by EGFR in Cancer | 2.445752e-01 | 0.612 |
| R-HSA-8874081 | MET activates PTK2 signaling | 2.445752e-01 | 0.612 |
| R-HSA-110373 | Resolution of AP sites via the multiple-nucleotide patch replacement pathway | 2.445752e-01 | 0.612 |
| R-HSA-525793 | Myogenesis | 2.445752e-01 | 0.612 |
| R-HSA-8934593 | Regulation of RUNX1 Expression and Activity | 2.445752e-01 | 0.612 |
| R-HSA-2122948 | Activated NOTCH1 Transmits Signal to the Nucleus | 2.445752e-01 | 0.612 |
| R-HSA-975871 | MyD88 cascade initiated on plasma membrane | 2.474201e-01 | 0.607 |
| R-HSA-168176 | Toll Like Receptor 5 (TLR5) Cascade | 2.474201e-01 | 0.607 |
| R-HSA-168142 | Toll Like Receptor 10 (TLR10) Cascade | 2.474201e-01 | 0.607 |
| R-HSA-167243 | Tat-mediated HIV elongation arrest and recovery | 2.511742e-01 | 0.600 |
| R-HSA-167238 | Pausing and recovery of Tat-mediated HIV elongation | 2.511742e-01 | 0.600 |
| R-HSA-3928663 | EPHA-mediated growth cone collapse | 2.511742e-01 | 0.600 |
| R-HSA-174414 | Processive synthesis on the C-strand of the telomere | 2.511742e-01 | 0.600 |
| R-HSA-9006115 | Signaling by NTRK2 (TRKB) | 2.511742e-01 | 0.600 |
| R-HSA-70171 | Glycolysis | 2.538791e-01 | 0.595 |
| R-HSA-9020702 | Interleukin-1 signaling | 2.571103e-01 | 0.590 |
| R-HSA-167287 | HIV elongation arrest and recovery | 2.577159e-01 | 0.589 |
| R-HSA-167290 | Pausing and recovery of HIV elongation | 2.577159e-01 | 0.589 |
| R-HSA-622312 | Inflammasomes | 2.577159e-01 | 0.589 |
| R-HSA-8940973 | RUNX2 regulates osteoblast differentiation | 2.577159e-01 | 0.589 |
| R-HSA-5654732 | Negative regulation of FGFR3 signaling | 2.577159e-01 | 0.589 |
| R-HSA-5620971 | Pyroptosis | 2.577159e-01 | 0.589 |
| R-HSA-1483255 | PI Metabolism | 2.603422e-01 | 0.584 |
| R-HSA-9709570 | Impaired BRCA2 binding to RAD51 | 2.642009e-01 | 0.578 |
| R-HSA-9664565 | Signaling by ERBB2 KD Mutants | 2.642009e-01 | 0.578 |
| R-HSA-9018679 | Biosynthesis of EPA-derived SPMs | 2.642009e-01 | 0.578 |
| R-HSA-5654733 | Negative regulation of FGFR4 signaling | 2.642009e-01 | 0.578 |
| R-HSA-5619107 | Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC... | 2.706296e-01 | 0.568 |
| R-HSA-68962 | Activation of the pre-replicative complex | 2.706296e-01 | 0.568 |
| R-HSA-1227990 | Signaling by ERBB2 in Cancer | 2.706296e-01 | 0.568 |
| R-HSA-456926 | Thrombin signalling through proteinase activated receptors (PARs) | 2.706296e-01 | 0.568 |
| R-HSA-8863795 | Downregulation of ERBB2 signaling | 2.706296e-01 | 0.568 |
| R-HSA-1474151 | Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation | 2.706296e-01 | 0.568 |
| R-HSA-8868773 | rRNA processing in the nucleus and cytosol | 2.724033e-01 | 0.565 |
| R-HSA-168164 | Toll Like Receptor 3 (TLR3) Cascade | 2.732726e-01 | 0.563 |
| R-HSA-1855196 | IP3 and IP4 transport between cytosol and nucleus | 2.770026e-01 | 0.558 |
| R-HSA-1855229 | IP6 and IP7 transport between cytosol and nucleus | 2.770026e-01 | 0.558 |
| R-HSA-186763 | Downstream signal transduction | 2.770026e-01 | 0.558 |
| R-HSA-69239 | Synthesis of DNA | 2.797359e-01 | 0.553 |
| R-HSA-211000 | Gene Silencing by RNA | 2.797359e-01 | 0.553 |
| R-HSA-9700206 | Signaling by ALK in cancer | 2.797359e-01 | 0.553 |
| R-HSA-9725370 | Signaling by ALK fusions and activated point mutants | 2.797359e-01 | 0.553 |
| R-HSA-9734779 | Developmental Cell Lineages of the Integumentary System | 2.829662e-01 | 0.548 |
| R-HSA-975138 | TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation | 2.829662e-01 | 0.548 |
| R-HSA-111465 | Apoptotic cleavage of cellular proteins | 2.833203e-01 | 0.548 |
| R-HSA-975155 | MyD88 dependent cascade initiated on endosome | 2.861954e-01 | 0.543 |
| R-HSA-937061 | TRIF (TICAM1)-mediated TLR4 signaling | 2.894232e-01 | 0.538 |
| R-HSA-166166 | MyD88-independent TLR4 cascade | 2.894232e-01 | 0.538 |
| R-HSA-1855170 | IPs transport between nucleus and cytosol | 2.895831e-01 | 0.538 |
| R-HSA-159227 | Transport of the SLBP independent Mature mRNA | 2.895831e-01 | 0.538 |
| R-HSA-5685938 | HDR through Single Strand Annealing (SSA) | 2.895831e-01 | 0.538 |
| R-HSA-5693568 | Resolution of D-loop Structures through Holliday Junction Intermediates | 2.895831e-01 | 0.538 |
| R-HSA-176187 | Activation of ATR in response to replication stress | 2.895831e-01 | 0.538 |
| R-HSA-8939243 | RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not kno... | 2.895831e-01 | 0.538 |
| R-HSA-5654726 | Negative regulation of FGFR1 signaling | 2.895831e-01 | 0.538 |
| R-HSA-159230 | Transport of the SLBP Dependant Mature mRNA | 2.957917e-01 | 0.529 |
| R-HSA-5693537 | Resolution of D-Loop Structures | 2.957917e-01 | 0.529 |
| R-HSA-170822 | Regulation of Glucokinase by Glucokinase Regulatory Protein | 2.957917e-01 | 0.529 |
| R-HSA-168181 | Toll Like Receptor 7/8 (TLR7/8) Cascade | 2.990959e-01 | 0.524 |
| R-HSA-5696400 | Dual Incision in GG-NER | 3.019463e-01 | 0.520 |
| R-HSA-9680350 | Signaling by CSF1 (M-CSF) in myeloid cells | 3.019463e-01 | 0.520 |
| R-HSA-9675136 | Diseases of DNA Double-Strand Break Repair | 3.019463e-01 | 0.520 |
| R-HSA-9701190 | Defective homologous recombination repair (HRR) due to BRCA2 loss of function | 3.019463e-01 | 0.520 |
| R-HSA-203615 | eNOS activation | 3.019463e-01 | 0.520 |
| R-HSA-5686938 | Regulation of TLR by endogenous ligand | 3.019463e-01 | 0.520 |
| R-HSA-180746 | Nuclear import of Rev protein | 3.019463e-01 | 0.520 |
| R-HSA-2142845 | Hyaluronan metabolism | 3.019463e-01 | 0.520 |
| R-HSA-5673000 | RAF activation | 3.019463e-01 | 0.520 |
| R-HSA-392518 | Signal amplification | 3.019463e-01 | 0.520 |
| R-HSA-3301854 | Nuclear Pore Complex (NPC) Disassembly | 3.080475e-01 | 0.511 |
| R-HSA-5693616 | Presynaptic phase of homologous DNA pairing and strand exchange | 3.080475e-01 | 0.511 |
| R-HSA-187687 | Signalling to ERKs | 3.080475e-01 | 0.511 |
| R-HSA-168138 | Toll Like Receptor 9 (TLR9) Cascade | 3.087484e-01 | 0.510 |
| R-HSA-432720 | Lysosome Vesicle Biogenesis | 3.140958e-01 | 0.503 |
| R-HSA-114604 | GPVI-mediated activation cascade | 3.140958e-01 | 0.503 |
| R-HSA-8941326 | RUNX2 regulates bone development | 3.140958e-01 | 0.503 |
| R-HSA-6804757 | Regulation of TP53 Degradation | 3.140958e-01 | 0.503 |
| R-HSA-70326 | Glucose metabolism | 3.183752e-01 | 0.497 |
| R-HSA-6802948 | Signaling by high-kinase activity BRAF mutants | 3.200916e-01 | 0.495 |
| R-HSA-180910 | Vpr-mediated nuclear import of PICs | 3.200916e-01 | 0.495 |
| R-HSA-196757 | Metabolism of folate and pterines | 3.200916e-01 | 0.495 |
| R-HSA-5693538 | Homology Directed Repair | 3.215775e-01 | 0.493 |
| R-HSA-166058 | MyD88:MAL(TIRAP) cascade initiated on plasma membrane | 3.247763e-01 | 0.488 |
| R-HSA-168188 | Toll Like Receptor TLR6:TLR2 Cascade | 3.247763e-01 | 0.488 |
| R-HSA-5693579 | Homologous DNA Pairing and Strand Exchange | 3.260353e-01 | 0.487 |
| R-HSA-202131 | Metabolism of nitric oxide: NOS3 activation and regulation | 3.260353e-01 | 0.487 |
| R-HSA-8875878 | MET promotes cell motility | 3.260353e-01 | 0.487 |
| R-HSA-165054 | Rev-mediated nuclear export of HIV RNA | 3.260353e-01 | 0.487 |
| R-HSA-68875 | Mitotic Prophase | 3.279712e-01 | 0.484 |
| R-HSA-397014 | Muscle contraction | 3.318853e-01 | 0.479 |
| R-HSA-167200 | Formation of HIV-1 elongation complex containing HIV-1 Tat | 3.319274e-01 | 0.479 |
| R-HSA-168276 | NS1 Mediated Effects on Host Pathways | 3.319274e-01 | 0.479 |
| R-HSA-201556 | Signaling by ALK | 3.319274e-01 | 0.479 |
| R-HSA-6806003 | Regulation of TP53 Expression and Degradation | 3.319274e-01 | 0.479 |
| R-HSA-9730414 | MITF-M-regulated melanocyte development | 3.342722e-01 | 0.476 |
| R-HSA-168179 | Toll Like Receptor TLR1:TLR2 Cascade | 3.343490e-01 | 0.476 |
| R-HSA-181438 | Toll Like Receptor 2 (TLR2) Cascade | 3.343490e-01 | 0.476 |
| R-HSA-167246 | Tat-mediated elongation of the HIV-1 transcript | 3.377684e-01 | 0.471 |
| R-HSA-167152 | Formation of HIV elongation complex in the absence of HIV Tat | 3.377684e-01 | 0.471 |
| R-HSA-8941858 | Regulation of RUNX3 expression and activity | 3.377684e-01 | 0.471 |
| R-HSA-167169 | HIV Transcription Elongation | 3.377684e-01 | 0.471 |
| R-HSA-177243 | Interactions of Rev with host cellular proteins | 3.377684e-01 | 0.471 |
| R-HSA-176033 | Interactions of Vpr with host cellular proteins | 3.377684e-01 | 0.471 |
| R-HSA-5260271 | Diseases of Immune System | 3.377684e-01 | 0.471 |
| R-HSA-5602358 | Diseases associated with the TLR signaling cascade | 3.377684e-01 | 0.471 |
| R-HSA-5696395 | Formation of Incision Complex in GG-NER | 3.377684e-01 | 0.471 |
| R-HSA-1251985 | Nuclear signaling by ERBB4 | 3.377684e-01 | 0.471 |
| R-HSA-451927 | Interleukin-2 family signaling | 3.377684e-01 | 0.471 |
| R-HSA-168271 | Transport of Ribonucleoproteins into the Host Nucleus | 3.435587e-01 | 0.464 |
| R-HSA-73933 | Resolution of Abasic Sites (AP sites) | 3.435587e-01 | 0.464 |
| R-HSA-9656223 | Signaling by RAF1 mutants | 3.492987e-01 | 0.457 |
| R-HSA-5674135 | MAP2K and MAPK activation | 3.492987e-01 | 0.457 |
| R-HSA-174417 | Telomere C-strand (Lagging Strand) Synthesis | 3.492987e-01 | 0.457 |
| R-HSA-69481 | G2/M Checkpoints | 3.533739e-01 | 0.452 |
| R-HSA-512988 | Interleukin-3, Interleukin-5 and GM-CSF signaling | 3.549889e-01 | 0.450 |
| R-HSA-379716 | Cytosolic tRNA aminoacylation | 3.549889e-01 | 0.450 |
| R-HSA-2173789 | TGF-beta receptor signaling activates SMADs | 3.606296e-01 | 0.443 |
| R-HSA-8854214 | TBC/RABGAPs | 3.606296e-01 | 0.443 |
| R-HSA-5654743 | Signaling by FGFR4 | 3.606296e-01 | 0.443 |
| R-HSA-373752 | Netrin-1 signaling | 3.662214e-01 | 0.436 |
| R-HSA-3928662 | EPHB-mediated forward signaling | 3.662214e-01 | 0.436 |
| R-HSA-3214858 | RMTs methylate histone arginines | 3.662214e-01 | 0.436 |
| R-HSA-69236 | G1 Phase | 3.662214e-01 | 0.436 |
| R-HSA-69231 | Cyclin D associated events in G1 | 3.662214e-01 | 0.436 |
| R-HSA-2142691 | Synthesis of Leukotrienes (LT) and Eoxins (EX) | 3.662214e-01 | 0.436 |
| R-HSA-162906 | HIV Infection | 3.676206e-01 | 0.435 |
| R-HSA-168333 | NEP/NS2 Interacts with the Cellular Export Machinery | 3.717646e-01 | 0.430 |
| R-HSA-9824585 | Regulation of MITF-M-dependent genes involved in pigmentation | 3.717646e-01 | 0.430 |
| R-HSA-5654741 | Signaling by FGFR3 | 3.717646e-01 | 0.430 |
| R-HSA-9909396 | Circadian clock | 3.722098e-01 | 0.429 |
| R-HSA-6802955 | Paradoxical activation of RAF signaling by kinase inactive BRAF | 3.772597e-01 | 0.423 |
| R-HSA-6802946 | Signaling by moderate kinase activity BRAF mutants | 3.772597e-01 | 0.423 |
| R-HSA-9649948 | Signaling downstream of RAS mutants | 3.772597e-01 | 0.423 |
| R-HSA-6802949 | Signaling by RAS mutants | 3.772597e-01 | 0.423 |
| R-HSA-72695 | Formation of the ternary complex, and subsequently, the 43S complex | 3.772597e-01 | 0.423 |
| R-HSA-168274 | Export of Viral Ribonucleoproteins from Nucleus | 3.772597e-01 | 0.423 |
| R-HSA-9675135 | Diseases of DNA repair | 3.772597e-01 | 0.423 |
| R-HSA-9664424 | Cell recruitment (pro-inflammatory response) | 3.772597e-01 | 0.423 |
| R-HSA-9660826 | Purinergic signaling in leishmaniasis infection | 3.772597e-01 | 0.423 |
| R-HSA-9839373 | Signaling by TGFBR3 | 3.772597e-01 | 0.423 |
| R-HSA-72312 | rRNA processing | 3.794739e-01 | 0.421 |
| R-HSA-3928665 | EPH-ephrin mediated repulsion of cells | 3.827071e-01 | 0.417 |
| R-HSA-9634597 | GPER1 signaling | 3.881071e-01 | 0.411 |
| R-HSA-425410 | Metal ion SLC transporters | 3.881071e-01 | 0.411 |
| R-HSA-9820952 | Respiratory Syncytial Virus Infection Pathway | 3.908262e-01 | 0.408 |
| R-HSA-9679506 | SARS-CoV Infections | 3.917985e-01 | 0.407 |
| R-HSA-389661 | Glyoxylate metabolism and glycine degradation | 3.934602e-01 | 0.405 |
| R-HSA-9766229 | Degradation of CDH1 | 3.934602e-01 | 0.405 |
| R-HSA-2162123 | Synthesis of Prostaglandins (PG) and Thromboxanes (TX) | 3.987668e-01 | 0.399 |
| R-HSA-9664417 | Leishmania phagocytosis | 4.000436e-01 | 0.398 |
| R-HSA-9664422 | FCGR3A-mediated phagocytosis | 4.000436e-01 | 0.398 |
| R-HSA-9664407 | Parasite infection | 4.000436e-01 | 0.398 |
| R-HSA-597592 | Post-translational protein modification | 4.004814e-01 | 0.397 |
| R-HSA-162599 | Late Phase of HIV Life Cycle | 4.091963e-01 | 0.388 |
| R-HSA-112382 | Formation of RNA Pol II elongation complex | 4.092422e-01 | 0.388 |
| R-HSA-68949 | Orc1 removal from chromatin | 4.092422e-01 | 0.388 |
| R-HSA-75955 | RNA Polymerase II Transcription Elongation | 4.144117e-01 | 0.383 |
| R-HSA-72649 | Translation initiation complex formation | 4.195363e-01 | 0.377 |
| R-HSA-453279 | Mitotic G1 phase and G1/S transition | 4.212944e-01 | 0.375 |
| R-HSA-3700989 | Transcriptional Regulation by TP53 | 4.216944e-01 | 0.375 |
| R-HSA-166016 | Toll Like Receptor 4 (TLR4) Cascade | 4.272965e-01 | 0.369 |
| R-HSA-69242 | S Phase | 4.272965e-01 | 0.369 |
| R-HSA-166520 | Signaling by NTRKs | 4.272965e-01 | 0.369 |
| R-HSA-72702 | Ribosomal scanning and start codon recognition | 4.296523e-01 | 0.367 |
| R-HSA-193648 | NRAGE signals death through JNK | 4.296523e-01 | 0.367 |
| R-HSA-5654736 | Signaling by FGFR1 | 4.296523e-01 | 0.367 |
| R-HSA-2980766 | Nuclear Envelope Breakdown | 4.346444e-01 | 0.362 |
| R-HSA-9764561 | Regulation of CDH1 Function | 4.346444e-01 | 0.362 |
| R-HSA-388841 | Regulation of T cell activation by CD28 family | 4.355829e-01 | 0.361 |
| R-HSA-2142753 | Arachidonate metabolism | 4.392031e-01 | 0.357 |
| R-HSA-6782135 | Dual incision in TC-NER | 4.395932e-01 | 0.357 |
| R-HSA-72662 | Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub... | 4.395932e-01 | 0.357 |
| R-HSA-69620 | Cell Cycle Checkpoints | 4.401821e-01 | 0.356 |
| R-HSA-69306 | DNA Replication | 4.421589e-01 | 0.354 |
| R-HSA-5693532 | DNA Double-Strand Break Repair | 4.421589e-01 | 0.354 |
| R-HSA-9609507 | Protein localization | 4.421589e-01 | 0.354 |
| R-HSA-194441 | Metabolism of non-coding RNA | 4.444989e-01 | 0.352 |
| R-HSA-191859 | snRNP Assembly | 4.444989e-01 | 0.352 |
| R-HSA-9033241 | Peroxisomal protein import | 4.444989e-01 | 0.352 |
| R-HSA-180786 | Extension of Telomeres | 4.444989e-01 | 0.352 |
| R-HSA-9845323 | Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) | 4.493620e-01 | 0.347 |
| R-HSA-379724 | tRNA Aminoacylation | 4.493620e-01 | 0.347 |
| R-HSA-168325 | Viral Messenger RNA Synthesis | 4.541829e-01 | 0.343 |
| R-HSA-6784531 | tRNA processing in the nucleus | 4.589618e-01 | 0.338 |
| R-HSA-1268020 | Mitochondrial protein import | 4.589618e-01 | 0.338 |
| R-HSA-186797 | Signaling by PDGF | 4.589618e-01 | 0.338 |
| R-HSA-375165 | NCAM signaling for neurite out-growth | 4.589618e-01 | 0.338 |
| R-HSA-877300 | Interferon gamma signaling | 4.597130e-01 | 0.338 |
| R-HSA-8848021 | Signaling by PTK6 | 4.636991e-01 | 0.334 |
| R-HSA-9006927 | Signaling by Non-Receptor Tyrosine Kinases | 4.636991e-01 | 0.334 |
| R-HSA-168643 | Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali... | 4.683953e-01 | 0.329 |
| R-HSA-6802952 | Signaling by BRAF and RAF1 fusions | 4.730507e-01 | 0.325 |
| R-HSA-5685942 | HDR through Homologous Recombination (HRR) | 4.822403e-01 | 0.317 |
| R-HSA-196807 | Nicotinate metabolism | 4.822403e-01 | 0.317 |
| R-HSA-9824439 | Bacterial Infection Pathways | 4.861667e-01 | 0.313 |
| R-HSA-167172 | Transcription of the HIV genome | 4.867752e-01 | 0.313 |
| R-HSA-9824443 | Parasitic Infection Pathways | 4.919620e-01 | 0.308 |
| R-HSA-9658195 | Leishmania infection | 4.919620e-01 | 0.308 |
| R-HSA-8978934 | Metabolism of cofactors | 5.001448e-01 | 0.301 |
| R-HSA-5578749 | Transcriptional regulation by small RNAs | 5.045240e-01 | 0.297 |
| R-HSA-9678108 | SARS-CoV-1 Infection | 5.076632e-01 | 0.294 |
| R-HSA-69052 | Switching of origins to a post-replicative state | 5.088651e-01 | 0.293 |
| R-HSA-204998 | Cell death signalling via NRAGE, NRIF and NADE | 5.088651e-01 | 0.293 |
| R-HSA-674695 | RNA Polymerase II Pre-transcription Events | 5.131685e-01 | 0.290 |
| R-HSA-69473 | G2/M DNA damage checkpoint | 5.131685e-01 | 0.290 |
| R-HSA-1236394 | Signaling by ERBB4 | 5.131685e-01 | 0.290 |
| R-HSA-6781827 | Transcription-Coupled Nucleotide Excision Repair (TC-NER) | 5.174344e-01 | 0.286 |
| R-HSA-1169408 | ISG15 antiviral mechanism | 5.174344e-01 | 0.286 |
| R-HSA-3000171 | Non-integrin membrane-ECM interactions | 5.174344e-01 | 0.286 |
| R-HSA-5689603 | UCH proteinases | 5.216632e-01 | 0.283 |
| R-HSA-1980143 | Signaling by NOTCH1 | 5.216632e-01 | 0.283 |
| R-HSA-6796648 | TP53 Regulates Transcription of DNA Repair Genes | 5.300107e-01 | 0.276 |
| R-HSA-416482 | G alpha (12/13) signalling events | 5.300107e-01 | 0.276 |
| R-HSA-216083 | Integrin cell surface interactions | 5.300107e-01 | 0.276 |
| R-HSA-6806834 | Signaling by MET | 5.382136e-01 | 0.269 |
| R-HSA-9856530 | High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR... | 5.382136e-01 | 0.269 |
| R-HSA-5693607 | Processing of DNA double-strand break ends | 5.422615e-01 | 0.266 |
| R-HSA-9018677 | Biosynthesis of DHA-derived SPMs | 5.422615e-01 | 0.266 |
| R-HSA-168898 | Toll-like Receptor Cascades | 5.502140e-01 | 0.259 |
| R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | 5.527872e-01 | 0.257 |
| R-HSA-5696399 | Global Genome Nucleotide Excision Repair (GG-NER) | 5.541952e-01 | 0.256 |
| R-HSA-6802957 | Oncogenic MAPK signaling | 5.581041e-01 | 0.253 |
| R-HSA-6794362 | Protein-protein interactions at synapses | 5.581041e-01 | 0.253 |
| R-HSA-141424 | Amplification of signal from the kinetochores | 5.619789e-01 | 0.250 |
| R-HSA-141444 | Amplification of signal from unattached kinetochores via a MAD2 inhibitory si... | 5.619789e-01 | 0.250 |
| R-HSA-163841 | Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation | 5.658200e-01 | 0.247 |
| R-HSA-1500931 | Cell-Cell communication | 5.659737e-01 | 0.247 |
| R-HSA-70268 | Pyruvate metabolism | 5.696276e-01 | 0.244 |
| R-HSA-1236974 | ER-Phagosome pathway | 5.771436e-01 | 0.239 |
| R-HSA-73884 | Base Excision Repair | 5.808527e-01 | 0.236 |
| R-HSA-2682334 | EPH-Ephrin signaling | 5.917870e-01 | 0.228 |
| R-HSA-9772573 | Late SARS-CoV-2 Infection Events | 5.917870e-01 | 0.228 |
| R-HSA-68867 | Assembly of the pre-replicative complex | 5.953684e-01 | 0.225 |
| R-HSA-2029481 | FCGR activation | 5.953684e-01 | 0.225 |
| R-HSA-381340 | Transcriptional regulation of white adipocyte differentiation | 6.093850e-01 | 0.215 |
| R-HSA-1296071 | Potassium Channels | 6.093850e-01 | 0.215 |
| R-HSA-5607764 | CLEC7A (Dectin-1) signaling | 6.093850e-01 | 0.215 |
| R-HSA-170834 | Signaling by TGF-beta Receptor Complex | 6.128131e-01 | 0.213 |
| R-HSA-8878159 | Transcriptional regulation by RUNX3 | 6.128131e-01 | 0.213 |
| R-HSA-157579 | Telomere Maintenance | 6.128131e-01 | 0.213 |
| R-HSA-193704 | p75 NTR receptor-mediated signalling | 6.195800e-01 | 0.208 |
| R-HSA-69618 | Mitotic Spindle Checkpoint | 6.229193e-01 | 0.206 |
| R-HSA-9842860 | Regulation of endogenous retroelements | 6.295108e-01 | 0.201 |
| R-HSA-2559580 | Oxidative Stress Induced Senescence | 6.295108e-01 | 0.201 |
| R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | 6.295108e-01 | 0.201 |
| R-HSA-9937383 | Mitochondrial ribosome-associated quality control | 6.327635e-01 | 0.199 |
| R-HSA-8856825 | Cargo recognition for clathrin-mediated endocytosis | 6.359879e-01 | 0.197 |
| R-HSA-9860931 | Response of endothelial cells to shear stress | 6.359879e-01 | 0.197 |
| R-HSA-8878171 | Transcriptional regulation by RUNX1 | 6.362970e-01 | 0.196 |
| R-HSA-5619507 | Activation of HOX genes during differentiation | 6.391841e-01 | 0.194 |
| R-HSA-5617472 | Activation of anterior HOX genes in hindbrain development during early embryogen... | 6.391841e-01 | 0.194 |
| R-HSA-5696398 | Nucleotide Excision Repair | 6.423525e-01 | 0.192 |
| R-HSA-168249 | Innate Immune System | 6.423737e-01 | 0.192 |
| R-HSA-196849 | Metabolism of water-soluble vitamins and cofactors | 6.450289e-01 | 0.190 |
| R-HSA-73894 | DNA Repair | 6.491820e-01 | 0.188 |
| R-HSA-1236975 | Antigen processing-Cross presentation | 6.516928e-01 | 0.186 |
| R-HSA-69002 | DNA Replication Pre-Initiation | 6.547521e-01 | 0.184 |
| R-HSA-196854 | Metabolism of vitamins and cofactors | 6.561631e-01 | 0.183 |
| R-HSA-202733 | Cell surface interactions at the vascular wall | 6.599135e-01 | 0.181 |
| R-HSA-1483249 | Inositol phosphate metabolism | 6.637709e-01 | 0.178 |
| R-HSA-5693567 | HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA) | 6.696530e-01 | 0.174 |
| R-HSA-9855142 | Cellular responses to mechanical stimuli | 6.696530e-01 | 0.174 |
| R-HSA-2980736 | Peptide hormone metabolism | 6.839151e-01 | 0.165 |
| R-HSA-9007101 | Rab regulation of trafficking | 6.839151e-01 | 0.165 |
| R-HSA-8878166 | Transcriptional regulation by RUNX2 | 6.894473e-01 | 0.161 |
| R-HSA-73886 | Chromosome Maintenance | 6.948832e-01 | 0.158 |
| R-HSA-162909 | Host Interactions of HIV factors | 7.028605e-01 | 0.153 |
| R-HSA-9841922 | MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesi... | 7.080633e-01 | 0.150 |
| R-HSA-9851695 | Epigenetic regulation of adipogenesis genes by MLL3 and MLL4 complexes | 7.080633e-01 | 0.150 |
| R-HSA-9818564 | Epigenetic regulation of gene expression by MLL3 and MLL4 complexes | 7.080633e-01 | 0.150 |
| R-HSA-69206 | G1/S Transition | 7.080633e-01 | 0.150 |
| R-HSA-9664323 | FCGR3A-mediated IL10 synthesis | 7.106307e-01 | 0.148 |
| R-HSA-9734767 | Developmental Cell Lineages | 7.108762e-01 | 0.148 |
| R-HSA-187037 | Signaling by NTRK1 (TRKA) | 7.156984e-01 | 0.145 |
| R-HSA-9843745 | Adipogenesis | 7.255709e-01 | 0.139 |
| R-HSA-446219 | Synthesis of substrates in N-glycan biosythesis | 7.255709e-01 | 0.139 |
| R-HSA-1474228 | Degradation of the extracellular matrix | 7.279854e-01 | 0.138 |
| R-HSA-211945 | Phase I - Functionalization of compounds | 7.372923e-01 | 0.132 |
| R-HSA-446728 | Cell junction organization | 7.372923e-01 | 0.132 |
| R-HSA-5368287 | Mitochondrial translation | 7.443062e-01 | 0.128 |
| R-HSA-8856828 | Clathrin-mediated endocytosis | 7.575190e-01 | 0.121 |
| R-HSA-9018678 | Biosynthesis of specialized proresolving mediators (SPMs) | 7.575190e-01 | 0.121 |
| R-HSA-1483257 | Phospholipid metabolism | 7.647353e-01 | 0.116 |
| R-HSA-2173782 | Binding and Uptake of Ligands by Scavenger Receptors | 7.720793e-01 | 0.112 |
| R-HSA-9917777 | Epigenetic regulation by WDR5-containing histone modifying complexes | 7.800062e-01 | 0.108 |
| R-HSA-73887 | Death Receptor Signaling | 7.800062e-01 | 0.108 |
| R-HSA-1989781 | PPARA activates gene expression | 7.819447e-01 | 0.107 |
| R-HSA-9610379 | HCMV Late Events | 7.857711e-01 | 0.105 |
| R-HSA-400206 | Regulation of lipid metabolism by PPARalpha | 7.857711e-01 | 0.105 |
| R-HSA-446193 | Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, L... | 7.857711e-01 | 0.105 |
| R-HSA-71387 | Metabolism of carbohydrates and carbohydrate derivatives | 7.898427e-01 | 0.102 |
| R-HSA-9006936 | Signaling by TGFB family members | 7.913860e-01 | 0.102 |
| R-HSA-5619102 | SLC transporter disorders | 8.039257e-01 | 0.095 |
| R-HSA-212165 | Epigenetic regulation of gene expression | 8.045544e-01 | 0.094 |
| R-HSA-72306 | tRNA processing | 8.107521e-01 | 0.091 |
| R-HSA-418555 | G alpha (s) signalling events | 8.124215e-01 | 0.090 |
| R-HSA-5621481 | C-type lectin receptors (CLRs) | 8.124215e-01 | 0.090 |
| R-HSA-71291 | Metabolism of amino acids and derivatives | 8.145244e-01 | 0.089 |
| R-HSA-1474244 | Extracellular matrix organization | 8.147857e-01 | 0.089 |
| R-HSA-9662851 | Anti-inflammatory response favouring Leishmania parasite infection | 8.157166e-01 | 0.088 |
| R-HSA-9664433 | Leishmania parasite growth and survival | 8.157166e-01 | 0.088 |
| R-HSA-9764274 | Regulation of Expression and Function of Type I Classical Cadherins | 8.157166e-01 | 0.088 |
| R-HSA-9764265 | Regulation of CDH1 Expression and Function | 8.157166e-01 | 0.088 |
| R-HSA-2559583 | Cellular Senescence | 8.268032e-01 | 0.083 |
| R-HSA-74160 | Gene expression (Transcription) | 8.428224e-01 | 0.074 |
| R-HSA-1630316 | Glycosaminoglycan metabolism | 8.456647e-01 | 0.073 |
| R-HSA-9759476 | Regulation of Homotypic Cell-Cell Adhesion | 8.497191e-01 | 0.071 |
| R-HSA-983169 | Class I MHC mediated antigen processing & presentation | 8.713132e-01 | 0.060 |
| R-HSA-418990 | Adherens junctions interactions | 8.774840e-01 | 0.057 |
| R-HSA-8951664 | Neddylation | 8.807077e-01 | 0.055 |
| R-HSA-8978868 | Fatty acid metabolism | 8.913214e-01 | 0.050 |
| R-HSA-3247509 | Chromatin modifying enzymes | 8.937313e-01 | 0.049 |
| R-HSA-73857 | RNA Polymerase II Transcription | 8.956535e-01 | 0.048 |
| R-HSA-157118 | Signaling by NOTCH | 8.992561e-01 | 0.046 |
| R-HSA-5619115 | Disorders of transmembrane transporters | 9.053421e-01 | 0.043 |
| R-HSA-4839726 | Chromatin organization | 9.070129e-01 | 0.042 |
| R-HSA-421270 | Cell-cell junction organization | 9.086545e-01 | 0.042 |
| R-HSA-416476 | G alpha (q) signalling events | 9.186449e-01 | 0.037 |
| R-HSA-983168 | Antigen processing: Ubiquitination & Proteasome degradation | 9.307106e-01 | 0.031 |
| R-HSA-212436 | Generic Transcription Pathway | 9.402271e-01 | 0.027 |
| R-HSA-211859 | Biological oxidations | 9.533765e-01 | 0.021 |
| R-HSA-1428517 | Aerobic respiration and respiratory electron transport | 9.591126e-01 | 0.018 |
| R-HSA-388396 | GPCR downstream signalling | 9.722665e-01 | 0.012 |
| R-HSA-425407 | SLC-mediated transmembrane transport | 9.754834e-01 | 0.011 |
| R-HSA-418594 | G alpha (i) signalling events | 9.775918e-01 | 0.010 |
| R-HSA-372790 | Signaling by GPCR | 9.845294e-01 | 0.007 |
| R-HSA-382551 | Transport of small molecules | 9.937365e-01 | 0.003 |
| R-HSA-556833 | Metabolism of lipids | 9.977074e-01 | 0.001 |
| R-HSA-9752946 | Expression and translocation of olfactory receptors | 9.993276e-01 | 0.000 |
| R-HSA-381753 | Olfactory Signaling Pathway | 9.996608e-01 | 0.000 |
| R-HSA-1430728 | Metabolism | 9.997761e-01 | 0.000 |
| R-HSA-9709957 | Sensory Perception | 9.999896e-01 | 0.000 |
Download
| kinase | JSD_mean | pearson_surrounding | kinase_max_IC_position | max_position_JSD |
|---|---|---|---|---|
NEK6 |
0.823 | 0.294 | -2 | 0.844 |
COT |
0.822 | 0.146 | 2 | 0.819 |
PRKD1 |
0.822 | 0.207 | -3 | 0.759 |
GCN2 |
0.819 | 0.184 | 2 | 0.796 |
PRKD2 |
0.816 | 0.176 | -3 | 0.712 |
DSTYK |
0.814 | 0.154 | 2 | 0.842 |
PIM3 |
0.814 | 0.126 | -3 | 0.751 |
ULK2 |
0.812 | 0.096 | 2 | 0.780 |
NEK7 |
0.812 | 0.182 | -3 | 0.760 |
SRPK1 |
0.811 | 0.129 | -3 | 0.715 |
RSK2 |
0.811 | 0.119 | -3 | 0.727 |
P90RSK |
0.811 | 0.115 | -3 | 0.733 |
CAMK1B |
0.811 | 0.100 | -3 | 0.777 |
PIM1 |
0.810 | 0.162 | -3 | 0.708 |
CLK3 |
0.809 | 0.090 | 1 | 0.779 |
PKN3 |
0.808 | 0.101 | -3 | 0.741 |
MAPKAPK3 |
0.808 | 0.130 | -3 | 0.720 |
CDKL5 |
0.808 | 0.115 | -3 | 0.750 |
RSK3 |
0.808 | 0.112 | -3 | 0.726 |
CDKL1 |
0.807 | 0.090 | -3 | 0.752 |
NEK9 |
0.806 | 0.149 | 2 | 0.825 |
TGFBR2 |
0.806 | 0.130 | -2 | 0.777 |
PRPK |
0.806 | -0.050 | -1 | 0.797 |
NDR1 |
0.805 | 0.091 | -3 | 0.739 |
WNK1 |
0.805 | 0.083 | -2 | 0.742 |
NDR2 |
0.804 | 0.074 | -3 | 0.733 |
PRKD3 |
0.804 | 0.140 | -3 | 0.707 |
MAPKAPK2 |
0.804 | 0.122 | -3 | 0.685 |
SRPK2 |
0.804 | 0.124 | -3 | 0.659 |
BMPR2 |
0.803 | 0.071 | -2 | 0.816 |
NUAK2 |
0.803 | 0.071 | -3 | 0.749 |
P70S6KB |
0.803 | 0.101 | -3 | 0.732 |
CDC7 |
0.803 | -0.011 | 1 | 0.772 |
MOS |
0.802 | 0.033 | 1 | 0.833 |
NLK |
0.802 | 0.031 | 1 | 0.798 |
HIPK4 |
0.801 | 0.081 | 1 | 0.802 |
TSSK2 |
0.801 | 0.072 | -5 | 0.832 |
NIK |
0.801 | 0.067 | -3 | 0.771 |
PKCD |
0.801 | 0.097 | 2 | 0.765 |
RAF1 |
0.801 | -0.039 | 1 | 0.805 |
CAMK2D |
0.801 | 0.083 | -3 | 0.759 |
AMPKA1 |
0.801 | 0.072 | -3 | 0.748 |
ERK5 |
0.801 | 0.051 | 1 | 0.810 |
LATS2 |
0.800 | 0.063 | -5 | 0.731 |
TSSK1 |
0.800 | 0.085 | -3 | 0.766 |
CAMLCK |
0.800 | 0.038 | -2 | 0.725 |
ATR |
0.800 | 0.007 | 1 | 0.845 |
AMPKA2 |
0.799 | 0.087 | -3 | 0.729 |
TBK1 |
0.799 | -0.064 | 1 | 0.715 |
MELK |
0.799 | 0.090 | -3 | 0.730 |
PLK1 |
0.799 | 0.135 | -2 | 0.839 |
RIPK3 |
0.798 | -0.029 | 3 | 0.587 |
PKN2 |
0.798 | 0.065 | -3 | 0.735 |
SRPK3 |
0.798 | 0.107 | -3 | 0.691 |
CHAK2 |
0.798 | 0.014 | -1 | 0.806 |
ULK1 |
0.798 | -0.023 | -3 | 0.722 |
CAMK2G |
0.798 | -0.040 | 2 | 0.777 |
SKMLCK |
0.798 | 0.028 | -2 | 0.715 |
MTOR |
0.798 | -0.061 | 1 | 0.760 |
ICK |
0.798 | 0.071 | -3 | 0.773 |
MLK1 |
0.797 | 0.004 | 2 | 0.780 |
NUAK1 |
0.797 | 0.065 | -3 | 0.722 |
ANKRD3 |
0.797 | 0.069 | 1 | 0.867 |
IKKB |
0.796 | -0.070 | -2 | 0.630 |
IKKE |
0.796 | -0.070 | 1 | 0.707 |
MST4 |
0.796 | 0.056 | 2 | 0.762 |
PDHK1 |
0.795 | -0.107 | 1 | 0.832 |
MNK2 |
0.795 | 0.074 | -2 | 0.686 |
PDHK4 |
0.795 | -0.199 | 1 | 0.831 |
DAPK2 |
0.795 | 0.025 | -3 | 0.779 |
MLK2 |
0.795 | 0.059 | 2 | 0.790 |
IRE1 |
0.795 | 0.037 | 1 | 0.851 |
MARK4 |
0.794 | -0.017 | 4 | 0.793 |
PKCB |
0.794 | 0.095 | 2 | 0.730 |
PKR |
0.794 | 0.169 | 1 | 0.869 |
BCKDK |
0.794 | -0.002 | -1 | 0.813 |
AURC |
0.794 | 0.061 | -2 | 0.540 |
NIM1 |
0.794 | -0.016 | 3 | 0.605 |
HUNK |
0.794 | -0.054 | 2 | 0.778 |
PHKG1 |
0.793 | 0.075 | -3 | 0.732 |
IRE2 |
0.793 | 0.031 | 2 | 0.755 |
MSK2 |
0.793 | 0.045 | -3 | 0.701 |
PKACG |
0.793 | 0.043 | -2 | 0.610 |
PERK |
0.792 | 0.226 | -2 | 0.786 |
CAMK2B |
0.792 | 0.073 | 2 | 0.737 |
PIM2 |
0.792 | 0.127 | -3 | 0.702 |
NEK2 |
0.791 | 0.075 | 2 | 0.811 |
PAK6 |
0.791 | 0.075 | -2 | 0.574 |
RSK4 |
0.790 | 0.091 | -3 | 0.693 |
WNK3 |
0.790 | -0.115 | 1 | 0.826 |
LATS1 |
0.790 | 0.079 | -3 | 0.754 |
MLK3 |
0.790 | 0.043 | 2 | 0.716 |
PAK1 |
0.790 | 0.019 | -2 | 0.635 |
HRI |
0.790 | 0.138 | -2 | 0.817 |
CAMK2A |
0.789 | 0.062 | 2 | 0.750 |
AKT2 |
0.789 | 0.106 | -3 | 0.659 |
PKCA |
0.789 | 0.073 | 2 | 0.721 |
PKACB |
0.788 | 0.074 | -2 | 0.561 |
MNK1 |
0.788 | 0.060 | -2 | 0.695 |
ATM |
0.788 | 0.025 | 1 | 0.774 |
PAK3 |
0.788 | -0.012 | -2 | 0.638 |
CAMK4 |
0.788 | -0.011 | -3 | 0.720 |
PKCZ |
0.788 | 0.060 | 2 | 0.781 |
CAMK1G |
0.788 | 0.081 | -3 | 0.713 |
PKCH |
0.788 | 0.068 | 2 | 0.728 |
FAM20C |
0.788 | 0.037 | 2 | 0.556 |
CHK1 |
0.787 | 0.062 | -3 | 0.732 |
MASTL |
0.787 | -0.116 | -2 | 0.714 |
SGK3 |
0.787 | 0.089 | -3 | 0.691 |
KIS |
0.787 | -0.002 | 1 | 0.667 |
RIPK1 |
0.787 | -0.096 | 1 | 0.849 |
DYRK2 |
0.786 | 0.040 | 1 | 0.699 |
PKG2 |
0.786 | 0.056 | -2 | 0.560 |
IKKA |
0.786 | -0.044 | -2 | 0.634 |
GRK5 |
0.786 | -0.142 | -3 | 0.705 |
CHAK1 |
0.786 | -0.004 | 2 | 0.756 |
AURB |
0.786 | 0.030 | -2 | 0.537 |
VRK2 |
0.785 | 0.039 | 1 | 0.893 |
PLK3 |
0.785 | 0.027 | 2 | 0.740 |
MAPKAPK5 |
0.785 | 0.023 | -3 | 0.698 |
NEK5 |
0.785 | 0.130 | 1 | 0.859 |
ALK4 |
0.785 | 0.017 | -2 | 0.737 |
MSK1 |
0.785 | 0.039 | -3 | 0.702 |
TGFBR1 |
0.785 | 0.049 | -2 | 0.715 |
CLK1 |
0.784 | 0.060 | -3 | 0.696 |
PKCG |
0.784 | 0.038 | 2 | 0.714 |
DCAMKL1 |
0.784 | 0.078 | -3 | 0.706 |
DLK |
0.784 | -0.118 | 1 | 0.827 |
PRKX |
0.784 | 0.100 | -3 | 0.612 |
CLK4 |
0.784 | 0.048 | -3 | 0.708 |
MLK4 |
0.783 | 0.008 | 2 | 0.706 |
GRK6 |
0.783 | -0.093 | 1 | 0.790 |
CAMK1D |
0.782 | 0.102 | -3 | 0.651 |
IRAK4 |
0.782 | 0.036 | 1 | 0.861 |
GRK4 |
0.782 | -0.082 | -2 | 0.714 |
TLK2 |
0.782 | 0.052 | 1 | 0.806 |
SIK |
0.782 | 0.012 | -3 | 0.695 |
CDK8 |
0.782 | -0.019 | 1 | 0.637 |
QSK |
0.782 | -0.012 | 4 | 0.765 |
QIK |
0.782 | -0.045 | -3 | 0.743 |
TTBK2 |
0.781 | -0.078 | 2 | 0.707 |
P70S6K |
0.781 | 0.075 | -3 | 0.677 |
MEKK1 |
0.780 | 0.040 | 1 | 0.838 |
YSK4 |
0.780 | -0.018 | 1 | 0.768 |
GRK1 |
0.780 | -0.027 | -2 | 0.613 |
BRSK2 |
0.780 | -0.009 | -3 | 0.730 |
BRAF |
0.780 | 0.035 | -4 | 0.747 |
AKT1 |
0.780 | 0.089 | -3 | 0.664 |
MYLK4 |
0.780 | 0.009 | -2 | 0.623 |
PHKG2 |
0.779 | 0.037 | -3 | 0.708 |
CDK5 |
0.779 | 0.005 | 1 | 0.654 |
SNRK |
0.779 | -0.068 | 2 | 0.696 |
PKCT |
0.779 | 0.052 | 2 | 0.734 |
SSTK |
0.778 | 0.026 | 4 | 0.763 |
TLK1 |
0.778 | 0.057 | -2 | 0.770 |
WNK4 |
0.778 | 0.008 | -2 | 0.745 |
PAK2 |
0.778 | -0.040 | -2 | 0.620 |
ACVR2A |
0.778 | 0.049 | -2 | 0.781 |
BRSK1 |
0.778 | -0.012 | -3 | 0.722 |
CLK2 |
0.778 | 0.075 | -3 | 0.703 |
HIPK1 |
0.777 | 0.044 | 1 | 0.724 |
SMG1 |
0.776 | -0.030 | 1 | 0.811 |
PKACA |
0.776 | 0.056 | -2 | 0.515 |
BMPR1B |
0.776 | 0.003 | 1 | 0.713 |
ACVR2B |
0.776 | 0.035 | -2 | 0.774 |
ZAK |
0.776 | 0.011 | 1 | 0.806 |
CDK19 |
0.776 | -0.022 | 1 | 0.594 |
PLK4 |
0.775 | -0.016 | 2 | 0.628 |
CDK7 |
0.775 | -0.034 | 1 | 0.631 |
DYRK1A |
0.775 | 0.028 | 1 | 0.709 |
CAMK1A |
0.775 | 0.111 | -3 | 0.627 |
P38A |
0.775 | 0.002 | 1 | 0.683 |
AURA |
0.774 | 0.004 | -2 | 0.513 |
PINK1 |
0.774 | -0.037 | 1 | 0.848 |
SMMLCK |
0.774 | 0.020 | -3 | 0.748 |
DCAMKL2 |
0.774 | 0.016 | -3 | 0.735 |
MEK1 |
0.774 | -0.128 | 2 | 0.790 |
MPSK1 |
0.774 | 0.111 | 1 | 0.865 |
MEKK2 |
0.774 | -0.002 | 2 | 0.789 |
DNAPK |
0.774 | 0.008 | 1 | 0.682 |
ALK2 |
0.773 | -0.014 | -2 | 0.721 |
HIPK2 |
0.773 | 0.033 | 1 | 0.606 |
NEK8 |
0.772 | 0.044 | 2 | 0.804 |
PKCI |
0.772 | 0.048 | 2 | 0.739 |
JNK2 |
0.772 | 0.015 | 1 | 0.561 |
CDK13 |
0.772 | -0.042 | 1 | 0.603 |
DYRK3 |
0.771 | 0.050 | 1 | 0.741 |
JNK3 |
0.771 | -0.009 | 1 | 0.605 |
CDK18 |
0.771 | -0.011 | 1 | 0.572 |
MARK3 |
0.771 | -0.038 | 4 | 0.721 |
PKN1 |
0.770 | 0.069 | -3 | 0.686 |
HIPK3 |
0.770 | 0.012 | 1 | 0.715 |
AKT3 |
0.770 | 0.096 | -3 | 0.612 |
MARK2 |
0.770 | -0.058 | 4 | 0.675 |
PKCE |
0.770 | 0.074 | 2 | 0.706 |
SGK1 |
0.769 | 0.101 | -3 | 0.597 |
NEK1 |
0.769 | 0.123 | 1 | 0.838 |
CAMKK1 |
0.769 | -0.004 | -2 | 0.671 |
MST3 |
0.768 | 0.027 | 2 | 0.781 |
DAPK3 |
0.768 | 0.046 | -3 | 0.723 |
GRK7 |
0.768 | -0.040 | 1 | 0.735 |
MEKK3 |
0.768 | -0.089 | 1 | 0.807 |
MEK5 |
0.768 | -0.123 | 2 | 0.792 |
LKB1 |
0.768 | 0.060 | -3 | 0.716 |
P38B |
0.767 | -0.011 | 1 | 0.603 |
ERK7 |
0.767 | 0.080 | 2 | 0.583 |
ERK1 |
0.767 | -0.019 | 1 | 0.590 |
CDK1 |
0.767 | -0.030 | 1 | 0.576 |
MRCKB |
0.767 | 0.099 | -3 | 0.676 |
BUB1 |
0.767 | 0.118 | -5 | 0.810 |
TAO3 |
0.767 | 0.014 | 1 | 0.793 |
NEK4 |
0.767 | 0.032 | 1 | 0.806 |
PAK4 |
0.767 | 0.018 | -2 | 0.522 |
MRCKA |
0.767 | 0.089 | -3 | 0.688 |
ROCK2 |
0.766 | 0.128 | -3 | 0.703 |
CDK9 |
0.766 | -0.044 | 1 | 0.612 |
CHK2 |
0.766 | 0.071 | -3 | 0.615 |
DRAK1 |
0.766 | -0.081 | 1 | 0.701 |
PAK5 |
0.766 | 0.007 | -2 | 0.512 |
ERK2 |
0.765 | -0.049 | 1 | 0.636 |
P38G |
0.765 | -0.005 | 1 | 0.498 |
GAK |
0.765 | 0.087 | 1 | 0.884 |
VRK1 |
0.765 | 0.110 | 2 | 0.804 |
PRP4 |
0.764 | -0.047 | -3 | 0.602 |
DYRK1B |
0.764 | -0.000 | 1 | 0.626 |
MARK1 |
0.764 | -0.084 | 4 | 0.745 |
IRAK1 |
0.764 | -0.120 | -1 | 0.709 |
MOK |
0.764 | 0.101 | 1 | 0.778 |
CDK2 |
0.764 | -0.073 | 1 | 0.668 |
DYRK4 |
0.764 | 0.003 | 1 | 0.602 |
TAO2 |
0.763 | -0.015 | 2 | 0.824 |
EEF2K |
0.763 | 0.017 | 3 | 0.617 |
CDK14 |
0.763 | -0.008 | 1 | 0.612 |
SBK |
0.763 | 0.090 | -3 | 0.579 |
CDK12 |
0.763 | -0.047 | 1 | 0.572 |
CDK16 |
0.763 | 0.010 | 1 | 0.528 |
CAMKK2 |
0.763 | -0.013 | -2 | 0.660 |
PDHK3_TYR |
0.762 | 0.116 | 4 | 0.887 |
PASK |
0.762 | -0.035 | -3 | 0.753 |
PDK1 |
0.762 | -0.014 | 1 | 0.783 |
MAK |
0.762 | 0.081 | -2 | 0.613 |
CDK3 |
0.761 | -0.019 | 1 | 0.524 |
CDK17 |
0.761 | -0.035 | 1 | 0.503 |
DMPK1 |
0.761 | 0.106 | -3 | 0.690 |
MEKK6 |
0.760 | -0.003 | 1 | 0.819 |
CDK10 |
0.760 | 0.014 | 1 | 0.596 |
TTK |
0.760 | 0.157 | -2 | 0.830 |
TNIK |
0.759 | 0.024 | 3 | 0.657 |
NEK3 |
0.759 | 0.064 | 1 | 0.803 |
BMPR1A |
0.758 | -0.025 | 1 | 0.689 |
HGK |
0.758 | -0.019 | 3 | 0.658 |
LOK |
0.758 | 0.013 | -2 | 0.681 |
GRK2 |
0.758 | -0.116 | -2 | 0.584 |
PBK |
0.757 | 0.121 | 1 | 0.832 |
TTBK1 |
0.757 | -0.113 | 2 | 0.618 |
GSK3B |
0.757 | -0.027 | 4 | 0.449 |
LRRK2 |
0.756 | -0.044 | 2 | 0.832 |
LIMK2_TYR |
0.756 | 0.092 | -3 | 0.779 |
ROCK1 |
0.756 | 0.096 | -3 | 0.682 |
DAPK1 |
0.755 | 0.008 | -3 | 0.708 |
CK1E |
0.755 | -0.084 | -3 | 0.387 |
MAP3K15 |
0.755 | -0.048 | 1 | 0.788 |
BIKE |
0.755 | 0.158 | 1 | 0.799 |
MST2 |
0.755 | -0.031 | 1 | 0.782 |
CRIK |
0.755 | 0.095 | -3 | 0.669 |
GSK3A |
0.755 | -0.016 | 4 | 0.461 |
TESK1_TYR |
0.755 | 0.006 | 3 | 0.674 |
P38D |
0.755 | -0.017 | 1 | 0.531 |
PLK2 |
0.755 | -0.014 | -3 | 0.682 |
NEK11 |
0.754 | -0.139 | 1 | 0.766 |
MINK |
0.754 | -0.029 | 1 | 0.779 |
YSK1 |
0.754 | 0.035 | 2 | 0.792 |
RET |
0.754 | 0.045 | 1 | 0.835 |
PKG1 |
0.753 | 0.024 | -2 | 0.490 |
PKMYT1_TYR |
0.752 | 0.006 | 3 | 0.663 |
MAP2K4_TYR |
0.750 | -0.029 | -1 | 0.818 |
RIPK2 |
0.750 | -0.130 | 1 | 0.757 |
GCK |
0.750 | -0.063 | 1 | 0.749 |
STK33 |
0.750 | -0.085 | 2 | 0.588 |
TAK1 |
0.750 | -0.050 | 1 | 0.792 |
CDK6 |
0.750 | -0.022 | 1 | 0.596 |
EPHA6 |
0.750 | 0.028 | -1 | 0.839 |
PINK1_TYR |
0.750 | -0.077 | 1 | 0.850 |
TYK2 |
0.750 | -0.004 | 1 | 0.831 |
CK1G1 |
0.750 | -0.090 | -3 | 0.389 |
CDK4 |
0.749 | -0.021 | 1 | 0.564 |
ABL2 |
0.749 | 0.071 | -1 | 0.766 |
PDHK4_TYR |
0.749 | -0.030 | 2 | 0.813 |
ROS1 |
0.749 | 0.005 | 3 | 0.615 |
EPHB4 |
0.749 | 0.030 | -1 | 0.832 |
MST1 |
0.749 | -0.056 | 1 | 0.779 |
MAP2K6_TYR |
0.748 | -0.046 | -1 | 0.840 |
KHS1 |
0.748 | -0.020 | 1 | 0.752 |
MST1R |
0.748 | -0.012 | 3 | 0.629 |
CK2A2 |
0.748 | -0.034 | 1 | 0.634 |
MAP2K7_TYR |
0.747 | -0.165 | 2 | 0.818 |
OSR1 |
0.747 | 0.038 | 2 | 0.759 |
LIMK1_TYR |
0.746 | -0.034 | 2 | 0.827 |
TNNI3K_TYR |
0.746 | 0.103 | 1 | 0.875 |
MEK2 |
0.746 | -0.104 | 2 | 0.785 |
ABL1 |
0.746 | 0.061 | -1 | 0.750 |
BMPR2_TYR |
0.746 | -0.044 | -1 | 0.823 |
TYRO3 |
0.745 | -0.054 | 3 | 0.625 |
CSF1R |
0.745 | -0.041 | 3 | 0.614 |
JAK2 |
0.745 | -0.039 | 1 | 0.824 |
JNK1 |
0.745 | -0.045 | 1 | 0.547 |
DDR1 |
0.745 | -0.037 | 4 | 0.825 |
SLK |
0.744 | -0.062 | -2 | 0.621 |
PDHK1_TYR |
0.744 | -0.077 | -1 | 0.858 |
PDGFRB |
0.743 | -0.019 | 3 | 0.620 |
FGR |
0.743 | 0.029 | 1 | 0.872 |
JAK3 |
0.743 | -0.024 | 1 | 0.814 |
KHS2 |
0.743 | -0.021 | 1 | 0.748 |
HPK1 |
0.743 | -0.083 | 1 | 0.733 |
CK1D |
0.743 | -0.103 | -3 | 0.337 |
TNK1 |
0.742 | 0.008 | 3 | 0.621 |
GRK3 |
0.742 | -0.111 | -2 | 0.529 |
MYO3B |
0.742 | 0.032 | 2 | 0.796 |
CK1A2 |
0.742 | -0.102 | -3 | 0.341 |
AAK1 |
0.742 | 0.175 | 1 | 0.710 |
INSRR |
0.741 | -0.031 | 3 | 0.571 |
YES1 |
0.740 | -0.027 | -1 | 0.762 |
TNK2 |
0.740 | -0.038 | 3 | 0.575 |
EPHB3 |
0.739 | -0.007 | -1 | 0.829 |
KDR |
0.739 | -0.039 | 3 | 0.572 |
FLT3 |
0.738 | -0.050 | 3 | 0.612 |
HCK |
0.738 | -0.006 | -1 | 0.757 |
HASPIN |
0.738 | -0.011 | -1 | 0.610 |
ASK1 |
0.738 | -0.056 | 1 | 0.775 |
JAK1 |
0.738 | 0.006 | 1 | 0.759 |
EPHB1 |
0.738 | -0.037 | 1 | 0.817 |
BLK |
0.737 | 0.049 | -1 | 0.771 |
TXK |
0.737 | 0.018 | 1 | 0.796 |
EPHB2 |
0.737 | -0.004 | -1 | 0.822 |
ITK |
0.737 | -0.026 | -1 | 0.743 |
DDR2 |
0.737 | 0.024 | 3 | 0.543 |
FGFR2 |
0.736 | -0.086 | 3 | 0.593 |
NEK10_TYR |
0.736 | -0.003 | 1 | 0.702 |
TAO1 |
0.736 | -0.026 | 1 | 0.737 |
LCK |
0.736 | 0.028 | -1 | 0.763 |
CK2A1 |
0.735 | -0.058 | 1 | 0.610 |
PDGFRA |
0.735 | -0.058 | 3 | 0.625 |
FER |
0.734 | -0.113 | 1 | 0.838 |
AXL |
0.734 | -0.084 | 3 | 0.595 |
KIT |
0.733 | -0.099 | 3 | 0.605 |
EPHA4 |
0.733 | -0.053 | 2 | 0.714 |
FGFR1 |
0.732 | -0.098 | 3 | 0.585 |
LTK |
0.732 | -0.062 | 3 | 0.573 |
SRMS |
0.731 | -0.080 | 1 | 0.814 |
WEE1_TYR |
0.730 | -0.030 | -1 | 0.709 |
MYO3A |
0.730 | -0.059 | 1 | 0.786 |
MERTK |
0.730 | -0.081 | 3 | 0.597 |
MET |
0.730 | -0.080 | 3 | 0.598 |
INSR |
0.729 | -0.068 | 3 | 0.565 |
ALK |
0.729 | -0.097 | 3 | 0.552 |
FLT4 |
0.728 | -0.062 | 3 | 0.582 |
TEK |
0.728 | -0.128 | 3 | 0.561 |
FLT1 |
0.728 | -0.045 | -1 | 0.836 |
NTRK1 |
0.728 | -0.087 | -1 | 0.804 |
PTK6 |
0.727 | -0.068 | -1 | 0.681 |
NTRK2 |
0.727 | -0.093 | 3 | 0.574 |
EPHA1 |
0.727 | -0.079 | 3 | 0.581 |
EPHA7 |
0.727 | -0.064 | 2 | 0.738 |
BMX |
0.726 | -0.054 | -1 | 0.661 |
FYN |
0.725 | -0.009 | -1 | 0.725 |
BTK |
0.725 | -0.127 | -1 | 0.706 |
STLK3 |
0.725 | -0.086 | 1 | 0.773 |
EPHA3 |
0.724 | -0.086 | 2 | 0.704 |
TEC |
0.724 | -0.086 | -1 | 0.662 |
LYN |
0.723 | -0.058 | 3 | 0.559 |
NTRK3 |
0.723 | -0.078 | -1 | 0.771 |
ALPHAK3 |
0.722 | -0.125 | -1 | 0.736 |
FRK |
0.721 | -0.084 | -1 | 0.795 |
FGFR3 |
0.721 | -0.134 | 3 | 0.564 |
MUSK |
0.721 | -0.021 | 1 | 0.698 |
EPHA5 |
0.719 | -0.068 | 2 | 0.716 |
ERBB2 |
0.719 | -0.128 | 1 | 0.766 |
PTK2B |
0.717 | -0.091 | -1 | 0.705 |
MATK |
0.717 | -0.102 | -1 | 0.725 |
EGFR |
0.716 | -0.052 | 1 | 0.692 |
YANK3 |
0.716 | -0.099 | 2 | 0.357 |
EPHA8 |
0.714 | -0.085 | -1 | 0.804 |
SRC |
0.714 | -0.074 | -1 | 0.720 |
CSK |
0.713 | -0.128 | 2 | 0.738 |
IGF1R |
0.711 | -0.107 | 3 | 0.509 |
EPHA2 |
0.710 | -0.076 | -1 | 0.775 |
CK1A |
0.708 | -0.104 | -3 | 0.255 |
FGFR4 |
0.707 | -0.120 | -1 | 0.756 |
PTK2 |
0.702 | -0.074 | -1 | 0.747 |
SYK |
0.700 | -0.060 | -1 | 0.764 |
ERBB4 |
0.696 | -0.093 | 1 | 0.677 |
CK1G3 |
0.689 | -0.131 | -3 | 0.212 |
FES |
0.682 | -0.189 | -1 | 0.639 |
YANK2 |
0.681 | -0.130 | 2 | 0.376 |
ZAP70 |
0.678 | -0.101 | -1 | 0.672 |
CK1G2 |
0.673 | -0.122 | -3 | 0.301 |