Motif 16 (n=142)
Position-wise Probabilities
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| uniprot | genes | site | source | protein | function |
|---|---|---|---|---|---|
| A2AJT9 | BCLAF3 | S489 | ochoa | BCLAF1 and THRAP3 family member 3 | None |
| A5YKK6 | CNOT1 | S2188 | ochoa | CCR4-NOT transcription complex subunit 1 (CCR4-associated factor 1) (Negative regulator of transcription subunit 1 homolog) (NOT1H) (hNOT1) | Scaffolding component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Its scaffolding function implies its interaction with the catalytic complex module and diverse RNA-binding proteins mediating the complex recruitment to selected mRNA 3'UTRs. Involved in degradation of AU-rich element (ARE)-containing mRNAs probably via association with ZFP36. Mediates the recruitment of the CCR4-NOT complex to miRNA targets and to the RISC complex via association with TNRC6A, TNRC6B or TNRC6C. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors. Involved in the maintenance of embryonic stem (ES) cell identity. Plays a role in rapid sperm motility via mediating timely mRNA turnover (By similarity). {ECO:0000250|UniProtKB:Q6ZQ08, ECO:0000269|PubMed:10637334, ECO:0000269|PubMed:16778766, ECO:0000269|PubMed:21278420, ECO:0000269|PubMed:21976065, ECO:0000269|PubMed:21984185, ECO:0000269|PubMed:22367759, ECO:0000269|PubMed:23644599, ECO:0000269|PubMed:27558897, ECO:0000269|PubMed:32354837}. |
| C9J4A7 | None | S89 | ochoa | PH domain-containing protein | None |
| O00534 | VWA5A | S202 | ochoa | von Willebrand factor A domain-containing protein 5A (Breast cancer suppressor candidate 1) (BCSC-1) (Loss of heterozygosity 11 chromosomal region 2 gene A protein) | May play a role in tumorigenesis as a tumor suppressor. Altered expression of this protein and disruption of the molecular pathway it is involved in, may contribute directly to or modify tumorigenesis. |
| O15015 | ZNF646 | S930 | ochoa | Zinc finger protein 646 | May be involved in transcriptional regulation. |
| O15344 | MID1 | S96 | ochoa|psp | E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (Putative transcription factor XPRF) (RING finger protein 59) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18) | Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. {ECO:0000269|PubMed:10400985, ECO:0000269|PubMed:11685209, ECO:0000269|PubMed:22613722}. |
| O43294 | TGFB1I1 | S141 | ochoa | Transforming growth factor beta-1-induced transcript 1 protein (Androgen receptor coactivator 55 kDa protein) (Androgen receptor-associated protein of 55 kDa) (Hydrogen peroxide-inducible clone 5 protein) (Hic-5) | Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity. {ECO:0000269|PubMed:10075738, ECO:0000269|PubMed:11463817, ECO:0000269|PubMed:11856738, ECO:0000269|PubMed:12177201, ECO:0000269|PubMed:12445807, ECO:0000269|PubMed:12700349, ECO:0000269|PubMed:15211577, ECO:0000269|PubMed:15561701, ECO:0000269|PubMed:16141357, ECO:0000269|PubMed:16624805, ECO:0000269|PubMed:16803896, ECO:0000269|PubMed:16849583, ECO:0000269|PubMed:17166536, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:9032249}. |
| O75179 | ANKRD17 | S1700 | ochoa | Ankyrin repeat domain-containing protein 17 (Gene trap ankyrin repeat protein) (Serologically defined breast cancer antigen NY-BR-16) | Could play pivotal roles in cell cycle and DNA regulation (PubMed:19150984). Involved in innate immune defense against viruse by positively regulating the viral dsRNA receptors DDX58 and IFIH1 signaling pathways (PubMed:22328336). Involves in NOD2- and NOD1-mediated responses to bacteria suggesting a role in innate antibacterial immune pathways too (PubMed:23711367). Target of enterovirus 71 which is the major etiological agent of HFMD (hand, foot and mouth disease) (PubMed:17276651). Could play a central role for the formation and/or maintenance of the blood vessels of the circulation system (By similarity). {ECO:0000250|UniProtKB:Q99NH0, ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984, ECO:0000269|PubMed:22328336, ECO:0000269|PubMed:23711367}. |
| O75208 | COQ9 | S78 | ochoa | Ubiquinone biosynthesis protein COQ9, mitochondrial | Membrane-associated protein that warps the membrane surface to access and bind aromatic isoprenes with high specificity, including ubiquinone (CoQ) isoprene intermediates and presents them directly to COQ7, therefore facilitating the COQ7-mediated hydroxylase step (PubMed:25339443, PubMed:30661980, PubMed:38425362). Participates in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:25339443, PubMed:30661980). {ECO:0000269|PubMed:25339443, ECO:0000269|PubMed:30661980, ECO:0000269|PubMed:38425362}. |
| O95163 | ELP1 | S1211 | ochoa | Elongator complex protein 1 (ELP1) (IkappaB kinase complex-associated protein) (IKK complex-associated protein) (p150) | Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:29332244). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (By similarity). ELP1 binds to tRNA, mediating interaction of the elongator complex with tRNA (By similarity). May act as a scaffold protein that assembles active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK) (PubMed:9751059). {ECO:0000250|UniProtKB:Q06706, ECO:0000250|UniProtKB:Q7TT37, ECO:0000269|PubMed:9751059, ECO:0000303|PubMed:29332244}. |
| P05023 | ATP1A1 | S452 | ochoa | Sodium/potassium-transporting ATPase subunit alpha-1 (Na(+)/K(+) ATPase alpha-1 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-1) | This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (PubMed:29499166, PubMed:30388404). Could also be part of an osmosensory signaling pathway that senses body-fluid sodium levels and controls salt intake behavior as well as voluntary water intake to regulate sodium homeostasis (By similarity). {ECO:0000250|UniProtKB:Q8VDN2, ECO:0000269|PubMed:29499166, ECO:0000269|PubMed:30388404}. |
| P07197 | NEFM | S620 | ochoa | Neurofilament medium polypeptide (NF-M) (160 kDa neurofilament protein) (Neurofilament 3) (Neurofilament triplet M protein) | Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08553}. |
| P07197 | NEFM | S633 | ochoa | Neurofilament medium polypeptide (NF-M) (160 kDa neurofilament protein) (Neurofilament 3) (Neurofilament triplet M protein) | Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08553}. |
| P07197 | NEFM | S672 | ochoa | Neurofilament medium polypeptide (NF-M) (160 kDa neurofilament protein) (Neurofilament 3) (Neurofilament triplet M protein) | Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08553}. |
| P07197 | NEFM | S685 | ochoa | Neurofilament medium polypeptide (NF-M) (160 kDa neurofilament protein) (Neurofilament 3) (Neurofilament triplet M protein) | Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08553}. |
| P0DMV8 | HSPA1A | S537 | ochoa | Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1) (Heat shock protein family A member 1A) | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:24318877, PubMed:26865365). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Required as a co-chaperone for optimal STUB1/CHIP ubiquitination of NFATC3 (By similarity). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation (PubMed:28842558). {ECO:0000250|UniProtKB:P0DMW0, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27137183, ECO:0000269|PubMed:27708256, ECO:0000269|PubMed:28842558, ECO:0000269|PubMed:9499401, ECO:0000303|PubMed:24012426, ECO:0000303|PubMed:26865365}.; FUNCTION: (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. {ECO:0000269|PubMed:16537599}. |
| P0DMV9 | HSPA1B | S537 | ochoa | Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2) (Heat shock protein family A member 1B) | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:24318877, PubMed:26865365). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). {ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27137183, ECO:0000269|PubMed:27708256, ECO:0000303|PubMed:24012426, ECO:0000303|PubMed:26865365}.; FUNCTION: (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. {ECO:0000269|PubMed:16537599}. |
| P11142 | HSPA8 | S537 | ochoa | Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8) (Heat shock protein family A member 8) (Lipopolysaccharide-associated protein 1) (LAP-1) (LPS-associated protein 1) | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661, PubMed:2799391, PubMed:36586411). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24121476, PubMed:24318877, PubMed:26865365, PubMed:27474739). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2 (PubMed:11559757, PubMed:2799391, PubMed:36586411). KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (PubMed:11559757, PubMed:2799391, PubMed:36586411). In conjunction with LAMP2, facilitates MHC class II presentation of cytoplasmic antigens by guiding antigens to the lysosomal membrane for interaction with LAMP2 which then elicits MHC class II presentation of peptides to the cell membrane (PubMed:15894275). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). It is recruited to clathrin-coated vesicles through its interaction with DNAJC6 leading to activation of HSPA8/HSC70 ATPase activity and therefore uncoating of clathrin-coated vesicles (By similarity). {ECO:0000250|UniProtKB:P19120, ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:11559757, ECO:0000269|PubMed:12526792, ECO:0000269|PubMed:15894275, ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:23990462, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27474739, ECO:0000269|PubMed:27916661, ECO:0000269|PubMed:2799391, ECO:0000269|PubMed:36586411, ECO:0000303|PubMed:24121476, ECO:0000303|PubMed:26865365}. |
| P12277 | CKB | S164 | ochoa | Creatine kinase B-type (EC 2.7.3.2) (Brain creatine kinase) (B-CK) (Creatine kinase B chain) (Creatine phosphokinase B-type) (CPK-B) | Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate) (PubMed:8186255). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (Probable). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating phosphorylation of creatine to initiate a futile cycle of creatine phosphorylation and dephosphorylation (By similarity). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity). {ECO:0000250|UniProtKB:Q04447, ECO:0000269|PubMed:8186255, ECO:0000305}. |
| P14625 | HSP90B1 | S501 | ochoa | Endoplasmin (EC 3.6.4.-) (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Heat shock protein family C member 4) (Tumor rejection antigen 1) (gp96 homolog) | ATP-dependent chaperone involved in the processing of proteins in the endoplasmic reticulum, regulating their transport (PubMed:23572575, PubMed:39509507). Together with MESD, acts as a modulator of the Wnt pathway by promoting the folding of LRP6, a coreceptor of the canonical Wnt pathway (PubMed:23572575, PubMed:39509507). When associated with CNPY3, required for proper folding of Toll-like receptors (PubMed:11584270). Promotes folding and trafficking of TLR4 to the cell surface (PubMed:11584270). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:11584270, ECO:0000269|PubMed:23572575, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:39509507}. |
| P14921 | ETS1 | S26 | ochoa | Protein C-ets-1 (p54) | Transcription factor (PubMed:10698492, PubMed:11909962). Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts (PubMed:20378371). May control the differentiation, survival and proliferation of lymphoid cells (PubMed:20378371). May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion (PubMed:15247905, PubMed:15592518). {ECO:0000269|PubMed:10698492, ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:15247905, ECO:0000269|PubMed:15592518, ECO:0000303|PubMed:20378371}.; FUNCTION: [Isoform Ets-1 p27]: Acts as a dominant-negative for isoform c-ETS-1A. {ECO:0000269|PubMed:19377509}. |
| P17036 | ZNF3 | S143 | ochoa | Zinc finger protein 3 (Zinc finger protein HF.12) (Zinc finger protein HZF3.1) (Zinc finger protein KOX25) | Involved in cell differentiation and/or proliferation. |
| P18583 | SON | S1688 | ochoa | Protein SON (Bax antagonist selected in saccharomyces 1) (BASS1) (Negative regulatory element-binding protein) (NRE-binding protein) (Protein DBP-5) (SON3) | RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'-GA[GT]AN[CG][AG]CC-3'. May indirectly repress hepatitis B virus (HBV) core promoter activity and transcription of HBV genes and production of HBV virions. Essential for correct RNA splicing of multiple genes critical for brain development, neuronal migration and metabolism, including TUBG1, FLNA, PNKP, WDR62, PSMD3, PCK2, PFKL, IDH2, and ACY1 (PubMed:27545680). {ECO:0000269|PubMed:20581448, ECO:0000269|PubMed:21504830, ECO:0000269|PubMed:27545680}. |
| P20042 | EIF2S2 | S286 | ochoa | Eukaryotic translation initiation factor 2 subunit 2 (Eukaryotic translation initiation factor 2 subunit beta) (eIF2-beta) | Component of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:31836389). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity). {ECO:0000250|UniProtKB:P05198, ECO:0000269|PubMed:31836389}. |
| P21333 | FLNA | S966 | ochoa | Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin) | Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNB may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (By similarity). During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons (PubMed:25358863). {ECO:0000250, ECO:0000250|UniProtKB:Q8BTM8, ECO:0000269|PubMed:22121117, ECO:0000269|PubMed:25358863}. |
| P25054 | APC | S744 | ochoa | Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5) | Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250|UniProtKB:Q61315, ECO:0000269|PubMed:10947987, ECO:0000269|PubMed:17293347, ECO:0000269|PubMed:17599059, ECO:0000269|PubMed:19151759, ECO:0000269|PubMed:19893577, ECO:0000269|PubMed:20937854}. |
| P28290 | ITPRID2 | S316 | ochoa | Protein ITPRID2 (Cleavage signal-1 protein) (CS-1) (ITPR-interacting domain-containing protein 2) (Ki-ras-induced actin-interacting protein) (Sperm-specific antigen 2) | None |
| P28290 | ITPRID2 | S803 | ochoa | Protein ITPRID2 (Cleavage signal-1 protein) (CS-1) (ITPR-interacting domain-containing protein 2) (Ki-ras-induced actin-interacting protein) (Sperm-specific antigen 2) | None |
| P28715 | ERCC5 | S341 | 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}. |
| P33981 | TTK | S821 | ochoa|psp | Dual specificity protein kinase TTK (EC 2.7.12.1) (Phosphotyrosine picked threonine-protein kinase) (PYT) | Involved in mitotic spindle assembly checkpoint signaling, a process that delays anaphase until chromosomes are bioriented on the spindle, and in the repair of incorrect mitotic kinetochore-spindle microtubule attachments (PubMed:18243099, PubMed:28441529, PubMed:29162720). Phosphorylates MAD1L1 to promote the mitotic spindle assembly checkpoint (PubMed:18243099, PubMed:29162720). Phosphorylates CDCA8/Borealin leading to enhanced AURKB activity at the kinetochore (PubMed:18243099). Phosphorylates SKA3 at 'Ser-34' leading to dissociation of the SKA complex from microtubules and destabilization of microtubule-kinetochore attachments (PubMed:28441529). Phosphorylates KNL1, KNTC1 and autophosphorylates (PubMed:28441529). Phosphorylates MCRS1 which enhances recruitment of KIF2A to the minus end of spindle microtubules and promotes chromosome alignment (PubMed:30785839). {ECO:0000269|PubMed:18243099, ECO:0000269|PubMed:28441529, ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:30785839}. |
| P43007 | SLC1A4 | S507 | ochoa | Neutral amino acid transporter A (Alanine/serine/cysteine/threonine transporter 1) (ASCT-1) (Solute carrier family 1 member 4) | Sodium-dependent neutral amino-acid transporter that mediates transport of alanine, serine, cysteine, proline, hydroxyproline and threonine. {ECO:0000269|PubMed:14502423, ECO:0000269|PubMed:26041762, ECO:0000269|PubMed:8101838, ECO:0000269|PubMed:8340364}. |
| P46013 | MKI67 | S1071 | ochoa | Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67) (Antigen KI-67) (Antigen Ki67) | Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636). {ECO:0000250|UniProtKB:E9PVX6, ECO:0000269|PubMed:10878551, ECO:0000269|PubMed:24867636, ECO:0000269|PubMed:27362226, ECO:0000269|PubMed:28935370, ECO:0000269|PubMed:32879492, ECO:0000269|PubMed:35513709, ECO:0000269|PubMed:39153474}. |
| P46013 | MKI67 | S1679 | ochoa | Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67) (Antigen KI-67) (Antigen Ki67) | Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636). {ECO:0000250|UniProtKB:E9PVX6, ECO:0000269|PubMed:10878551, ECO:0000269|PubMed:24867636, ECO:0000269|PubMed:27362226, ECO:0000269|PubMed:28935370, ECO:0000269|PubMed:32879492, ECO:0000269|PubMed:35513709, ECO:0000269|PubMed:39153474}. |
| P46013 | MKI67 | S2528 | ochoa | Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67) (Antigen KI-67) (Antigen Ki67) | Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636). {ECO:0000250|UniProtKB:E9PVX6, ECO:0000269|PubMed:10878551, ECO:0000269|PubMed:24867636, ECO:0000269|PubMed:27362226, ECO:0000269|PubMed:28935370, ECO:0000269|PubMed:32879492, ECO:0000269|PubMed:35513709, ECO:0000269|PubMed:39153474}. |
| P46013 | MKI67 | S2588 | ochoa | Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67) (Antigen KI-67) (Antigen Ki67) | Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636). {ECO:0000250|UniProtKB:E9PVX6, ECO:0000269|PubMed:10878551, ECO:0000269|PubMed:24867636, ECO:0000269|PubMed:27362226, ECO:0000269|PubMed:28935370, ECO:0000269|PubMed:32879492, ECO:0000269|PubMed:35513709, ECO:0000269|PubMed:39153474}. |
| P49591 | SARS1 | S331 | ochoa | Serine--tRNA ligase, cytoplasmic (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) | Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser) (PubMed:22353712, PubMed:24095058, PubMed:26433229, PubMed:28236339, PubMed:34570399, PubMed:36041817, PubMed:9431993). Is probably also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (PubMed:26433229, PubMed:28236339, PubMed:34570399, PubMed:9431993). In the nucleus, binds to the VEGFA core promoter and prevents MYC binding and transcriptional activation by MYC (PubMed:24940000). Recruits SIRT2 to the VEGFA promoter, promoting deacetylation of histone H4 at 'Lys-16' (H4K16). Thereby, inhibits the production of VEGFA and sprouting angiogenesis mediated by VEGFA (PubMed:19423847, PubMed:19423848, PubMed:24940000). {ECO:0000269|PubMed:19423847, ECO:0000269|PubMed:19423848, ECO:0000269|PubMed:22353712, ECO:0000269|PubMed:24095058, ECO:0000269|PubMed:24940000, ECO:0000269|PubMed:26433229, ECO:0000269|PubMed:28236339, ECO:0000269|PubMed:34570399, ECO:0000269|PubMed:36041817, ECO:0000269|PubMed:9431993}. |
| P50993 | ATP1A2 | S450 | ochoa | Sodium/potassium-transporting ATPase subunit alpha-2 (Na(+)/K(+) ATPase alpha-2 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-2) | This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients. {ECO:0000269|PubMed:33880529}. |
| P54132 | BLM | S1296 | ochoa|psp | RecQ-like DNA helicase BLM (EC 5.6.2.4) (Bloom syndrome protein) (DNA 3'-5' helicase BLM) (DNA helicase, RecQ-like type 2) (RecQ2) (RecQ protein-like 3) | ATP-dependent DNA helicase that unwinds double-stranded (ds)DNA in a 3'-5' direction (PubMed:24816114, PubMed:25901030, PubMed:9388193, PubMed:9765292). Participates in DNA replication and repair (PubMed:12019152, PubMed:21325134, PubMed:23509288, PubMed:34606619). Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA (PubMed:21325134). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (PubMed:25901030). Binds single-stranded DNA (ssDNA), forked duplex DNA and Holliday junction DNA (PubMed:20639533, PubMed:24257077, PubMed:25901030). Unwinds G-quadruplex DNA; unwinding occurs in the 3'-5' direction and requires a 3' single-stranded end of at least 7 nucleotides (PubMed:18426915, PubMed:9765292). Helicase activity is higher on G-quadruplex substrates than on duplex DNA substrates (PubMed:9765292). Telomeres, immunoglobulin heavy chain switch regions and rDNA are notably G-rich; formation of G-quadruplex DNA would block DNA replication and transcription (PubMed:18426915, PubMed:9765292). Negatively regulates sister chromatid exchange (SCE) (PubMed:25901030). Recruited by the KHDC3L-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks (By similarity). {ECO:0000250|UniProtKB:O88700, ECO:0000269|PubMed:12019152, ECO:0000269|PubMed:18426915, ECO:0000269|PubMed:20639533, ECO:0000269|PubMed:21325134, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:24257077, ECO:0000269|PubMed:24816114, ECO:0000269|PubMed:25901030, ECO:0000269|PubMed:34606619, ECO:0000269|PubMed:9388193, ECO:0000269|PubMed:9765292}.; FUNCTION: (Microbial infection) Eliminates nuclear HIV-1 cDNA, thereby suppressing immune sensing and proviral hyper-integration. {ECO:0000269|PubMed:32690953}. |
| P55265 | ADAR | S614 | ochoa | Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (136 kDa double-stranded RNA-binding protein) (p136) (Interferon-inducible protein 4) (IFI-4) (K88DSRBP) | Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing (PubMed:12618436, PubMed:7565688, PubMed:7972084). This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins since the translational machinery read the inosine as a guanosine; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication. {ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:15556947, ECO:0000269|PubMed:15858013, ECO:0000269|PubMed:16120648, ECO:0000269|PubMed:16475990, ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:19605474, ECO:0000269|PubMed:19651874, ECO:0000269|PubMed:19710021, ECO:0000269|PubMed:19908260, ECO:0000269|PubMed:21289159, ECO:0000269|PubMed:22278222, ECO:0000269|PubMed:7565688, ECO:0000269|PubMed:7972084}. |
| P78524 | DENND2B | S465 | ochoa | DENN domain-containing protein 2B (HeLa tumor suppression 1) (Suppression of tumorigenicity 5 protein) | [Isoform 1]: May be involved in cytoskeletal organization and tumorogenicity. Seems to be involved in a signaling transduction pathway leading to activation of MAPK1/ERK2. Plays a role in EGFR trafficking from recycling endosomes back to the cell membrane (PubMed:29030480). {ECO:0000269|PubMed:29030480, ECO:0000269|PubMed:9632734}.; FUNCTION: [Isoform 2]: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269|PubMed:20937701}.; FUNCTION: [Isoform 3]: May block ERK2 activation stimulated by ABL1 (Probable). May alter cell morphology and cell growth (Probable). {ECO:0000305|PubMed:10229203, ECO:0000305|PubMed:9632734}. |
| P83111 | LACTB | S207 | ochoa | Serine beta-lactamase-like protein LACTB, mitochondrial (EC 3.4.-.-) | Mitochondrial serine protease that acts as a regulator of mitochondrial lipid metabolism (PubMed:28329758). Acts by decreasing protein levels of PISD, a mitochondrial enzyme that converts phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn), thereby affecting mitochondrial lipid metabolism (PubMed:28329758). It is unclear whether it acts directly by mediating proteolysis of PISD or by mediating proteolysis of another lipid metabolism protein (PubMed:28329758). Acts as a tumor suppressor that has the ability to inhibit proliferation of multiple types of breast cancer cells: probably by promoting decreased levels of PISD, thereby affecting mitochondrial lipid metabolism (PubMed:28329758). {ECO:0000269|PubMed:28329758}. |
| P98175 | RBM10 | S723 | ochoa | RNA-binding protein 10 (G patch domain-containing protein 9) (RNA-binding motif protein 10) (RNA-binding protein S1-1) (S1-1) | Binds to ssRNA containing the consensus sequence 5'-AGGUAA-3' (PubMed:21256132). May be involved in post-transcriptional processing, most probably in mRNA splicing (PubMed:18315527). Binds to RNA homopolymers, with a preference for poly(G) and poly(U) and little for poly(A) (By similarity). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000250|UniProtKB:P70501, ECO:0000269|PubMed:18315527, ECO:0000269|PubMed:21256132, ECO:0000269|PubMed:28431233}. |
| Q00059 | TFAM | S177 | psp | Transcription factor A, mitochondrial (mtTFA) (Mitochondrial transcription factor 1) (MtTF1) (Transcription factor 6) (TCF-6) (Transcription factor 6-like 2) | Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation (PubMed:29445193, PubMed:32183942). Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA (PubMed:29149603). In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (PubMed:20410300). Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase (PubMed:22037172). Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites (PubMed:22037172). Is able to unwind DNA (PubMed:22037172). Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes (PubMed:1737790). Required for maintenance of normal levels of mitochondrial DNA (PubMed:19304746, PubMed:22841477). May play a role in organizing and compacting mitochondrial DNA (PubMed:22037171). {ECO:0000269|PubMed:1737790, ECO:0000269|PubMed:19304746, ECO:0000269|PubMed:20410300, ECO:0000269|PubMed:22037171, ECO:0000269|PubMed:22037172, ECO:0000269|PubMed:22841477, ECO:0000269|PubMed:29149603, ECO:0000269|PubMed:29445193, ECO:0000269|PubMed:32183942}. |
| Q00536 | CDK16 | S95 | ochoa|psp | Cyclin-dependent kinase 16 (EC 2.7.11.22) (Cell division protein kinase 16) (PCTAIRE-motif protein kinase 1) (Serine/threonine-protein kinase PCTAIRE-1) | Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro). {ECO:0000250, ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189, ECO:0000269|PubMed:22798068}. |
| Q00537 | CDK17 | S122 | ochoa | Cyclin-dependent kinase 17 (EC 2.7.11.22) (Cell division protein kinase 17) (PCTAIRE-motif protein kinase 2) (Serine/threonine-protein kinase PCTAIRE-2) | May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1 (By similarity). {ECO:0000250}. |
| Q01484 | ANK2 | S2458 | ochoa | Ankyrin-2 (ANK-2) (Ankyrin-B) (Brain ankyrin) (Non-erythroid ankyrin) | Plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in several cell types, including cardiomyocytes, as well as in striated muscle cells. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions. In cardiomyocytes, required for coordinate assembly of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma sites. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate (PubMed:12571597). In the inner segment of rod photoreceptors, required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) (By similarity). Plays a role in endocytosis and intracellular protein transport. Associates with phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds dynactin to promote long-range motility of cells. Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (By similarity). {ECO:0000250|UniProtKB:Q8C8R3, ECO:0000269|PubMed:12571597}. |
| Q05209 | PTPN12 | S673 | ochoa | Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48) (PTP-PEST) (Protein-tyrosine phosphatase G1) (PTPG1) | Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades (PubMed:18559503). Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2 (PubMed:17329398, PubMed:27134172). Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (PubMed:27134172). {ECO:0000269|PubMed:17329398, ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:27134172}. |
| Q08050 | FOXM1 | S451 | ochoa|psp | Forkhead box protein M1 (Forkhead-related protein FKHL16) (Hepatocyte nuclear factor 3 forkhead homolog 11) (HFH-11) (HNF-3/fork-head homolog 11) (M-phase phosphoprotein 2) (MPM-2 reactive phosphoprotein 2) (Transcription factor Trident) (Winged-helix factor from INS-1 cells) | Transcription factor regulating the expression of cell cycle genes essential for DNA replication and mitosis (PubMed:19160488, PubMed:20360045). Plays a role in the control of cell proliferation (PubMed:19160488). Also plays a role in DNA break repair, participating in the DNA damage checkpoint response (PubMed:17101782). Promotes transcription of PHB2 (PubMed:33754036). {ECO:0000269|PubMed:17101782, ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:20360045, ECO:0000269|PubMed:33754036}. |
| Q12770 | SCAP | S937 | ochoa|psp | Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein) | Escort protein required for cholesterol as well as lipid homeostasis (By similarity). Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:26311497). At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum (By similarity). Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway (PubMed:26311497). Binds cholesterol via its SSD domain (By similarity). {ECO:0000250|UniProtKB:P97260, ECO:0000269|PubMed:26311497}. |
| Q12873 | CHD3 | S1601 | ochoa | Chromodomain-helicase-DNA-binding protein 3 (CHD-3) (EC 3.6.4.-) (ATP-dependent helicase CHD3) (Mi-2 autoantigen 240 kDa protein) (Mi2-alpha) (Zinc finger helicase) (hZFH) | ATP-dependent chromatin-remodeling factor that binds and distorts nucleosomal DNA (PubMed:28977666). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666, PubMed:30397230, PubMed:9804427). Involved in transcriptional repression as part of the NuRD complex (PubMed:27068747). Required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity (PubMed:17626165). {ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:27068747, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:30397230, ECO:0000269|PubMed:9804427}. |
| Q12888 | TP53BP1 | S1028 | ochoa|psp | TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1) | Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250|UniProtKB:P70399, ECO:0000269|PubMed:12364621, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:22553214, ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112, ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:31135337, ECO:0000269|PubMed:37696958}. |
| Q12959 | DLG1 | S122 | ochoa|psp | Disks large homolog 1 (Synapse-associated protein 97) (SAP-97) (SAP97) (hDlg) | Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Promotes epithelial cell layer barrier function via maintaining cell-cell adhesion (By similarity). May also play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel. During long-term depression in hippocampal neurons, it recruits ADAM10 to the plasma membrane (PubMed:23676497). {ECO:0000250|UniProtKB:A0A8C0TYJ0, ECO:0000250|UniProtKB:Q811D0, ECO:0000269|PubMed:10656683, ECO:0000269|PubMed:12445884, ECO:0000269|PubMed:14699157, ECO:0000269|PubMed:15263016, ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:20605917, ECO:0000269|PubMed:23676497}. |
| Q13427 | PPIG | S290 | ochoa | Peptidyl-prolyl cis-trans isomerase G (PPIase G) (Peptidyl-prolyl isomerase G) (EC 5.2.1.8) (CASP10) (Clk-associating RS-cyclophilin) (CARS-Cyp) (CARS-cyclophilin) (SR-cyclophilin) (SR-cyp) (SRcyp) (Cyclophilin G) (Rotamase G) | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing. {ECO:0000269|PubMed:20676357}. |
| Q13442 | PDAP1 | S19 | ochoa | 28 kDa heat- and acid-stable phosphoprotein (PDGF-associated protein) (PAP) (PDGFA-associated protein 1) (PAP1) | Enhances PDGFA-stimulated cell growth in fibroblasts, but inhibits the mitogenic effect of PDGFB. {ECO:0000250}. |
| Q13459 | MYO9B | S1926 | ochoa | Unconventional myosin-IXb (Unconventional myosin-9b) | Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions (PubMed:9490638). Also acts as a GTPase activator for RHOA (PubMed:26529257, PubMed:9490638). Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). {ECO:0000269|PubMed:26529257, ECO:0000269|PubMed:9490638}. |
| Q13936 | CACNA1C | S815 | ochoa | Voltage-dependent L-type calcium channel subunit alpha-1C (Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) (Voltage-gated calcium channel subunit alpha Cav1.2) | Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:12181424, PubMed:15454078, PubMed:15863612, PubMed:16299511, PubMed:17224476, PubMed:20953164, PubMed:23677916, PubMed:24728418, PubMed:26253506, PubMed:27218670, PubMed:29078335, PubMed:29742403, PubMed:30023270, PubMed:30172029, PubMed:34163037, PubMed:8099908). Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity). Plays an important role in excitation-contraction coupling in the heart. Required for normal heart development and normal regulation of heart rhythm (PubMed:15454078, PubMed:15863612, PubMed:17224476, PubMed:24728418, PubMed:26253506). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (PubMed:28119464). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (Probable). {ECO:0000250|UniProtKB:P15381, ECO:0000269|PubMed:12181424, ECO:0000269|PubMed:15454078, ECO:0000269|PubMed:15863612, ECO:0000269|PubMed:16299511, ECO:0000269|PubMed:17224476, ECO:0000269|PubMed:20953164, ECO:0000269|PubMed:23677916, ECO:0000269|PubMed:24728418, ECO:0000269|PubMed:25260352, ECO:0000269|PubMed:25633834, ECO:0000269|PubMed:26253506, ECO:0000269|PubMed:27218670, ECO:0000269|PubMed:28119464, ECO:0000269|PubMed:29078335, ECO:0000269|PubMed:29742403, ECO:0000269|PubMed:30023270, ECO:0000269|PubMed:30172029, ECO:0000269|PubMed:31430211, ECO:0000269|PubMed:34163037, ECO:0000269|PubMed:8099908, ECO:0000305}.; FUNCTION: [Isoform 12]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:12176756, ECO:0000269|PubMed:7737988}.; FUNCTION: [Isoform 13]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:17071743}.; FUNCTION: [Isoform 14]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:17071743}.; FUNCTION: [Isoform 15]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:17071743}.; FUNCTION: [Isoform 16]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9087614}.; FUNCTION: [Isoform 17]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9087614}.; FUNCTION: [Isoform 18]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:8392192}.; FUNCTION: [Isoform 19]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:7737988}.; FUNCTION: [Isoform 20]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:7737988}.; FUNCTION: [Isoform 21]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9607315}.; FUNCTION: [Isoform 22]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9607315}.; FUNCTION: [Isoform 23]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9607315}.; FUNCTION: [Isoform 24]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:17071743}.; FUNCTION: [Isoform 25]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:17071743}.; FUNCTION: [Isoform 26]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9013606}.; FUNCTION: [Isoform 27]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9013606}.; FUNCTION: [Isoform 34]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:11741969}.; FUNCTION: (Microbial infection) Acts as a receptor for Influenzavirus (PubMed:29779930). May play a critical role in allowing virus entry when sialylated and expressed on lung tissues (PubMed:29779930). {ECO:0000269|PubMed:29779930}. |
| Q15181 | PPA1 | S30 | ochoa | Inorganic pyrophosphatase (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase) | None |
| Q15468 | STIL | S1225 | ochoa | SCL-interrupting locus protein (TAL-1-interrupting locus protein) | Immediate-early gene. Plays an important role in embryonic development as well as in cellular growth and proliferation; its long-term silencing affects cell survival and cell cycle distribution as well as decreases CDK1 activity correlated with reduced phosphorylation of CDK1. Plays a role as a positive regulator of the sonic hedgehog pathway, acting downstream of PTCH1 (PubMed:16024801, PubMed:9372240). Plays an important role in the regulation of centriole duplication. Required for the onset of procentriole formation and proper mitotic progression. During procentriole formation, is essential for the correct loading of SASS6 and CPAP to the base of the procentriole to initiate procentriole assembly (PubMed:22020124). In complex with STIL acts as a modulator of PLK4-driven cytoskeletal rearrangements and directional cell motility (PubMed:29712910, PubMed:32107292). {ECO:0000269|PubMed:16024801, ECO:0000269|PubMed:22020124, ECO:0000269|PubMed:29712910, ECO:0000269|PubMed:32107292, ECO:0000269|PubMed:9372240}. |
| Q15652 | JMJD1C | S2007 | ochoa | Probable JmjC domain-containing histone demethylation protein 2C (EC 1.14.11.-) (Jumonji domain-containing protein 1C) (Thyroid receptor-interacting protein 8) (TR-interacting protein 8) (TRIP-8) | Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity). {ECO:0000250}. |
| Q16665 | HIF1A | S687 | ochoa|psp | Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha) (ARNT-interacting protein) (Basic-helix-loop-helix-PAS protein MOP1) (Class E basic helix-loop-helix protein 78) (bHLHe78) (Member of PAS protein 1) (PAS domain-containing protein 8) | Functions as a master transcriptional regulator of the adaptive response to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:18658046, PubMed:20624928, PubMed:22009797, PubMed:30125331, PubMed:9887100). Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:20624928, PubMed:22009797, PubMed:30125331, PubMed:9887100). Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease (PubMed:22009797). Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300 (PubMed:16543236, PubMed:9887100). Activity is enhanced by interaction with NCOA1 and/or NCOA2 (PubMed:10594042). Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP (PubMed:10202154, PubMed:10594042). Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (PubMed:19528298). {ECO:0000250|UniProtKB:Q61221, ECO:0000269|PubMed:10202154, ECO:0000269|PubMed:10594042, ECO:0000269|PubMed:11292861, ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:15465032, ECO:0000269|PubMed:16543236, ECO:0000269|PubMed:16973622, ECO:0000269|PubMed:17610843, ECO:0000269|PubMed:18658046, ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20624928, ECO:0000269|PubMed:22009797, ECO:0000269|PubMed:30125331, ECO:0000269|PubMed:9887100}.; FUNCTION: (Microbial infection) Upon infection by human coronavirus SARS-CoV-2, is required for induction of glycolysis in monocytes and the consequent pro-inflammatory state (PubMed:32697943). In monocytes, induces expression of ACE2 and cytokines such as IL1B, TNF, IL6, and interferons (PubMed:32697943). Promotes human coronavirus SARS-CoV-2 replication and monocyte inflammatory response (PubMed:32697943). {ECO:0000269|PubMed:32697943}. |
| Q16799 | RTN1 | S336 | ochoa | Reticulon-1 (Neuroendocrine-specific protein) | Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity. {ECO:0000269|PubMed:15286784}. |
| Q3KQU3 | MAP7D1 | S742 | ochoa | MAP7 domain-containing protein 1 (Arginine/proline-rich coiled-coil domain-containing protein 1) (Proline/arginine-rich coiled-coil domain-containing protein 1) | Microtubule-stabilizing protein involved in the control of cell motility and neurite outgrowth. Facilitate microtubule stabilization through the maintenance of acetylated stable microtubules. {ECO:0000250|UniProtKB:A2AJI0}. |
| Q58FF3 | HSP90B2P | S158 | ochoa | Putative endoplasmin-like protein (Putative heat shock protein 90 kDa beta member 2) | Putative molecular chaperone. {ECO:0000250}. |
| Q5HYI7 | MTX3 | S284 | ochoa | Metaxin-3 | Could function in transport of proteins into the mitochondrion. {ECO:0000250}. |
| Q5T2T1 | MPP7 | S64 | ochoa | MAGUK p55 subfamily member 7 | Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact. {ECO:0000269|PubMed:17332497}. |
| Q5TCZ1 | SH3PXD2A | S593 | ochoa | SH3 and PX domain-containing protein 2A (Adapter protein TKS5) (Five SH3 domain-containing protein) (SH3 multiple domains protein 1) (Tyrosine kinase substrate with five SH3 domains) | Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells (PubMed:27789576). Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of amyloid-beta peptide. {ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:15710328, ECO:0000269|PubMed:15710903, ECO:0000269|PubMed:19755710, ECO:0000269|PubMed:20609497, ECO:0000269|PubMed:27789576}. |
| Q5UIP0 | RIF1 | S1772 | ochoa | Telomere-associated protein RIF1 (Rap1-interacting factor 1 homolog) | Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs (PubMed:15342490, PubMed:28241136). In response to DNA damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23333306, PubMed:28241136). Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs (PubMed:28241136). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs (PubMed:23333306). In the same time, RIF1 and TP53BP1 specifically counteract the function of BRCA1 by blocking DSBs resection via homologous recombination (HR) during G1 phase (PubMed:23333306). Also required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (By similarity). Promotes NHEJ of dysfunctional telomeres (By similarity). {ECO:0000250|UniProtKB:Q6PR54, ECO:0000269|PubMed:15342490, ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:28241136}. |
| Q5VT06 | CEP350 | S2839 | ochoa | Centrosome-associated protein 350 (Cep350) (Centrosome-associated protein of 350 kDa) | Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CPAP (PubMed:19052644). Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network (PubMed:16314388, PubMed:17878239, PubMed:28659385). Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity (PubMed:15615782). Required for ciliation (PubMed:28659385). {ECO:0000269|PubMed:15615782, ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:17878239, ECO:0000269|PubMed:19052644, ECO:0000269|PubMed:28659385}. |
| Q5VWQ0 | RSBN1 | S81 | ochoa | Lysine-specific demethylase 9 (KDM9) (EC 1.14.11.-) (Round spermatid basic protein 1) | Histone demethylase that specifically demethylates dimethylated 'Lys-20' of histone H4 (H4K20me2), thereby modulating chromosome architecture. {ECO:0000250|UniProtKB:Q80T69}. |
| Q676U5 | ATG16L1 | S255 | ochoa | Autophagy-related protein 16-1 (APG16-like 1) | Plays an essential role in both canonical and non-canonical autophagy: interacts with ATG12-ATG5 to mediate the lipidation to ATG8 family proteins (MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP) (PubMed:23376921, PubMed:23392225, PubMed:24553140, PubMed:24954904, PubMed:27273576, PubMed:29317426, PubMed:30778222, PubMed:33909989). Acts as a molecular hub, coordinating autophagy pathways via distinct domains that support either canonical or non-canonical signaling (PubMed:29317426, PubMed:30778222). During canonical autophagy, interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to ATG8 proteins, to produce a membrane-bound activated form of ATG8 (PubMed:23376921, PubMed:23392225, PubMed:24553140, PubMed:24954904, PubMed:27273576). Thereby, controls the elongation of the nascent autophagosomal membrane (PubMed:23376921, PubMed:23392225, PubMed:24553140, PubMed:24954904, PubMed:27273576). As part of the ATG8 conjugation system with ATG5 and ATG12, required for recruitment of LRRK2 to stressed lysosomes and induction of LRRK2 kinase activity in response to lysosomal stress (By similarity). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, probably by catalyzing conjugation of phosphatidylserine (PS) to ATG8 (PubMed:33909989). Non-canonical autophagy plays a key role in epithelial cells to limit lethal infection by influenza A (IAV) virus (By similarity). Regulates mitochondrial antiviral signaling (MAVS)-dependent type I interferon (IFN-I) production (PubMed:22749352, PubMed:25645662). Negatively regulates NOD1- and NOD2-driven inflammatory cytokine response (PubMed:24238340). Instead, promotes an autophagy-dependent antibacterial pathway together with NOD1 or NOD2 (PubMed:20637199). Plays a role in regulating morphology and function of Paneth cell (PubMed:18849966). {ECO:0000250|UniProtKB:Q8C0J2, ECO:0000269|PubMed:18849966, ECO:0000269|PubMed:20637199, ECO:0000269|PubMed:22749352, ECO:0000269|PubMed:23376921, ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:24238340, ECO:0000269|PubMed:24553140, ECO:0000269|PubMed:24954904, ECO:0000269|PubMed:25645662, ECO:0000269|PubMed:27273576, ECO:0000269|PubMed:29317426, ECO:0000269|PubMed:30778222, ECO:0000269|PubMed:33909989}. |
| Q69YN4 | VIRMA | S222 | ochoa | Protein virilizer homolog | Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:24981863, PubMed:29507755). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs in the 3'-UTR near the stop codon: recruits the catalytic core components METTL3 and METTL14, thereby guiding m6A methylation at specific sites (PubMed:29507755). Required for mRNA polyadenylation via its role in selective m6A methylation: m6A methylation of mRNAs in the 3'-UTR near the stop codon correlating with alternative polyadenylation (APA) (PubMed:29507755). {ECO:0000269|PubMed:24981863, ECO:0000269|PubMed:29507755}. |
| Q6JBY9 | RCSD1 | S284 | ochoa | CapZ-interacting protein (Protein kinase substrate CapZIP) (RCSD domain-containing protein 1) | Stress-induced phosphorylation of CAPZIP may regulate the ability of F-actin-capping protein to remodel actin filament assembly. {ECO:0000269|PubMed:15850461}. |
| Q6N021 | TET2 | S334 | ochoa | Methylcytosine dioxygenase TET2 (EC 1.14.11.80) | Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in active DNA demethylation. Has a preference for 5-hydroxymethylcytosine in CpG motifs. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT. {ECO:0000269|PubMed:19483684, ECO:0000269|PubMed:21057493, ECO:0000269|PubMed:21817016, ECO:0000269|PubMed:23222540, ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:24315485, ECO:0000269|PubMed:32518946}. |
| Q6NT76 | HMBOX1 | S133 | ochoa | Homeobox-containing protein 1 (Homeobox telomere-binding protein 1) (Telomere-associated homeobox-containing protein 1) | Binds directly to 5'-TTAGGG-3' repeats in telomeric DNA (PubMed:23685356, PubMed:23813958). Associates with the telomerase complex at sites of active telomere processing and positively regulates telomere elongation (PubMed:23685356). Important for TERT binding to chromatin, indicating a role in recruitment of the telomerase complex to telomeres (By similarity). Also plays a role in the alternative lengthening of telomeres (ALT) pathway in telomerase-negative cells where it promotes formation and/or maintenance of ALT-associated promyelocytic leukemia bodies (APBs) (PubMed:23813958). Enhances formation of telomere C-circles in ALT cells, suggesting a possible role in telomere recombination (PubMed:23813958). Might also be involved in the DNA damage response at telomeres (PubMed:23813958). {ECO:0000250|UniProtKB:Q8BJA3, ECO:0000269|PubMed:23685356, ECO:0000269|PubMed:23813958}. |
| Q6ZRV2 | FAM83H | S998 | ochoa | Protein FAM83H | May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688). {ECO:0000269|PubMed:18252228, ECO:0000269|PubMed:23902688}. |
| Q6ZU35 | CRACD | S53 | ochoa | Capping protein-inhibiting regulator of actin dynamics (Cancer-related regulator of actin dynamics) | Involved in epithelial cell integrity by acting on the maintenance of the actin cytoskeleton. Positively regulates the actin polymerization, by inhibiting the interaction of actin-capping proteins with actin. {ECO:0000269|PubMed:30361697}. |
| Q6ZU52 | KIAA0408 | S128 | ochoa | Uncharacterized protein KIAA0408 | None |
| Q7Z2Z1 | TICRR | S1064 | ochoa | Treslin (TopBP1-interacting checkpoint and replication regulator) (TopBP1-interacting, replication-stimulating protein) | Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with TOPBP1 by participating in CDK2-mediated loading of CDC45L onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation. {ECO:0000269|PubMed:20116089}. |
| Q7Z6Z7 | HUWE1 | S2636 | ochoa|psp | E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1) | E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250|UniProtKB:P51593, ECO:0000250|UniProtKB:Q7TMY8, ECO:0000269|PubMed:15567145, ECO:0000269|PubMed:15767685, ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:15989957, ECO:0000269|PubMed:17567951, ECO:0000269|PubMed:18488021, ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:20534529, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:27746020, ECO:0000269|PubMed:30217973, ECO:0000269|PubMed:35776542}. |
| Q86W56 | PARG | S302 | ochoa | Poly(ADP-ribose) glycohydrolase (EC 3.2.1.143) | Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose) (PubMed:15450800, PubMed:21892188, PubMed:23102699, PubMed:23474714, PubMed:33186521, PubMed:34019811, PubMed:34321462). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers (PubMed:23102699, PubMed:23481255). It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated (PubMed:21892188, PubMed:23474714, PubMed:33186521). Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG (PubMed:23102699, PubMed:34019811). Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress (PubMed:24906880). Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond (PubMed:33186521). Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters (PubMed:23102699). Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). {ECO:0000269|PubMed:15450800, ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:23102699, ECO:0000269|PubMed:23474714, ECO:0000269|PubMed:23481255, ECO:0000269|PubMed:24906880, ECO:0000269|PubMed:27257257, ECO:0000269|PubMed:33186521, ECO:0000269|PubMed:34019811, ECO:0000269|PubMed:34321462}. |
| Q8IUD2 | ERC1 | S110 | ochoa | ELKS/Rab6-interacting/CAST family member 1 (ERC-1) (Rab6-interacting protein 2) | Regulatory subunit of the IKK complex. Probably recruits IkappaBalpha/NFKBIA to the complex. May be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. May be involved in vesicle trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to Golgi transport. {ECO:0000269|PubMed:15218148}. |
| Q8IVB4 | SLC9A9 | S600 | ochoa | Sodium/hydrogen exchanger 9 (Na(+)/H(+) exchanger 9) (NHE-9) (Solute carrier family 9 member 9) | Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+) (Probable). By facilitating proton efflux, SLC9A9 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Regulates organellar pH and consequently, e.g., endosome maturation and endocytic trafficking of plasma membrane receptors and neurotransporters (PubMed:15522866, PubMed:24065030, PubMed:28130443). Promotes the recycling of transferrin receptors back to the cell surface to facilitate additional iron uptake in the brain (PubMed:28130443). Regulates synaptic transmission by regulating the luminal pH of axonal endosomes (By similarity). Regulates phagosome lumenal pH, thus affecting phagosome maturation, and consequently, microbicidal activity in macrophages (By similarity). Can also be active at the cell surface of specialized cells, e.g., in the inner ear hair bundles uses the high K(+) of the endolymph to regulate intracelular pH (By similarity). {ECO:0000250|UniProtKB:Q8BZ00, ECO:0000269|PubMed:15522866, ECO:0000269|PubMed:24065030, ECO:0000269|PubMed:28130443, ECO:0000305|PubMed:15522866}. |
| Q8IWZ3 | ANKHD1 | S1670 | ochoa | Ankyrin repeat and KH domain-containing protein 1 (HIV-1 Vpr-binding ankyrin repeat protein) (Multiple ankyrin repeats single KH domain) (hMASK) | May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases. {ECO:0000269|PubMed:16098192}. |
| Q8IZN3 | ZDHHC14 | S446 | ochoa | Palmitoyltransferase ZDHHC14 (EC 2.3.1.225) (DHHC domain-containing cysteine-rich protein 14) (DHHC-14) (NEW1 domain-containing protein) (NEW1CP) (Zinc finger DHHC domain-containing protein 14) | Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. May have a palmitoyltransferase activity toward the beta-2 adrenergic receptor/ADRB2 and thereby regulate G protein-coupled receptor signaling (PubMed:27481942). May play a role in cell differentiation and apoptosis (PubMed:21151021, PubMed:24407904). {ECO:0000269|PubMed:21151021, ECO:0000269|PubMed:24407904, ECO:0000269|PubMed:27481942}. |
| Q8NCN4 | RNF169 | S506 | ochoa | E3 ubiquitin-protein ligase RNF169 (EC 2.3.2.27) (RING finger protein 169) (RING-type E3 ubiquitin transferase RNF169) | Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization (PubMed:22492721, PubMed:30773093). Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1 (PubMed:30104380, PubMed:30773093). E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair. {ECO:0000269|PubMed:22492721, ECO:0000269|PubMed:22733822, ECO:0000269|PubMed:22742833, ECO:0000269|PubMed:30104380, ECO:0000269|PubMed:30773093}. |
| Q8NFQ8 | TOR1AIP2 | S120 | ochoa | Torsin-1A-interacting protein 2 (Lumenal domain-like LAP1) | Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity. {ECO:0000269|PubMed:19339278, ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647}. |
| Q8TB72 | PUM2 | S136 | ochoa | Pumilio homolog 2 (Pumilio-2) | Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (, PubMed:21397187). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:22345517). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm (PubMed:26724866). May regulate DCUN1D3 mRNA levels (PubMed:25349211). May support proliferation and self-renewal of stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A expression at a postranscriptional level (PubMed:28431233). {ECO:0000269|PubMed:18776931, ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:22345517, ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26724866, ECO:0000269|PubMed:28431233}. |
| Q8TC44 | POC1B | S321 | ochoa | POC1 centriolar protein homolog B (Pix1) (Proteome of centriole protein 1B) (WD repeat-containing protein 51B) | Plays an important role in centriole assembly and/or stability and ciliogenesis (PubMed:20008567, PubMed:32060285). Involved in early steps of centriole duplication, as well as in the later steps of centriole length control (PubMed:19109428). Acts in concert with POC1A to ensure centriole integrity and proper mitotic spindle formation (PubMed:32060285). Required for primary cilia formation, ciliary length and also cell proliferation (PubMed:23015594). Required for retinal integrity (PubMed:25044745). Acts as a positive regulator of centriole elongation (PubMed:37934472). {ECO:0000269|PubMed:19109428, ECO:0000269|PubMed:20008567, ECO:0000269|PubMed:23015594, ECO:0000269|PubMed:25044745, ECO:0000269|PubMed:32060285, ECO:0000269|PubMed:37934472}. |
| Q8TC90 | CCER1 | S226 | ochoa | Coiled-coil domain-containing glutamate-rich protein 1 | Regulator of histone epigenetic modifications and chromatin compaction into the sperm head, required for histone-to-protamine (HTP) transition. HTP is a key event in which somatic histones are first replaced by testis-specific histone variants, then transition proteins (TNPs) are incorporated into the spermatid nucleus, and finally protamines (PRMs) replace the TNPs to promote chromatin condensation. {ECO:0000250|UniProtKB:Q9CQL2}. |
| Q8TD55 | PLEKHO2 | S89 | ochoa | Pleckstrin homology domain-containing family O member 2 (PH domain-containing family O member 2) (Pleckstrin homology domain-containing family Q member 1) (PH domain-containing family Q member 1) | None |
| Q8WUF5 | PPP1R13L | S489 | ochoa | RelA-associated inhibitor (Inhibitor of ASPP protein) (Protein iASPP) (NFkB-interacting protein 1) (PPP1R13B-like protein) | Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis (PubMed:12524540). Is involved in NF-kappa-B dependent negative regulation of inflammatory response (PubMed:28069640). {ECO:0000269|PubMed:10336463, ECO:0000269|PubMed:12134007, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:15489900, ECO:0000269|PubMed:28069640}. |
| Q8WWM7 | ATXN2L | S306 | ochoa | Ataxin-2-like protein (Ataxin-2 domain protein) (Ataxin-2-related protein) | Involved in the regulation of stress granule and P-body formation. {ECO:0000269|PubMed:23209657}. |
| Q8WXG6 | MADD | S930 | ochoa | MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP) | Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250|UniProtKB:O08873, ECO:0000250|UniProtKB:Q80U28, ECO:0000269|PubMed:11577081, ECO:0000269|PubMed:18559336, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:32761064, ECO:0000269|PubMed:9115275}. |
| Q8WXI2 | CNKSR2 | S390 | ochoa | Connector enhancer of kinase suppressor of ras 2 (Connector enhancer of KSR 2) (CNK homolog protein 2) (CNK2) | May function as an adapter protein or regulator of Ras signaling pathways. {ECO:0000269|PubMed:14597674}. |
| Q8WYQ5 | DGCR8 | S377 | ochoa|psp | Microprocessor complex subunit DGCR8 (DiGeorge syndrome critical region 8) | Component of the microprocessor complex that acts as a RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs (PubMed:26027739, PubMed:26748718). The heme-bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is active in triggering pri-miRNA cleavage, whereas the heme-free DGCR8 monomer binds pri-miRNAs as a dimer and is much less active. Both double-stranded and single-stranded regions of a pri-miRNA are required for its binding (PubMed:15531877, PubMed:15574589, PubMed:15589161, PubMed:16751099, PubMed:16906129, PubMed:16963499, PubMed:17159994). Specifically recognizes and binds N6-methyladenosine (m6A)-containing pri-miRNAs, a modification required for pri-miRNAs processing (PubMed:25799998). Involved in the silencing of embryonic stem cell self-renewal (By similarity). Also plays a role in DNA repair by promoting the recruitment of RNF168 to RNF8 and MDC1 at DNA double-strand breaks and subsequently the clearance of DNA breaks (PubMed:34188037). {ECO:0000250|UniProtKB:Q9EQM6, ECO:0000269|PubMed:15531877, ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:15589161, ECO:0000269|PubMed:16751099, ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:16963499, ECO:0000269|PubMed:17159994, ECO:0000269|PubMed:25799998, ECO:0000269|PubMed:26027739, ECO:0000269|PubMed:26748718}. |
| Q92539 | LPIN2 | S229 | ochoa | Phosphatidate phosphatase LPIN2 (EC 3.1.3.4) (Lipin-2) | Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the endoplasmic reticulum membrane. Plays important roles in controlling the metabolism of fatty acids at different levels. Also acts as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism. {ECO:0000250|UniProtKB:Q99PI5}. |
| Q92543 | SNX19 | S699 | ochoa | Sorting nexin-19 | Plays a role in intracellular vesicle trafficking and exocytosis (PubMed:24843546). May play a role in maintaining insulin-containing dense core vesicles in pancreatic beta-cells and in preventing their degradation. May play a role in insulin secretion (PubMed:24843546). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (By similarity). {ECO:0000250|UniProtKB:Q6P4T1, ECO:0000269|PubMed:24843546}. |
| Q92574 | TSC1 | S644 | ochoa | Hamartin (Tuberous sclerosis 1 protein) | Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12906785, PubMed:15340059, PubMed:24529379, PubMed:28215400). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12906785, PubMed:15340059, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12271141, PubMed:24529379, PubMed:28215400, PubMed:33215753). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (PubMed:10585443, PubMed:28215400). Acts as a tumor suppressor (PubMed:9242607). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (PubMed:16464865, PubMed:29127155). {ECO:0000250|UniProtKB:Q9Z136, ECO:0000269|PubMed:10585443, ECO:0000269|PubMed:12172553, ECO:0000269|PubMed:12271141, ECO:0000269|PubMed:12906785, ECO:0000269|PubMed:15340059, ECO:0000269|PubMed:16464865, ECO:0000269|PubMed:24529379, ECO:0000269|PubMed:28215400, ECO:0000269|PubMed:29127155, ECO:0000269|PubMed:33215753, ECO:0000269|PubMed:9242607}. |
| Q92974 | ARHGEF2 | S932 | ochoa | Rho guanine nucleotide exchange factor 2 (Guanine nucleotide exchange factor H1) (GEF-H1) (Microtubule-regulated Rho-GEF) (Proliferating cell nucleolar antigen p40) | Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability (By similarity). Involved in neuronal progenitor cell division and differentiation (PubMed:28453519). Involved in the migration of precerebellar neurons (By similarity). {ECO:0000250|UniProtKB:Q60875, ECO:0000250|UniProtKB:Q865S3, ECO:0000269|PubMed:19043560, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:28453519, ECO:0000269|PubMed:9857026}. |
| Q969R5 | L3MBTL2 | S67 | ochoa | Lethal(3)malignant brain tumor-like protein 2 (H-l(3)mbt-like protein 2) (L(3)mbt-like protein 2) | Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. {ECO:0000269|PubMed:19233876}. |
| Q969V6 | MRTFA | S482 | ochoa | Myocardin-related transcription factor A (MRTF-A) (MKL/myocardin-like protein 1) (Megakaryoblastic leukemia 1 protein) (Megakaryocytic acute leukemia protein) | Transcription coactivator that associates with the serum response factor (SRF) transcription factor to control expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration (PubMed:26224645). The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. MRTFA binds G-actin via its RPEL repeats, regulating activity of the MRTFA-SRF complex. Activity is also regulated by filamentous actin (F-actin) in the nucleus. {ECO:0000250|UniProtKB:Q8K4J6, ECO:0000269|PubMed:26224645}. |
| Q96R06 | SPAG5 | S249 | ochoa|psp | Sperm-associated antigen 5 (Astrin) (Deepest) (Mitotic spindle-associated protein p126) (MAP126) | Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase (PubMed:11724960, PubMed:12356910, PubMed:27462074). Required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture (PubMed:17664331, PubMed:27462074). In complex with SKAP, promotes stable microtubule-kinetochore attachments. May contribute to the regulation of separase activity. May regulate AURKA localization to mitotic spindle, but not to centrosomes and CCNB1 localization to both mitotic spindle and centrosomes (PubMed:18361916, PubMed:21402792). Involved in centriole duplication. Required for CDK5RAP2, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). In non-mitotic cells, upon stress induction, inhibits mammalian target of rapamycin complex 1 (mTORC1) association and recruits the mTORC1 component RPTOR to stress granules (SGs), thereby preventing mTORC1 hyperactivation-induced apoptosis (PubMed:23953116). May enhance GSK3B-mediated phosphorylation of other substrates, such as MAPT/TAU (PubMed:18055457). {ECO:0000269|PubMed:12356910, ECO:0000269|PubMed:17664331, ECO:0000269|PubMed:18055457, ECO:0000269|PubMed:18361916, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:23953116, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:27462074, ECO:0000305|PubMed:11724960}. |
| Q96T58 | SPEN | S1287 | ochoa | Msx2-interacting protein (SMART/HDAC1-associated repressor protein) (SPEN homolog) | May serve as a nuclear matrix platform that organizes and integrates transcriptional responses. In osteoblasts, supports transcription activation: synergizes with RUNX2 to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Has also been shown to be an essential corepressor protein, which probably regulates different key pathways such as the Notch pathway. Negative regulator of the Notch pathway via its interaction with RBPSUH, which prevents the association between NOTCH1 and RBPSUH, and therefore suppresses the transactivation activity of Notch signaling. Blocks the differentiation of precursor B-cells into marginal zone B-cells. Probably represses transcription via the recruitment of large complexes containing histone deacetylase proteins. May bind both to DNA and RNA. {ECO:0000250|UniProtKB:Q62504, ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:12374742}. |
| Q99567 | NUP88 | S517 | ochoa | Nuclear pore complex protein Nup88 (88 kDa nucleoporin) (Nucleoporin Nup88) | Component of nuclear pore complex. {ECO:0000269|PubMed:30543681}. |
| Q9BQ52 | ELAC2 | S199 | ochoa | Zinc phosphodiesterase ELAC protein 2 (EC 3.1.26.11) (ElaC homolog protein 2) (Heredity prostate cancer protein 2) (Ribonuclease Z 2) (RNase Z 2) (tRNA 3 endonuclease 2) (tRNase Z 2) | Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (PubMed:21593607). Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly (PubMed:24703694). {ECO:0000269|PubMed:21593607, ECO:0000269|PubMed:24703694}. |
| Q9BRK5 | SDF4 | S209 | ochoa | 45 kDa calcium-binding protein (Cab45) (Stromal cell-derived factor 4) (SDF-4) | May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. {ECO:0000250}.; FUNCTION: Isoform 5 may be involved in the exocytosis of zymogens by pancreatic acini. |
| Q9BVV6 | KIAA0586 | S1151 | ochoa | Protein TALPID3 | Required for ciliogenesis and sonic hedgehog/SHH signaling. Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1. May play a role in early ciliogenesis in the disappearance of centriolar satellites that preceeds ciliary vesicle formation (PubMed:24421332). Involved in regulation of cell intracellular organization. Involved in regulation of cell polarity (By similarity). Required for asymmetrical localization of CEP120 to daughter centrioles (By similarity). {ECO:0000250|UniProtKB:E9PV87, ECO:0000250|UniProtKB:Q1G7G9, ECO:0000269|PubMed:24421332}. |
| Q9BZH6 | WDR11 | S619 | ochoa | WD repeat-containing protein 11 (Bromodomain and WD repeat-containing protein 2) (WD repeat-containing protein 15) | Involved in the Hedgehog (Hh) signaling pathway, is essential for normal ciliogenesis (PubMed:29263200). Regulates the proteolytic processing of GLI3 and cooperates with the transcription factor EMX1 in the induction of downstream Hh pathway gene expression and gonadotropin-releasing hormone production (PubMed:29263200). WDR11 complex facilitates the tethering of Adaptor protein-1 complex (AP-1)-derived vesicles. WDR11 complex acts together with TBC1D23 to facilitate the golgin-mediated capture of vesicles generated using AP-1 (PubMed:29426865). {ECO:0000269|PubMed:29263200, ECO:0000269|PubMed:29426865}. |
| Q9C0C2 | TNKS1BP1 | S1652 | ochoa | 182 kDa tankyrase-1-binding protein | None |
| Q9C0G0 | ZNF407 | S952 | ochoa | Zinc finger protein 407 | May be involved in transcriptional regulation. |
| Q9H1E3 | NUCKS1 | S214 | ochoa | Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1 (P1) | Chromatin-associated protein involved in DNA repair by promoting homologous recombination (HR) (PubMed:26323318). Binds double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures, but with less affinity than RAD51AP1 (PubMed:26323318). {ECO:0000269|PubMed:26323318}. |
| Q9H3Q1 | CDC42EP4 | S174 | ochoa | Cdc42 effector protein 4 (Binder of Rho GTPases 4) | Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts. |
| Q9HB65 | ELL3 | S239 | ochoa | RNA polymerase II elongation factor ELL3 | Enhancer-binding elongation factor that specifically binds enhancers in embryonic stem cells (ES cells), marks them, and is required for their future activation during stem cell specification. Does not only bind to enhancer regions of active genes, but also marks the enhancers that are in a poised or inactive state in ES cells and is required for establishing proper RNA polymerase II occupancy at developmentally regulated genes in a cohesin-dependent manner. Probably required for priming developmentally regulated genes for later recruitment of the super elongation complex (SEC), for transcriptional activation during differentiation. Required for recruitment of P-TEFb within SEC during differentiation. Probably preloaded on germ cell chromatin, suggesting that it may prime gene activation by marking enhancers as early as in the germ cells. Promoting epithelial-mesenchymal transition (EMT) (By similarity). Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). {ECO:0000250, ECO:0000269|PubMed:10882741, ECO:0000269|PubMed:22195968}. |
| Q9NRE2 | TSHZ2 | S69 | ochoa | Teashirt homolog 2 (Ovarian cancer-related protein 10-2) (OVC10-2) (Zinc finger protein 218) | Probable transcriptional regulator involved in developmental processes. May act as a transcriptional repressor (Potential). {ECO:0000305}. |
| Q9NRH2 | SNRK | S275 | ochoa | SNF-related serine/threonine-protein kinase (EC 2.7.11.1) (SNF1-related kinase) | May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis. {ECO:0000250|UniProtKB:Q63553, ECO:0000269|PubMed:12234663, ECO:0000269|PubMed:15733851}. |
| Q9NVT9 | ARMC1 | S246 | ochoa | Armadillo repeat-containing protein 1 | In association with mitochondrial contact site and cristae organizing system (MICOS) complex components and mitochondrial outer membrane sorting assembly machinery (SAM) complex components may regulate mitochondrial dynamics playing a role in determining mitochondrial length, distribution and motility. {ECO:0000269|PubMed:31644573}. |
| Q9NYF8 | BCLAF1 | S512 | ochoa | Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1) | Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269|PubMed:18794151}. |
| Q9NZB2 | FAM120A | S638 | ochoa | Constitutive coactivator of PPAR-gamma-like protein 1 (Oxidative stress-associated SRC activator) (Protein FAM120A) | Component of the oxidative stress-induced survival signaling. May regulate the activation of SRC family protein kinases (PubMed:19015244). May act as a scaffolding protein enabling SRC family protein kinases to phosphorylate and activate PI3-kinase (PubMed:19015244). Binds IGF2 RNA and promotes the production of IGF2 protein (PubMed:19015244). {ECO:0000269|PubMed:19015244}. |
| Q9P0K7 | RAI14 | S512 | ochoa | Ankycorbin (Ankyrin repeat and coiled-coil structure-containing protein) (Novel retinal pigment epithelial cell protein) (Retinoic acid-induced protein 14) | Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier. {ECO:0000250|UniProtKB:Q5U312}. |
| Q9P0L9 | PKD2L1 | S686 | psp | Polycystin-2-like protein 1 (Polycystin-2L1) (Polycystic kidney disease 2-like 1 protein) (Polycystin-2 homolog) (Polycystin-L) (Polycystin-L1) | Homotetrameric, non-selective cation channel that is permeable to sodium, potassium, magnesium and calcium (PubMed:10517637, PubMed:11959145, PubMed:25820328, PubMed:27754867, PubMed:29425510, PubMed:30004384). Also forms functionnal heteromeric channels with PKD1, PKD1L1 and PKD1L3 (PubMed:23212381, PubMed:24336289). Pore-forming subunit of a heterotetrameric, non-selective cation channel, formed by PKD1L2 and PKD1L3, that is permeable to sodium, potassium, magnesium and calcium and which may act as a sour taste receptor in gustatory cells; however, its contribution to sour taste perception is unclear in vivo and may be indirect (PubMed:19812697, PubMed:23212381). The homomeric and heteromeric channels formed by PKD1L2 and PKD1L3 are activated by low pH and Ca(2+), but opens only when the extracellular pH rises again and after the removal of acid stimulus (PubMed:23212381). Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in primary cilia, where it controls cilium calcium concentration, without affecting cytoplasmic calcium concentration, and regulates sonic hedgehog/SHH signaling and GLI2 transcription (PubMed:24336289). The PKD1L1:PKD2L1 complex channel is mechanosensitive only at high pressures and is highly temperature sensitive (PubMed:24336289). Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1 that produces a transient increase in intracellular calcium concentration upon hypo-osmotic stimulation (200 mOsm) (By similarity). May play a role in the perception of carbonation taste (By similarity). May play a role in the sensory perception of water, via a mechanism that activates the channel in response to dilution of salivary bicarbonate and changes in salivary pH (By similarity). {ECO:0000250|UniProtKB:A2A259, ECO:0000269|PubMed:10517637, ECO:0000269|PubMed:11959145, ECO:0000269|PubMed:19812697, ECO:0000269|PubMed:23212381, ECO:0000269|PubMed:24336289, ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:27754867, ECO:0000269|PubMed:29425510, ECO:0000269|PubMed:30004384}. |
| Q9P0V3 | SH3BP4 | S42 | ochoa | SH3 domain-binding protein 4 (EH-binding protein 10) (Transferrin receptor-trafficking protein) | May function in transferrin receptor internalization at the plasma membrane through a cargo-specific control of clathrin-mediated endocytosis. Alternatively, may act as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy. {ECO:0000269|PubMed:16325581, ECO:0000269|PubMed:22575674}. |
| Q9P243 | ZFAT | S21 | ochoa | Zinc finger protein ZFAT (Zinc finger gene in AITD susceptibility region) (Zinc finger protein 406) | May be involved in transcriptional regulation. Overexpression causes down-regulation of a number of genes involved in the immune response. Some genes are also up-regulated (By similarity). {ECO:0000250}. |
| Q9P266 | JCAD | S901 | ochoa | Junctional cadherin 5-associated protein (Junctional protein associated with coronary artery disease) (JCAD) | None |
| Q9P2P5 | HECW2 | S407 | ochoa | E3 ubiquitin-protein ligase HECW2 (EC 2.3.2.26) (HECT, C2 and WW domain-containing protein 2) (HECT-type E3 ubiquitin transferase HECW2) (NEDD4-like E3 ubiquitin-protein ligase 2) | E3 ubiquitin-protein ligase that mediates ubiquitination of TP73. Acts to stabilize TP73 and enhance activation of transcription by TP73 (PubMed:12890487). Involved in the regulation of mitotic metaphase/anaphase transition (PubMed:24163370). {ECO:0000269|PubMed:12890487, ECO:0000269|PubMed:24163370}. |
| Q9P2R6 | RERE | S642 | ochoa | Arginine-glutamic acid dipeptide repeats protein (Atrophin-1-like protein) (Atrophin-1-related protein) | Plays a role as a transcriptional repressor during development. May play a role in the control of cell survival. Overexpression of RERE recruits BAX to the nucleus particularly to POD and triggers caspase-3 activation, leading to cell death. {ECO:0000269|PubMed:11331249}. |
| Q9UBW5 | BIN2 | S369 | ochoa | Bridging integrator 2 (Breast cancer-associated protein 1) | Promotes cell motility and migration, probably via its interaction with the cell membrane and with podosome proteins that mediate interaction with the cytoskeleton. Modulates membrane curvature and mediates membrane tubulation. Plays a role in podosome formation. Inhibits phagocytosis. {ECO:0000269|PubMed:23285027}. |
| Q9UKL0 | RCOR1 | S139 | ochoa | REST corepressor 1 (Protein CoREST) | Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. {ECO:0000269|PubMed:11171972, ECO:0000269|PubMed:11516394, ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:12399542, ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:16079794, ECO:0000269|PubMed:16140033}. |
| Q9ULW0 | TPX2 | S486 | ochoa|psp | Targeting protein for Xklp2 (Differentially expressed in cancerous and non-cancerous lung cells 2) (DIL-2) (Hepatocellular carcinoma-associated antigen 519) (Hepatocellular carcinoma-associated antigen 90) (Protein fls353) (Restricted expression proliferation-associated protein 100) (p100) | Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules (PubMed:18663142, PubMed:19208764, PubMed:37728657). Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation (PubMed:18663142, PubMed:19208764). TPX2 is inactivated upon binding to importin-alpha (PubMed:26165940). At the onset of mitosis, GOLGA2 interacts with importin-alpha, liberating TPX2 from importin-alpha, allowing TPX2 to activate AURKA kinase and stimulate local microtubule nucleation (PubMed:26165940). {ECO:0000269|PubMed:18663142, ECO:0000269|PubMed:19208764, ECO:0000269|PubMed:26165940}. |
| Q9UPT8 | ZC3H4 | S908 | ochoa | Zinc finger CCCH domain-containing protein 4 | RNA-binding protein that suppresses transcription of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806). LncRNAs are defined as transcripts more than 200 nucleotides that are not translated into protein (PubMed:33767452, PubMed:33913806). Together with WDR82, part of a transcription termination checkpoint that promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452, PubMed:33913806). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs (PubMed:33767452). {ECO:0000269|PubMed:33767452, ECO:0000269|PubMed:33913806}. |
| Q9UPY3 | DICER1 | S1852 | ochoa|psp | Endoribonuclease Dicer (EC 3.1.26.3) (Helicase with RNase motif) (Helicase MOI) | Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes. {ECO:0000269|PubMed:15242644, ECO:0000269|PubMed:15973356, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:18178619}. |
| Q9UQ35 | SRRM2 | S1219 | ochoa | Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803) | Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269|PubMed:19854871, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:9531537, ECO:0000305|PubMed:33509932}. |
| Q9Y2D9 | ZNF652 | S57 | ochoa | Zinc finger protein 652 | Functions as a transcriptional repressor. {ECO:0000269|PubMed:16966434}. |
| Q9Y4C1 | KDM3A | S819 | ochoa | Lysine-specific demethylase 3A (EC 1.14.11.65) (JmjC domain-containing histone demethylation protein 2A) (Jumonji domain-containing protein 1A) ([histone H3]-dimethyl-L-lysine(9) demethylase 3A) | Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Preferentially demethylates mono- and dimethylated H3 'Lys-9' residue, with a preference for dimethylated residue, while it has weak or no activity on trimethylated H3 'Lys-9'. Demethylation of Lys residue generates formaldehyde and succinate. Involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes, resulting in H3 'Lys-9' demethylation and transcriptional activation. Involved in spermatogenesis by regulating expression of target genes such as PRM1 and TNP1 which are required for packaging and condensation of sperm chromatin. Involved in obesity resistance through regulation of metabolic genes such as PPARA and UCP1. {ECO:0000269|PubMed:16603237, ECO:0000269|PubMed:28262558}. |
| Q9Y5T5 | USP16 | S552 | ochoa|psp | Ubiquitin carboxyl-terminal hydrolase 16 (EC 3.4.19.12) (Deubiquitinating enzyme 16) (Ubiquitin thioesterase 16) (Ubiquitin-processing protease UBP-M) (Ubiquitin-specific-processing protease 16) | Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator (PubMed:17914355). Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis (PubMed:17914355). In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination (PubMed:17914355). Prefers nucleosomal substrates (PubMed:17914355). Does not deubiquitinate histone H2B (PubMed:17914355). Also deubiquitinates non-histone proteins, such as ribosomal protein RPS27A: deubiquitination of monoubiquitinated RPS27A promotes maturation of the 40S ribosomal subunit (PubMed:32129764). Also mediates deubiquitination of tektin proteins (TEKT1, TEKT2, TEK3, TEKT4 and TEKT5), promoting their stability. {ECO:0000255|HAMAP-Rule:MF_03062, ECO:0000269|PubMed:17914355, ECO:0000269|PubMed:32129764}. |
| Q9Y6D6 | ARFGEF1 | S243 | ochoa | Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1) | Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269|PubMed:12571360, ECO:0000269|PubMed:15644318, ECO:0000269|PubMed:17227842, ECO:0000269|PubMed:20360857, ECO:0000269|PubMed:22084092}. |
| Q9Y6K1 | DNMT3A | S75 | ochoa | DNA (cytosine-5)-methyltransferase 3A (Dnmt3a) (EC 2.1.1.37) (Cysteine methyltransferase DNMT3A) (EC 2.1.1.-) (DNA methyltransferase HsaIIIA) (DNA MTase HsaIIIA) (M.HsaIIIA) | Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development (PubMed:12138111, PubMed:16357870, PubMed:30478443). DNA methylation is coordinated with methylation of histones (PubMed:12138111, PubMed:16357870, PubMed:30478443). It modifies DNA in a non-processive manner and also methylates non-CpG sites (PubMed:12138111, PubMed:16357870, PubMed:30478443). May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1 (By similarity). Plays a role in paternal and maternal imprinting (By similarity). Required for methylation of most imprinted loci in germ cells (By similarity). Acts as a transcriptional corepressor for ZBTB18 (By similarity). Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites (By similarity). Can actively repress transcription through the recruitment of HDAC activity (By similarity). Also has weak auto-methylation activity on Cys-710 in absence of DNA (By similarity). {ECO:0000250|UniProtKB:O88508, ECO:0000269|PubMed:12138111, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:30478443}. |
| Q9Y6R4 | MAP3K4 | S431 | ochoa | Mitogen-activated protein kinase kinase kinase 4 (EC 2.7.11.25) (MAP three kinase 1) (MAPK/ERK kinase kinase 4) (MEK kinase 4) (MEKK 4) | Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. {ECO:0000269|PubMed:12052864, ECO:0000269|PubMed:9305639}. |
| R4GMW8 | BIVM-ERCC5 | S795 | ochoa | DNA excision repair protein ERCC-5 | None |
| O95861 | BPNT1 | S57 | Sugiyama | 3'(2'),5'-bisphosphate nucleotidase 1 (EC 3.1.3.7) (3'-phosphoadenosine 5'-phosphate phosphatase) (PAP phosphatase) (Bisphosphate 3'-nucleotidase 1) (BPntase 1) (HsPIP) (Inositol-polyphosphate 1-phosphatase) (EC 3.1.3.57) | Phosphatase that converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP and inositol 1,4-bisphosphate (Ins(1,4)P2) to inositol 4-phosphate (PubMed:10675562). Is also able to hydrolyze adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) (By similarity). Probably prevents the toxic accumulation of PAP, a compound which inhibits a variety of proteins, including PAPS-utilizing enzymes such as sulfotransferases, and RNA processing enzymes. Could also play a role in inositol recycling and phosphoinositide metabolism. Is not active on 3'-AMP, inositol-1-phosphate and inositol-1,4,5-triphosphate (PubMed:10675562). {ECO:0000250|UniProtKB:Q9Z1N4, ECO:0000269|PubMed:10675562}. |
| O94768 | STK17B | S348 | Sugiyama | Serine/threonine-protein kinase 17B (EC 2.7.11.1) (DAP kinase-related apoptosis-inducing protein kinase 2) | Phosphorylates myosin light chains (By similarity). Acts as a positive regulator of apoptosis. {ECO:0000250, ECO:0000269|PubMed:9786912}. |
| P22061 | PCMT1 | S133 | Sugiyama | Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl/D-aspartyl methyltransferase) (Protein-beta-aspartate methyltransferase) | Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins (PubMed:3167043, PubMed:6469980). Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin C-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein (By similarity). {ECO:0000250|UniProtKB:P23506, ECO:0000269|PubMed:3167043, ECO:0000269|PubMed:6469980}. |
| Q3KR16 | PLEKHG6 | S697 | PSP | Pleckstrin homology domain-containing family G member 6 (PH domain-containing family G member 6) (Myosin-interacting guanine nucleotide exchange factor) (MyoGEF) | Guanine nucleotide exchange factor activating the small GTPase RHOA, which, in turn, induces myosin filament formation. Also activates RHOG. Does not activate RAC1, or to a much lower extent than RHOA and RHOG. Part of a functional unit, involving PLEKHG6, MYH10 and RHOA, at the cleavage furrow to advance furrow ingression during cytokinesis. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with EZR, required for normal macropinocytosis. {ECO:0000269|PubMed:16721066, ECO:0000269|PubMed:17881735}. |
Download
| reactome_id | name | p | -log10_p |
|---|---|---|---|
| R-HSA-3371568 | Attenuation phase | 4.218847e-15 | 14.375 |
| R-HSA-3371571 | HSF1-dependent transactivation | 7.249756e-14 | 13.140 |
| R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | 1.595613e-11 | 10.797 |
| R-HSA-3371511 | HSF1 activation | 3.500955e-11 | 10.456 |
| R-HSA-3371556 | Cellular response to heat stress | 1.591540e-10 | 9.798 |
| R-HSA-9708296 | tRNA-derived small RNA (tsRNA or tRNA-related fragment, tRF) biogenesis | 7.932649e-04 | 3.101 |
| R-HSA-9820841 | M-decay: degradation of maternal mRNAs by maternally stored factors | 1.535485e-03 | 2.814 |
| R-HSA-447038 | NrCAM interactions | 2.381485e-03 | 2.623 |
| R-HSA-9833482 | PKR-mediated signaling | 2.152379e-03 | 2.667 |
| R-HSA-1169410 | Antiviral mechanism by IFN-stimulated genes | 1.988030e-03 | 2.702 |
| R-HSA-2262752 | Cellular responses to stress | 4.394338e-03 | 2.357 |
| R-HSA-451308 | Activation of Ca-permeable Kainate Receptor | 7.894192e-03 | 2.103 |
| R-HSA-913531 | Interferon Signaling | 8.486742e-03 | 2.071 |
| R-HSA-451306 | Ionotropic activity of kainate receptors | 9.095223e-03 | 2.041 |
| R-HSA-5467333 | APC truncation mutants are not K63 polyubiquitinated | 1.007159e-02 | 1.997 |
| R-HSA-381183 | ATF6 (ATF6-alpha) activates chaperone genes | 1.037238e-02 | 1.984 |
| R-HSA-381033 | ATF6 (ATF6-alpha) activates chaperones | 1.314856e-02 | 1.881 |
| R-HSA-8953897 | Cellular responses to stimuli | 1.461758e-02 | 1.835 |
| R-HSA-9701898 | STAT3 nuclear events downstream of ALK signaling | 1.620993e-02 | 1.790 |
| R-HSA-163282 | Mitochondrial transcription initiation | 2.991331e-02 | 1.524 |
| R-HSA-5619052 | Defective SLC9A9 causes autism 16 (AUTS16) | 2.991331e-02 | 1.524 |
| R-HSA-8941237 | Invadopodia formation | 4.935972e-02 | 1.307 |
| R-HSA-9673768 | Signaling by membrane-tethered fusions of PDGFRA or PDGFRB | 6.841866e-02 | 1.165 |
| R-HSA-8985586 | SLIT2:ROBO1 increases RHOA activity | 7.780522e-02 | 1.109 |
| R-HSA-72731 | Recycling of eIF2:GDP | 9.629728e-02 | 1.016 |
| R-HSA-9613354 | Lipophagy | 1.144208e-01 | 0.941 |
| R-HSA-438066 | Unblocking of NMDA receptors, glutamate binding and activation | 3.106492e-02 | 1.508 |
| R-HSA-442982 | Ras activation upon Ca2+ influx through NMDA receptor | 3.106492e-02 | 1.508 |
| R-HSA-4839744 | Signaling by APC mutants | 1.321830e-01 | 0.879 |
| R-HSA-5467337 | APC truncation mutants have impaired AXIN binding | 1.321830e-01 | 0.879 |
| R-HSA-5467348 | Truncations of AMER1 destabilize the destruction complex | 1.321830e-01 | 0.879 |
| R-HSA-5467340 | AXIN missense mutants destabilize the destruction complex | 1.321830e-01 | 0.879 |
| R-HSA-1234158 | Regulation of gene expression by Hypoxia-inducible Factor | 1.409308e-01 | 0.851 |
| R-HSA-5339716 | Signaling by GSK3beta mutants | 1.409308e-01 | 0.851 |
| R-HSA-4839743 | Signaling by CTNNB1 phospho-site mutants | 1.495910e-01 | 0.825 |
| R-HSA-5358752 | CTNNB1 T41 mutants aren't phosphorylated | 1.495910e-01 | 0.825 |
| R-HSA-5358749 | CTNNB1 S37 mutants aren't phosphorylated | 1.495910e-01 | 0.825 |
| R-HSA-5358751 | CTNNB1 S45 mutants aren't phosphorylated | 1.495910e-01 | 0.825 |
| R-HSA-5358747 | CTNNB1 S33 mutants aren't phosphorylated | 1.495910e-01 | 0.825 |
| R-HSA-196299 | Beta-catenin phosphorylation cascade | 1.750545e-01 | 0.757 |
| R-HSA-9709603 | Impaired BRCA2 binding to PALB2 | 2.158205e-01 | 0.666 |
| R-HSA-9701193 | Defective homologous recombination repair (HRR) due to PALB2 loss of function | 2.237302e-01 | 0.650 |
| R-HSA-9704646 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 2.237302e-01 | 0.650 |
| R-HSA-9704331 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 2.237302e-01 | 0.650 |
| R-HSA-9701192 | Defective homologous recombination repair (HRR) due to BRCA1 loss of function | 2.237302e-01 | 0.650 |
| R-HSA-5693554 | Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD... | 2.695503e-01 | 0.569 |
| R-HSA-445095 | Interaction between L1 and Ankyrins | 2.842182e-01 | 0.546 |
| R-HSA-9845323 | Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) | 1.515258e-01 | 0.820 |
| R-HSA-9615710 | Late endosomal microautophagy | 2.985933e-01 | 0.525 |
| R-HSA-9709570 | Impaired BRCA2 binding to RAD51 | 2.985933e-01 | 0.525 |
| R-HSA-5619107 | Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC... | 3.056729e-01 | 0.515 |
| R-HSA-1855196 | IP3 and IP4 transport between cytosol and nucleus | 3.126815e-01 | 0.505 |
| R-HSA-1855229 | IP6 and IP7 transport between cytosol and nucleus | 3.126815e-01 | 0.505 |
| R-HSA-1855170 | IPs transport between nucleus and cytosol | 3.264883e-01 | 0.486 |
| R-HSA-159227 | Transport of the SLBP independent Mature mRNA | 3.264883e-01 | 0.486 |
| R-HSA-159230 | Transport of the SLBP Dependant Mature mRNA | 3.332881e-01 | 0.477 |
| R-HSA-5696400 | Dual Incision in GG-NER | 3.400196e-01 | 0.468 |
| R-HSA-3301854 | Nuclear Pore Complex (NPC) Disassembly | 3.466835e-01 | 0.460 |
| R-HSA-159231 | Transport of Mature mRNA Derived from an Intronless Transcript | 3.726771e-01 | 0.429 |
| R-HSA-72163 | mRNA Splicing - Major Pathway | 1.709837e-01 | 0.767 |
| R-HSA-156711 | Polo-like kinase mediated events | 2.078307e-01 | 0.682 |
| R-HSA-5693537 | Resolution of D-Loop Structures | 3.332881e-01 | 0.477 |
| R-HSA-72172 | mRNA Splicing | 1.930192e-01 | 0.714 |
| R-HSA-72203 | Processing of Capped Intron-Containing Pre-mRNA | 1.876639e-01 | 0.727 |
| R-HSA-75944 | Transcription from mitochondrial promoters | 3.968544e-02 | 1.401 |
| R-HSA-8849473 | PTK6 Expression | 9.629728e-02 | 1.016 |
| R-HSA-5576893 | Phase 2 - plateau phase | 1.916077e-01 | 0.718 |
| R-HSA-5693568 | Resolution of D-loop Structures through Holliday Junction Intermediates | 3.264883e-01 | 0.486 |
| R-HSA-5685938 | HDR through Single Strand Annealing (SSA) | 3.264883e-01 | 0.486 |
| R-HSA-6802948 | Signaling by high-kinase activity BRAF mutants | 3.598114e-01 | 0.444 |
| R-HSA-6785470 | tRNA processing in the mitochondrion | 3.662767e-01 | 0.436 |
| R-HSA-426486 | Small interfering RNA (siRNA) biogenesis | 8.709778e-02 | 1.060 |
| R-HSA-5221030 | TET1,2,3 and TDG demethylate DNA | 1.233466e-01 | 0.909 |
| R-HSA-5693567 | HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA) | 3.648268e-01 | 0.438 |
| R-HSA-5693607 | Processing of DNA double-strand break ends | 2.277409e-01 | 0.643 |
| R-HSA-4791275 | Signaling by WNT in cancer | 3.196197e-01 | 0.495 |
| R-HSA-9675136 | Diseases of DNA Double-Strand Break Repair | 3.400196e-01 | 0.468 |
| R-HSA-77042 | Formation of editosomes by ADAR proteins | 2.004236e-02 | 1.698 |
| R-HSA-75064 | mRNA Editing: A to I Conversion | 3.968544e-02 | 1.401 |
| R-HSA-75102 | C6 deamination of adenosine | 3.968544e-02 | 1.401 |
| R-HSA-165181 | Inhibition of TSC complex formation by PKB | 5.893714e-02 | 1.230 |
| R-HSA-4839735 | Signaling by AXIN mutants | 1.409308e-01 | 0.851 |
| R-HSA-4839748 | Signaling by AMER1 mutants | 1.409308e-01 | 0.851 |
| R-HSA-203927 | MicroRNA (miRNA) biogenesis | 3.989857e-02 | 1.399 |
| R-HSA-450408 | AUF1 (hnRNP D0) binds and destabilizes mRNA | 7.103542e-02 | 1.149 |
| R-HSA-4419969 | Depolymerization of the Nuclear Lamina | 2.078307e-01 | 0.682 |
| R-HSA-5576892 | Phase 0 - rapid depolarisation | 2.914420e-01 | 0.535 |
| R-HSA-9701190 | Defective homologous recombination repair (HRR) due to BRCA2 loss of function | 3.400196e-01 | 0.468 |
| R-HSA-212300 | PRC2 methylates histones and DNA | 3.532805e-01 | 0.452 |
| R-HSA-180910 | Vpr-mediated nuclear import of PICs | 3.598114e-01 | 0.444 |
| R-HSA-9613829 | Chaperone Mediated Autophagy | 2.078307e-01 | 0.682 |
| R-HSA-983168 | Antigen processing: Ubiquitination & Proteasome degradation | 3.656388e-01 | 0.437 |
| R-HSA-9620244 | Long-term potentiation | 3.989857e-02 | 1.399 |
| R-HSA-2142789 | Ubiquinol biosynthesis | 3.598114e-01 | 0.444 |
| R-HSA-168274 | Export of Viral Ribonucleoproteins from Nucleus | 1.044107e-01 | 0.981 |
| R-HSA-3214815 | HDACs deacetylate histones | 1.342270e-01 | 0.872 |
| R-HSA-170822 | Regulation of Glucokinase by Glucokinase Regulatory Protein | 3.332881e-01 | 0.477 |
| R-HSA-5693579 | Homologous DNA Pairing and Strand Exchange | 3.662767e-01 | 0.436 |
| R-HSA-2980766 | Nuclear Envelope Breakdown | 1.410919e-01 | 0.850 |
| R-HSA-3371497 | HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig... | 4.271071e-02 | 1.369 |
| R-HSA-5693532 | DNA Double-Strand Break Repair | 2.505753e-01 | 0.601 |
| R-HSA-71737 | Pyrophosphate hydrolysis | 6.841866e-02 | 1.165 |
| R-HSA-8857538 | PTK6 promotes HIF1A stabilization | 8.709778e-02 | 1.060 |
| R-HSA-75072 | mRNA Editing | 1.144208e-01 | 0.941 |
| R-HSA-168330 | Viral RNP Complexes in the Host Cell Nucleus | 1.409308e-01 | 0.851 |
| R-HSA-451326 | Activation of kainate receptors upon glutamate binding | 4.706904e-02 | 1.327 |
| R-HSA-1250196 | SHC1 events in ERBB2 signaling | 3.056729e-01 | 0.515 |
| R-HSA-110331 | Cleavage of the damaged purine | 3.598114e-01 | 0.444 |
| R-HSA-73927 | Depurination | 3.662767e-01 | 0.436 |
| R-HSA-5693571 | Nonhomologous End-Joining (NHEJ) | 1.108678e-01 | 0.955 |
| R-HSA-9609736 | Assembly and cell surface presentation of NMDA receptors | 8.875915e-02 | 1.052 |
| R-HSA-6794362 | Protein-protein interactions at synapses | 2.426243e-01 | 0.615 |
| R-HSA-110330 | Recognition and association of DNA glycosylase with site containing an affected ... | 3.196197e-01 | 0.495 |
| R-HSA-1679131 | Trafficking and processing of endosomal TLR | 1.495910e-01 | 0.825 |
| R-HSA-442742 | CREB1 phosphorylation through NMDA receptor-mediated activation of RAS signaling | 5.995986e-02 | 1.222 |
| R-HSA-4641262 | Disassembly of the destruction complex and recruitment of AXIN to the membrane | 2.842182e-01 | 0.546 |
| R-HSA-6784531 | tRNA processing in the nucleus | 1.585647e-01 | 0.800 |
| R-HSA-5334118 | DNA methylation | 2.985933e-01 | 0.525 |
| R-HSA-380972 | Energy dependent regulation of mTOR by LKB1-AMPK | 3.056729e-01 | 0.515 |
| R-HSA-180746 | Nuclear import of Rev protein | 3.400196e-01 | 0.468 |
| R-HSA-5693616 | Presynaptic phase of homologous DNA pairing and strand exchange | 3.466835e-01 | 0.460 |
| R-HSA-211000 | Gene Silencing by RNA | 3.358444e-02 | 1.474 |
| R-HSA-442755 | Activation of NMDA receptors and postsynaptic events | 3.171648e-01 | 0.499 |
| R-HSA-425986 | Sodium/Proton exchangers | 1.054046e-01 | 0.977 |
| R-HSA-9617324 | Negative regulation of NMDA receptor-mediated neuronal transmission | 3.106492e-02 | 1.508 |
| R-HSA-429947 | Deadenylation of mRNA | 3.760972e-02 | 1.425 |
| R-HSA-9648895 | Response of EIF2AK1 (HRI) to heme deficiency | 2.545837e-01 | 0.594 |
| R-HSA-399719 | Trafficking of AMPA receptors | 3.126815e-01 | 0.505 |
| R-HSA-69473 | G2/M DNA damage checkpoint | 2.018831e-01 | 0.695 |
| R-HSA-8953750 | Transcriptional Regulation by E2F6 | 3.726771e-01 | 0.429 |
| R-HSA-447041 | CHL1 interactions | 9.629728e-02 | 1.016 |
| R-HSA-110362 | POLB-Dependent Long Patch Base Excision Repair | 1.409308e-01 | 0.851 |
| R-HSA-8943724 | Regulation of PTEN gene transcription | 1.515258e-01 | 0.820 |
| R-HSA-888590 | GABA synthesis, release, reuptake and degradation | 3.056729e-01 | 0.515 |
| R-HSA-9930044 | Nuclear RNA decay | 3.264883e-01 | 0.486 |
| R-HSA-165054 | Rev-mediated nuclear export of HIV RNA | 3.662767e-01 | 0.436 |
| R-HSA-6798695 | Neutrophil degranulation | 2.121022e-01 | 0.673 |
| R-HSA-69275 | G2/M Transition | 3.437628e-01 | 0.464 |
| R-HSA-8876198 | RAB GEFs exchange GTP for GDP on RABs | 2.463527e-01 | 0.608 |
| R-HSA-453274 | Mitotic G2-G2/M phases | 3.492694e-01 | 0.457 |
| R-HSA-381042 | PERK regulates gene expression | 3.466835e-01 | 0.460 |
| R-HSA-9842860 | Regulation of endogenous retroelements | 3.171648e-01 | 0.499 |
| R-HSA-73894 | DNA Repair | 1.892780e-01 | 0.723 |
| R-HSA-8953854 | Metabolism of RNA | 2.508594e-01 | 0.601 |
| R-HSA-9612973 | Autophagy | 2.586865e-01 | 0.587 |
| R-HSA-9840373 | Cellular response to mitochondrial stress | 1.144208e-01 | 0.941 |
| R-HSA-71288 | Creatine metabolism | 2.237302e-01 | 0.650 |
| R-HSA-400042 | Adrenaline,noradrenaline inhibits insulin secretion | 2.769212e-01 | 0.558 |
| R-HSA-168276 | NS1 Mediated Effects on Host Pathways | 3.726771e-01 | 0.429 |
| R-HSA-2559585 | Oncogene Induced Senescence | 3.466835e-01 | 0.460 |
| R-HSA-9828642 | Respiratory syncytial virus genome transcription | 1.666520e-01 | 0.778 |
| R-HSA-5676934 | Protein repair | 1.750545e-01 | 0.757 |
| R-HSA-174414 | Processive synthesis on the C-strand of the telomere | 2.842182e-01 | 0.546 |
| R-HSA-75109 | Triglyceride biosynthesis | 2.842182e-01 | 0.546 |
| R-HSA-9007101 | Rab regulation of trafficking | 1.482768e-01 | 0.829 |
| R-HSA-3769402 | Deactivation of the beta-catenin transactivating complex | 3.598114e-01 | 0.444 |
| R-HSA-9824594 | Regulation of MITF-M-dependent genes involved in apoptosis | 2.899496e-02 | 1.538 |
| R-HSA-438064 | Post NMDA receptor activation events | 2.538156e-01 | 0.595 |
| R-HSA-110357 | Displacement of DNA glycosylase by APEX1 | 9.629728e-02 | 1.016 |
| R-HSA-8849932 | Synaptic adhesion-like molecules | 2.313903e-02 | 1.636 |
| R-HSA-9634285 | Constitutive Signaling by Overexpressed ERBB2 | 1.495910e-01 | 0.825 |
| R-HSA-432720 | Lysosome Vesicle Biogenesis | 3.532805e-01 | 0.452 |
| R-HSA-2151201 | Transcriptional activation of mitochondrial biogenesis | 2.277409e-01 | 0.643 |
| R-HSA-5576891 | Cardiac conduction | 6.328229e-02 | 1.199 |
| R-HSA-5578775 | Ion homeostasis | 2.780778e-02 | 1.556 |
| R-HSA-936837 | Ion transport by P-type ATPases | 3.737464e-02 | 1.427 |
| R-HSA-3214842 | HDMs demethylate histones | 2.695503e-01 | 0.569 |
| R-HSA-430116 | GP1b-IX-V activation signalling | 1.144208e-01 | 0.941 |
| R-HSA-8876725 | Protein methylation | 1.750545e-01 | 0.757 |
| R-HSA-373760 | L1CAM interactions | 4.400351e-02 | 1.357 |
| R-HSA-1483213 | Synthesis of PE | 2.842182e-01 | 0.546 |
| R-HSA-399721 | Glutamate binding, activation of AMPA receptors and synaptic plasticity | 3.264883e-01 | 0.486 |
| R-HSA-9816359 | Maternal to zygotic transition (MZT) | 5.147730e-02 | 1.288 |
| R-HSA-9827857 | Specification of primordial germ cells | 2.130970e-02 | 1.671 |
| R-HSA-110373 | Resolution of AP sites via the multiple-nucleotide patch replacement pathway | 2.769212e-01 | 0.558 |
| R-HSA-6804759 | Regulation of TP53 Activity through Association with Co-factors | 1.581645e-01 | 0.801 |
| R-HSA-446353 | Cell-extracellular matrix interactions | 1.750545e-01 | 0.757 |
| R-HSA-429914 | Deadenylation-dependent mRNA decay | 1.480306e-01 | 0.830 |
| R-HSA-419037 | NCAM1 interactions | 3.598114e-01 | 0.444 |
| R-HSA-379716 | Cytosolic tRNA aminoacylation | 9.182974e-02 | 1.037 |
| R-HSA-1632852 | Macroautophagy | 2.159539e-01 | 0.666 |
| R-HSA-1474165 | Reproduction | 1.850208e-01 | 0.733 |
| R-HSA-69273 | Cyclin A/B1/B2 associated events during G2/M transition | 5.995986e-02 | 1.222 |
| R-HSA-73884 | Base Excision Repair | 2.650191e-01 | 0.577 |
| R-HSA-9671555 | Signaling by PDGFR in disease | 2.393124e-01 | 0.621 |
| R-HSA-549127 | SLC-mediated transport of organic cations | 3.598114e-01 | 0.444 |
| R-HSA-909733 | Interferon alpha/beta signaling | 3.756582e-01 | 0.425 |
| R-HSA-450531 | Regulation of mRNA stability by proteins that bind AU-rich elements | 1.945583e-01 | 0.711 |
| R-HSA-6804756 | Regulation of TP53 Activity through Phosphorylation | 2.500833e-01 | 0.602 |
| R-HSA-397014 | Muscle contraction | 2.095773e-01 | 0.679 |
| R-HSA-6804115 | TP53 regulates transcription of additional cell cycle genes whose exact role in ... | 3.319158e-02 | 1.479 |
| R-HSA-9008059 | Interleukin-37 signaling | 5.209030e-02 | 1.283 |
| R-HSA-8863795 | Downregulation of ERBB2 signaling | 3.056729e-01 | 0.515 |
| R-HSA-6804758 | Regulation of TP53 Activity through Acetylation | 3.264883e-01 | 0.486 |
| R-HSA-5689896 | Ovarian tumor domain proteases | 3.598114e-01 | 0.444 |
| R-HSA-3247509 | Chromatin modifying enzymes | 1.169295e-01 | 0.932 |
| R-HSA-73933 | Resolution of Abasic Sites (AP sites) | 8.572027e-02 | 1.067 |
| R-HSA-8983711 | OAS antiviral response | 1.495910e-01 | 0.825 |
| R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | 6.447665e-02 | 1.191 |
| R-HSA-4839726 | Chromatin organization | 1.388927e-01 | 0.857 |
| R-HSA-9679191 | Potential therapeutics for SARS | 2.888480e-02 | 1.539 |
| R-HSA-9841251 | Mitochondrial unfolded protein response (UPRmt) | 4.462948e-02 | 1.350 |
| R-HSA-201556 | Signaling by ALK | 7.974146e-02 | 1.098 |
| R-HSA-379724 | tRNA Aminoacylation | 1.515258e-01 | 0.820 |
| R-HSA-182971 | EGFR downregulation | 3.126815e-01 | 0.505 |
| R-HSA-5633007 | Regulation of TP53 Activity | 1.079187e-01 | 0.967 |
| R-HSA-983712 | Ion channel transport | 3.520210e-01 | 0.453 |
| R-HSA-3700989 | Transcriptional Regulation by TP53 | 2.237271e-01 | 0.650 |
| R-HSA-381119 | Unfolded Protein Response (UPR) | 2.107204e-01 | 0.676 |
| R-HSA-111465 | Apoptotic cleavage of cellular proteins | 3.196197e-01 | 0.495 |
| R-HSA-5357905 | Regulation of TNFR1 signaling | 1.044107e-01 | 0.981 |
| R-HSA-6791312 | TP53 Regulates Transcription of Cell Cycle Genes | 1.410919e-01 | 0.850 |
| R-HSA-1280215 | Cytokine Signaling in Immune system | 8.958063e-02 | 1.048 |
| R-HSA-75893 | TNF signaling | 1.376498e-01 | 0.861 |
| R-HSA-73887 | Death Receptor Signaling | 2.532748e-01 | 0.596 |
| R-HSA-1227990 | Signaling by ERBB2 in Cancer | 3.056729e-01 | 0.515 |
| R-HSA-9820965 | Respiratory syncytial virus (RSV) genome replication, transcription and translat... | 3.726771e-01 | 0.429 |
| R-HSA-9679506 | SARS-CoV Infections | 3.659707e-01 | 0.437 |
| R-HSA-159234 | Transport of Mature mRNAs Derived from Intronless Transcripts | 3.790132e-01 | 0.421 |
| R-HSA-427389 | ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression | 3.790132e-01 | 0.421 |
| R-HSA-9843743 | Transcriptional regulation of brown and beige adipocyte differentiation | 3.790132e-01 | 0.421 |
| R-HSA-9844594 | Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 | 3.790132e-01 | 0.421 |
| R-HSA-177243 | Interactions of Rev with host cellular proteins | 3.790132e-01 | 0.421 |
| R-HSA-176033 | Interactions of Vpr with host cellular proteins | 3.790132e-01 | 0.421 |
| R-HSA-5696395 | Formation of Incision Complex in GG-NER | 3.790132e-01 | 0.421 |
| R-HSA-8868766 | rRNA processing in the mitochondrion | 3.790132e-01 | 0.421 |
| R-HSA-1592230 | Mitochondrial biogenesis | 3.828377e-01 | 0.417 |
| R-HSA-168271 | Transport of Ribonucleoproteins into the Host Nucleus | 3.852858e-01 | 0.414 |
| R-HSA-5693538 | Homology Directed Repair | 3.864143e-01 | 0.413 |
| R-HSA-5674135 | MAP2K and MAPK activation | 3.914953e-01 | 0.407 |
| R-HSA-9656223 | Signaling by RAF1 mutants | 3.914953e-01 | 0.407 |
| R-HSA-3000480 | Scavenging by Class A Receptors | 3.914953e-01 | 0.407 |
| R-HSA-174417 | Telomere C-strand (Lagging Strand) Synthesis | 3.914953e-01 | 0.407 |
| R-HSA-68875 | Mitotic Prophase | 3.935406e-01 | 0.405 |
| R-HSA-73762 | RNA Polymerase I Transcription Initiation | 3.976426e-01 | 0.401 |
| R-HSA-165159 | MTOR signalling | 3.976426e-01 | 0.401 |
| R-HSA-9710421 | Defective pyroptosis | 4.037281e-01 | 0.394 |
| R-HSA-8854214 | TBC/RABGAPs | 4.037281e-01 | 0.394 |
| R-HSA-3214858 | RMTs methylate histone arginines | 4.097524e-01 | 0.387 |
| R-HSA-168333 | NEP/NS2 Interacts with the Cellular Export Machinery | 4.157163e-01 | 0.381 |
| R-HSA-72695 | Formation of the ternary complex, and subsequently, the 43S complex | 4.216203e-01 | 0.375 |
| R-HSA-6802946 | Signaling by moderate kinase activity BRAF mutants | 4.216203e-01 | 0.375 |
| R-HSA-9649948 | Signaling downstream of RAS mutants | 4.216203e-01 | 0.375 |
| R-HSA-6802955 | Paradoxical activation of RAF signaling by kinase inactive BRAF | 4.216203e-01 | 0.375 |
| R-HSA-6802949 | Signaling by RAS mutants | 4.216203e-01 | 0.375 |
| R-HSA-9675135 | Diseases of DNA repair | 4.216203e-01 | 0.375 |
| R-HSA-75153 | Apoptotic execution phase | 4.216203e-01 | 0.375 |
| R-HSA-69481 | G2/M Checkpoints | 4.216602e-01 | 0.375 |
| R-HSA-1483191 | Synthesis of PC | 4.274650e-01 | 0.369 |
| R-HSA-9725371 | Nuclear events stimulated by ALK signaling in cancer | 4.332510e-01 | 0.363 |
| R-HSA-425410 | Metal ion SLC transporters | 4.332510e-01 | 0.363 |
| R-HSA-2122947 | NOTCH1 Intracellular Domain Regulates Transcription | 4.389789e-01 | 0.358 |
| R-HSA-8951664 | Neddylation | 4.414308e-01 | 0.355 |
| R-HSA-1234176 | Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha | 4.502627e-01 | 0.347 |
| R-HSA-912446 | Meiotic recombination | 4.502627e-01 | 0.347 |
| R-HSA-156584 | Cytosolic sulfonation of small molecules | 4.502627e-01 | 0.347 |
| R-HSA-6794361 | Neurexins and neuroligins | 4.558196e-01 | 0.341 |
| R-HSA-9692916 | SARS-CoV-1 activates/modulates innate immune responses | 4.558196e-01 | 0.341 |
| R-HSA-432722 | Golgi Associated Vesicle Biogenesis | 4.613208e-01 | 0.336 |
| R-HSA-9639288 | Amino acids regulate mTORC1 | 4.613208e-01 | 0.336 |
| R-HSA-72649 | Translation initiation complex formation | 4.667667e-01 | 0.331 |
| R-HSA-73929 | Base-Excision Repair, AP Site Formation | 4.667667e-01 | 0.331 |
| R-HSA-6807070 | PTEN Regulation | 4.692038e-01 | 0.329 |
| R-HSA-72702 | Ribosomal scanning and start codon recognition | 4.774948e-01 | 0.321 |
| R-HSA-193648 | NRAGE signals death through JNK | 4.774948e-01 | 0.321 |
| R-HSA-177929 | Signaling by EGFR | 4.774948e-01 | 0.321 |
| R-HSA-449147 | Signaling by Interleukins | 4.813424e-01 | 0.318 |
| R-HSA-6782135 | Dual incision in TC-NER | 4.880084e-01 | 0.312 |
| R-HSA-72662 | Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub... | 4.880084e-01 | 0.312 |
| R-HSA-9029569 | NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflu... | 4.880084e-01 | 0.312 |
| R-HSA-191859 | snRNP Assembly | 4.931861e-01 | 0.307 |
| R-HSA-194441 | Metabolism of non-coding RNA | 4.931861e-01 | 0.307 |
| R-HSA-5693565 | Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at... | 4.931861e-01 | 0.307 |
| R-HSA-352230 | Amino acid transport across the plasma membrane | 4.931861e-01 | 0.307 |
| R-HSA-8979227 | Triglyceride metabolism | 4.931861e-01 | 0.307 |
| R-HSA-180786 | Extension of Telomeres | 4.931861e-01 | 0.307 |
| R-HSA-1227986 | Signaling by ERBB2 | 4.983118e-01 | 0.302 |
| R-HSA-168325 | Viral Messenger RNA Synthesis | 5.033859e-01 | 0.298 |
| R-HSA-9856651 | MITF-M-dependent gene expression | 5.080668e-01 | 0.294 |
| R-HSA-375165 | NCAM signaling for neurite out-growth | 5.084090e-01 | 0.294 |
| R-HSA-186797 | Signaling by PDGF | 5.084090e-01 | 0.294 |
| R-HSA-422475 | Axon guidance | 5.120946e-01 | 0.291 |
| R-HSA-9006927 | Signaling by Non-Receptor Tyrosine Kinases | 5.133816e-01 | 0.290 |
| R-HSA-8848021 | Signaling by PTK6 | 5.133816e-01 | 0.290 |
| R-HSA-446652 | Interleukin-1 family signaling | 5.143634e-01 | 0.289 |
| R-HSA-1234174 | Cellular response to hypoxia | 5.231773e-01 | 0.281 |
| R-HSA-6802952 | Signaling by BRAF and RAF1 fusions | 5.231773e-01 | 0.281 |
| R-HSA-8854518 | AURKA Activation by TPX2 | 5.280015e-01 | 0.277 |
| R-HSA-9909649 | Regulation of PD-L1(CD274) transcription | 5.280015e-01 | 0.277 |
| R-HSA-5688426 | Deubiquitination | 5.282549e-01 | 0.277 |
| R-HSA-5685942 | HDR through Homologous Recombination (HRR) | 5.327771e-01 | 0.273 |
| R-HSA-5693606 | DNA Double Strand Break Response | 5.327771e-01 | 0.273 |
| R-HSA-9958863 | SLC-mediated transport of amino acids | 5.327771e-01 | 0.273 |
| R-HSA-9711097 | Cellular response to starvation | 5.329338e-01 | 0.273 |
| R-HSA-877300 | Interferon gamma signaling | 5.359818e-01 | 0.271 |
| R-HSA-195253 | Degradation of beta-catenin by the destruction complex | 5.468177e-01 | 0.262 |
| R-HSA-9843940 | Regulation of endogenous retroelements by KRAB-ZFP proteins | 5.468177e-01 | 0.262 |
| R-HSA-5250913 | Positive epigenetic regulation of rRNA expression | 5.514040e-01 | 0.259 |
| R-HSA-8978934 | Metabolism of cofactors | 5.514040e-01 | 0.259 |
| R-HSA-5578749 | Transcriptional regulation by small RNAs | 5.559443e-01 | 0.255 |
| R-HSA-199992 | trans-Golgi Network Vesicle Budding | 5.559443e-01 | 0.255 |
| R-HSA-5619102 | SLC transporter disorders | 5.598747e-01 | 0.252 |
| R-HSA-159236 | Transport of Mature mRNA derived from an Intron-Containing Transcript | 5.604388e-01 | 0.251 |
| R-HSA-204998 | Cell death signalling via NRAGE, NRIF and NADE | 5.604388e-01 | 0.251 |
| R-HSA-6781827 | Transcription-Coupled Nucleotide Excision Repair (TC-NER) | 5.692928e-01 | 0.245 |
| R-HSA-1169408 | ISG15 antiviral mechanism | 5.692928e-01 | 0.245 |
| R-HSA-72306 | tRNA processing | 5.714908e-01 | 0.243 |
| R-HSA-73854 | RNA Polymerase I Promoter Clearance | 5.736530e-01 | 0.241 |
| R-HSA-1980143 | Signaling by NOTCH1 | 5.736530e-01 | 0.241 |
| R-HSA-9675108 | Nervous system development | 5.741714e-01 | 0.241 |
| R-HSA-9024446 | NR1H2 and NR1H3-mediated signaling | 5.779694e-01 | 0.238 |
| R-HSA-5689880 | Ub-specific processing proteases | 5.800571e-01 | 0.237 |
| R-HSA-73864 | RNA Polymerase I Transcription | 5.822424e-01 | 0.235 |
| R-HSA-416482 | G alpha (12/13) signalling events | 5.822424e-01 | 0.235 |
| R-HSA-983231 | Factors involved in megakaryocyte development and platelet production | 5.856984e-01 | 0.232 |
| R-HSA-983169 | Class I MHC mediated antigen processing & presentation | 5.864475e-01 | 0.232 |
| R-HSA-1655829 | Regulation of cholesterol biosynthesis by SREBP (SREBF) | 5.864723e-01 | 0.232 |
| R-HSA-168255 | Influenza Infection | 5.968138e-01 | 0.224 |
| R-HSA-72202 | Transport of Mature Transcript to Cytoplasm | 5.989085e-01 | 0.223 |
| R-HSA-5696399 | Global Genome Nucleotide Excision Repair (GG-NER) | 6.069921e-01 | 0.217 |
| R-HSA-5673001 | RAF/MAP kinase cascade | 6.071679e-01 | 0.217 |
| R-HSA-1640170 | Cell Cycle | 6.096168e-01 | 0.215 |
| R-HSA-6802957 | Oncogenic MAPK signaling | 6.109729e-01 | 0.214 |
| R-HSA-1500620 | Meiosis | 6.109729e-01 | 0.214 |
| R-HSA-6807505 | RNA polymerase II transcribes snRNA genes | 6.188148e-01 | 0.208 |
| R-HSA-5684996 | MAPK1/MAPK3 signaling | 6.222974e-01 | 0.206 |
| R-HSA-9663891 | Selective autophagy | 6.264995e-01 | 0.203 |
| R-HSA-9645723 | Diseases of programmed cell death | 6.264995e-01 | 0.203 |
| R-HSA-112310 | Neurotransmitter release cycle | 6.340302e-01 | 0.198 |
| R-HSA-5663202 | Diseases of signal transduction by growth factor receptors and second messengers | 6.346096e-01 | 0.197 |
| R-HSA-8986944 | Transcriptional Regulation by MECP2 | 6.377388e-01 | 0.195 |
| R-HSA-9837999 | Mitochondrial protein degradation | 6.522033e-01 | 0.186 |
| R-HSA-6807878 | COPI-mediated anterograde transport | 6.626737e-01 | 0.179 |
| R-HSA-157579 | Telomere Maintenance | 6.660937e-01 | 0.176 |
| R-HSA-8957275 | Post-translational protein phosphorylation | 6.694793e-01 | 0.174 |
| R-HSA-422356 | Regulation of insulin secretion | 6.694793e-01 | 0.174 |
| R-HSA-3214847 | HATs acetylate histones | 6.728307e-01 | 0.172 |
| R-HSA-193704 | p75 NTR receptor-mediated signalling | 6.728307e-01 | 0.172 |
| R-HSA-70171 | Glycolysis | 6.761484e-01 | 0.170 |
| R-HSA-382556 | ABC-family proteins mediated transport | 6.761484e-01 | 0.170 |
| R-HSA-112315 | Transmission across Chemical Synapses | 6.769014e-01 | 0.169 |
| R-HSA-212165 | Epigenetic regulation of gene expression | 6.769014e-01 | 0.169 |
| R-HSA-2408557 | Selenocysteine synthesis | 6.794326e-01 | 0.168 |
| R-HSA-112314 | Neurotransmitter receptors and postsynaptic signal transmission | 6.823439e-01 | 0.166 |
| R-HSA-9730414 | MITF-M-regulated melanocyte development | 6.846212e-01 | 0.165 |
| R-HSA-9633012 | Response of EIF2AK4 (GCN2) to amino acid deficiency | 6.890880e-01 | 0.162 |
| R-HSA-5696398 | Nucleotide Excision Repair | 6.953638e-01 | 0.158 |
| R-HSA-9692914 | SARS-CoV-1-host interactions | 6.984543e-01 | 0.156 |
| R-HSA-9725370 | Signaling by ALK fusions and activated point mutants | 7.015136e-01 | 0.154 |
| R-HSA-9700206 | Signaling by ALK in cancer | 7.015136e-01 | 0.154 |
| R-HSA-156827 | L13a-mediated translational silencing of Ceruloplasmin expression | 7.045421e-01 | 0.152 |
| R-HSA-72706 | GTP hydrolysis and joining of the 60S ribosomal subunit | 7.045421e-01 | 0.152 |
| R-HSA-69278 | Cell Cycle, Mitotic | 7.119998e-01 | 0.148 |
| R-HSA-1483249 | Inositol phosphate metabolism | 7.163538e-01 | 0.145 |
| R-HSA-5683057 | MAPK family signaling cascades | 7.203990e-01 | 0.142 |
| R-HSA-381426 | Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-l... | 7.249034e-01 | 0.140 |
| R-HSA-5628897 | TP53 Regulates Metabolic Genes | 7.276960e-01 | 0.138 |
| R-HSA-4420097 | VEGFA-VEGFR2 Pathway | 7.304604e-01 | 0.136 |
| R-HSA-597592 | Post-translational protein modification | 7.329140e-01 | 0.135 |
| R-HSA-72737 | Cap-dependent Translation Initiation | 7.331969e-01 | 0.135 |
| R-HSA-72613 | Eukaryotic Translation Initiation | 7.331969e-01 | 0.135 |
| R-HSA-70326 | Glucose metabolism | 7.359058e-01 | 0.133 |
| R-HSA-162582 | Signal Transduction | 7.456100e-01 | 0.127 |
| R-HSA-73886 | Chromosome Maintenance | 7.464707e-01 | 0.127 |
| R-HSA-162909 | Host Interactions of HIV factors | 7.541177e-01 | 0.123 |
| R-HSA-5619115 | Disorders of transmembrane transporters | 7.543965e-01 | 0.122 |
| R-HSA-194138 | Signaling by VEGF | 7.590880e-01 | 0.120 |
| R-HSA-114608 | Platelet degranulation | 7.639583e-01 | 0.117 |
| R-HSA-69620 | Cell Cycle Checkpoints | 7.739557e-01 | 0.111 |
| R-HSA-9843745 | Adipogenesis | 7.757103e-01 | 0.110 |
| R-HSA-76005 | Response to elevated platelet cytosolic Ca2+ | 7.802466e-01 | 0.108 |
| R-HSA-163685 | Integration of energy metabolism | 7.890474e-01 | 0.103 |
| R-HSA-9820952 | Respiratory Syncytial Virus Infection Pathway | 7.911923e-01 | 0.102 |
| R-HSA-9664407 | Parasite infection | 7.974979e-01 | 0.098 |
| R-HSA-9664417 | Leishmania phagocytosis | 7.974979e-01 | 0.098 |
| R-HSA-9664422 | FCGR3A-mediated phagocytosis | 7.974979e-01 | 0.098 |
| R-HSA-425407 | SLC-mediated transmembrane transport | 7.976518e-01 | 0.098 |
| R-HSA-2029482 | Regulation of actin dynamics for phagocytic cup formation | 7.995574e-01 | 0.097 |
| R-HSA-9705671 | SARS-CoV-2 activates/modulates innate and adaptive immune responses | 8.036141e-01 | 0.095 |
| R-HSA-162599 | Late Phase of HIV Life Cycle | 8.036141e-01 | 0.095 |
| R-HSA-74160 | Gene expression (Transcription) | 8.051474e-01 | 0.094 |
| R-HSA-8856828 | Clathrin-mediated endocytosis | 8.056118e-01 | 0.094 |
| R-HSA-199991 | Membrane Trafficking | 8.110358e-01 | 0.091 |
| R-HSA-199977 | ER to Golgi Anterograde Transport | 8.134025e-01 | 0.090 |
| R-HSA-2173782 | Binding and Uptake of Ligands by Scavenger Receptors | 8.190412e-01 | 0.087 |
| R-HSA-168273 | Influenza Viral RNA Transcription and Replication | 8.280650e-01 | 0.082 |
| R-HSA-9824446 | Viral Infection Pathways | 8.283436e-01 | 0.082 |
| R-HSA-1257604 | PIP3 activates AKT signaling | 8.301280e-01 | 0.081 |
| R-HSA-9610379 | HCMV Late Events | 8.315481e-01 | 0.080 |
| R-HSA-162587 | HIV Life Cycle | 8.315481e-01 | 0.080 |
| R-HSA-72766 | Translation | 8.364488e-01 | 0.078 |
| R-HSA-168256 | Immune System | 8.382251e-01 | 0.077 |
| R-HSA-109581 | Apoptosis | 8.399519e-01 | 0.076 |
| R-HSA-2408522 | Selenoamino acid metabolism | 8.431955e-01 | 0.074 |
| R-HSA-5653656 | Vesicle-mediated transport | 8.490384e-01 | 0.071 |
| R-HSA-9909648 | Regulation of PD-L1(CD274) expression | 8.570019e-01 | 0.067 |
| R-HSA-2029480 | Fcgamma receptor (FCGR) dependent phagocytosis | 8.599020e-01 | 0.066 |
| R-HSA-1852241 | Organelle biogenesis and maintenance | 8.606629e-01 | 0.065 |
| R-HSA-9678108 | SARS-CoV-1 Infection | 8.613300e-01 | 0.065 |
| R-HSA-2559583 | Cellular Senescence | 8.682561e-01 | 0.061 |
| R-HSA-392499 | Metabolism of proteins | 8.693491e-01 | 0.061 |
| R-HSA-201681 | TCF dependent signaling in response to WNT | 8.722455e-01 | 0.059 |
| R-HSA-112316 | Neuronal System | 8.749731e-01 | 0.058 |
| R-HSA-168898 | Toll-like Receptor Cascades | 8.823067e-01 | 0.054 |
| R-HSA-9006925 | Intracellular signaling by second messengers | 8.833131e-01 | 0.054 |
| R-HSA-382551 | Transport of small molecules | 8.863971e-01 | 0.052 |
| R-HSA-9006934 | Signaling by Receptor Tyrosine Kinases | 8.872322e-01 | 0.052 |
| R-HSA-9609690 | HCMV Early Events | 8.881908e-01 | 0.051 |
| R-HSA-389948 | Co-inhibition by PD-1 | 8.926869e-01 | 0.049 |
| R-HSA-948021 | Transport to the Golgi and subsequent modification | 8.948670e-01 | 0.048 |
| R-HSA-376176 | Signaling by ROBO receptors | 8.959405e-01 | 0.048 |
| R-HSA-1483206 | Glycerophospholipid biosynthesis | 8.959405e-01 | 0.048 |
| R-HSA-5357801 | Programmed Cell Death | 8.990961e-01 | 0.046 |
| R-HSA-68886 | M Phase | 9.167274e-01 | 0.038 |
| R-HSA-162906 | HIV Infection | 9.195075e-01 | 0.036 |
| R-HSA-9705683 | SARS-CoV-2-host interactions | 9.203307e-01 | 0.036 |
| R-HSA-72312 | rRNA processing | 9.235409e-01 | 0.035 |
| R-HSA-156580 | Phase II - Conjugation of compounds | 9.288523e-01 | 0.032 |
| R-HSA-157118 | Signaling by NOTCH | 9.295806e-01 | 0.032 |
| R-HSA-168249 | Innate Immune System | 9.353894e-01 | 0.029 |
| R-HSA-9609646 | HCMV Infection | 9.364675e-01 | 0.029 |
| R-HSA-388841 | Regulation of T cell activation by CD28 family | 9.402738e-01 | 0.027 |
| R-HSA-76002 | Platelet activation, signaling and aggregation | 9.503854e-01 | 0.022 |
| R-HSA-446728 | Cell junction organization | 9.523902e-01 | 0.021 |
| R-HSA-9658195 | Leishmania infection | 9.538408e-01 | 0.021 |
| R-HSA-9824443 | Parasitic Infection Pathways | 9.538408e-01 | 0.021 |
| R-HSA-1483257 | Phospholipid metabolism | 9.600504e-01 | 0.018 |
| R-HSA-195721 | Signaling by WNT | 9.612689e-01 | 0.017 |
| R-HSA-212436 | Generic Transcription Pathway | 9.624205e-01 | 0.017 |
| R-HSA-73857 | RNA Polymerase II Transcription | 9.662324e-01 | 0.015 |
| R-HSA-1500931 | Cell-Cell communication | 9.678419e-01 | 0.014 |
| R-HSA-8957322 | Metabolism of steroids | 9.703951e-01 | 0.013 |
| R-HSA-1474244 | Extracellular matrix organization | 9.724633e-01 | 0.012 |
| R-HSA-9694516 | SARS-CoV-2 Infection | 9.771454e-01 | 0.010 |
| R-HSA-9006931 | Signaling by Nuclear Receptors | 9.802323e-01 | 0.009 |
| R-HSA-196854 | Metabolism of vitamins and cofactors | 9.804362e-01 | 0.009 |
| R-HSA-5663205 | Infectious disease | 9.829429e-01 | 0.007 |
| R-HSA-1266738 | Developmental Biology | 9.834910e-01 | 0.007 |
| R-HSA-1280218 | Adaptive Immune System | 9.852647e-01 | 0.006 |
| R-HSA-109582 | Hemostasis | 9.891935e-01 | 0.005 |
| R-HSA-446203 | Asparagine N-linked glycosylation | 9.894014e-01 | 0.005 |
| R-HSA-71291 | Metabolism of amino acids and derivatives | 9.894770e-01 | 0.005 |
| R-HSA-71387 | Metabolism of carbohydrates and carbohydrate derivatives | 9.924852e-01 | 0.003 |
| R-HSA-1643685 | Disease | 9.930507e-01 | 0.003 |
| R-HSA-211859 | Biological oxidations | 9.963085e-01 | 0.002 |
| R-HSA-388396 | GPCR downstream signalling | 9.997394e-01 | 0.000 |
| R-HSA-372790 | Signaling by GPCR | 9.998926e-01 | 0.000 |
| R-HSA-556833 | Metabolism of lipids | 9.999981e-01 | 0.000 |
| R-HSA-1430728 | Metabolism | 1.000000e+00 | 0.000 |
Download
| kinase | JSD_mean | pearson_surrounding | kinase_max_IC_position | max_position_JSD |
|---|---|---|---|---|
KIS |
0.866 | 0.748 | 1 | 0.843 |
CDK19 |
0.866 | 0.834 | 1 | 0.889 |
P38G |
0.863 | 0.875 | 1 | 0.916 |
CDK8 |
0.863 | 0.836 | 1 | 0.862 |
P38D |
0.862 | 0.868 | 1 | 0.929 |
CDK1 |
0.862 | 0.824 | 1 | 0.876 |
CDK18 |
0.861 | 0.832 | 1 | 0.892 |
JNK2 |
0.861 | 0.876 | 1 | 0.891 |
CDK17 |
0.860 | 0.846 | 1 | 0.910 |
CDK3 |
0.857 | 0.741 | 1 | 0.910 |
ERK1 |
0.857 | 0.849 | 1 | 0.878 |
P38B |
0.856 | 0.859 | 1 | 0.867 |
CDK13 |
0.855 | 0.817 | 1 | 0.878 |
HIPK2 |
0.853 | 0.753 | 1 | 0.875 |
JNK3 |
0.853 | 0.862 | 1 | 0.874 |
CDK7 |
0.853 | 0.805 | 1 | 0.865 |
CDK16 |
0.851 | 0.814 | 1 | 0.901 |
CDK5 |
0.851 | 0.794 | 1 | 0.842 |
CDK12 |
0.851 | 0.814 | 1 | 0.891 |
DYRK2 |
0.847 | 0.739 | 1 | 0.809 |
CLK3 |
0.846 | 0.512 | 1 | 0.606 |
P38A |
0.845 | 0.830 | 1 | 0.812 |
CDK9 |
0.841 | 0.786 | 1 | 0.870 |
DYRK4 |
0.841 | 0.748 | 1 | 0.890 |
CDK10 |
0.840 | 0.751 | 1 | 0.871 |
ERK2 |
0.838 | 0.821 | 1 | 0.831 |
CDK14 |
0.837 | 0.785 | 1 | 0.858 |
NLK |
0.835 | 0.719 | 1 | 0.626 |
JNK1 |
0.834 | 0.776 | 1 | 0.889 |
DYRK1B |
0.834 | 0.709 | 1 | 0.852 |
HIPK4 |
0.833 | 0.486 | 1 | 0.618 |
HIPK1 |
0.833 | 0.667 | 1 | 0.792 |
CDK6 |
0.830 | 0.773 | 1 | 0.874 |
CDK4 |
0.829 | 0.793 | 1 | 0.897 |
CDK2 |
0.827 | 0.610 | 1 | 0.768 |
ERK5 |
0.827 | 0.421 | 1 | 0.552 |
DYRK1A |
0.826 | 0.604 | 1 | 0.777 |
SRPK1 |
0.826 | 0.325 | -3 | 0.637 |
HIPK3 |
0.821 | 0.641 | 1 | 0.761 |
MTOR |
0.819 | 0.228 | 1 | 0.419 |
CLK2 |
0.817 | 0.393 | -3 | 0.623 |
ICK |
0.815 | 0.392 | -3 | 0.737 |
SRPK2 |
0.814 | 0.255 | -3 | 0.560 |
MAK |
0.814 | 0.542 | -2 | 0.861 |
COT |
0.814 | -0.031 | 2 | 0.871 |
DYRK3 |
0.814 | 0.518 | 1 | 0.757 |
CDKL5 |
0.813 | 0.197 | -3 | 0.696 |
CLK1 |
0.812 | 0.372 | -3 | 0.622 |
PRP4 |
0.811 | 0.483 | -3 | 0.751 |
CLK4 |
0.809 | 0.338 | -3 | 0.649 |
CDKL1 |
0.808 | 0.155 | -3 | 0.705 |
CDC7 |
0.806 | -0.075 | 1 | 0.280 |
MOS |
0.806 | 0.019 | 1 | 0.323 |
SRPK3 |
0.804 | 0.228 | -3 | 0.614 |
PRPK |
0.801 | -0.078 | -1 | 0.828 |
TBK1 |
0.800 | -0.125 | 1 | 0.225 |
MOK |
0.797 | 0.472 | 1 | 0.688 |
ATR |
0.797 | -0.039 | 1 | 0.309 |
IKKE |
0.797 | -0.145 | 1 | 0.225 |
PIM3 |
0.797 | -0.046 | -3 | 0.724 |
IKKB |
0.796 | -0.149 | -2 | 0.705 |
DSTYK |
0.796 | -0.131 | 2 | 0.868 |
GRK1 |
0.795 | 0.006 | -2 | 0.755 |
CHAK2 |
0.795 | -0.025 | -1 | 0.850 |
BMPR2 |
0.795 | -0.143 | -2 | 0.842 |
ERK7 |
0.794 | 0.278 | 2 | 0.551 |
NEK6 |
0.794 | -0.069 | -2 | 0.813 |
RAF1 |
0.794 | -0.192 | 1 | 0.260 |
GCN2 |
0.794 | -0.190 | 2 | 0.756 |
PDHK4 |
0.793 | -0.185 | 1 | 0.321 |
NDR2 |
0.793 | -0.041 | -3 | 0.731 |
MST4 |
0.792 | -0.052 | 2 | 0.844 |
CAMK2G |
0.791 | -0.089 | 2 | 0.765 |
IKKA |
0.790 | -0.064 | -2 | 0.699 |
CAMK1B |
0.790 | -0.079 | -3 | 0.762 |
ULK2 |
0.790 | -0.206 | 2 | 0.751 |
WNK1 |
0.788 | -0.095 | -2 | 0.843 |
TGFBR2 |
0.788 | -0.086 | -2 | 0.766 |
MLK1 |
0.788 | -0.115 | 2 | 0.793 |
NEK7 |
0.788 | -0.170 | -3 | 0.809 |
PKN3 |
0.787 | -0.077 | -3 | 0.727 |
GRK5 |
0.787 | -0.127 | -3 | 0.804 |
PDHK1 |
0.786 | -0.210 | 1 | 0.301 |
GRK7 |
0.786 | 0.044 | 1 | 0.272 |
PRKD1 |
0.786 | -0.054 | -3 | 0.714 |
NUAK2 |
0.786 | -0.032 | -3 | 0.733 |
BMPR1B |
0.786 | -0.018 | 1 | 0.246 |
GSK3A |
0.785 | 0.232 | 4 | 0.503 |
NIK |
0.785 | -0.114 | -3 | 0.786 |
MARK4 |
0.785 | -0.071 | 4 | 0.891 |
MLK3 |
0.785 | -0.028 | 2 | 0.730 |
RSK2 |
0.784 | -0.040 | -3 | 0.660 |
SKMLCK |
0.784 | -0.081 | -2 | 0.821 |
RIPK3 |
0.784 | -0.152 | 3 | 0.720 |
PIM1 |
0.784 | -0.016 | -3 | 0.664 |
CAMLCK |
0.783 | -0.064 | -2 | 0.810 |
NDR1 |
0.783 | -0.094 | -3 | 0.721 |
IRE1 |
0.782 | -0.087 | 1 | 0.252 |
ULK1 |
0.782 | -0.186 | -3 | 0.782 |
DAPK2 |
0.781 | -0.095 | -3 | 0.773 |
PKCD |
0.781 | -0.057 | 2 | 0.778 |
P90RSK |
0.781 | -0.048 | -3 | 0.664 |
TGFBR1 |
0.780 | -0.028 | -2 | 0.762 |
ALK4 |
0.780 | -0.040 | -2 | 0.794 |
PKN2 |
0.780 | -0.103 | -3 | 0.727 |
MLK2 |
0.780 | -0.119 | 2 | 0.799 |
PRKD2 |
0.780 | -0.052 | -3 | 0.649 |
HUNK |
0.780 | -0.169 | 2 | 0.783 |
GRK6 |
0.780 | -0.104 | 1 | 0.256 |
ATM |
0.778 | -0.077 | 1 | 0.271 |
AMPKA1 |
0.778 | -0.096 | -3 | 0.745 |
PINK1 |
0.778 | 0.148 | 1 | 0.465 |
WNK3 |
0.778 | -0.218 | 1 | 0.254 |
PKR |
0.778 | -0.075 | 1 | 0.279 |
MPSK1 |
0.778 | 0.087 | 1 | 0.325 |
IRE2 |
0.778 | -0.063 | 2 | 0.731 |
AURC |
0.777 | -0.019 | -2 | 0.637 |
BCKDK |
0.777 | -0.185 | -1 | 0.739 |
RSK3 |
0.777 | -0.071 | -3 | 0.657 |
LATS1 |
0.776 | -0.009 | -3 | 0.748 |
MASTL |
0.775 | -0.216 | -2 | 0.778 |
FAM20C |
0.775 | -0.030 | 2 | 0.558 |
NEK9 |
0.775 | -0.210 | 2 | 0.811 |
P70S6KB |
0.775 | -0.067 | -3 | 0.681 |
VRK2 |
0.775 | 0.018 | 1 | 0.362 |
DLK |
0.775 | -0.214 | 1 | 0.265 |
ACVR2B |
0.775 | -0.060 | -2 | 0.769 |
PKACG |
0.775 | -0.072 | -2 | 0.713 |
LATS2 |
0.774 | -0.084 | -5 | 0.799 |
DNAPK |
0.774 | -0.055 | 1 | 0.274 |
ACVR2A |
0.774 | -0.064 | -2 | 0.765 |
YSK4 |
0.773 | -0.155 | 1 | 0.234 |
ANKRD3 |
0.773 | -0.209 | 1 | 0.274 |
TSSK1 |
0.773 | -0.078 | -3 | 0.768 |
TSSK2 |
0.772 | -0.109 | -5 | 0.868 |
CAMK2D |
0.772 | -0.157 | -3 | 0.737 |
MAPKAPK3 |
0.772 | -0.121 | -3 | 0.651 |
AMPKA2 |
0.772 | -0.084 | -3 | 0.705 |
TTBK2 |
0.772 | -0.191 | 2 | 0.670 |
SMG1 |
0.772 | -0.091 | 1 | 0.289 |
MAPKAPK2 |
0.771 | -0.078 | -3 | 0.602 |
PKCA |
0.771 | -0.048 | 2 | 0.723 |
GRK4 |
0.771 | -0.165 | -2 | 0.778 |
MLK4 |
0.771 | -0.087 | 2 | 0.698 |
ALK2 |
0.771 | -0.058 | -2 | 0.767 |
PLK1 |
0.771 | -0.125 | -2 | 0.749 |
PKCG |
0.770 | -0.067 | 2 | 0.729 |
RSK4 |
0.770 | -0.030 | -3 | 0.627 |
RIPK1 |
0.770 | -0.239 | 1 | 0.237 |
BMPR1A |
0.769 | -0.029 | 1 | 0.236 |
PKCB |
0.769 | -0.066 | 2 | 0.734 |
CHAK1 |
0.769 | -0.139 | 2 | 0.744 |
NEK2 |
0.769 | -0.155 | 2 | 0.790 |
QSK |
0.768 | -0.067 | 4 | 0.869 |
PAK1 |
0.768 | -0.088 | -2 | 0.753 |
MNK2 |
0.768 | -0.081 | -2 | 0.746 |
NIM1 |
0.768 | -0.145 | 3 | 0.752 |
PKCZ |
0.768 | -0.080 | 2 | 0.766 |
PLK3 |
0.768 | -0.073 | 2 | 0.726 |
MEK1 |
0.767 | -0.178 | 2 | 0.795 |
MARK3 |
0.766 | -0.051 | 4 | 0.846 |
CAMK2A |
0.766 | -0.068 | 2 | 0.756 |
TLK2 |
0.766 | -0.134 | 1 | 0.251 |
PRKD3 |
0.766 | -0.075 | -3 | 0.619 |
NUAK1 |
0.765 | -0.092 | -3 | 0.670 |
PHKG1 |
0.765 | -0.124 | -3 | 0.705 |
QIK |
0.765 | -0.141 | -3 | 0.734 |
PAK3 |
0.765 | -0.124 | -2 | 0.741 |
GRK2 |
0.765 | -0.078 | -2 | 0.682 |
GSK3B |
0.765 | 0.063 | 4 | 0.495 |
PKG2 |
0.765 | -0.046 | -2 | 0.658 |
MNK1 |
0.765 | -0.065 | -2 | 0.755 |
CK1E |
0.765 | -0.026 | -3 | 0.521 |
PKACB |
0.764 | -0.033 | -2 | 0.641 |
CAMK2B |
0.764 | -0.104 | 2 | 0.737 |
PIM2 |
0.764 | -0.025 | -3 | 0.630 |
AURB |
0.764 | -0.054 | -2 | 0.627 |
PRKX |
0.764 | -0.007 | -3 | 0.553 |
AKT2 |
0.763 | -0.030 | -3 | 0.570 |
PAK6 |
0.763 | -0.063 | -2 | 0.674 |
CAMK4 |
0.763 | -0.179 | -3 | 0.705 |
CK2A2 |
0.763 | 0.003 | 1 | 0.218 |
MSK2 |
0.763 | -0.102 | -3 | 0.628 |
PKCH |
0.763 | -0.097 | 2 | 0.705 |
PERK |
0.763 | -0.155 | -2 | 0.808 |
MARK2 |
0.762 | -0.066 | 4 | 0.812 |
HRI |
0.762 | -0.165 | -2 | 0.820 |
SGK3 |
0.762 | -0.063 | -3 | 0.648 |
MELK |
0.761 | -0.142 | -3 | 0.684 |
MST3 |
0.761 | -0.074 | 2 | 0.832 |
MEKK3 |
0.760 | -0.166 | 1 | 0.254 |
TAO3 |
0.760 | -0.064 | 1 | 0.278 |
DRAK1 |
0.760 | -0.160 | 1 | 0.209 |
MEK5 |
0.760 | -0.189 | 2 | 0.788 |
SIK |
0.760 | -0.099 | -3 | 0.636 |
MEKK2 |
0.760 | -0.131 | 2 | 0.774 |
GAK |
0.760 | -0.022 | 1 | 0.319 |
MEKK1 |
0.759 | -0.173 | 1 | 0.266 |
PASK |
0.759 | -0.041 | -3 | 0.758 |
MYLK4 |
0.759 | -0.093 | -2 | 0.722 |
ZAK |
0.759 | -0.177 | 1 | 0.240 |
MSK1 |
0.758 | -0.076 | -3 | 0.631 |
CHK1 |
0.758 | -0.111 | -3 | 0.733 |
PAK2 |
0.758 | -0.126 | -2 | 0.736 |
BRSK2 |
0.758 | -0.132 | -3 | 0.695 |
BRSK1 |
0.757 | -0.113 | -3 | 0.668 |
WNK4 |
0.757 | -0.154 | -2 | 0.843 |
IRAK4 |
0.757 | -0.149 | 1 | 0.235 |
NEK5 |
0.756 | -0.181 | 1 | 0.256 |
CK1D |
0.755 | -0.015 | -3 | 0.465 |
BRAF |
0.755 | -0.173 | -4 | 0.833 |
PLK4 |
0.755 | -0.170 | 2 | 0.573 |
TLK1 |
0.754 | -0.164 | -2 | 0.777 |
CAMK1G |
0.754 | -0.111 | -3 | 0.641 |
AURA |
0.754 | -0.068 | -2 | 0.592 |
MARK1 |
0.754 | -0.109 | 4 | 0.855 |
CK2A1 |
0.753 | -0.010 | 1 | 0.204 |
SSTK |
0.752 | -0.080 | 4 | 0.854 |
TAO2 |
0.752 | -0.085 | 2 | 0.833 |
PKCI |
0.752 | -0.071 | 2 | 0.730 |
DCAMKL1 |
0.751 | -0.119 | -3 | 0.660 |
LKB1 |
0.751 | -0.090 | -3 | 0.783 |
GCK |
0.751 | -0.093 | 1 | 0.260 |
GRK3 |
0.751 | -0.079 | -2 | 0.637 |
EEF2K |
0.751 | -0.050 | 3 | 0.848 |
AKT1 |
0.750 | -0.054 | -3 | 0.583 |
PHKG2 |
0.750 | -0.130 | -3 | 0.676 |
PKCT |
0.750 | -0.108 | 2 | 0.716 |
SMMLCK |
0.750 | -0.097 | -3 | 0.710 |
NEK11 |
0.749 | -0.176 | 1 | 0.269 |
MAPKAPK5 |
0.749 | -0.166 | -3 | 0.610 |
TTBK1 |
0.749 | -0.170 | 2 | 0.595 |
MST2 |
0.749 | -0.135 | 1 | 0.252 |
NEK8 |
0.748 | -0.187 | 2 | 0.797 |
CK1A2 |
0.748 | -0.040 | -3 | 0.463 |
PLK2 |
0.748 | 0.000 | -3 | 0.836 |
PKCE |
0.748 | -0.041 | 2 | 0.715 |
SNRK |
0.747 | -0.228 | 2 | 0.637 |
PKACA |
0.747 | -0.051 | -2 | 0.605 |
HGK |
0.747 | -0.097 | 3 | 0.874 |
DCAMKL2 |
0.746 | -0.117 | -3 | 0.685 |
PDK1 |
0.746 | -0.119 | 1 | 0.284 |
TNIK |
0.746 | -0.077 | 3 | 0.869 |
BUB1 |
0.746 | -0.002 | -5 | 0.805 |
LRRK2 |
0.746 | -0.058 | 2 | 0.818 |
CAMKK1 |
0.746 | -0.221 | -2 | 0.706 |
P70S6K |
0.746 | -0.095 | -3 | 0.594 |
MINK |
0.746 | -0.135 | 1 | 0.239 |
MAP3K15 |
0.746 | -0.129 | 1 | 0.250 |
CK1G1 |
0.745 | -0.089 | -3 | 0.495 |
PBK |
0.745 | -0.047 | 1 | 0.301 |
CAMKK2 |
0.745 | -0.181 | -2 | 0.721 |
PAK5 |
0.744 | -0.089 | -2 | 0.618 |
HASPIN |
0.744 | 0.018 | -1 | 0.699 |
HPK1 |
0.743 | -0.109 | 1 | 0.254 |
MEKK6 |
0.742 | -0.159 | 1 | 0.264 |
TAK1 |
0.742 | -0.194 | 1 | 0.250 |
KHS1 |
0.742 | -0.072 | 1 | 0.252 |
NEK4 |
0.742 | -0.204 | 1 | 0.235 |
SLK |
0.742 | -0.084 | -2 | 0.704 |
MST1 |
0.741 | -0.142 | 1 | 0.238 |
LOK |
0.741 | -0.111 | -2 | 0.742 |
KHS2 |
0.741 | -0.046 | 1 | 0.262 |
VRK1 |
0.740 | -0.160 | 2 | 0.825 |
PKN1 |
0.740 | -0.093 | -3 | 0.607 |
PDHK3_TYR |
0.739 | 0.167 | 4 | 0.904 |
PAK4 |
0.739 | -0.081 | -2 | 0.622 |
SGK1 |
0.739 | -0.022 | -3 | 0.491 |
AKT3 |
0.738 | -0.044 | -3 | 0.505 |
DAPK3 |
0.738 | -0.100 | -3 | 0.675 |
NEK1 |
0.738 | -0.192 | 1 | 0.232 |
SBK |
0.737 | 0.044 | -3 | 0.447 |
IRAK1 |
0.737 | -0.264 | -1 | 0.735 |
BIKE |
0.735 | -0.031 | 1 | 0.300 |
CAMK1D |
0.735 | -0.112 | -3 | 0.553 |
YSK1 |
0.735 | -0.141 | 2 | 0.792 |
MRCKB |
0.735 | -0.061 | -3 | 0.612 |
MRCKA |
0.734 | -0.067 | -3 | 0.627 |
ROCK2 |
0.734 | -0.063 | -3 | 0.666 |
DAPK1 |
0.733 | -0.099 | -3 | 0.662 |
STK33 |
0.732 | -0.152 | 2 | 0.586 |
PDHK4_TYR |
0.731 | 0.077 | 2 | 0.852 |
DMPK1 |
0.730 | -0.025 | -3 | 0.633 |
TESK1_TYR |
0.730 | 0.024 | 3 | 0.873 |
CHK2 |
0.729 | -0.093 | -3 | 0.508 |
MEK2 |
0.729 | -0.237 | 2 | 0.759 |
RIPK2 |
0.728 | -0.253 | 1 | 0.221 |
AAK1 |
0.728 | 0.005 | 1 | 0.294 |
PKMYT1_TYR |
0.728 | 0.084 | 3 | 0.835 |
NEK3 |
0.728 | -0.171 | 1 | 0.255 |
TTK |
0.727 | -0.083 | -2 | 0.775 |
OSR1 |
0.727 | -0.107 | 2 | 0.776 |
BMPR2_TYR |
0.726 | 0.036 | -1 | 0.859 |
LIMK2_TYR |
0.726 | 0.076 | -3 | 0.809 |
MAP2K6_TYR |
0.725 | 0.017 | -1 | 0.855 |
PDHK1_TYR |
0.725 | 0.003 | -1 | 0.882 |
MAP2K4_TYR |
0.725 | -0.028 | -1 | 0.837 |
MAP2K7_TYR |
0.724 | -0.077 | 2 | 0.821 |
CAMK1A |
0.724 | -0.099 | -3 | 0.519 |
TAO1 |
0.724 | -0.108 | 1 | 0.239 |
MYO3B |
0.723 | -0.103 | 2 | 0.806 |
PKG1 |
0.722 | -0.082 | -2 | 0.581 |
ASK1 |
0.721 | -0.160 | 1 | 0.248 |
ALPHAK3 |
0.721 | -0.086 | -1 | 0.761 |
PINK1_TYR |
0.720 | -0.125 | 1 | 0.309 |
CRIK |
0.719 | -0.051 | -3 | 0.587 |
ROCK1 |
0.719 | -0.076 | -3 | 0.627 |
MYO3A |
0.719 | -0.120 | 1 | 0.250 |
EPHA6 |
0.718 | -0.061 | -1 | 0.846 |
LIMK1_TYR |
0.716 | -0.040 | 2 | 0.820 |
RET |
0.716 | -0.134 | 1 | 0.272 |
YANK3 |
0.716 | -0.072 | 2 | 0.396 |
JAK2 |
0.714 | -0.120 | 1 | 0.284 |
CSF1R |
0.713 | -0.074 | 3 | 0.775 |
MST1R |
0.713 | -0.117 | 3 | 0.790 |
TYK2 |
0.713 | -0.197 | 1 | 0.265 |
CK1A |
0.713 | -0.061 | -3 | 0.379 |
TXK |
0.712 | -0.053 | 1 | 0.247 |
EPHB4 |
0.712 | -0.109 | -1 | 0.800 |
ROS1 |
0.710 | -0.137 | 3 | 0.764 |
LCK |
0.709 | -0.048 | -1 | 0.826 |
YES1 |
0.709 | -0.075 | -1 | 0.826 |
JAK3 |
0.709 | -0.119 | 1 | 0.263 |
NEK10_TYR |
0.709 | -0.114 | 1 | 0.233 |
DDR1 |
0.707 | -0.140 | 4 | 0.843 |
ABL2 |
0.707 | -0.105 | -1 | 0.780 |
BLK |
0.707 | -0.039 | -1 | 0.833 |
JAK1 |
0.707 | -0.093 | 1 | 0.245 |
FGR |
0.706 | -0.151 | 1 | 0.258 |
TYRO3 |
0.706 | -0.185 | 3 | 0.791 |
STLK3 |
0.706 | -0.209 | 1 | 0.222 |
TNNI3K_TYR |
0.706 | -0.060 | 1 | 0.302 |
HCK |
0.706 | -0.113 | -1 | 0.812 |
EPHA4 |
0.705 | -0.079 | 2 | 0.741 |
FGFR2 |
0.705 | -0.059 | 3 | 0.766 |
ABL1 |
0.704 | -0.114 | -1 | 0.770 |
FER |
0.703 | -0.174 | 1 | 0.274 |
KIT |
0.702 | -0.117 | 3 | 0.774 |
INSRR |
0.702 | -0.133 | 3 | 0.732 |
FYN |
0.702 | -0.030 | -1 | 0.817 |
EPHB1 |
0.701 | -0.155 | 1 | 0.251 |
FGFR1 |
0.701 | -0.071 | 3 | 0.743 |
FLT3 |
0.701 | -0.156 | 3 | 0.782 |
ITK |
0.701 | -0.128 | -1 | 0.774 |
TEK |
0.701 | -0.050 | 3 | 0.716 |
KDR |
0.700 | -0.102 | 3 | 0.726 |
SRMS |
0.700 | -0.164 | 1 | 0.246 |
EPHB2 |
0.700 | -0.129 | -1 | 0.786 |
TNK2 |
0.700 | -0.143 | 3 | 0.730 |
TNK1 |
0.699 | -0.105 | 3 | 0.764 |
EPHB3 |
0.698 | -0.160 | -1 | 0.785 |
MET |
0.697 | -0.105 | 3 | 0.761 |
WEE1_TYR |
0.697 | -0.091 | -1 | 0.715 |
PDGFRB |
0.696 | -0.218 | 3 | 0.789 |
BMX |
0.696 | -0.109 | -1 | 0.692 |
FRK |
0.695 | -0.110 | -1 | 0.824 |
FLT1 |
0.695 | -0.114 | -1 | 0.830 |
BTK |
0.695 | -0.188 | -1 | 0.729 |
FGFR3 |
0.695 | -0.071 | 3 | 0.734 |
TEC |
0.693 | -0.145 | -1 | 0.690 |
PDGFRA |
0.693 | -0.216 | 3 | 0.787 |
EPHA7 |
0.693 | -0.123 | 2 | 0.742 |
ERBB2 |
0.692 | -0.152 | 1 | 0.241 |
EGFR |
0.692 | -0.086 | 1 | 0.205 |
LYN |
0.692 | -0.107 | 3 | 0.696 |
DDR2 |
0.690 | -0.062 | 3 | 0.717 |
ALK |
0.689 | -0.170 | 3 | 0.706 |
PTK2 |
0.689 | -0.029 | -1 | 0.799 |
MERTK |
0.689 | -0.187 | 3 | 0.743 |
SRC |
0.689 | -0.090 | -1 | 0.803 |
AXL |
0.688 | -0.219 | 3 | 0.752 |
EPHA8 |
0.688 | -0.095 | -1 | 0.799 |
EPHA3 |
0.687 | -0.157 | 2 | 0.711 |
MATK |
0.687 | -0.102 | -1 | 0.733 |
FLT4 |
0.687 | -0.163 | 3 | 0.717 |
SYK |
0.686 | -0.050 | -1 | 0.790 |
PTK6 |
0.686 | -0.209 | -1 | 0.694 |
EPHA1 |
0.686 | -0.180 | 3 | 0.738 |
LTK |
0.685 | -0.189 | 3 | 0.716 |
CK1G3 |
0.685 | -0.077 | -3 | 0.329 |
NTRK1 |
0.684 | -0.232 | -1 | 0.774 |
INSR |
0.684 | -0.173 | 3 | 0.709 |
CSK |
0.684 | -0.118 | 2 | 0.743 |
PTK2B |
0.683 | -0.128 | -1 | 0.731 |
NTRK2 |
0.683 | -0.228 | 3 | 0.729 |
EPHA5 |
0.682 | -0.145 | 2 | 0.721 |
FGFR4 |
0.682 | -0.098 | -1 | 0.747 |
YANK2 |
0.682 | -0.090 | 2 | 0.406 |
MUSK |
0.682 | -0.134 | 1 | 0.193 |
NTRK3 |
0.682 | -0.174 | -1 | 0.730 |
ERBB4 |
0.680 | -0.074 | 1 | 0.215 |
EPHA2 |
0.675 | -0.120 | -1 | 0.755 |
CK1G2 |
0.671 | -0.069 | -3 | 0.418 |
IGF1R |
0.670 | -0.153 | 3 | 0.643 |
ZAP70 |
0.665 | -0.066 | -1 | 0.703 |
FES |
0.660 | -0.151 | -1 | 0.673 |