Motif 1087 (n=220)
Position-wise Probabilities
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uniprot | genes | site | source | protein | function |
---|---|---|---|---|---|
A0A0G2JPF8 | HNRNPCL4 | T25 | ochoa | Heterogeneous nuclear ribonucleoprotein C like 4 | None |
A2RU67 | FAM234B | T26 | ochoa | Protein FAM234B | None |
A6NKT7 | RGPD3 | T1030 | ochoa | RanBP2-like and GRIP domain-containing protein 3 | None |
B7ZW38 | HNRNPCL3 | T25 | ochoa | Heterogeneous nuclear ribonucleoprotein C-like 3 | None |
O00425 | IGF2BP3 | T249 | ochoa | Insulin-like growth factor 2 mRNA-binding protein 3 (IGF2 mRNA-binding protein 3) (IMP-3) (IGF-II mRNA-binding protein 3) (KH domain-containing protein overexpressed in cancer) (hKOC) (VICKZ family member 3) | RNA-binding factor that may recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to beta-actin/ACTB and MYC transcripts. Increases MYC mRNA stability by binding to the coding region instability determinant (CRD) and binding is enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. {ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:29476152}. |
O00562 | PITPNM1 | T369 | ochoa | Membrane-associated phosphatidylinositol transfer protein 1 (Drosophila retinal degeneration B homolog) (Phosphatidylinositol transfer protein, membrane-associated 1) (PITPnm 1) (Pyk2 N-terminal domain-interacting receptor 2) (NIR-2) | Catalyzes the transfer of phosphatidylinositol (PI) between membranes (PubMed:10531358, PubMed:22822086). Binds PI, phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding affinity order of PI > PA > PC (PubMed:22822086). Regulates RHOA activity, and plays a role in cytoskeleton remodeling (PubMed:11909959). Necessary for normal completion of cytokinesis (PubMed:15125835). Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus (PubMed:15723057). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus (PubMed:15545272). Required for protein export from the endoplasmic reticulum and the Golgi (PubMed:15723057). Binds calcium ions (PubMed:10022914). {ECO:0000269|PubMed:10022914, ECO:0000269|PubMed:10531358, ECO:0000269|PubMed:11909959, ECO:0000269|PubMed:15545272, ECO:0000269|PubMed:15723057, ECO:0000269|PubMed:22822086}. |
O14715 | RGPD8 | T1029 | ochoa | RANBP2-like and GRIP domain-containing protein 8 (Ran-binding protein 2-like 3) (RanBP2-like 3) (RanBP2L3) | None |
O14776 | TCERG1 | T591 | ochoa | Transcription elongation regulator 1 (TATA box-binding protein-associated factor 2S) (Transcription factor CA150) | Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter. {ECO:0000269|PubMed:11604498, ECO:0000269|PubMed:9315662}. |
O14983 | ATP2A1 | T533 | ochoa | Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (SERCA1) (SR Ca(2+)-ATPase 1) (EC 7.2.2.10) (Calcium pump 1) (Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) | Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (By similarity). Contributes to calcium sequestration involved in muscular excitation/contraction (PubMed:10914677). {ECO:0000250|UniProtKB:P04191, ECO:0000269|PubMed:10914677}. |
O43741 | PRKAB2 | T40 | ochoa | 5'-AMP-activated protein kinase subunit beta-2 (AMPK subunit beta-2) | Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3). |
O43815 | STRN | T265 | ochoa | Striatin | Calmodulin-binding scaffolding protein which is the center of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (Probable). {ECO:0000269|PubMed:18782753, ECO:0000305|PubMed:26876214}. |
O60812 | HNRNPCL1 | T25 | ochoa | Heterogeneous nuclear ribonucleoprotein C-like 1 (hnRNP C-like-1) (hnRNP core protein C-like 1) | May play a role in nucleosome assembly by neutralizing basic proteins such as A and B core hnRNPs. {ECO:0000250}. |
O75449 | KATNA1 | T133 | psp | Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (p60 katanin) | Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:11870226, ECO:0000269|PubMed:19287380}. |
O94906 | PRPF6 | T275 | ochoa | Pre-mRNA-processing factor 6 (Androgen receptor N-terminal domain-transactivating protein 1) (ANT-1) (PRP6 homolog) (U5 snRNP-associated 102 kDa protein) (U5-102 kDa protein) | Involved in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome (PubMed:20118938, PubMed:21549338, PubMed:28781166). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation. {ECO:0000269|PubMed:12039962, ECO:0000269|PubMed:20118938, ECO:0000269|PubMed:21549338, ECO:0000269|PubMed:28781166}. |
O95425 | SVIL | T1111 | ochoa | Supervillin (Archvillin) (p205/p250) | [Isoform 1]: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420). {ECO:0000269|PubMed:12711699, ECO:0000269|PubMed:19109420}.; FUNCTION: [Isoform 2]: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250|UniProtKB:O46385}. |
O95835 | LATS1 | T1012 | psp | Serine/threonine-protein kinase LATS1 (EC 2.7.11.1) (Large tumor suppressor homolog 1) (WARTS protein kinase) (h-warts) | Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:10518011, PubMed:10831611, PubMed:18158288, PubMed:26437443, PubMed:28068668). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288, PubMed:26437443, PubMed:28068668). Phosphorylation of YAP1 by LATS1 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration (PubMed:18158288, PubMed:26437443, PubMed:28068668). Acts as a tumor suppressor which plays a critical role in maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint (PubMed:15122335, PubMed:19927127). Negatively regulates G2/M transition by down-regulating CDK1 kinase activity (PubMed:9988268). Involved in the control of p53 expression (PubMed:15122335). Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1 (PubMed:15220930). May also play a role in endocrine function. Plays a role in mammary gland epithelial cell differentiation, both through the Hippo signaling pathway and the intracellular estrogen receptor signaling pathway by promoting the degradation of ESR1 (PubMed:28068668). Acts as an activator of the NLRP3 inflammasome by mediating phosphorylation of 'Ser-265' of NLRP3 following NLRP3 palmitoylation, promoting NLRP3 activation by NEK7 (PubMed:39173637). {ECO:0000269|PubMed:10518011, ECO:0000269|PubMed:10831611, ECO:0000269|PubMed:15122335, ECO:0000269|PubMed:15220930, ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:19927127, ECO:0000269|PubMed:26437443, ECO:0000269|PubMed:28068668, ECO:0000269|PubMed:39173637, ECO:0000269|PubMed:9988268}. |
P04406 | GAPDH | T177 | ochoa | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-) | Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:23332158, ECO:0000269|PubMed:27387501, ECO:0000269|PubMed:3170585}. |
P05556 | ITGB1 | T777 | ochoa | Integrin beta-1 (Fibronectin receptor subunit beta) (Glycoprotein IIa) (GPIIA) (VLA-4 subunit beta) (CD antigen CD29) | Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (By similarity). Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415, PubMed:24789099). ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881). ITGA5:ITGB1 acts as a receptor for fibronectin FN1 and mediates R-G-D-dependent cell adhesion to FN1 (PubMed:33962943). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (PubMed:29030430). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (PubMed:31331973). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity). ITGA9:ITGB1 may play a crucial role in SVEP1/polydom-mediated myoblast cell adhesion (By similarity). Integrins ITGA9:ITGB1 and ITGA4:ITGB1 repress PRKCA-mediated L-type voltage-gated channel Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells via their interaction with SVEP1, thereby inhibit vasocontraction (PubMed:35802072). {ECO:0000250|UniProtKB:P07228, ECO:0000250|UniProtKB:P09055, ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:16256741, ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:24789099, ECO:0000269|PubMed:25398877, ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:31331973, ECO:0000269|PubMed:33962943, ECO:0000269|PubMed:35802072, ECO:0000269|PubMed:7523423}.; FUNCTION: [Isoform 2]: Interferes with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro). {ECO:0000305|PubMed:2249781}.; FUNCTION: [Isoform 5]: Isoform 5 displaces isoform 1 in striated muscles. {ECO:0000250|UniProtKB:P09055}.; FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human echoviruses 1 and 8. {ECO:0000269|PubMed:8411387}.; FUNCTION: (Microbial infection) Acts as a receptor for Cytomegalovirus/HHV-5. {ECO:0000269|PubMed:20660204}.; FUNCTION: (Microbial infection) Acts as a receptor for Epstein-Barr virus/HHV-4. {ECO:0000269|PubMed:17945327}.; FUNCTION: (Microbial infection) Integrin ITGA5:ITGB1 acts as a receptor for Human parvovirus B19. {ECO:0000269|PubMed:12907437}.; FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human rotavirus. {ECO:0000269|PubMed:12941907}.; FUNCTION: (Microbial infection) Acts as a receptor for Mammalian reovirus. {ECO:0000269|PubMed:16501085}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, integrin ITGA5:ITGB1 binding to extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. {ECO:0000269|PubMed:10397733}.; FUNCTION: (Microbial infection) Interacts with CotH proteins expressed by fungi of the order mucorales, the causative agent of mucormycosis, which plays an important role in epithelial cell invasion by the fungi (PubMed:32487760). Integrin ITGA3:ITGB1 may act as a receptor for R.delemar CotH7 in alveolar epithelial cells, which may be an early step in pulmonary mucormycosis disease progression (PubMed:32487760). {ECO:0000269|PubMed:32487760}.; FUNCTION: (Microbial infection) May serve as a receptor for adhesin A (nadA) of N.meningitidis. {ECO:0000305|PubMed:21471204}.; FUNCTION: (Microbial infection) Facilitates rabies infection in a fibronectin-dependent manner and participates in rabies virus traffic after internalization. {ECO:0000269|PubMed:31666383}. |
P06733 | ENO1 | T72 | ochoa | Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (C-myc promoter-binding protein) (Enolase 1) (MBP-1) (MPB-1) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase) (Plasminogen-binding protein) | Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:1369209, PubMed:29775581). In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:10802057, PubMed:12666133, PubMed:2005901, PubMed:29775581). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons (PubMed:12666133). Stimulates immunoglobulin production (PubMed:1369209). {ECO:0000269|PubMed:10802057, ECO:0000269|PubMed:12666133, ECO:0000269|PubMed:1369209, ECO:0000269|PubMed:2005901, ECO:0000269|PubMed:29775581}.; FUNCTION: [Isoform MBP-1]: Binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor. {ECO:0000269|PubMed:10082554}. |
P07910 | HNRNPC | T25 | ochoa | Heterogeneous nuclear ribonucleoproteins C1/C2 (hnRNP C1/C2) | Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides (PubMed:8264621). May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671). {ECO:0000269|PubMed:12509468, ECO:0000269|PubMed:16010978, ECO:0000269|PubMed:25719671, ECO:0000269|PubMed:7567451, ECO:0000269|PubMed:8264621}. |
P07951 | TPM2 | T216 | ochoa | Tropomyosin beta chain (Beta-tropomyosin) (Tropomyosin-2) | Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization. {ECO:0000250|UniProtKB:P58774, ECO:0000250|UniProtKB:P58775}. |
P0DJD0 | RGPD1 | T1014 | ochoa | RANBP2-like and GRIP domain-containing protein 1 (Ran-binding protein 2-like 6) (RanBP2-like 6) (RanBP2L6) | None |
P0DJD1 | RGPD2 | T1022 | ochoa | RANBP2-like and GRIP domain-containing protein 2 (Ran-binding protein 2-like 2) (RanBP2-like 2) (RanBP2L2) | None |
P0DMR1 | HNRNPCL4 | T25 | ochoa | Heterogeneous nuclear ribonucleoprotein C-like 4 | None |
P0DMV8 | HSPA1A | T111 | 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 | T111 | 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}. |
P10074 | ZBTB48 | T295 | ochoa | Zinc finger and BTB domain-containing protein 48 (Krueppel-related zinc finger protein 3) (hKR3) (Telomere zinc finger-associated protein) (TZAP) (Telomere-binding protein and transcriptional activator ZBTB48) (Zinc finger protein 855) | Plays a critical role in transcriptional regulation and chromatin remodeling. Acts as a regulator of telomere length (PubMed:28082411, PubMed:28500257). Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat (PubMed:28082411, PubMed:28500257). Preferentially binds to telomeres that have a low concentration of shelterin complex and acts as a regulator of telomere length by initiating telomere trimming, a process that prevents the accumulation of aberrantly long telomeres (PubMed:28082411). Also acts as a transcription regulator that binds to promoter regions (PubMed:24382891, PubMed:28500257, PubMed:7969177). Regulates expression of a small subset of genes, including MTFP1 (PubMed:28500257). Acts as a negative regulator of cell proliferation by specifically activating expression of ARF, a tumor suppressor isoform of CDKN2A (PubMed:24382891). Acts as a transcription regulator of CIITA, the major factor regulating MHC class II gene expression (PubMed:39562739). In addition, regulates cellular m6A/m6Am methylation on RNA by facilitating the recruitment of the RNA demethylase, FTO, to target mRNAs (PubMed:39300486). {ECO:0000269|PubMed:24382891, ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257, ECO:0000269|PubMed:39300486, ECO:0000269|PubMed:39562739, ECO:0000269|PubMed:7969177}. |
P10809 | HSPD1 | T163 | ochoa | 60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (Heat shock protein family D member 1) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein) | Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable). {ECO:0000269|PubMed:11422376, ECO:0000269|PubMed:1346131, ECO:0000305|PubMed:25918392}. |
P11142 | HSPA8 | T111 | 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}. |
P11142 | HSPA8 | T226 | 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}. |
P13639 | EEF2 | T54 | ochoa | Elongation factor 2 (EF-2) (EC 3.6.5.-) | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:26593721). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (PubMed:26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:26593721). {ECO:0000269|PubMed:26593721}. |
P14618 | PKM | T45 | ochoa|psp | Pyruvate kinase PKM (EC 2.7.1.40) (Cytosolic thyroid hormone-binding protein) (CTHBP) (Opa-interacting protein 3) (OIP-3) (Pyruvate kinase 2/3) (Pyruvate kinase muscle isozyme) (Threonine-protein kinase PKM2) (EC 2.7.11.1) (Thyroid hormone-binding protein 1) (THBP1) (Tumor M2-PK) (Tyrosine-protein kinase PKM2) (EC 2.7.10.2) (p58) | Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:15996096, PubMed:1854723, PubMed:20847263). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed:15996096, PubMed:1854723, PubMed:20847263). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:15996096, PubMed:1854723, PubMed:20847263). {ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723, ECO:0000269|PubMed:20847263}.; FUNCTION: [Isoform M2]: Isoform specifically expressed during embryogenesis that has low pyruvate kinase activity by itself and requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for pyruvate kinase activity (PubMed:18337823, PubMed:20847263). In addition to its pyruvate kinase activity in the cytoplasm, also acts as a regulator of transcription in the nucleus by acting as a protein kinase (PubMed:18191611, PubMed:21620138, PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661). Translocates into the nucleus in response to various signals, such as EGF receptor activation, and homodimerizes, leading to its conversion into a protein threonine- and tyrosine-protein kinase (PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661, PubMed:26787900). Catalyzes phosphorylation of STAT3 at 'Tyr-705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate transcription (PubMed:22306293, PubMed:22901803, PubMed:24120661). Its ability to activate transcription plays a role in cancer cells by promoting cell proliferation and promote tumorigenesis (PubMed:18337823, PubMed:22901803, PubMed:26787900). Promotes the expression of the immune checkpoint protein CD274 in BMAL1-deficient macrophages (By similarity). May also act as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs (By similarity). Plays a role in caspase independent cell death of tumor cells (PubMed:17308100). {ECO:0000250|UniProtKB:P52480, ECO:0000269|PubMed:17308100, ECO:0000269|PubMed:18191611, ECO:0000269|PubMed:18337823, ECO:0000269|PubMed:20847263, ECO:0000269|PubMed:21620138, ECO:0000269|PubMed:22056988, ECO:0000269|PubMed:22306293, ECO:0000269|PubMed:22901803, ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900}.; FUNCTION: [Isoform M1]: Pyruvate kinase isoform expressed in adult tissues, which replaces isoform M2 after birth (PubMed:18337823). In contrast to isoform M2, has high pyruvate kinase activity by itself and does not require allosteric activation by D-fructose 1,6-bisphosphate (FBP) for activity (PubMed:20847263). {ECO:0000269|PubMed:18337823, ECO:0000269|PubMed:20847263}. |
P15259 | PGAM2 | T96 | ochoa | Phosphoglycerate mutase 2 (EC 5.4.2.11) (EC 5.4.2.4) (BPG-dependent PGAM 2) (Muscle-specific phosphoglycerate mutase) (Phosphoglycerate mutase isozyme M) (PGAM-M) | Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity. |
P16615 | ATP2A2 | T443 | ochoa | Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2+)-ATPase 2) (EC 7.2.2.10) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (PubMed:12542527, PubMed:16402920). Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation (PubMed:28890335). Also modulates ER contacts with lipid droplets, mitochondria and endosomes (PubMed:28890335). In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis (By similarity). {ECO:0000250|UniProtKB:O55143, ECO:0000269|PubMed:12542527, ECO:0000269|PubMed:16402920, ECO:0000269|PubMed:28890335}.; FUNCTION: [Isoform 2]: Involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca(2+) signaling cascades that promote osteoclast differentiation and activation. {ECO:0000250|UniProtKB:O55143}. |
P16615 | ATP2A2 | T532 | ochoa | Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2+)-ATPase 2) (EC 7.2.2.10) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (PubMed:12542527, PubMed:16402920). Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation (PubMed:28890335). Also modulates ER contacts with lipid droplets, mitochondria and endosomes (PubMed:28890335). In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis (By similarity). {ECO:0000250|UniProtKB:O55143, ECO:0000269|PubMed:12542527, ECO:0000269|PubMed:16402920, ECO:0000269|PubMed:28890335}.; FUNCTION: [Isoform 2]: Involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca(2+) signaling cascades that promote osteoclast differentiation and activation. {ECO:0000250|UniProtKB:O55143}. |
P18206 | VCL | T719 | ochoa | Vinculin (Metavinculin) (MV) | Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. {ECO:0000269|PubMed:20484056}. |
P18669 | PGAM1 | T96 | ochoa | Phosphoglycerate mutase 1 (EC 5.4.2.11) (EC 5.4.2.4) (BPG-dependent PGAM 1) (Phosphoglycerate mutase isozyme B) (PGAM-B) | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglyceratea crucial step in glycolysis, by using 2,3-bisphosphoglycerate (PubMed:23653202). Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate (PubMed:23653202). {ECO:0000269|PubMed:23653202}. |
P18754 | RCC1 | T103 | ochoa | Regulator of chromosome condensation (Cell cycle regulatory protein) (Chromosome condensation protein 1) | Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP, and thereby plays an important role in RAN-mediated functions in nuclear import and mitosis (PubMed:11336674, PubMed:17435751, PubMed:1944575, PubMed:20668449, PubMed:22215983, PubMed:29042532). Contributes to the generation of high levels of chromosome-associated, GTP-bound RAN, which is important for mitotic spindle assembly and normal progress through mitosis (PubMed:12194828, PubMed:17435751, PubMed:22215983). Via its role in maintaining high levels of GTP-bound RAN in the nucleus, contributes to the release of cargo proteins from importins after nuclear import (PubMed:22215983). Involved in the regulation of onset of chromosome condensation in the S phase (PubMed:3678831). Binds both to the nucleosomes and double-stranded DNA (PubMed:17435751, PubMed:18762580). {ECO:0000269|PubMed:11336674, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17435751, ECO:0000269|PubMed:18762580, ECO:0000269|PubMed:1944575, ECO:0000269|PubMed:20668449, ECO:0000269|PubMed:22215983, ECO:0000269|PubMed:29042532, ECO:0000269|PubMed:3678831}. |
P18848 | ATF4 | T115 | psp | Cyclic AMP-dependent transcription factor ATF-4 (cAMP-dependent transcription factor ATF-4) (Activating transcription factor 4) (Cyclic AMP-responsive element-binding protein 2) (CREB-2) (cAMP-responsive element-binding protein 2) (Tax-responsive enhancer element-binding protein 67) (TaxREB67) | Transcription factor that binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3') and displays two biological functions, as regulator of metabolic and redox processes under normal cellular conditions, and as master transcription factor during integrated stress response (ISR) (PubMed:16682973, PubMed:17684156, PubMed:31023583, PubMed:31444471, PubMed:32132707). Binds to asymmetric CRE's as a heterodimer and to palindromic CRE's as a homodimer (By similarity). Core effector of the ISR, which is required for adaptation to various stress such as endoplasmic reticulum (ER) stress, amino acid starvation, mitochondrial stress or oxidative stress (PubMed:31023583, PubMed:32132707). During ISR, ATF4 translation is induced via an alternative ribosome translation re-initiation mechanism in response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced ATF4 acts as a master transcription factor of stress-responsive genes in order to promote cell recovery (PubMed:31023583, PubMed:32132706, PubMed:32132707). Promotes the transcription of genes linked to amino acid sufficiency and resistance to oxidative stress to protect cells against metabolic consequences of ER oxidation (By similarity). Activates the transcription of NLRP1, possibly in concert with other factors in response to ER stress (PubMed:26086088). Activates the transcription of asparagine synthetase (ASNS) in response to amino acid deprivation or ER stress (PubMed:11960987). However, when associated with DDIT3/CHOP, the transcriptional activation of the ASNS gene is inhibited in response to amino acid deprivation (PubMed:18940792). Together with DDIT3/CHOP, mediates programmed cell death by promoting the expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the terminal unfolded protein response (terminal UPR), a cellular response that elicits programmed cell death when ER stress is prolonged and unresolved (By similarity). Activates the expression of COX7A2L/SCAF1 downstream of the EIF2AK3/PERK-mediated unfolded protein response, thereby promoting formation of respiratory chain supercomplexes and increasing mitochondrial oxidative phosphorylation (PubMed:31023583). Together with DDIT3/CHOP, activates the transcription of the IRS-regulator TRIB3 and promotes ER stress-induced neuronal cell death by regulating the expression of BBC3/PUMA in response to ER stress (PubMed:15775988). May cooperate with the UPR transcriptional regulator QRICH1 to regulate ER protein homeostasis which is critical for cell viability in response to ER stress (PubMed:33384352). In the absence of stress, ATF4 translation is at low levels and it is required for normal metabolic processes such as embryonic lens formation, fetal liver hematopoiesis, bone development and synaptic plasticity (By similarity). Acts as a regulator of osteoblast differentiation in response to phosphorylation by RPS6KA3/RSK2: phosphorylation in osteoblasts enhances transactivation activity and promotes expression of osteoblast-specific genes and post-transcriptionally regulates the synthesis of Type I collagen, the main constituent of the bone matrix (PubMed:15109498). Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production (By similarity). Activates transcription of SIRT4 (By similarity). Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4 (By similarity). Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes (By similarity). Mainly acts as a transcriptional activator in cellular stress adaptation, but it can also act as a transcriptional repressor: acts as a regulator of synaptic plasticity by repressing transcription, thereby inhibiting induction and maintenance of long-term memory (By similarity). Regulates synaptic functions via interaction with DISC1 in neurons, which inhibits ATF4 transcription factor activity by disrupting ATF4 dimerization and DNA-binding (PubMed:31444471). {ECO:0000250|UniProtKB:Q06507, ECO:0000269|PubMed:11960987, ECO:0000269|PubMed:15109498, ECO:0000269|PubMed:15775988, ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:17684156, ECO:0000269|PubMed:18940792, ECO:0000269|PubMed:26086088, ECO:0000269|PubMed:31023583, ECO:0000269|PubMed:31444471, ECO:0000269|PubMed:32132706, ECO:0000269|PubMed:32132707, ECO:0000269|PubMed:33384352}.; FUNCTION: (Microbial infection) Binds to a Tax-responsive enhancer element in the long terminal repeat of HTLV-I. {ECO:0000269|PubMed:1847461}. |
P19367 | HK1 | T336 | ochoa | Hexokinase-1 (EC 2.7.1.1) (Brain form hexokinase) (Hexokinase type I) (HK I) (Hexokinase-A) | Catalyzes the phosphorylation of various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate, respectively) (PubMed:1637300, PubMed:25316723, PubMed:27374331). Does not phosphorylate N-acetyl-D-glucosamine (PubMed:27374331). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (By similarity). Involved in innate immunity and inflammation by acting as a pattern recognition receptor for bacterial peptidoglycan (PubMed:27374331). When released in the cytosol, N-acetyl-D-glucosamine component of bacterial peptidoglycan inhibits the hexokinase activity of HK1 and causes its dissociation from mitochondrial outer membrane, thereby activating the NLRP3 inflammasome (PubMed:27374331). {ECO:0000250|UniProtKB:P05708, ECO:0000269|PubMed:1637300, ECO:0000269|PubMed:25316723, ECO:0000269|PubMed:27374331}. |
P21796 | VDAC1 | T98 | ochoa | Non-selective voltage-gated ion channel VDAC1 (Outer mitochondrial membrane protein porin 1) (Plasmalemmal porin) (Porin 31HL) (Porin 31HM) (Voltage-dependent anion-selective channel protein 1) (VDAC-1) (hVDAC1) | Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:30061676, PubMed:8420959). The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:8420959). It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (PubMed:10661876, PubMed:18755977, PubMed:8420959). The open state has a weak anion selectivity whereas the closed state is cation-selective (PubMed:18755977, PubMed:8420959). Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:18755977, PubMed:31015432). In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:32047033). May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis (PubMed:15033708, PubMed:25296756). May mediate ATP export from cells (PubMed:30061676). Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity). Mediates cytochrome c efflux (PubMed:20230784). {ECO:0000250|UniProtKB:Q60932, ECO:0000269|PubMed:10661876, ECO:0000269|PubMed:11845315, ECO:0000269|PubMed:15033708, ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:20230784, ECO:0000269|PubMed:25296756, ECO:0000269|PubMed:30061676, ECO:0000269|PubMed:31015432, ECO:0000269|PubMed:32047033, ECO:0000269|PubMed:8420959}.; FUNCTION: Catalyzes the scrambling of phospholipids across the outer mitochondrial membrane; the mechanism is unrelated to channel activity and is capable of translocating both anionic and zwitterionic phospholipids. {ECO:0000269|PubMed:38065946}. |
P21964 | COMT | T81 | ochoa | Catechol O-methyltransferase (EC 2.1.1.6) | Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. {ECO:0000269|PubMed:11559542, ECO:0000269|PubMed:21846718}. |
P25100 | ADRA1D | T328 | psp | Alpha-1D adrenergic receptor (Alpha-1A adrenergic receptor) (Alpha-1D adrenoreceptor) (Alpha-1D adrenoceptor) (Alpha-adrenergic receptor 1a) | This alpha-adrenergic receptor mediates its effect through the influx of extracellular calcium. |
P25205 | MCM3 | T731 | ochoa | DNA replication licensing factor MCM3 (EC 3.6.4.12) (DNA polymerase alpha holoenzyme-associated protein P1) (P1-MCM3) (RLF subunit beta) (p102) | Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:32453425). Required for the entry in S phase and for cell division (Probable). {ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232, ECO:0000305|PubMed:35585232}. |
P26045 | PTPN3 | T326 | ochoa | Tyrosine-protein phosphatase non-receptor type 3 (EC 3.1.3.48) (Protein-tyrosine phosphatase H1) (PTP-H1) | May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity. |
P30405 | PPIF | T158 | ochoa | Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIase F) (EC 5.2.1.8) (Cyclophilin D) (CyP-D) (CypD) (Cyclophilin F) (Mitochondrial cyclophilin) (CyP-M) (Rotamase F) | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:26387735). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated (PubMed:26387735). In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:22726440). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (PubMed:19228691). {ECO:0000250|UniProtKB:Q99KR7, ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:26387735}. |
P32298 | GRK4 | T256 | psp | G protein-coupled receptor kinase 4 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK4) (ITI1) | Specifically phosphorylates the activated forms of G protein-coupled receptors. GRK4-alpha can phosphorylate rhodopsin and its activity is inhibited by calmodulin; the other three isoforms do not phosphorylate rhodopsin and do not interact with calmodulin. GRK4-alpha and GRK4-gamma phosphorylate DRD3. Phosphorylates ADRB2. {ECO:0000269|PubMed:19520868, ECO:0000269|PubMed:8626439}. |
P33981 | TTK | T675 | 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}. |
P35659 | DEK | T67 | psp | Protein DEK | Involved in chromatin organization. {ECO:0000269|PubMed:17524367}. |
P40121 | CAPG | T130 | ochoa | Macrophage-capping protein (Actin regulatory protein CAP-G) | Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA. |
P40259 | CD79B | T206 | ochoa | B-cell antigen receptor complex-associated protein beta chain (B-cell-specific glycoprotein B29) (Ig-beta) (Immunoglobulin-associated B29 protein) (CD antigen CD79b) | Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation. {ECO:0000269|PubMed:12097390, ECO:0000269|PubMed:8617796, ECO:0000269|PubMed:9057631}. |
P45880 | VDAC2 | T109 | ochoa | Non-selective voltage-gated ion channel VDAC2 (VDAC-2) (hVDAC2) (Outer mitochondrial membrane protein porin 2) | Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:8420959). The channel adopts an open conformation at zero mV and a closed conformation at both positive and negative potentials (PubMed:8420959). There are two populations of channels; the main that functions in a lower open-state conductance with lower ion selectivity, that switch, in a voltage-dependent manner, from the open to a low-conducting 'closed' state and the other that has a normal ion selectivity in the typical high conductance, 'open' state (PubMed:8420959). Binds various lipids, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:31015432). Binding of ceramide promotes the mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway (PubMed:31015432). {ECO:0000269|PubMed:31015432, ECO:0000269|PubMed:8420959}.; FUNCTION: Catalyzes the scrambling of phospholipids across the outer mitochondrial membrane; the mechanism is unrelated to channel activity and is capable of translocating both anionic and zwitterionic phospholipids. {ECO:0000269|PubMed:38065946}. |
P48059 | LIMS1 | T280 | ochoa | LIM and senescent cell antigen-like-containing domain protein 1 (Particularly interesting new Cys-His protein 1) (PINCH-1) (Renal carcinoma antigen NY-REN-48) | Within the IPP (ILK-PINCH-PARVIN) complex, binds to F-actin, promoting F-actin bundling, a process required to generate force for actin cytoskeleton reorganization and subsequent dynamic cell adhesion events such as cell spreading and migration. {ECO:0000269|PubMed:30367047}. |
P49792 | RANBP2 | T2005 | ochoa | E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270) | E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22194619, ECO:0000269|PubMed:22902403, ECO:0000269|PubMed:23353830, ECO:0000269|PubMed:7775481, ECO:0000303|PubMed:10078529}. |
P49915 | GMPS | T308 | ochoa | GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (Glutamine amidotransferase) | Catalyzes the conversion of xanthine monophosphate (XMP) to GMP in the presence of glutamine and ATP through an adenyl-XMP intermediate. {ECO:0000269|PubMed:8089153}. |
P50454 | SERPINH1 | T327 | ochoa | Serpin H1 (47 kDa heat shock protein) (Arsenic-transactivated protein 3) (AsTP3) (Cell proliferation-inducing gene 14 protein) (Collagen-binding protein) (Colligin) (Rheumatoid arthritis-related antigen RA-A47) | Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. |
P50990 | CCT8 | T517 | psp | T-complex protein 1 subunit theta (TCP-1-theta) (EC 3.6.1.-) (CCT-theta) (Chaperonin containing T-complex polypeptide 1 subunit 8) (Renal carcinoma antigen NY-REN-15) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
P51587 | BRCA2 | T772 | ochoa | Breast cancer type 2 susceptibility protein (Fanconi anemia group D1 protein) | Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180). {ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15199141, ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:18317453, ECO:0000269|PubMed:20729832, ECO:0000269|PubMed:20729858, ECO:0000269|PubMed:20729859, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:21719596, ECO:0000269|PubMed:24485656, ECO:0000269|PubMed:24896180}. |
P51587 | BRCA2 | T1526 | ochoa | Breast cancer type 2 susceptibility protein (Fanconi anemia group D1 protein) | Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180). {ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15199141, ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:18317453, ECO:0000269|PubMed:20729832, ECO:0000269|PubMed:20729858, ECO:0000269|PubMed:20729859, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:21719596, ECO:0000269|PubMed:24485656, ECO:0000269|PubMed:24896180}. |
P52948 | NUP98 | T660 | ochoa | Nuclear pore complex protein Nup98-Nup96 (EC 3.4.21.-) [Cleaved into: Nuclear pore complex protein Nup98 (98 kDa nucleoporin) (Nucleoporin Nup98) (Nup98); Nuclear pore complex protein Nup96 (96 kDa nucleoporin) (Nucleoporin Nup96) (Nup96)] | Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC (PubMed:33097660). May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed:28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed:28221134). {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:33097660}.; FUNCTION: (Microbial infection) Interacts with HIV-1 capsid protein P24 and nucleocapsid protein P7 and may thereby promote the integration of the virus in the host nucleus (in vitro) (PubMed:23523133). Binding affinity to HIV-1 CA-NC complexes bearing the capsid change Asn-74-Asp is reduced (in vitro) (PubMed:23523133). {ECO:0000269|PubMed:23523133}. |
P54132 | BLM | T99 | 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}. |
P54278 | PMS2 | T597 | ochoa | Mismatch repair endonuclease PMS2 (EC 3.1.-.-) (DNA mismatch repair protein PMS2) (PMS1 protein homolog 2) | Component of the post-replicative DNA mismatch repair system (MMR) (PubMed:30653781, PubMed:35189042). Heterodimerizes with MLH1 to form MutL alpha. DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Possesses an ATPase activity, but in the absence of gross structural changes, ATP hydrolysis may not be necessary for proficient mismatch repair (PubMed:35189042). {ECO:0000269|PubMed:16873062, ECO:0000269|PubMed:18206974, ECO:0000269|PubMed:23709753, ECO:0000269|PubMed:30653781, ECO:0000269|PubMed:35189042}. |
P54652 | HSPA2 | T112 | ochoa | Heat shock-related 70 kDa protein 2 (Heat shock 70 kDa protein 2) (Heat shock protein family A member 2) | 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 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 (PubMed:26865365). Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (By similarity). {ECO:0000250|UniProtKB:P17156, ECO:0000303|PubMed:26865365}. |
P54652 | HSPA2 | T229 | ochoa | Heat shock-related 70 kDa protein 2 (Heat shock 70 kDa protein 2) (Heat shock protein family A member 2) | 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 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 (PubMed:26865365). Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (By similarity). {ECO:0000250|UniProtKB:P17156, ECO:0000303|PubMed:26865365}. |
P61981 | YWHAG | T145 | ochoa | 14-3-3 protein gamma (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein gamma, N-terminally processed] | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:15696159, PubMed:16511572, PubMed:36732624). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:15696159, PubMed:16511572, PubMed:36732624). Binding generally results in the modulation of the activity of the binding partner (PubMed:16511572). Promotes inactivation of WDR24 component of the GATOR2 complex by binding to phosphorylated WDR24 (PubMed:36732624). Participates in the positive regulation of NMDA glutamate receptor activity by promoting the L-glutamate secretion through interaction with BEST1 (PubMed:29121962). Reduces keratinocyte intercellular adhesion, via interacting with PKP1 and sequestering it in the cytoplasm, thereby reducing its incorporation into desmosomes (PubMed:29678907). Plays a role in mitochondrial protein catabolic process (also named MALM) that promotes the degradation of damaged proteins inside mitochondria (PubMed:22532927). {ECO:0000269|PubMed:15696159, ECO:0000269|PubMed:16511572, ECO:0000269|PubMed:22532927, ECO:0000269|PubMed:29121962, ECO:0000269|PubMed:29678907, ECO:0000269|PubMed:36732624}. |
P62937 | PPIA | T116 | ochoa | Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin A) (Cyclosporin A-binding protein) (Rotamase A) [Cleaved into: Peptidyl-prolyl cis-trans isomerase A, N-terminally processed] | Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357, PubMed:21245143, PubMed:21593166, PubMed:25678563). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143). Activates endothelial cells (ECs) in a pro-inflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (PubMed:15130913). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (PubMed:23180369). Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (PubMed:26095851). Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (PubMed:25678563). Plays an important role in platelet activation and aggregation (By similarity). Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity). Binds heparan sulfate glycosaminoglycans (PubMed:11943775). Inhibits replication of influenza A virus (IAV) (PubMed:19207730). Inhibits ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by impairing the interaction of ITCH/AIP4 with M1, followed by the suppression of the nuclear export of M1, and finally reduction of the replication of IAV (PubMed:22347431, PubMed:30328013). {ECO:0000250|UniProtKB:P17742, ECO:0000269|PubMed:11943775, ECO:0000269|PubMed:15130913, ECO:0000269|PubMed:19207730, ECO:0000269|PubMed:2001362, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:21245143, ECO:0000269|PubMed:21593166, ECO:0000269|PubMed:22347431, ECO:0000269|PubMed:23180369, ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:26095851, ECO:0000269|PubMed:30328013, ECO:0000269|PubMed:31063815}.; FUNCTION: (Microbial infection) May act as a mediator between human SARS coronavirus nucleoprotein and BSG/CD147 in the process of invasion of host cells by the virus (PubMed:15688292). {ECO:0000269|PubMed:15688292}.; FUNCTION: (Microbial infection) Stimulates RNA-binding ability of HCV NS5A in a peptidyl-prolyl cis-trans isomerase activity-dependent manner. {ECO:0000269|PubMed:21593166}. |
P78347 | GTF2I | T97 | ochoa | General transcription factor II-I (GTFII-I) (TFII-I) (Bruton tyrosine kinase-associated protein 135) (BAP-135) (BTK-associated protein 135) (SRF-Phox1-interacting protein) (SPIN) (Williams-Beuren syndrome chromosomal region 6 protein) | Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. {ECO:0000269|PubMed:10373551, ECO:0000269|PubMed:11373296, ECO:0000269|PubMed:16738337}. |
P78347 | GTF2I | T556 | ochoa | General transcription factor II-I (GTFII-I) (TFII-I) (Bruton tyrosine kinase-associated protein 135) (BAP-135) (BTK-associated protein 135) (SRF-Phox1-interacting protein) (SPIN) (Williams-Beuren syndrome chromosomal region 6 protein) | Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. {ECO:0000269|PubMed:10373551, ECO:0000269|PubMed:11373296, ECO:0000269|PubMed:16738337}. |
Q00872 | MYBPC1 | T802 | ochoa | Myosin-binding protein C, slow-type (Slow MyBP-C) (C-protein, skeletal muscle slow isoform) | Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. Slow skeletal protein that binds to both myosin and actin (PubMed:31025394, PubMed:31264822). In vitro, binds to native thin filaments and modifies the activity of actin-activated myosin ATPase. May modulate muscle contraction or may play a more structural role. {ECO:0000269|PubMed:31025394, ECO:0000269|PubMed:31264822}. |
Q02952 | AKAP12 | T1717 | ochoa | A-kinase anchor protein 12 (AKAP-12) (A-kinase anchor protein 250 kDa) (AKAP 250) (Gravin) (Myasthenia gravis autoantigen) | Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC). |
Q03001 | DST | T5357 | ochoa | Dystonin (230 kDa bullous pemphigoid antigen) (230/240 kDa bullous pemphigoid antigen) (Bullous pemphigoid antigen 1) (BPA) (Bullous pemphigoid antigen) (Dystonia musculorum protein) (Hemidesmosomal plaque protein) | Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1 (By similarity). {ECO:0000250|UniProtKB:Q91ZU6}.; FUNCTION: [Isoform 3]: Plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity.; FUNCTION: [Isoform 6]: Required for bundling actin filaments around the nucleus. {ECO:0000250, ECO:0000269|PubMed:10428034, ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692}.; FUNCTION: [Isoform 7]: Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. |
Q03164 | KMT2A | T204 | ochoa | Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.364) (ALL-1) (CXXC-type zinc finger protein 7) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)] | Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250|UniProtKB:P55200, ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:12453419, ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:19187761, ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:20010842, ECO:0000269|PubMed:21220120, ECO:0000269|PubMed:24235145, ECO:0000269|PubMed:26886794, ECO:0000305|PubMed:20677832}. |
Q04637 | EIF4G1 | T1054 | ochoa | Eukaryotic translation initiation factor 4 gamma 1 (eIF-4-gamma 1) (eIF-4G 1) (eIF-4G1) (p220) | Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:29987188). Exists in two complexes, either with EIF1 or with EIF4E (mutually exclusive) (PubMed:29987188). Together with EIF1, is required for leaky scanning, in particular for avoiding cap-proximal start codon (PubMed:29987188). Together with EIF4E, antagonizes the scanning promoted by EIF1-EIF4G1 and locates the start codon (through a TISU element) without scanning (PubMed:29987188). As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). {ECO:0000269|PubMed:29062139, ECO:0000269|PubMed:29987188}. |
Q07157 | TJP1 | T770 | psp | Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1) | TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250|UniProtKB:O97758, ECO:0000250|UniProtKB:P39447, ECO:0000269|PubMed:20930113, ECO:0000269|PubMed:21240187}. |
Q07343 | PDE4B | T323 | ochoa | 3',5'-cyclic-AMP phosphodiesterase 4B (EC 3.1.4.53) (DPDE4) (PDE32) (cAMP-specific phosphodiesterase 4B) | Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (PubMed:15260978). May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents. {ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978}. |
Q09666 | AHNAK | T161 | ochoa | Neuroblast differentiation-associated protein AHNAK (Desmoyokin) | May be required for neuronal cell differentiation. |
Q09666 | AHNAK | T324 | ochoa | Neuroblast differentiation-associated protein AHNAK (Desmoyokin) | May be required for neuronal cell differentiation. |
Q0ZGT2 | NEXN | T172 | ochoa | Nexilin (F-actin-binding protein) (Nelin) | Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity. {ECO:0000269|PubMed:12053183, ECO:0000269|PubMed:15823560, ECO:0000269|PubMed:19881492}. |
Q12802 | AKAP13 | T2467 | ochoa|psp | A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc) (Breast cancer nuclear receptor-binding auxiliary protein) (Guanine nucleotide exchange factor Lbc) (Human thyroid-anchoring protein 31) (Lymphoid blast crisis oncogene) (LBC oncogene) (Non-oncogenic Rho GTPase-specific GTP exchange factor) (Protein kinase A-anchoring protein 13) (PRKA13) (p47) | Scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. Activates RHOA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor (PubMed:11546812, PubMed:15229649, PubMed:23090968, PubMed:24993829, PubMed:25186459). May also activate other Rho family members (PubMed:11546812). Part of a kinase signaling complex that links ADRA1A and ADRA1B adrenergic receptor signaling to the activation of downstream p38 MAP kinases, such as MAPK11 and MAPK14 (PubMed:17537920, PubMed:21224381, PubMed:23716597). Part of a signaling complex that links ADRA1B signaling to the activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B transcriptional activity (PubMed:23090968). Part of a RHOA-dependent signaling cascade that mediates responses to lysophosphatidic acid (LPA), a signaling molecule that activates G-protein coupled receptors and potentiates transcriptional activation of the glucocorticoid receptor NR3C1 (PubMed:16469733). Part of a signaling cascade that stimulates MEF2C-dependent gene expression in response to lysophosphatidic acid (LPA) (By similarity). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2 (PubMed:11579095, PubMed:9627117). Part of a signaling cascade that links cAMP and EGFR signaling to BRAF signaling and to PKA-mediated phosphorylation of KSR1, leading to the activation of downstream MAP kinases, such as MAPK1 or MAPK3 (PubMed:21102438). Functions as a scaffold protein that anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading to increased phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy (By similarity). Has no guanine nucleotide exchange activity on CDC42, Ras or Rac (PubMed:11546812). Required for normal embryonic heart development, and in particular for normal sarcomere formation in the developing cardiomyocytes (By similarity). Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol (PubMed:17537920, PubMed:23090968). Required for normal adaptive cardiac hypertrophy in response to pressure overload (PubMed:23716597). Plays a role in osteogenesis (By similarity). {ECO:0000250|UniProtKB:E9Q394, ECO:0000269|PubMed:11546812, ECO:0000269|PubMed:11579095, ECO:0000269|PubMed:17537920, ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:23716597, ECO:0000269|PubMed:24993829, ECO:0000269|PubMed:25186459, ECO:0000269|PubMed:9627117, ECO:0000269|PubMed:9891067}. |
Q12912 | IRAG2 | T440 | ochoa | Inositol 1,4,5-triphosphate receptor associated 2 (Lymphoid-restricted membrane protein) (Protein Jaw1) [Cleaved into: Processed inositol 1,4,5-triphosphate receptor associated 2] | Plays a role in the delivery of peptides to major histocompatibility complex (MHC) class I molecules; this occurs in a transporter associated with antigen processing (TAP)-independent manner. May play a role in taste signal transduction via ITPR3. May play a role during fertilization in pronucleus congression and fusion. Plays a role in maintaining nuclear shape, maybe as a component of the LINC complex and through interaction with microtubules. Plays a role in the regulation of cellular excitability by regulating the hyperpolarization-activated cyclic nucleotide-gated HCN4 channel activity (By similarity). {ECO:0000250|UniProtKB:Q60664}. |
Q12913 | PTPRJ | T1314 | ochoa | Receptor-type tyrosine-protein phosphatase eta (Protein-tyrosine phosphatase eta) (R-PTP-eta) (EC 3.1.3.48) (Density-enhanced phosphatase 1) (DEP-1) (HPTP eta) (Protein-tyrosine phosphatase receptor type J) (R-PTP-J) (CD antigen CD148) | Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2 (PubMed:10821867, PubMed:12062403, PubMed:12370829, PubMed:12475979, PubMed:18348712, PubMed:19494114, PubMed:19922411, PubMed:21262971). Plays a role in cell adhesion, migration, proliferation and differentiation (PubMed:12370829, PubMed:14709717, PubMed:16682945, PubMed:19836242). Has a role in megakaryocytes and platelet formation (PubMed:30591527). Involved in vascular development (By similarity). Regulator of macrophage adhesion and spreading (By similarity). Positively affects cell-matrix adhesion (By similarity). Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation (PubMed:16682945). Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR (PubMed:21091576). Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation (PubMed:18936167). Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation (PubMed:19836242). Enhances the barrier function of epithelial junctions during reassembly (PubMed:19332538). Negatively regulates T-cell receptor (TCR) signaling (PubMed:11259588, PubMed:9531590, PubMed:9780142). Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling (PubMed:11259588, PubMed:12913111). {ECO:0000250|UniProtKB:Q64455, ECO:0000269|PubMed:10821867, ECO:0000269|PubMed:11259588, ECO:0000269|PubMed:12062403, ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:12913111, ECO:0000269|PubMed:14709717, ECO:0000269|PubMed:16682945, ECO:0000269|PubMed:18348712, ECO:0000269|PubMed:18936167, ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:19494114, ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:19922411, ECO:0000269|PubMed:21091576, ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:30591527, ECO:0000269|PubMed:9531590, ECO:0000269|PubMed:9780142}.; FUNCTION: [Isoform 2]: Activates angiogenesis and cell migration (PubMed:28052032). Downregulates the expression of the endothelial adhesion molecules ICAM1 and VCAM1 (PubMed:28052032). {ECO:0000269|PubMed:28052032}. |
Q13535 | ATR | T1578 | psp | Serine/threonine-protein kinase ATR (EC 2.7.11.1) (Ataxia telangiectasia and Rad3-related protein) (FRAP-related protein 1) | Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor (PubMed:10597277, PubMed:10608806, PubMed:10859164, PubMed:11721054, PubMed:12791985, PubMed:12814551, PubMed:14657349, PubMed:14729973, PubMed:14742437, PubMed:15210935, PubMed:15496423, PubMed:16260606, PubMed:21144835, PubMed:21777809, PubMed:23273981, PubMed:25083873, PubMed:27723717, PubMed:27723720, PubMed:30139873, PubMed:33848395, PubMed:37788673, PubMed:37832547, PubMed:9427750, PubMed:9636169). Recognizes the substrate consensus sequence [ST]-Q (PubMed:10597277, PubMed:10608806, PubMed:10859164, PubMed:11721054, PubMed:12791985, PubMed:12814551, PubMed:14657349, PubMed:14729973, PubMed:14742437, PubMed:15210935, PubMed:15496423, PubMed:16260606, PubMed:21144835, PubMed:23273981, PubMed:27723717, PubMed:27723720, PubMed:33848395, PubMed:9427750, PubMed:9636169). Phosphorylates BRCA1, CHEK1, MCM2, RAD17, RBBP8, RPA2, SMC1 and p53/TP53, which collectively inhibit DNA replication and mitosis and promote DNA repair, recombination and apoptosis (PubMed:11114888, PubMed:11418864, PubMed:11865061, PubMed:21777809, PubMed:23273981, PubMed:25083873, PubMed:9925639). Phosphorylates 'Ser-139' of histone variant H2AX at sites of DNA damage, thereby regulating DNA damage response mechanism (PubMed:11673449). Required for FANCD2 ubiquitination (PubMed:15314022). Critical for maintenance of fragile site stability and efficient regulation of centrosome duplication (PubMed:12526805). Acts as a regulator of the S-G2 transition by restricting the activity of CDK1 during S-phase to prevent premature entry into G2 (PubMed:30139873). Acts as a regulator of the nuclear envelope integrity in response to DNA damage and stress (PubMed:25083873, PubMed:37788673, PubMed:37832547). Acts as a mechanical stress sensor at the nuclear envelope: relocalizes to the nuclear envelope in response to mechanical stress and mediates a checkpoint via phosphorylation of CHEK1 (PubMed:25083873). Also promotes nuclear envelope rupture in response to DNA damage by mediating phosphorylation of LMNA at 'Ser-282', leading to lamin disassembly (PubMed:37832547). Involved in the inflammatory response to genome instability and double-stranded DNA breaks: acts by localizing to micronuclei arising from genome instability and catalyzing phosphorylation of LMNA at 'Ser-395', priming LMNA for subsequent phosphorylation by CDK1 and micronuclei envelope rupture (PubMed:37788673). The rupture of micronuclear envelope triggers the cGAS-STING pathway thereby activating the type I interferon response and innate immunity (PubMed:37788673). Positively regulates the restart of stalled replication forks following activation by the KHDC3L-OOEP scaffold complex (By similarity). {ECO:0000250|UniProtKB:Q9JKK8, ECO:0000269|PubMed:10597277, ECO:0000269|PubMed:10608806, ECO:0000269|PubMed:10859164, ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:11721054, ECO:0000269|PubMed:11865061, ECO:0000269|PubMed:12526805, ECO:0000269|PubMed:12791985, ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:14657349, ECO:0000269|PubMed:14729973, ECO:0000269|PubMed:14742437, ECO:0000269|PubMed:15210935, ECO:0000269|PubMed:15314022, ECO:0000269|PubMed:15496423, ECO:0000269|PubMed:16260606, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:21777809, ECO:0000269|PubMed:23273981, ECO:0000269|PubMed:25083873, ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720, ECO:0000269|PubMed:30139873, ECO:0000269|PubMed:33848395, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547, ECO:0000269|PubMed:9427750, ECO:0000269|PubMed:9636169, ECO:0000269|PubMed:9925639}. |
Q13546 | RIPK1 | T608 | ochoa | Receptor-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (Cell death protein RIP) (Receptor-interacting protein 1) (RIP-1) | Serine-threonine kinase which is a key regulator of TNF-mediated apoptosis, necroptosis and inflammatory pathways (PubMed:17703191, PubMed:24144979, PubMed:31827280, PubMed:31827281, PubMed:32657447, PubMed:35831301). Exhibits kinase activity-dependent functions that regulate cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival (PubMed:11101870, PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Has kinase-independent scaffold functions: upon binding of TNF to TNFR1, RIPK1 is recruited to the TNF-R1 signaling complex (TNF-RSC also known as complex I) where it acts as a scaffold protein promoting cell survival, in part, by activating the canonical NF-kappa-B pathway (By similarity). Kinase activity is essential to regulate necroptosis and apoptosis, two parallel forms of cell death: upon activation of its protein kinase activity, regulates assembly of two death-inducing complexes, namely complex IIa (RIPK1-FADD-CASP8), which drives apoptosis, and the complex IIb (RIPK1-RIPK3-MLKL), which drives necroptosis (By similarity). RIPK1 is required to limit CASP8-dependent TNFR1-induced apoptosis (By similarity). In normal conditions, RIPK1 acts as an inhibitor of RIPK3-dependent necroptosis, a process mediated by RIPK3 component of complex IIb, which catalyzes phosphorylation of MLKL upon induction by ZBP1 (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Inhibits RIPK3-mediated necroptosis via FADD-mediated recruitment of CASP8, which cleaves RIPK1 and limits TNF-induced necroptosis (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Required to inhibit apoptosis and necroptosis during embryonic development: acts by preventing the interaction of TRADD with FADD thereby limiting aberrant activation of CASP8 (By similarity). In addition to apoptosis and necroptosis, also involved in inflammatory response by promoting transcriptional production of pro-inflammatory cytokines, such as interleukin-6 (IL6) (PubMed:31827280, PubMed:31827281). Phosphorylates RIPK3: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade (PubMed:15310755, PubMed:17389591). Required for ZBP1-induced NF-kappa-B activation in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:Q60855, ECO:0000269|PubMed:11101870, ECO:0000269|PubMed:15310755, ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:17703191, ECO:0000269|PubMed:19524512, ECO:0000269|PubMed:19524513, ECO:0000269|PubMed:24144979, ECO:0000269|PubMed:29440439, ECO:0000269|PubMed:30988283, ECO:0000269|PubMed:31827280, ECO:0000269|PubMed:31827281, ECO:0000269|PubMed:32657447, ECO:0000269|PubMed:35831301}. |
Q13561 | DCTN2 | T79 | ochoa | Dynactin subunit 2 (50 kDa dynein-associated polypeptide) (Dynactin complex 50 kDa subunit) (DCTN-50) (p50 dynamitin) | Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In the dynactin soulder domain, binds the ACTR1A filament and acts as a molecular ruler to determine the length (By similarity). Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development (By similarity). {ECO:0000250|UniProtKB:A0A5G2QD80, ECO:0000250|UniProtKB:Q99KJ8}. |
Q13769 | THOC5 | T321 | ochoa | THO complex subunit 5 (Functional spliceosome-associated protein 79) (fSAP79) (NF2/meningioma region protein pK1.3) (Placental protein 39.2) (PP39.2) (hTREX90) | Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Plays a key structural role in the oligomerization of the THO-DDX39B complex (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in transcription elongation and genome stability (PubMed:18974867). Involved in alternative polyadenylation site choice by recruiting CPSF6 to 5' region of target genes; probably mediates association of the TREX and CFIm complexes (PubMed:23685434). {ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:18974867, ECO:0000269|PubMed:23685434, ECO:0000269|PubMed:33191911}.; FUNCTION: Regulates the expression of myeloid transcription factors CEBPA, CEBPB and GAB2 by enhancing the levels of phosphatidylinositol 3,4,5-trisphosphate. May be involved in the differentiation of granulocytes and adipocytes. Essential for hematopoietic primitive cell survival and plays an integral role in monocytic development. {ECO:0000250|UniProtKB:Q8BKT7}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269|PubMed:18974867}. |
Q14004 | CDK13 | T500 | ochoa | Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller) | Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. {ECO:0000269|PubMed:16721827, ECO:0000269|PubMed:1731328, ECO:0000269|PubMed:18480452, ECO:0000269|PubMed:20952539}. |
Q14315 | FLNC | T2446 | ochoa | Filamin-C (FLN-C) (FLNc) (ABP-280-like protein) (ABP-L) (Actin-binding-like protein) (Filamin-2) (Gamma-filamin) | Muscle-specific filamin, which plays a central role in sarcomere assembly and organization (PubMed:34405687). Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events (By similarity). {ECO:0000250|UniProtKB:Q8VHX6, ECO:0000269|PubMed:34405687}. |
Q14690 | PDCD11 | T42 | ochoa | Protein RRP5 homolog (NF-kappa-B-binding protein) (NFBP) (Programmed cell death protein 11) | Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA. {ECO:0000269|PubMed:17654514}.; FUNCTION: Involved in the biogenesis of rRNA. {ECO:0000250}. |
Q14966 | ZNF638 | T790 | ochoa | Zinc finger protein 638 (Cutaneous T-cell lymphoma-associated antigen se33-1) (CTCL-associated antigen se33-1) (Nuclear protein 220) (Zinc finger matrin-like protein) | Transcription factor that binds to cytidine clusters in double-stranded DNA (PubMed:30487602, PubMed:8647861). Plays a key role in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Mediates transcriptional repression of unintegrated viral DNA by specifically binding to the cytidine clusters of retroviral DNA and mediating the recruitment of chromatin silencers, such as the HUSH complex, SETDB1 and the histone deacetylases HDAC1 and HDAC4 (PubMed:30487602). Acts as an early regulator of adipogenesis by acting as a transcription cofactor of CEBPs (CEBPA, CEBPD and/or CEBPG), controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (By similarity). May also regulate alternative splicing of target genes during adipogenesis (By similarity). {ECO:0000250|UniProtKB:Q61464, ECO:0000269|PubMed:30487602, ECO:0000269|PubMed:8647861}. |
Q15003 | NCAPH | T614 | ochoa | Condensin complex subunit 2 (Barren homolog protein 1) (Chromosome-associated protein H) (hCAP-H) (Non-SMC condensin I complex subunit H) (XCAP-H homolog) | Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (PubMed:11136719). Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size (PubMed:27737959). {ECO:0000269|PubMed:11136719, ECO:0000269|PubMed:27737959}. |
Q15063 | POSTN | T772 | ochoa | Periostin (PN) (Osteoblast-specific factor 2) (OSF-2) | Induces cell attachment and spreading and plays a role in cell adhesion (PubMed:12235007). Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity). {ECO:0000250|UniProtKB:Q62009, ECO:0000269|PubMed:12235007}. |
Q15286 | RAB35 | T49 | ochoa | Ras-related protein Rab-35 (EC 3.6.5.2) (GTP-binding protein RAY) (Ras-related protein Rab-1C) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:30905672). RAB35 is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane (PubMed:21951725). During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge (PubMed:16950109). May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes (By similarity). {ECO:0000250|UniProtKB:Q6PHN9, ECO:0000269|PubMed:16950109, ECO:0000269|PubMed:21951725, ECO:0000269|PubMed:30905672}. |
Q15438 | CYTH1 | T54 | ochoa | Cytohesin-1 (PH, SEC7 and coiled-coil domain-containing protein 1) (SEC7 homolog B2-1) | Promotes guanine-nucleotide exchange on ARF1, ARF5 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization, through regulation of ARF6 activity. {ECO:0000250|UniProtKB:Q9QX11, ECO:0000269|PubMed:10652308, ECO:0000269|PubMed:29420262, ECO:0000269|PubMed:9653114}. |
Q15847 | ADIRF | T53 | ochoa | Adipogenesis regulatory factor (Adipogenesis factor rich in obesity) (Adipose most abundant gene transcript 2 protein) (Adipose-specific protein 2) (apM-2) | Plays a role in fat cell development; promotes adipogenic differentiation and stimulates transcription initiation of master adipogenesis factors like PPARG and CEBPA at early stages of preadipocyte differentiation. Its overexpression confers resistance to the anticancer chemotherapeutic drug cisplatin. {ECO:0000269|PubMed:19444912, ECO:0000269|PubMed:23239344}. |
Q16531 | DDB1 | T657 | ochoa | DNA damage-binding protein 1 (DDB p127 subunit) (DNA damage-binding protein a) (DDBa) (Damage-specific DNA-binding protein 1) (HBV X-associated protein 1) (XAP-1) (UV-damaged DNA-binding factor) (UV-damaged DNA-binding protein 1) (UV-DDB 1) (XPE-binding factor) (XPE-BF) (Xeroderma pigmentosum group E-complementing protein) (XPCe) | Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:14739464, PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16407252, PubMed:16482215, PubMed:16940174, PubMed:17079684). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:25043012, PubMed:25108355, PubMed:28886238). The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:25043012, PubMed:25108355). DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (PubMed:16473935, PubMed:16678110, PubMed:17041588, PubMed:18593899). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16473935, PubMed:16678110, PubMed:17041588, PubMed:18593899). DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:15882621). DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication (PubMed:17041588). DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed:12732143, PubMed:32355176, PubMed:38316879). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). Maternal factor required for proper zygotic genome activation and genome reprogramming (By similarity). {ECO:0000250|UniProtKB:Q3U1J4, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15882621, ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16407242, ECO:0000269|PubMed:16407252, ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16482215, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16940174, ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:17079684, ECO:0000269|PubMed:18332868, ECO:0000269|PubMed:18381890, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19966799, ECO:0000269|PubMed:22118460, ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355, ECO:0000269|PubMed:26431207, ECO:0000269|PubMed:28886238, ECO:0000269|PubMed:32355176, ECO:0000269|PubMed:38316879}. |
Q32MZ4 | LRRFIP1 | T676 | ochoa | Leucine-rich repeat flightless-interacting protein 1 (LRR FLII-interacting protein 1) (GC-binding factor 2) (TAR RNA-interacting protein) | Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding. {ECO:0000269|PubMed:10364563, ECO:0000269|PubMed:14522076, ECO:0000269|PubMed:16199883, ECO:0000269|PubMed:19265123, ECO:0000269|PubMed:9705290}. |
Q32P44 | EML3 | T843 | ochoa | Echinoderm microtubule-associated protein-like 3 (EMAP-3) | Regulates mitotic spindle assembly, microtubule (MT)-kinetochore attachment and chromosome separation via recruitment of HAUS augmin-like complex and TUBG1 to the existing MTs and promoting MT-based MT nucleation (PubMed:30723163). Required for proper alignnment of chromosomes during metaphase (PubMed:18445686). {ECO:0000269|PubMed:18445686, ECO:0000269|PubMed:30723163}. |
Q53GQ0 | HSD17B12 | T59 | ochoa | Very-long-chain 3-oxoacyl-CoA reductase (EC 1.1.1.330) (17-beta-hydroxysteroid dehydrogenase 12) (17-beta-HSD 12) (3-ketoacyl-CoA reductase) (KAR) (Estradiol 17-beta-dehydrogenase 12) (EC 1.1.1.62) (Short chain dehydrogenase/reductase family 12C member 1) | Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation. {ECO:0000269|PubMed:12482854, ECO:0000269|PubMed:16166196}. |
Q56NI9 | ESCO2 | T233 | psp | N-acetyltransferase ESCO2 (EC 2.3.1.-) (Establishment factor-like protein 2) (EFO2) (EFO2p) (hEFO2) (Establishment of cohesion 1 homolog 2) (ECO1 homolog 2) | Acetyltransferase required for the establishment of sister chromatid cohesion (PubMed:15821733, PubMed:15958495). Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during the S phase. Acetylates the cohesin component SMC3 (PubMed:21111234). {ECO:0000269|PubMed:15821733, ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:21111234}. |
Q58FF8 | HSP90AB2P | T104 | ochoa | Putative heat shock protein HSP 90-beta 2 (Heat shock protein 90-beta b) (Heat shock protein 90Bb) | Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}. |
Q5S007 | LRRK2 | T1357 | psp | Leucine-rich repeat serine/threonine-protein kinase 2 (EC 2.7.11.1) (EC 3.6.5.-) (Dardarin) | Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, innate immunity, autophagy, and vesicle trafficking (PubMed:17114044, PubMed:20949042, PubMed:21850687, PubMed:22012985, PubMed:23395371, PubMed:24687852, PubMed:25201882, PubMed:26014385, PubMed:26824392, PubMed:27830463, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421). Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation (PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421). Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB29, RAB35, and RAB43 (PubMed:23395371, PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421, PubMed:38127736). Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A (PubMed:26824392). Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A (PubMed:26824392). Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain (PubMed:29125462, PubMed:30398148). Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose-6-phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:23395371). Regulates neuronal process morphology in the intact central nervous system (CNS) (PubMed:17114044). Plays a role in synaptic vesicle trafficking (PubMed:24687852). Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization (PubMed:25201882). Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway (PubMed:22012985). The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes (PubMed:22012985). Phosphorylates PRDX3 (PubMed:21850687). By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis (PubMed:28720718). Acts as a positive regulator of innate immunity by mediating phosphorylation of RIPK2 downstream of NOD1 and NOD2, thereby enhancing RIPK2 activation (PubMed:27830463). Independent of its kinase activity, inhibits the proteasomal degradation of MAPT, thus promoting MAPT oligomerization and secretion (PubMed:26014385). In addition, has GTPase activity via its Roc domain which regulates LRRK2 kinase activity (PubMed:18230735, PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29212815). Recruited by RAB29/RAB7L1 to overloaded lysosomes where it phosphorylates and stabilizes RAB8A and RAB10 which promote lysosomal content release and suppress lysosomal enlargement through the EHBP1 and EHBP1L1 effector proteins (PubMed:30209220, PubMed:38227290). {ECO:0000269|PubMed:17114044, ECO:0000269|PubMed:18230735, ECO:0000269|PubMed:20949042, ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:22012985, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24687852, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:26014385, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:27830463, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:30635421, ECO:0000269|PubMed:38127736, ECO:0000269|PubMed:38227290}. |
Q5SW79 | CEP170 | T1055 | ochoa | Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein) | Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269|PubMed:15616186, ECO:0000269|PubMed:28422092}. |
Q68CP9 | ARID2 | T1475 | ochoa | AT-rich interactive domain-containing protein 2 (ARID domain-containing protein 2) (BRG1-associated factor 200) (BAF200) (Zinc finger protein with activation potential) (Zipzap/p200) | Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes. {ECO:0000269|PubMed:16782067, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
Q7Z3J3 | RGPD4 | T1030 | ochoa | RanBP2-like and GRIP domain-containing protein 4 | None |
Q7Z3K3 | POGZ | T463 | ochoa | Pogo transposable element with ZNF domain (Suppressor of hairy wing homolog 5) (Zinc finger protein 280E) (Zinc finger protein 635) | Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms (PubMed:20562864). Promotes the repair of DNA double-strand breaks through the homologous recombination pathway (PubMed:26721387). {ECO:0000269|PubMed:20562864, ECO:0000269|PubMed:26721387}. |
Q86T24 | ZBTB33 | T606 | psp | Transcriptional regulator Kaiso (Zinc finger and BTB domain-containing protein 33) | Transcriptional regulator with bimodal DNA-binding specificity. Binds to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' and also binds to the non-methylated consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso binding site (KBS). Recruits the N-CoR repressor complex to promote histone deacetylation and the formation of repressive chromatin structures in target gene promoters. May contribute to the repression of target genes of the Wnt signaling pathway. May also activate transcription of a subset of target genes by the recruitment of CTNND2. Represses expression of MMP7 in conjunction with transcriptional corepressors CBFA2T3, CBFA2T2 and RUNX1T1 (PubMed:23251453). {ECO:0000269|PubMed:11445535, ECO:0000269|PubMed:14527417, ECO:0000269|PubMed:15548582, ECO:0000269|PubMed:15817151, ECO:0000269|PubMed:16354688, ECO:0000269|PubMed:23251453}. |
Q86UP2 | KTN1 | T268 | ochoa | Kinectin (CG-1 antigen) (Kinesin receptor) | Receptor for kinesin thus involved in kinesin-driven vesicle motility. Accumulates in integrin-based adhesion complexes (IAC) upon integrin aggregation by fibronectin. |
Q8IX12 | CCAR1 | T629 | ochoa | Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) (Death inducer with SAP domain) | Associates with components of the Mediator and p160 coactivator complexes that play a role as intermediaries transducing regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Recruited to endogenous nuclear receptor target genes in response to the appropriate hormone. Also functions as a p53 coactivator. May thus play an important role in transcriptional regulation (By similarity). May be involved in apoptosis signaling in the presence of the reinoid CD437. Apoptosis induction involves sequestration of 14-3-3 protein(s) and mediated altered expression of multiple cell cycle regulatory genes including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or cell proliferation (PubMed:12816952). In association with CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). Can act as a both a coactivator and corepressor of AR-mediated transcription. Contributes to chromatin looping and AR transcription complex assembly by stabilizing AR-GATA2 association on chromatin and facilitating MED1 and RNA polymerase II recruitment to AR-binding sites. May play an important role in the growth and tumorigenesis of prostate cancer cells (PubMed:23887938). {ECO:0000250|UniProtKB:Q8CH18, ECO:0000269|PubMed:12816952, ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:24245781}. |
Q8IZ21 | PHACTR4 | T31 | ochoa | Phosphatase and actin regulator 4 | Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Acts as an activator of PP1 by interacting with PPP1CA and preventing phosphorylation of PPP1CA at 'Thr-320'. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation within cranial neural tissue and the neural retina. Also acts as a regulator of migration of enteric neural crest cells (ENCCs) by activating PP1, leading to dephosphorylation and subsequent activation of cofilin (COF1 or COF2) and repression of the integrin signaling through the RHO/ROCK pathway (By similarity). {ECO:0000250}. |
Q8N0Y7 | PGAM4 | T96 | ochoa | Probable phosphoglycerate mutase 4 (EC 5.4.2.11) (EC 5.4.2.4) | None |
Q8NFQ8 | TOR1AIP2 | T66 | 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}. |
Q8NI77 | KIF18A | T681 | ochoa | Kinesin-like protein KIF18A (Marrow stromal KIF18A) (MS-KIF18A) | Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression. {ECO:0000269|PubMed:17346968, ECO:0000269|PubMed:18267093, ECO:0000269|PubMed:18513970, ECO:0000269|PubMed:19625775}. |
Q8WY36 | BBX | T838 | ochoa | HMG box transcription factor BBX (Bobby sox homolog) (HMG box-containing protein 2) | Transcription factor that is necessary for cell cycle progression from G1 to S phase. {ECO:0000269|PubMed:11680820}. |
Q92598 | HSPH1 | T486 | ochoa | Heat shock protein 105 kDa (Antigen NY-CO-25) (Heat shock 110 kDa protein) (Heat shock protein family H member 1) | Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release (PubMed:24318877). Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity). {ECO:0000250|UniProtKB:Q60446, ECO:0000250|UniProtKB:Q61699, ECO:0000269|PubMed:24318877}. |
Q92879 | CELF1 | T173 | psp | CUGBP Elav-like family member 1 (CELF-1) (50 kDa nuclear polyadenylated RNA-binding protein) (Bruno-like protein 2) (CUG triplet repeat RNA-binding protein 1) (CUG-BP1) (CUG-BP- and ETR-3-like factor 1) (Deadenylation factor CUG-BP) (Embryo deadenylation element-binding protein homolog) (EDEN-BP homolog) (RNA-binding protein BRUNOL-2) | RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Acts both as an activator and as a repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB. Promotes exclusion of exon 11 of the INSR pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Increases translation and controls the choice of translation initiation codon of CEBPB mRNA. Increases mRNA translation of CEBPB in aging liver (By similarity). Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3. Mediates rapid cytoplasmic mRNA deadenylation. Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation. Required for completion of spermatogenesis (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA. Binds to the 5'-region of CDKN1A and CEBPB mRNAs. Binds with the 5'-region of CEBPB mRNA in aging liver. May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF2, negatively regulates the processing to mature miRNA (PubMed:28431233). {ECO:0000250, ECO:0000269|PubMed:10536163, ECO:0000269|PubMed:11124939, ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12649496, ECO:0000269|PubMed:12799066, ECO:0000269|PubMed:14726956, ECO:0000269|PubMed:16601207, ECO:0000269|PubMed:16946708, ECO:0000269|PubMed:28431233}. |
Q92922 | SMARCC1 | T404 | ochoa | SWI/SNF complex subunit SMARCC1 (BRG1-associated factor 155) (BAF155) (SWI/SNF complex 155 kDa subunit) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1) | Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. May stimulate the ATPase activity of the catalytic subunit of the complex (PubMed:10078207, PubMed:29374058). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250|UniProtKB:P97496, ECO:0000269|PubMed:10078207, ECO:0000269|PubMed:11018012, ECO:0000269|PubMed:29374058, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
Q96A70 | AZIN2 | T35 | ochoa | Antizyme inhibitor 2 (AzI2) (Arginine decarboxylase) (ADC) (ARGDC) (Ornithine decarboxylase-like protein) (ODC-like protein) (ornithine decarboxylase paralog) (ODC-p) | Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding (PubMed:17900240). Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production (PubMed:17900240). Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking (PubMed:20188728). {ECO:0000269|PubMed:17900240, ECO:0000269|PubMed:20188728}. |
Q96AX2 | RAB37 | T172 | psp | Ras-related protein Rab-37 (EC 3.6.5.2) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:38536817). Acts as an organizer for autophagosome biogenesis in a GTP-dependent manner (PubMed:38536817). Involved in retinal homeostasis by autophagy regulation (PubMed:38536817). {ECO:0000269|PubMed:38536817}. |
Q96EA4 | SPDL1 | T552 | ochoa | Protein Spindly (hSpindly) (Arsenite-related gene 1 protein) (Coiled-coil domain-containing protein 99) (Rhabdomyosarcoma antigen MU-RMS-40.4A) (Spindle apparatus coiled-coil domain-containing protein 1) | Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment (PubMed:17576797, PubMed:19468067). Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (PubMed:25035494). Plays a role in cell migration (PubMed:30258100). {ECO:0000255|HAMAP-Rule:MF_03041, ECO:0000269|PubMed:17576797, ECO:0000269|PubMed:19468067, ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:30258100}. |
Q96L73 | NSD1 | T563 | ochoa | Histone-lysine N-methyltransferase, H3 lysine-36 specific (EC 2.1.1.357) (Androgen receptor coactivator 267 kDa protein) (Androgen receptor-associated protein of 267 kDa) (H3-K36-HMTase) (Lysine N-methyltransferase 3B) (Nuclear receptor-binding SET domain-containing protein 1) (NR-binding SET domain-containing protein) | Histone methyltransferase that dimethylates Lys-36 of histone H3 (H3K36me2). Transcriptional intermediary factor capable of both negatively or positively influencing transcription, depending on the cellular context. {ECO:0000269|PubMed:21196496}. |
Q96LT9 | RNPC3 | T112 | ochoa | RNA-binding region-containing protein 3 (RNA-binding motif protein 40) (RNA-binding protein 40) (U11/U12 small nuclear ribonucleoprotein 65 kDa protein) (U11/U12 snRNP 65 kDa protein) (U11/U12-65K) | Participates in pre-mRNA U12-dependent splicing, performed by the minor spliceosome which removes U12-type introns. U12-type introns comprises less than 1% of all non-coding sequences. Binds to the 3'-stem-loop of m(7)G-capped U12 snRNA. {ECO:0000269|PubMed:16096647, ECO:0000269|PubMed:19447915, ECO:0000269|PubMed:24480542, ECO:0000269|PubMed:29255062}. |
Q96N46 | TTC14 | T543 | ochoa | Tetratricopeptide repeat protein 14 (TPR repeat protein 14) | None |
Q96Q45 | TMEM237 | T56 | ochoa | Transmembrane protein 237 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein) | Component of the transition zone in primary cilia. Required for ciliogenesis. {ECO:0000269|PubMed:22152675}. |
Q99661 | KIF2C | T87 | ochoa | Kinesin-like protein KIF2C (Kinesin-like protein 6) (Mitotic centromere-associated kinesin) (MCAK) | In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (PubMed:21820309). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis (PubMed:19060894). Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment (PubMed:23891108). {ECO:0000269|PubMed:19060894, ECO:0000269|PubMed:21820309, ECO:0000269|PubMed:23891108}. |
Q99666 | RGPD5 | T1029 | ochoa | RANBP2-like and GRIP domain-containing protein 5/6 (Ran-binding protein 2-like 1/2) (RanBP2-like 1/2) (RanBP2L1) (RanBP2L2) (Sperm membrane protein BS-63) | None |
Q9BQ39 | DDX50 | T118 | ochoa | ATP-dependent RNA helicase DDX50 (EC 3.6.4.13) (DEAD box protein 50) (Gu-beta) (Nucleolar protein Gu2) | ATP-dependent RNA helicase that may play a role in various aspects of RNA metabolism including pre-mRNA splicing or ribosomal RNA production (PubMed:12027455). Also acts as a viral restriction factor and promotes the activation of the NF-kappa-B and IRF3 signaling pathways following its stimulation with viral RNA or infection with RNA and DNA viruses (PubMed:35215908). For instance, decreases vaccinia virus, herpes simplex virus, Zika virus or dengue virus replication during the early stage of infection (PubMed:28181036, PubMed:35215908). Mechanistically, acts via the adapter TICAM1 and independently of the DDX1-DDX21-DHX36 helicase complex to induce the production of interferon-beta (PubMed:35215908). {ECO:0000269|PubMed:12027455, ECO:0000269|PubMed:28181036, ECO:0000269|PubMed:35215908}. |
Q9BQ70 | TCF25 | T111 | ochoa | Ribosome quality control complex subunit TCF25 (Nuclear localized protein 1) (Transcription factor 25) (TCF-25) | Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:30244831). In the RQC complex, required to promote formation of 'Lys-48'-linked polyubiquitin chains during ubiquitination of incompletely synthesized proteins by LTN1 (PubMed:30244831). May negatively regulate the calcineurin-NFAT signaling cascade by suppressing the activity of transcription factor NFATC4 (By similarity). May play a role in cell death control (By similarity). {ECO:0000250|UniProtKB:A0A8I6ASZ5, ECO:0000250|UniProtKB:Q8R3L2, ECO:0000269|PubMed:30244831}. |
Q9BXF6 | RAB11FIP5 | T438 | ochoa | Rab11 family-interacting protein 5 (Rab11-FIP5) (Gamma-SNAP-associated factor 1) (Gaf-1) (Phosphoprotein pp75) (Rab11-interacting protein Rip11) | Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269|PubMed:11163216, ECO:0000269|PubMed:20717956}. |
Q9BY44 | EIF2A | T255 | ochoa | Eukaryotic translation initiation factor 2A (eIF-2A) (65 kDa eukaryotic translation initiation factor 2A) [Cleaved into: Eukaryotic translation initiation factor 2A, N-terminally processed] | Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner. {ECO:0000269|PubMed:12133843}. |
Q9BYT3 | STK33 | T382 | psp | Serine/threonine-protein kinase 33 (EC 2.7.11.1) | Serine/threonine protein kinase required for spermatid differentiation and male fertility (PubMed:37146716, PubMed:38781365). Promotes sperm flagella assembly during spermatogenesis by mediating phosphorylation of fibrous sheath proteins AKAP3 and AKAP4 (By similarity). Also phosphorylates vimentin/VIM, thereby regulating the dynamic behavior of the intermediate filament cytoskeleton (By similarity). {ECO:0000250|UniProtKB:Q924X7, ECO:0000269|PubMed:37146716, ECO:0000269|PubMed:38781365}. |
Q9C0C9 | UBE2O | T1219 | ochoa | (E3-independent) E2 ubiquitin-conjugating enzyme (EC 2.3.2.24) (E2/E3 hybrid ubiquitin-protein ligase UBE2O) (Ubiquitin carrier protein O) (Ubiquitin-conjugating enzyme E2 O) (Ubiquitin-conjugating enzyme E2 of 230 kDa) (Ubiquitin-conjugating enzyme E2-230K) (Ubiquitin-protein ligase O) | E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins (PubMed:23455153, PubMed:24703950). Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity (PubMed:23381138). Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis (PubMed:23455153). Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location (PubMed:24703950). Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASHC1, leading to promote endosomal F-actin assembly (PubMed:23452853). {ECO:0000269|PubMed:23381138, ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:23455153, ECO:0000269|PubMed:24703950}. |
Q9H0H5 | RACGAP1 | T161 | ochoa | Rac GTPase-activating protein 1 (Male germ cell RacGap) (MgcRacGAP) (Protein CYK4 homolog) (CYK4) (HsCYK-4) | Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Sequentially binds to ECT2 and RAB11FIP3 which regulates cleavage furrow ingression and abscission during cytokinesis (PubMed:18511905). Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity (PubMed:10979956). Has a critical role in erythropoiesis (PubMed:34818416). Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269|PubMed:10979956, ECO:0000269|PubMed:11085985, ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:11782313, ECO:0000269|PubMed:14729465, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16129829, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:18511905, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:23235882, ECO:0000269|PubMed:9497316}. |
Q9H4G0 | EPB41L1 | T799 | ochoa | Band 4.1-like protein 1 (Erythrocyte membrane protein band 4.1-like 1) (Neuronal protein 4.1) (4.1N) | May function to confer stability and plasticity to neuronal membrane via multiple interactions, including the spectrin-actin-based cytoskeleton, integral membrane channels and membrane-associated guanylate kinases. |
Q9H4I2 | ZHX3 | T649 | ochoa | Zinc fingers and homeoboxes protein 3 (Triple homeobox protein 1) (Zinc finger and homeodomain protein 3) | Acts as a transcriptional repressor. Involved in the early stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a regulator of podocyte gene expression during primary glomerula disease. Binds to promoter DNA. {ECO:0000269|PubMed:12659632, ECO:0000269|PubMed:21174497}. |
Q9H5Q4 | TFB2M | T184 | psp | Dimethyladenosine transferase 2, mitochondrial (EC 2.1.1.-) (Hepatitis C virus NS5A-transactivated protein 5) (HCV NS5A-transactivated protein 5) (Mitochondrial 12S rRNA dimethylase 2) (Mitochondrial transcription factor B2) (h-mtTFB) (h-mtTFB2) (hTFB2M) (mtTFB2) (S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2) | S-adenosyl-L-methionine-dependent rRNA methyltransferase which may methylate two specific adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 12S mitochondrial rRNA (Probable). 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:12068295, PubMed:15526033, PubMed:20410300, 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:15526033, PubMed:29149603). Stimulates transcription independently of the methyltransferase activity (PubMed:12897151). {ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:12897151, ECO:0000269|PubMed:15526033, ECO:0000269|PubMed:20410300, ECO:0000269|PubMed:29149603, ECO:0000305|PubMed:12897151, ECO:0000305|PubMed:17031457}. |
Q9H9A7 | RMI1 | T359 | ochoa | RecQ-mediated genome instability protein 1 (BLM-associated protein of 75 kDa) (BLAP75) (FAAP75) | Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability. {ECO:0000269|PubMed:15775963, ECO:0000269|PubMed:16537486, ECO:0000269|PubMed:16595695}. |
Q9NQW6 | ANLN | T416 | ochoa | Anillin | Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis (PubMed:23870127). May play a significant role in podocyte cell migration (PubMed:24676636). {ECO:0000269|PubMed:10931866, ECO:0000269|PubMed:12479805, ECO:0000269|PubMed:15496454, ECO:0000269|PubMed:16040610, ECO:0000269|PubMed:16357138, ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:24676636}. |
Q9NV70 | EXOC1 | T568 | ochoa | Exocyst complex component 1 (Exocyst complex component Sec3) | Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; FUNCTION: (Microbial infection) Has an antiviral effect against flaviviruses by affecting viral RNA transcription and translation through the sequestration of elongation factor 1-alpha (EEF1A1). This results in decreased viral RNA synthesis and decreased viral protein translation. {ECO:0000269|PubMed:19889084}. |
Q9NZI8 | IGF2BP1 | T249 | ochoa | Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2 mRNA-binding protein 1) (IMP-1) (IMP1) (Coding region determinant-binding protein) (CRD-BP) (IGF-II mRNA-binding protein 1) (VICKZ family member 1) (Zipcode-binding protein 1) (ZBP-1) | RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152, PubMed:32245947). Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence preventing MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD (PubMed:29476152). Binding to MYC mRNA is enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts. {ECO:0000250, ECO:0000269|PubMed:10875929, ECO:0000269|PubMed:16356927, ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:16778892, ECO:0000269|PubMed:17101699, ECO:0000269|PubMed:17255263, ECO:0000269|PubMed:17893325, ECO:0000269|PubMed:18385235, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19541769, ECO:0000269|PubMed:19647520, ECO:0000269|PubMed:20080952, ECO:0000269|PubMed:22279049, ECO:0000269|PubMed:29476152, ECO:0000269|PubMed:32245947, ECO:0000269|PubMed:8132663, ECO:0000269|PubMed:9891060}. |
Q9P2E9 | RRBP1 | T274 | ochoa | Ribosome-binding protein 1 (180 kDa ribosome receptor homolog) (RRp) (ES/130-related protein) (Ribosome receptor protein) | Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane. {ECO:0000250}. |
Q9UHD1 | CHORDC1 | T204 | ochoa | Cysteine and histidine-rich domain-containing protein 1 (CHORD domain-containing protein 1) (CHORD-containing protein 1) (CHP-1) (Protein morgana) | Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2 (PubMed:20230755). Proposed to act as co-chaperone for HSP90 (PubMed:20230755). May play a role in the regulation of NOD1 via a HSP90 chaperone complex (PubMed:20230755). In vitro, has intrinsic chaperone activity (PubMed:20230755). This function may be achieved by inhibiting association of ROCK2 with NPM1 (PubMed:20230755). Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling (PubMed:32053105). Involved in stress response (PubMed:20230755). Prevents tumorigenesis (PubMed:20230755). {ECO:0000269|PubMed:20230755, ECO:0000269|PubMed:32053105}. |
Q9UHI6 | DDX20 | T461 | ochoa | Probable ATP-dependent RNA helicase DDX20 (EC 3.6.1.15) (EC 3.6.4.13) (Component of gems 3) (DEAD box protein 20) (DEAD box protein DP 103) (Gemin-3) | The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). {ECO:0000269|PubMed:18984161}. |
Q9UHL0 | DDX25 | T239 | psp | ATP-dependent RNA helicase DDX25 (EC 3.6.4.13) (DEAD box protein 25) (Gonadotropin-regulated testicular RNA helicase) | ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development (By similarity). {ECO:0000250, ECO:0000269|PubMed:10608860}. |
Q9UHR4 | BAIAP2L1 | T166 | ochoa | BAR/IMD domain-containing adapter protein 2-like 1 (Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1) (BAI1-associated protein 2-like protein 1) (Insulin receptor tyrosine kinase substrate) | May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. {ECO:0000269|PubMed:17430976, ECO:0000269|PubMed:19366662, ECO:0000269|PubMed:22921828}. |
Q9UIF8 | BAZ2B | T2014 | ochoa | Bromodomain adjacent to zinc finger domain protein 2B (hWALp4) | Regulatory subunit of the ATP-dependent BRF-1 and BRF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). The BRF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the BRF-5 ISWI chromatin remodeling complex (PubMed:28801535). Chromatin reader protein, which may play a role in transcriptional regulation via interaction with ISWI (By similarity) (PubMed:10662543). Involved in positively modulating the rate of age-related behavioral deterioration (By similarity). Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with histone methyltransferase EHMT1 (By similarity). {ECO:0000250|UniProtKB:A2AUY4, ECO:0000269|PubMed:28801535, ECO:0000303|PubMed:10662543}. |
Q9UJS0 | SLC25A13 | T243 | ochoa | Electrogenic aspartate/glutamate antiporter SLC25A13, mitochondrial (Calcium-binding mitochondrial carrier protein Aralar2) (ARALAR-related gene 2) (ARALAR2) (Citrin) (Mitochondrial aspartate glutamate carrier 2) (Solute carrier family 25 member 13) | Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle (PubMed:11566871, PubMed:38945283). Also mediates the uptake of L-cysteinesulfinate (3-sulfino-L-alanine) by mitochondria in exchange of L-glutamate and proton (PubMed:11566871). Can also exchange L-cysteinesulfinate with aspartate in their anionic form without any proton translocation (PubMed:11566871). Lacks transport activity towards gamma-aminobutyric acid (GABA) (PubMed:38945283). {ECO:0000269|PubMed:11566871, ECO:0000269|PubMed:38945283}. |
Q9UKL0 | RCOR1 | T449 | 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}. |
Q9UKX7 | NUP50 | T259 | ochoa | Nuclear pore complex protein Nup50 (50 kDa nucleoporin) (Nuclear pore-associated protein 60 kDa-like) (Nucleoporin Nup50) | Component of the nuclear pore complex that has a direct role in nuclear protein import (PubMed:20016008). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling (PubMed:20016008). Interacts with regulatory proteins of cell cycle progression including CDKN1B (By similarity). This interaction is required for correct intracellular transport and degradation of CDKN1B (By similarity). {ECO:0000250|UniProtKB:Q9JIH2, ECO:0000269|PubMed:20016008}. |
Q9UNF0 | PACSIN2 | T373 | ochoa | Protein kinase C and casein kinase substrate in neurons protein 2 (Syndapin-2) (Syndapin-II) (SdpII) | Regulates the morphogenesis and endocytosis of caveolae (By similarity). Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus (PubMed:21693584, PubMed:23129763, PubMed:23236520, PubMed:23596323). Essential for endothelial organization in sprouting angiogenesis, modulates CDH5-based junctions. Facilitates endothelial front-rear polarity during migration by recruiting EHD4 and MICALL1 to asymmetric adherens junctions between leader and follower cells (By similarity). {ECO:0000250|UniProtKB:Q9WVE8, ECO:0000269|PubMed:21693584, ECO:0000269|PubMed:23129763, ECO:0000269|PubMed:23236520, ECO:0000269|PubMed:23596323}.; FUNCTION: (Microbial infection) Specifically enhances the efficiency of HIV-1 virion spread by cell-to-cell transfer (PubMed:29891700). Also promotes the protrusion engulfment during cell-to-cell spread of bacterial pathogens like Listeria monocytogenes (PubMed:31242077). Involved in lipid droplet formation, which is important for HCV virion assembly (PubMed:31801866). {ECO:0000269|PubMed:29891700, ECO:0000269|PubMed:31242077, ECO:0000269|PubMed:31801866}. |
Q9UQR0 | SCML2 | T496 | ochoa | Sex comb on midleg-like protein 2 | Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). {ECO:0000250}. |
Q9Y2K5 | R3HDM2 | T147 | ochoa | R3H domain-containing protein 2 | None |
Q9Y2X9 | ZNF281 | T399 | ochoa | Zinc finger protein 281 (GC-box-binding zinc finger protein 1) (Transcription factor ZBP-99) (Zinc finger DNA-binding protein 99) | Transcription repressor that plays a role in regulation of embryonic stem cells (ESCs) differentiation. Required for ESCs differentiation and acts by mediating autorepression of NANOG in ESCs: binds to the NANOG promoter and promotes association of NANOG protein to its own promoter and recruits the NuRD complex, which deacetylates histones. Not required for establishement and maintenance of ESCs (By similarity). Represses the transcription of a number of genes including GAST, ODC1 and VIM. Binds to the G-rich box in the enhancer region of these genes. {ECO:0000250, ECO:0000269|PubMed:10448078, ECO:0000269|PubMed:12771217}. |
Q9Y5S2 | CDC42BPB | T1108 | psp | Serine/threonine-protein kinase MRCK beta (EC 2.7.11.1) (CDC42-binding protein kinase beta) (CDC42BP-beta) (DMPK-like beta) (Myotonic dystrophy kinase-related CDC42-binding kinase beta) (MRCK beta) (Myotonic dystrophy protein kinase-like beta) | Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2 (PubMed:21457715, PubMed:21949762). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates PPP1R12A (PubMed:21457715). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). {ECO:0000250|UniProtKB:Q7TT50, ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:21949762}. |
Q15084 | PDIA6 | T166 | Sugiyama | Protein disulfide-isomerase A6 (EC 5.3.4.1) (Endoplasmic reticulum protein 5) (ER protein 5) (ERp5) (Protein disulfide isomerase P5) (Thioredoxin domain-containing protein 7) | May function as a chaperone that inhibits aggregation of misfolded proteins (PubMed:12204115). Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling (PubMed:24508390). May also regulate the UPR via the EIF2AK3 UPR sensor (PubMed:24508390). Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (PubMed:15466936). {ECO:0000269|PubMed:12204115, ECO:0000269|PubMed:15466936, ECO:0000269|PubMed:24508390}. |
P17066 | HSPA6 | T228 | Sugiyama | Heat shock 70 kDa protein 6 (Heat shock 70 kDa protein B') (Heat shock protein family A member 6) | 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 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 (PubMed:26865365). {ECO:0000303|PubMed:26865365}. |
P34931 | HSPA1L | T228 | Sugiyama | Heat shock 70 kDa protein 1-like (Heat shock 70 kDa protein 1L) (Heat shock 70 kDa protein 1-Hom) (HSP70-Hom) (Heat shock protein family A member 1L) | 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 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 (PubMed:26865365). Positive regulator of PRKN translocation to damaged mitochondria (PubMed:24270810). {ECO:0000269|PubMed:24270810, ECO:0000303|PubMed:26865365}. |
P48741 | HSPA7 | T228 | Sugiyama | Putative heat shock 70 kDa protein 7 (Heat shock 70 kDa protein B) (Heat shock protein family A member 7) | None |
P08195 | SLC3A2 | T325 | Sugiyama | Amino acid transporter heavy chain SLC3A2 (4F2 cell-surface antigen heavy chain) (4F2hc) (4F2 heavy chain antigen) (Lymphocyte activation antigen 4F2 large subunit) (Solute carrier family 3 member 2) (CD antigen CD98) | Acts as a chaperone that facilitates biogenesis and trafficking of functional transporters heterodimers to the plasma membrane. Forms heterodimer with SLC7 family transporters (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A10 and SLC7A11), a group of amino-acid antiporters (PubMed:10574970, PubMed:10903140, PubMed:11557028, PubMed:30867591, PubMed:33298890, PubMed:33758168, PubMed:34880232, PubMed:9751058, PubMed:9829974, PubMed:9878049). Heterodimers function as amino acids exchangers, the specificity of the substrate depending on the SLC7A subunit. Heterodimers SLC3A2/SLC7A6 or SLC3A2/SLC7A7 mediate the uptake of dibasic amino acids (PubMed:10903140, PubMed:9829974). Heterodimer SLC3A2/SLC7A11 functions as an antiporter by mediating the exchange of extracellular anionic L-cystine and intracellular L-glutamate across the cellular plasma membrane (PubMed:34880232). SLC3A2/SLC7A10 translocates small neutral L- and D-amino acids across the plasma membrane (By similarity). SLC3A2/SLC75 or SLC3A2/SLC7A8 translocates neutral amino acids with broad specificity, thyroid hormones and L-DOPA (PubMed:10574970, PubMed:11389679, PubMed:11557028, PubMed:11564694, PubMed:11742812, PubMed:12117417, PubMed:12225859, PubMed:12716892, PubMed:15980244, PubMed:30867591, PubMed:33298890, PubMed:33758168). SLC3A2 is essential for plasma membrane localization, stability, and the transport activity of SLC7A5 and SLC7A8 (PubMed:10391915, PubMed:10574970, PubMed:11311135, PubMed:15769744, PubMed:33066406). When associated with LAPTM4B, the heterodimer SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation (PubMed:25998567). Modulates integrin-related signaling and is essential for integrin-dependent cell spreading, migration and tumor progression (PubMed:11121428, PubMed:15625115). {ECO:0000250|UniProtKB:P63115, ECO:0000269|PubMed:10391915, ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:10903140, ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:12716892, ECO:0000269|PubMed:15625115, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:15980244, ECO:0000269|PubMed:25998567, ECO:0000269|PubMed:30867591, ECO:0000269|PubMed:33066406, ECO:0000269|PubMed:33298890, ECO:0000269|PubMed:33758168, ECO:0000269|PubMed:34880232, ECO:0000269|PubMed:9751058, ECO:0000269|PubMed:9829974, ECO:0000269|PubMed:9878049}.; FUNCTION: (Microbial infection) In case of hepatitis C virus/HCV infection, the complex formed by SLC3A2 and SLC7A5/LAT1 plays a role in HCV propagation by facilitating viral entry into host cell and increasing L-leucine uptake-mediated mTORC1 signaling activation, thereby contributing to HCV-mediated pathogenesis. {ECO:0000269|PubMed:30341327}.; FUNCTION: (Microbial infection) Acts as a receptor for malaria parasite Plasmodium vivax (Thai isolate) in immature red blood cells. {ECO:0000269|PubMed:34294905}. |
P18621 | RPL17 | T79 | Sugiyama | Large ribosomal subunit protein uL22 (60S ribosomal protein L17) (60S ribosomal protein L23) (PD-1) | Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}. |
P18669 | PGAM1 | T159 | Sugiyama | Phosphoglycerate mutase 1 (EC 5.4.2.11) (EC 5.4.2.4) (BPG-dependent PGAM 1) (Phosphoglycerate mutase isozyme B) (PGAM-B) | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglyceratea crucial step in glycolysis, by using 2,3-bisphosphoglycerate (PubMed:23653202). Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate (PubMed:23653202). {ECO:0000269|PubMed:23653202}. |
P40926 | MDH2 | T224 | Sugiyama | Malate dehydrogenase, mitochondrial (EC 1.1.1.37) | None |
P54136 | RARS1 | T383 | Sugiyama | Arginine--tRNA ligase, cytoplasmic (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) | Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis (PubMed:25288775). Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 (PubMed:17443684). {ECO:0000269|PubMed:17443684, ECO:0000269|PubMed:25288775}. |
P61254 | RPL26 | T93 | Sugiyama | Large ribosomal subunit protein uL24 (60S ribosomal protein L26) | Component of the large ribosomal subunit (PubMed:23636399, PubMed:26100019, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:26100019, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:26100019}. |
P78371 | CCT2 | T103 | Sugiyama | T-complex protein 1 subunit beta (TCP-1-beta) (EC 3.6.1.-) (CCT-beta) (Chaperonin containing T-complex polypeptide 1 subunit 2) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
Q9UNX3 | RPL26L1 | T93 | Sugiyama | Ribosomal protein uL24-like (60S ribosomal protein L26-like 1) (Large ribosomal subunit protein uL24-like 1) | None |
Q13310 | PABPC4 | T191 | Sugiyama | Polyadenylate-binding protein 4 (PABP-4) (Poly(A)-binding protein 4) (Activated-platelet protein 1) (APP-1) (Inducible poly(A)-binding protein) (iPABP) | Binds the poly(A) tail of mRNA (PubMed:8524242). Binds to SMIM26 mRNA and plays a role in its post-transcriptional regulation (PubMed:37009826). May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo (By similarity). {ECO:0000250|UniProtKB:P11940, ECO:0000269|PubMed:37009826, ECO:0000269|PubMed:8524242}. |
Q9H2U2 | PPA2 | T303 | Sugiyama | Inorganic pyrophosphatase 2, mitochondrial (EC 3.6.1.1) (Pyrophosphatase SID6-306) (Pyrophosphate phospho-hydrolase 2) (PPase 2) | Hydrolyzes inorganic pyrophosphate (PubMed:27523597). This activity is essential for correct regulation of mitochondrial membrane potential, and mitochondrial organization and function (PubMed:27523598). {ECO:0000269|PubMed:27523597, ECO:0000269|PubMed:27523598}. |
P27348 | YWHAQ | T141 | Sugiyama | 14-3-3 protein theta (14-3-3 protein T-cell) (14-3-3 protein tau) (Protein HS1) | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1. {ECO:0000269|PubMed:12177059}. |
P23284 | PPIB | T81 | Sugiyama | Peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (CYP-S1) (Cyclophilin B) (Rotamase B) (S-cyclophilin) (SCYLP) | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. {ECO:0000269|PubMed:20676357}. |
Q8WWM7 | ATXN2L | T204 | Sugiyama | 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}. |
P18827 | SDC1 | T240 | Sugiyama | Syndecan-1 (SYND1) (CD antigen CD138) | Cell surface proteoglycan that contains both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix (By similarity). Regulates exosome biogenesis in concert with SDCBP and PDCD6IP (PubMed:22660413). Able to induce its own expression in dental mesenchymal cells and also in the neighboring dental epithelial cells via an MSX1-mediated pathway (By similarity). {ECO:0000250|UniProtKB:P18828, ECO:0000269|PubMed:22660413}. |
P27816 | MAP4 | T287 | Sugiyama | Microtubule-associated protein 4 (MAP-4) | Non-neuronal microtubule-associated protein. Promotes microtubule assembly. {ECO:0000269|PubMed:10791892, ECO:0000269|PubMed:34782749}. |
P13674 | P4HA1 | T140 | Sugiyama | Prolyl 4-hydroxylase subunit alpha-1 (4-PH alpha-1) (EC 1.14.11.2) (Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1) | Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. {ECO:0000269|PubMed:9211872}. |
O95721 | SNAP29 | T137 | Sugiyama | Synaptosomal-associated protein 29 (SNAP-29) (Soluble 29 kDa NSF attachment protein) (Vesicle-membrane fusion protein SNAP-29) | SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also plays a role in ciliogenesis by regulating membrane fusions. {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686250, ECO:0000269|PubMed:25686604}. |
P02545 | LMNA | T519 | Sugiyama | Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)] | [Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:18551513, ECO:0000269|PubMed:18611980, ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:23666920, ECO:0000269|PubMed:23990565, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:31434876, ECO:0000269|PubMed:31548606, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269|PubMed:20458013}. |
P00338 | LDHA | T248 | EPSD|PSP | L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (Cell proliferation-inducing gene 19 protein) (LDH muscle subunit) (LDH-M) (Renal carcinoma antigen NY-REN-59) | Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). {ECO:0000269|PubMed:11276087}. |
P12272 | PTHLH | T108 | GPS6|ELM|iPTMNet|EPSD | Parathyroid hormone-related protein (PTH-rP) (PTHrP) (Parathyroid hormone-like protein) (PLP) [Cleaved into: PTHrP[1-36]; PTHrP[38-94]; Osteostatin (PTHrP[107-139])] | Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport (PubMed:12538599, PubMed:35932760, PubMed:3616618). Acts by binding to its receptor, PTH1R, activating G protein-coupled receptor signaling (PubMed:19674967, PubMed:35932760). Regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teeth (By similarity). Required for skeletal homeostasis (PubMed:12538599). Promotes mammary mesenchyme differentiation and bud outgrowth by modulating mesenchymal cell responsiveness to BMPs (PubMed:12538599). Up-regulates BMPR1A expression in the mammary mesenchyme and this increases the sensitivity of these cells to BMPs and allows them to respond to BMP4 in a paracrine and/or autocrine fashion (By similarity). BMP4 signaling in the mesenchyme, in turn, triggers epithelial outgrowth and augments MSX2 expression, which causes the mammary mesenchyme to inhibit hair follicle formation within the nipple sheath (By similarity). Promotes colon cancer cell migration and invasion in an integrin alpha-6/beta-1-dependent manner through activation of Rac1 (PubMed:20637541). {ECO:0000250|UniProtKB:P22858, ECO:0000269|PubMed:19674967, ECO:0000269|PubMed:20637541, ECO:0000269|PubMed:35932760, ECO:0000269|PubMed:3616618, ECO:0000303|PubMed:12538599}.; FUNCTION: [Osteostatin]: Potent inhibitor of osteoclastic bone resorption. {ECO:0000269|PubMed:1915066, ECO:0000269|PubMed:1954916, ECO:0000269|PubMed:20637541, ECO:0000269|PubMed:9048639, ECO:0000269|PubMed:9144344}. |
Q9NXV6 | CDKN2AIP | T110 | Sugiyama | CDKN2A-interacting protein (Collaborator of ARF) | Regulates DNA damage response in a dose-dependent manner through a number of signaling pathways involved in cell proliferation, apoptosis and senescence. {ECO:0000269|PubMed:15109303, ECO:0000269|PubMed:24825908}. |
Q9Y262 | EIF3L | T44 | Sugiyama | Eukaryotic translation initiation factor 3 subunit L (eIF3l) (Eukaryotic translation initiation factor 3 subunit 6-interacting protein) (Eukaryotic translation initiation factor 3 subunit E-interacting protein) | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03011, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.; FUNCTION: (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}. |
P08253 | MMP2 | T250 | EPSD|PSP | 72 kDa type IV collagenase (EC 3.4.24.24) (72 kDa gelatinase) (Gelatinase A) (Matrix metalloproteinase-2) (MMP-2) (TBE-1) [Cleaved into: PEX] | Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.; FUNCTION: PEX, the C-terminal non-catalytic fragment of MMP2, possesses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.; FUNCTION: [Isoform 2]: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways. |
P53041 | PPP5C | T121 | Sugiyama | Serine/threonine-protein phosphatase 5 (PP5) (EC 3.1.3.16) (Protein phosphatase T) (PP-T) (PPT) | Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT (PubMed:14734805, PubMed:14764652, PubMed:14871926, PubMed:15383005, PubMed:15546861, PubMed:16260606, PubMed:16790549, PubMed:16892053, PubMed:19176521, PubMed:19948726, PubMed:21144835, PubMed:22399290, PubMed:22781750, PubMed:23102700, PubMed:30699359, PubMed:9000529). Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses (PubMed:14734805, PubMed:14764652, PubMed:14871926, PubMed:15383005, PubMed:15546861, PubMed:16260606, PubMed:16790549, PubMed:16892053, PubMed:19176521, PubMed:19948726, PubMed:21144835, PubMed:22399290, PubMed:22781750, PubMed:23102700, PubMed:30699359, PubMed:9000529). Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1 (PubMed:14871926, PubMed:16260606, PubMed:21144835). Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress (PubMed:23102700). Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function (By similarity). Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1 (By similarity). Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E (PubMed:16790549). May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels (PubMed:22781750). Dephosphorylates and may play a role in the regulation of TAU/MAPT (PubMed:15546861). Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2 (By similarity). Dephosphorylate FNIP1, disrupting interaction with HSP90AA1/Hsp90 (PubMed:30699359). {ECO:0000250|UniProtKB:P53042, ECO:0000250|UniProtKB:Q60676, ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:14764652, ECO:0000269|PubMed:14871926, ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16260606, ECO:0000269|PubMed:16790549, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:19948726, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:22399290, ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:23102700, ECO:0000269|PubMed:30699359, ECO:0000269|PubMed:9000529}. |
Q5VTB9 | RNF220 | T368 | Sugiyama | E3 ubiquitin-protein ligase RNF220 (EC 2.3.2.27) (RING finger protein 220) (RING-type E3 ubiquitin transferase RNF220) | E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of SIN3B (By similarity). Independently of its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-mediated deubiquitination of CTNNB1 promoting Wnt signaling (PubMed:25266658, PubMed:33964137). Plays a critical role in the regulation of nuclear lamina (PubMed:33964137). {ECO:0000250|UniProtKB:Q6PDX6, ECO:0000269|PubMed:25266658, ECO:0000269|PubMed:33964137}. |
P24752 | ACAT1 | T185 | Sugiyama | Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) (T2) | This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA (PubMed:1715688, PubMed:7728148, PubMed:9744475). Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms (PubMed:1715688, PubMed:7728148, PubMed:9744475). The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA (PubMed:17371050). Thereby, it plays a major role in ketone body metabolism (PubMed:1715688, PubMed:17371050, PubMed:7728148, PubMed:9744475). {ECO:0000269|PubMed:1715688, ECO:0000269|PubMed:17371050, ECO:0000269|PubMed:7728148, ECO:0000269|PubMed:9744475}. |
Q13153 | PAK1 | T292 | SIGNOR | Serine/threonine-protein kinase PAK 1 (EC 2.7.11.1) (Alpha-PAK) (p21-activated kinase 1) (PAK-1) (p65-PAK) | Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes (PubMed:10551809, PubMed:11896197, PubMed:12876277, PubMed:14585966, PubMed:15611088, PubMed:17726028, PubMed:17989089, PubMed:30290153, PubMed:17420447). Can directly phosphorylate BAD and protects cells against apoptosis (By similarity). Activated by interaction with CDC42 and RAC1 (PubMed:8805275, PubMed:9528787). Functions as a GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway (PubMed:8805275, PubMed:9528787). Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases (By similarity). Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes (PubMed:9032240, PubMed:9395435). Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton (PubMed:15831477). Plays a role in the regulation of insulin secretion in response to elevated glucose levels (PubMed:22669945). Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ) (By similarity). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2 (PubMed:12624090). Phosphorylates MYL9/MLC2 (By similarity). Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2 (PubMed:11733498). Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus (PubMed:15833848). In podocytes, promotes NR3C2 nuclear localization (By similarity). Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (PubMed:23633677). In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation (By similarity). Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion (PubMed:25766321). In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling (PubMed:23260667). In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in F-actin stabilization (By similarity). In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC) (By similarity). Along with GIT1, positively regulates microtubule nucleation during interphase (PubMed:27012601). Phosphorylates FXR1, promoting its localization to stress granules and activity (PubMed:20417602). Phosphorylates ILK on 'Thr-173' and 'Ser-246', promoting nuclear export of ILK (PubMed:17420447). {ECO:0000250|UniProtKB:O88643, ECO:0000250|UniProtKB:P35465, ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:11733498, ECO:0000269|PubMed:11896197, ECO:0000269|PubMed:12624090, ECO:0000269|PubMed:12876277, ECO:0000269|PubMed:14585966, ECO:0000269|PubMed:15611088, ECO:0000269|PubMed:15831477, ECO:0000269|PubMed:15833848, ECO:0000269|PubMed:17420447, ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089, ECO:0000269|PubMed:20417602, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:23260667, ECO:0000269|PubMed:23633677, ECO:0000269|PubMed:25766321, ECO:0000269|PubMed:27012601, ECO:0000269|PubMed:30290153, ECO:0000269|PubMed:8805275, ECO:0000269|PubMed:9032240, ECO:0000269|PubMed:9395435, ECO:0000269|PubMed:9528787}. |
Q16543 | CDC37 | T243 | Sugiyama | Hsp90 co-chaperone Cdc37 (Hsp90 chaperone protein kinase-targeting subunit) (p50Cdc37) [Cleaved into: Hsp90 co-chaperone Cdc37, N-terminally processed] | Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (PubMed:8666233). Inhibits HSP90AA1 ATPase activity (PubMed:23569206). {ECO:0000269|PubMed:23569206, ECO:0000269|PubMed:8666233}. |
P31948 | STIP1 | T445 | Sugiyama | Stress-induced-phosphoprotein 1 (STI1) (Hsc70/Hsp90-organizing protein) (Hop) (Renal carcinoma antigen NY-REN-11) (Transformation-sensitive protein IEF SSP 3521) | Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity). {ECO:0000250|UniProtKB:O35814, ECO:0000303|PubMed:27353360}. |
P36896 | ACVR1B | T366 | Sugiyama | Activin receptor type-1B (EC 2.7.11.30) (Activin receptor type IB) (ACTR-IB) (Activin receptor-like kinase 4) (ALK-4) (Serine/threonine-protein kinase receptor R2) (SKR2) | Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. ACVR1B also phosphorylates TDP2. {ECO:0000269|PubMed:12364468, ECO:0000269|PubMed:12639945, ECO:0000269|PubMed:18039968, ECO:0000269|PubMed:20226172, ECO:0000269|PubMed:8196624, ECO:0000269|PubMed:9032295, ECO:0000269|PubMed:9892009}. |
P36897 | TGFBR1 | T364 | Sugiyama | TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I) | Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis (PubMed:33914044). The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation. {ECO:0000269|PubMed:15761148, ECO:0000269|PubMed:16754747, ECO:0000269|PubMed:18758450, ECO:0000269|PubMed:33914044, ECO:0000269|PubMed:7774578, ECO:0000269|PubMed:8752209, ECO:0000269|PubMed:8980228, ECO:0000269|PubMed:9346908}. |
P43403 | ZAP70 | T207 | Sugiyama | Tyrosine-protein kinase ZAP-70 (EC 2.7.10.2) (70 kDa zeta-chain associated protein) (Syk-related tyrosine kinase) | Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Also contributes to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD247/CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. ZAP70 is also required for TCR-CD247/CD3Z internalization and degradation through interaction with the E3 ubiquitin-protein ligase CBL and adapter proteins SLA and SLA2. Thus, ZAP70 regulates both T-cell activation switch on and switch off by modulating TCR expression at the T-cell surface. During thymocyte development, ZAP70 promotes survival and cell-cycle progression of developing thymocytes before positive selection (when cells are still CD4/CD8 double negative). Additionally, ZAP70-dependent signaling pathway may also contribute to primary B-cells formation and activation through B-cell receptor (BCR). {ECO:0000269|PubMed:11353765, ECO:0000269|PubMed:12051764, ECO:0000269|PubMed:1423621, ECO:0000269|PubMed:20135127, ECO:0000269|PubMed:26903241, ECO:0000269|PubMed:38614099, ECO:0000269|PubMed:8124727, ECO:0000269|PubMed:8702662, ECO:0000269|PubMed:9489702}. |
P49137 | MAPKAPK2 | T195 | Sugiyama | MAP kinase-activated protein kinase 2 (MAPK-activated protein kinase 2) (MAPKAP kinase 2) (MAPKAP-K2) (MAPKAPK-2) (MK-2) (MK2) (EC 2.7.11.1) | Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities (PubMed:16278218). Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to the dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to the regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity, leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress induced by ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites (PubMed:26616734). Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. {ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:11844797, ECO:0000269|PubMed:12456657, ECO:0000269|PubMed:12565831, ECO:0000269|PubMed:14499342, ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:15629715, ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:16456544, ECO:0000269|PubMed:17481585, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:20932473, ECO:0000269|PubMed:26616734, ECO:0000269|PubMed:8093612, ECO:0000269|PubMed:8280084, ECO:0000269|PubMed:8774846}. |
Q16644 | MAPKAPK3 | T175 | Sugiyama | MAP kinase-activated protein kinase 3 (MAPK-activated protein kinase 3) (MAPKAP kinase 3) (MAPKAP-K3) (MAPKAPK-3) (MK-3) (EC 2.7.11.1) (Chromosome 3p kinase) (3pK) | Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins, such as TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression. {ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:15563468, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:20599781, ECO:0000269|PubMed:8626550, ECO:0000269|PubMed:8774846}. |
P08238 | HSP90AB1 | T94 | Sugiyama | Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84) (Heat shock protein family C member 3) | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:19696785, ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:32272059, ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.; FUNCTION: (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes (PubMed:21949862). Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable). {ECO:0000269|PubMed:21949862, ECO:0000305|PubMed:22066472}. |
Q14247 | CTTN | T344 | Sugiyama | Src substrate cortactin (Amplaxin) (Oncogene EMS1) | Contributes to the organization of the actin cytoskeleton and cell shape (PubMed:21296879). Plays a role in the formation of lamellipodia and in cell migration. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (By similarity). Plays a role in focal adhesion assembly and turnover (By similarity). In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (PubMed:20861316). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (PubMed:17959782). Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity). Required for stabilization of KCNH1 channels at the cell membrane (PubMed:23144454). Plays a role in the invasiveness of cancer cells, and the formation of metastases (PubMed:16636290). {ECO:0000250|UniProtKB:Q60598, ECO:0000250|UniProtKB:Q66HL2, ECO:0000269|PubMed:16636290, ECO:0000269|PubMed:17959782, ECO:0000269|PubMed:21296879, ECO:0000269|PubMed:23144454}. |
Q9Y266 | NUDC | T56 | Sugiyama | Nuclear migration protein nudC (Nuclear distribution protein C homolog) | Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis (PubMed:12679384, PubMed:12852857, PubMed:25789526). Necessary for cytokinesis and cell proliferation (PubMed:12679384, PubMed:12852857). {ECO:0000250|UniProtKB:O35685, ECO:0000269|PubMed:12679384, ECO:0000269|PubMed:12852857, ECO:0000269|PubMed:25789526}. |
P10809 | HSPD1 | T79 | Sugiyama | 60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (Heat shock protein family D member 1) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein) | Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable). {ECO:0000269|PubMed:11422376, ECO:0000269|PubMed:1346131, ECO:0000305|PubMed:25918392}. |
P31946 | YWHAB | T143 | SIGNOR|iPTMNet | 14-3-3 protein beta/alpha (Protein 1054) (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein beta/alpha, N-terminally processed] | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13. {ECO:0000269|PubMed:17717073, ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21224381}. |
P51692 | STAT5B | T684 | Sugiyama | Signal transducer and activator of transcription 5B | Carries out a dual function: signal transduction and activation of transcription (PubMed:29844444). Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. Positively regulates hematopoietic/erythroid differentiation. {ECO:0000269|PubMed:20702587, ECO:0000269|PubMed:29844444, ECO:0000269|PubMed:8732682}. |
Q08881 | ITK | T274 | Sugiyama | Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (Interleukin-2-inducible T-cell kinase) (IL-2-inducible T-cell kinase) (Kinase EMT) (T-cell-specific kinase) (Tyrosine-protein kinase Lyk) | Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation (PubMed:12186560, PubMed:12682224, PubMed:21725281). Required for TCR-mediated calcium response in gamma-delta T-cells, may also be involved in the modulation of the transcriptomic signature in the Vgamma2-positive subset of immature gamma-delta T-cells (By similarity). Phosphorylates TBX21 at 'Tyr-530' and mediates its interaction with GATA3 (By similarity). {ECO:0000250|UniProtKB:Q03526, ECO:0000269|PubMed:12186560, ECO:0000269|PubMed:12682224, ECO:0000269|PubMed:21725281}. |
Q12851 | MAP4K2 | T36 | Sugiyama | Mitogen-activated protein kinase kinase kinase kinase 2 (EC 2.7.11.1) (B lymphocyte serine/threonine-protein kinase) (Germinal center kinase) (GC kinase) (MAPK/ERK kinase kinase kinase 2) (MEK kinase kinase 2) (MEKKK 2) (Rab8-interacting protein) | Serine/threonine-protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Acts as a MAPK kinase kinase kinase (MAP4K) and is an upstream activator of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway and to a lesser extent of the p38 MAPKs signaling pathway. Required for the efficient activation of JNKs by TRAF6-dependent stimuli, including pathogen-associated molecular patterns (PAMPs) such as polyinosine-polycytidine (poly(IC)), lipopolysaccharides (LPS), lipid A, peptidoglycan (PGN), or bacterial flagellin. To a lesser degree, IL-1 and engagement of CD40 also stimulate MAP4K2-mediated JNKs activation. The requirement for MAP4K2/GCK is most pronounced for LPS signaling, and extends to LPS stimulation of c-Jun phosphorylation and induction of IL-8. Enhances MAP3K1 oligomerization, which may relieve N-terminal mediated MAP3K1 autoinhibition and lead to activation following autophosphorylation. Also mediates the SAP/JNK signaling pathway and the p38 MAPKs signaling pathway through activation of the MAP3Ks MAP3K10/MLK2 and MAP3K11/MLK3. May play a role in the regulation of vesicle targeting or fusion. regulation of vesicle targeting or fusion. Activator of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. MAP4Ks act in parallel to and are partially redundant with STK3/MST2 and STK4/MST2 in the phosphorylation and activation of LATS1/2, and establish MAP4Ks as components of the expanded Hippo pathway (PubMed:26437443). {ECO:0000269|PubMed:11784851, ECO:0000269|PubMed:15456887, ECO:0000269|PubMed:17584736, ECO:0000269|PubMed:26437443, ECO:0000269|PubMed:7477268, ECO:0000269|PubMed:7515885, ECO:0000269|PubMed:9712898}. |
P46060 | RANGAP1 | T60 | Sugiyama | Ran GTPase-activating protein 1 (RanGAP1) | GTPase activator for RAN (PubMed:16428860, PubMed:8146159, PubMed:8896452). Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export (PubMed:27160050, PubMed:8896452). Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (PubMed:27160050). {ECO:0000269|PubMed:16428860, ECO:0000269|PubMed:27160050, ECO:0000269|PubMed:8146159, ECO:0000269|PubMed:8896452}. |
P30405 | PPIF | T74 | Sugiyama | Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIase F) (EC 5.2.1.8) (Cyclophilin D) (CyP-D) (CypD) (Cyclophilin F) (Mitochondrial cyclophilin) (CyP-M) (Rotamase F) | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:26387735). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated (PubMed:26387735). In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:22726440). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (PubMed:19228691). {ECO:0000250|UniProtKB:Q99KR7, ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:26387735}. |
P49411 | TUFM | T74 | Sugiyama | Elongation factor Tu, mitochondrial (EF-Tu) (EC 3.6.5.3) (P43) | GTP hydrolase that promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Also plays a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIGI-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy. {ECO:0000269|PubMed:22749352, ECO:0000269|PubMed:28407488}. |
P08133 | ANXA6 | T391 | Sugiyama | Annexin A6 (67 kDa calelectrin) (Annexin VI) (Annexin-6) (Calphobindin-II) (CPB-II) (Chromobindin-20) (Lipocortin VI) (Protein III) (p68) (p70) | May associate with CD21. May regulate the release of Ca(2+) from intracellular stores. |
P07814 | EPRS1 | T1460 | Sugiyama | Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)] | Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activated by ATP to form a covalent intermediate with AMP. Subsequently, the activated amino acid is transferred to the acceptor end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro) (PubMed:23263184, PubMed:24100331, PubMed:29576217, PubMed:3290852, PubMed:37212275). Upon interferon-gamma stimulation, EPRS1 undergoes phosphorylation, causing its dissociation from the aminoacyl-tRNA synthetase multienzyme complex. It is recruited to form the GAIT complex, which binds to stem loop-containing GAIT elements found in the 3'-UTR of various inflammatory mRNAs, such as ceruloplasmin. The GAIT complex inhibits the translation of these mRNAs, allowing interferon-gamma to redirect the function of EPRS1 from protein synthesis to translation inhibition in specific cell contexts (PubMed:15479637, PubMed:23071094). Furthermore, it can function as a downstream effector in the mTORC1 signaling pathway, by promoting the translocation of SLC27A1 from the cytoplasm to the plasma membrane where it mediates the uptake of long-chain fatty acid by adipocytes. Thereby, EPRS1 also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239). {ECO:0000269|PubMed:15479637, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331, ECO:0000269|PubMed:28178239, ECO:0000269|PubMed:29576217, ECO:0000269|PubMed:3290852, ECO:0000269|PubMed:37212275}. |
P38646 | HSPA9 | T271 | Sugiyama | Stress-70 protein, mitochondrial (EC 3.6.4.10) (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Heat shock protein family A member 9) (Mortalin) (MOT) (Peptide-binding protein 74) (PBP74) | Mitochondrial chaperone that plays a key role in mitochondrial protein import, folding, and assembly. Plays an essential role in the protein quality control system, the correct folding of proteins, the re-folding of misfolded proteins, and the targeting of proteins for subsequent degradation. These processes are achieved through cycles of ATP binding, ATP hydrolysis, and ADP release, mediated by co-chaperones (PubMed:18632665, PubMed:25615450, PubMed:28848044, PubMed:30933555, PubMed:31177526). In mitochondria, it associates with the TIM (translocase of the inner membrane) protein complex to assist in the import and folding of mitochondrial proteins (By similarity). Plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis, interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU (PubMed:26702583). Regulates erythropoiesis via stabilization of ISC assembly (PubMed:21123823, PubMed:26702583). Regulates mitochondrial calcium-dependent apoptosis by coupling two calcium channels, ITPR1 and VDAC1, at the mitochondria-associated endoplasmic reticulum (ER) membrane to facilitate calcium transport from the ER lumen to the mitochondria intermembrane space, providing calcium for the downstream calcium channel MCU, which releases it into the mitochondrial matrix (By similarity). Although primarily located in the mitochondria, it is also found in other cellular compartments. In the cytosol, it associates with proteins involved in signaling, apoptosis, or senescence. It may play a role in cell cycle regulation via its interaction with and promotion of degradation of TP53 (PubMed:24625977, PubMed:26634371). May play a role in the control of cell proliferation and cellular aging (By similarity). Protects against reactive oxygen species (ROS) (By similarity). Extracellular HSPA9 plays a cytoprotective role by preventing cell lysis following immune attack by the membrane attack complex by disrupting formation of the complex (PubMed:16091382). {ECO:0000250|UniProtKB:P0CS90, ECO:0000250|UniProtKB:P38647, ECO:0000269|PubMed:16091382, ECO:0000269|PubMed:18632665, ECO:0000269|PubMed:21123823, ECO:0000269|PubMed:24625977, ECO:0000269|PubMed:25615450, ECO:0000269|PubMed:26634371, ECO:0000269|PubMed:26702583, ECO:0000269|PubMed:28848044, ECO:0000269|PubMed:30933555, ECO:0000269|PubMed:31177526}. |
Q8IY84 | NIM1K | T208 | Sugiyama | Serine/threonine-protein kinase NIM1 (EC 2.7.11.1) (NIM1 serine/threonine-protein kinase) | None |
P31947 | SFN | T197 | Sugiyama | 14-3-3 protein sigma (Epithelial cell marker protein 1) (Stratifin) | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010). Binding generally results in the modulation of the activity of the binding partner (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010). Promotes cytosolic retention of GBP1 GTPase by binding to phosphorylated GBP1, thereby inhibiting the innate immune response (PubMed:37797010). Also acts as a TP53/p53-regulated inhibitor of G2/M progression (PubMed:9659898). When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). Acts to maintain desmosome cell junction adhesion in epithelial cells via interacting with and sequestering PKP3 to the cytoplasm, thereby restricting its translocation to existing desmosome structures and therefore maintaining desmosome protein homeostasis (PubMed:24124604). Also acts to facilitate PKP3 exchange at desmosome plaques, thereby maintaining keratinocyte intercellular adhesion (PubMed:29678907). May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53 (PubMed:18382127). {ECO:0000250|UniProtKB:O70456, ECO:0000269|PubMed:15731107, ECO:0000269|PubMed:18382127, ECO:0000269|PubMed:22634725, ECO:0000269|PubMed:24124604, ECO:0000269|PubMed:28202711, ECO:0000269|PubMed:29678907, ECO:0000269|PubMed:37797010, ECO:0000269|PubMed:9659898}. |
Q8N129 | CNPY4 | T55 | Sugiyama | Protein canopy homolog 4 | Plays a role in the regulation of the cell surface expression of TLR4. {ECO:0000269|PubMed:16338228}. |
Q9H422 | HIPK3 | T177 | Sugiyama | Homeodomain-interacting protein kinase 3 (EC 2.7.11.1) (Androgen receptor-interacting nuclear protein kinase) (ANPK) (Fas-interacting serine/threonine-protein kinase) (FIST) (Homolog of protein kinase YAK1) | Serine/threonine-protein kinase involved in transcription regulation, apoptosis and steroidogenic gene expression. Phosphorylates JUN and RUNX2. Seems to negatively regulate apoptosis by promoting FADD phosphorylation. Enhances androgen receptor-mediated transcription. May act as a transcriptional corepressor for NK homeodomain transcription factors. The phosphorylation of NR5A1 activates SF1 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. In osteoblasts, supports transcription activation: phosphorylates RUNX2 that synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE). {ECO:0000269|PubMed:14766760, ECO:0000269|PubMed:17210646}. |
P49792 | RANBP2 | T2703 | Sugiyama | E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270) | E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22194619, ECO:0000269|PubMed:22902403, ECO:0000269|PubMed:23353830, ECO:0000269|PubMed:7775481, ECO:0000303|PubMed:10078529}. |
Q9NYY3 | PLK2 | T103 | Sugiyama | Serine/threonine-protein kinase PLK2 (EC 2.7.11.21) (Polo-like kinase 2) (PLK-2) (hPlk2) (Serine/threonine-protein kinase SNK) (hSNK) (Serum-inducible kinase) | Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CPAP, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CPAP and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress. {ECO:0000269|PubMed:15242618, ECO:0000269|PubMed:19001868, ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:20531387}. |
P00492 | HPRT1 | T124 | Sugiyama | Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (HGPRTase) (EC 2.4.2.8) | Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway. |
P06576 | ATP5F1B | T334 | Sugiyama | ATP synthase F(1) complex subunit beta, mitochondrial (EC 7.1.2.2) (ATP synthase F1 subunit beta) | Catalytic subunit beta, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (Probable) (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the subunit alpha (ATP5F1A), forms the catalytic core in the F(1) domain (PubMed:37244256). {ECO:0000250|UniProtKB:P19483, ECO:0000269|PubMed:37244256, ECO:0000305|PubMed:25168243, ECO:0000305|PubMed:36239646, ECO:0000305|PubMed:37244256}. |
P62937 | PPIA | T32 | Sugiyama | Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin A) (Cyclosporin A-binding protein) (Rotamase A) [Cleaved into: Peptidyl-prolyl cis-trans isomerase A, N-terminally processed] | Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357, PubMed:21245143, PubMed:21593166, PubMed:25678563). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143). Activates endothelial cells (ECs) in a pro-inflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (PubMed:15130913). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (PubMed:23180369). Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (PubMed:26095851). Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (PubMed:25678563). Plays an important role in platelet activation and aggregation (By similarity). Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity). Binds heparan sulfate glycosaminoglycans (PubMed:11943775). Inhibits replication of influenza A virus (IAV) (PubMed:19207730). Inhibits ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by impairing the interaction of ITCH/AIP4 with M1, followed by the suppression of the nuclear export of M1, and finally reduction of the replication of IAV (PubMed:22347431, PubMed:30328013). {ECO:0000250|UniProtKB:P17742, ECO:0000269|PubMed:11943775, ECO:0000269|PubMed:15130913, ECO:0000269|PubMed:19207730, ECO:0000269|PubMed:2001362, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:21245143, ECO:0000269|PubMed:21593166, ECO:0000269|PubMed:22347431, ECO:0000269|PubMed:23180369, ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:26095851, ECO:0000269|PubMed:30328013, ECO:0000269|PubMed:31063815}.; FUNCTION: (Microbial infection) May act as a mediator between human SARS coronavirus nucleoprotein and BSG/CD147 in the process of invasion of host cells by the virus (PubMed:15688292). {ECO:0000269|PubMed:15688292}.; FUNCTION: (Microbial infection) Stimulates RNA-binding ability of HCV NS5A in a peptidyl-prolyl cis-trans isomerase activity-dependent manner. {ECO:0000269|PubMed:21593166}. |
P18621 | RPL17 | T29 | Sugiyama | Large ribosomal subunit protein uL22 (60S ribosomal protein L17) (60S ribosomal protein L23) (PD-1) | Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}. |
P68104 | EEF1A1 | T279 | Sugiyama | Elongation factor 1-alpha 1 (EF-1-alpha-1) (EC 3.6.5.-) (Elongation factor Tu) (EF-Tu) (Eukaryotic elongation factor 1 A-1) (eEF1A-1) (Leukocyte receptor cluster member 7) | Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623). Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976). Also plays a role in cytoskeleton organization by promoting actin bundling (By similarity). {ECO:0000250|UniProtKB:P68105, ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:26593721, ECO:0000269|PubMed:26651998, ECO:0000269|PubMed:36123449, ECO:0000269|PubMed:36264623, ECO:0000269|PubMed:36638793}.; FUNCTION: (Microbial infection) Required for the translation of viral proteins and viral replication during human coronavirus SARS-CoV-2 infection. {ECO:0000269|PubMed:33495306}. |
Q04637 | EIF4G1 | T718 | Sugiyama | Eukaryotic translation initiation factor 4 gamma 1 (eIF-4-gamma 1) (eIF-4G 1) (eIF-4G1) (p220) | Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:29987188). Exists in two complexes, either with EIF1 or with EIF4E (mutually exclusive) (PubMed:29987188). Together with EIF1, is required for leaky scanning, in particular for avoiding cap-proximal start codon (PubMed:29987188). Together with EIF4E, antagonizes the scanning promoted by EIF1-EIF4G1 and locates the start codon (through a TISU element) without scanning (PubMed:29987188). As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). {ECO:0000269|PubMed:29062139, ECO:0000269|PubMed:29987188}. |
Q5VTE0 | EEF1A1P5 | T279 | Sugiyama | Putative elongation factor 1-alpha-like 3 (EF-1-alpha-like 3) (Eukaryotic elongation factor 1 A-like 3) (eEF1A-like 3) (Eukaryotic translation elongation factor 1 alpha-1 pseudogene 5) | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. {ECO:0000250}. |
O76021 | RSL1D1 | T328 | Sugiyama | Ribosomal L1 domain-containing protein 1 (CATX-11) (Cellular senescence-inhibited gene protein) (Protein PBK1) | Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage. {ECO:0000269|PubMed:18678645, ECO:0000269|PubMed:22419112}. |
Q99575 | POP1 | T103 | Sugiyama | Ribonucleases P/MRP protein subunit POP1 (hPOP1) | Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:30454648, PubMed:8918471). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465). {ECO:0000269|PubMed:28115465, ECO:0000269|PubMed:30454648, ECO:0000269|PubMed:8918471}. |
Download
reactome_id | name | p | -log10_p |
---|---|---|---|
R-HSA-3371568 | Attenuation phase | 1.110223e-16 | 15.955 |
R-HSA-3371511 | HSF1 activation | 1.110223e-16 | 15.955 |
R-HSA-3371556 | Cellular response to heat stress | 1.110223e-16 | 15.955 |
R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | 1.110223e-16 | 15.955 |
R-HSA-3371571 | HSF1-dependent transactivation | 1.110223e-16 | 15.955 |
R-HSA-2262752 | Cellular responses to stress | 2.762235e-13 | 12.559 |
R-HSA-8953897 | Cellular responses to stimuli | 1.799672e-12 | 11.745 |
R-HSA-70171 | Glycolysis | 3.520599e-07 | 6.453 |
R-HSA-70326 | Glucose metabolism | 1.938995e-06 | 5.712 |
R-HSA-1169410 | Antiviral mechanism by IFN-stimulated genes | 5.757765e-06 | 5.240 |
R-HSA-165054 | Rev-mediated nuclear export of HIV RNA | 1.029718e-05 | 4.987 |
R-HSA-177243 | Interactions of Rev with host cellular proteins | 1.358683e-05 | 4.867 |
R-HSA-9841251 | Mitochondrial unfolded protein response (UPRmt) | 1.881575e-05 | 4.725 |
R-HSA-1640170 | Cell Cycle | 2.221178e-05 | 4.653 |
R-HSA-3371497 | HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig... | 3.887289e-05 | 4.410 |
R-HSA-69620 | Cell Cycle Checkpoints | 5.589068e-05 | 4.253 |
R-HSA-180746 | Nuclear import of Rev protein | 6.219704e-05 | 4.206 |
R-HSA-9614399 | Regulation of localization of FOXO transcription factors | 8.770034e-05 | 4.057 |
R-HSA-2980766 | Nuclear Envelope Breakdown | 1.030047e-04 | 3.987 |
R-HSA-75035 | Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex | 1.836133e-04 | 3.736 |
R-HSA-9679506 | SARS-CoV Infections | 1.879205e-04 | 3.726 |
R-HSA-9705683 | SARS-CoV-2-host interactions | 2.297209e-04 | 3.639 |
R-HSA-111447 | Activation of BAD and translocation to mitochondria | 2.793936e-04 | 3.554 |
R-HSA-168274 | Export of Viral Ribonucleoproteins from Nucleus | 2.730765e-04 | 3.564 |
R-HSA-9755779 | SARS-CoV-2 targets host intracellular signalling and regulatory pathways | 2.793936e-04 | 3.554 |
R-HSA-9735871 | SARS-CoV-1 targets host intracellular signalling and regulatory pathways | 2.793936e-04 | 3.554 |
R-HSA-5619107 | Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC... | 3.259582e-04 | 3.487 |
R-HSA-68886 | M Phase | 3.379402e-04 | 3.471 |
R-HSA-1855196 | IP3 and IP4 transport between cytosol and nucleus | 3.689953e-04 | 3.433 |
R-HSA-1855229 | IP6 and IP7 transport between cytosol and nucleus | 3.689953e-04 | 3.433 |
R-HSA-69473 | G2/M DNA damage checkpoint | 4.163284e-04 | 3.381 |
R-HSA-1855170 | IPs transport between nucleus and cytosol | 4.678075e-04 | 3.330 |
R-HSA-159227 | Transport of the SLBP independent Mature mRNA | 4.678075e-04 | 3.330 |
R-HSA-1169408 | ISG15 antiviral mechanism | 4.471269e-04 | 3.350 |
R-HSA-159230 | Transport of the SLBP Dependant Mature mRNA | 5.240988e-04 | 3.281 |
R-HSA-170822 | Regulation of Glucokinase by Glucokinase Regulatory Protein | 5.240988e-04 | 3.281 |
R-HSA-3301854 | Nuclear Pore Complex (NPC) Disassembly | 6.517846e-04 | 3.186 |
R-HSA-9692914 | SARS-CoV-1-host interactions | 7.394552e-04 | 3.131 |
R-HSA-68877 | Mitotic Prometaphase | 7.474406e-04 | 3.126 |
R-HSA-191859 | snRNP Assembly | 8.384820e-04 | 3.077 |
R-HSA-194441 | Metabolism of non-coding RNA | 8.384820e-04 | 3.077 |
R-HSA-180910 | Vpr-mediated nuclear import of PICs | 8.014454e-04 | 3.096 |
R-HSA-6798695 | Neutrophil degranulation | 8.455724e-04 | 3.073 |
R-HSA-141444 | Amplification of signal from unattached kinetochores via a MAD2 inhibitory si... | 9.214271e-04 | 3.036 |
R-HSA-141424 | Amplification of signal from the kinetochores | 9.214271e-04 | 3.036 |
R-HSA-159231 | Transport of Mature mRNA Derived from an Intronless Transcript | 9.753515e-04 | 3.011 |
R-HSA-168276 | NS1 Mediated Effects on Host Pathways | 9.753515e-04 | 3.011 |
R-HSA-159234 | Transport of Mature mRNAs Derived from Intronless Transcripts | 1.072124e-03 | 2.970 |
R-HSA-6784531 | tRNA processing in the nucleus | 1.048077e-03 | 2.980 |
R-HSA-176033 | Interactions of Vpr with host cellular proteins | 1.072124e-03 | 2.970 |
R-HSA-168271 | Transport of Ribonucleoproteins into the Host Nucleus | 1.175840e-03 | 2.930 |
R-HSA-8953854 | Metabolism of RNA | 1.544554e-03 | 2.811 |
R-HSA-69278 | Cell Cycle, Mitotic | 1.470332e-03 | 2.833 |
R-HSA-168333 | NEP/NS2 Interacts with the Cellular Export Machinery | 1.809190e-03 | 2.743 |
R-HSA-9675135 | Diseases of DNA repair | 1.960978e-03 | 2.708 |
R-HSA-162909 | Host Interactions of HIV factors | 1.971635e-03 | 2.705 |
R-HSA-159236 | Transport of Mature mRNA derived from an Intron-Containing Transcript | 2.175863e-03 | 2.662 |
R-HSA-69618 | Mitotic Spindle Checkpoint | 2.348246e-03 | 2.629 |
R-HSA-1445148 | Translocation of SLC2A4 (GLUT4) to the plasma membrane | 2.175863e-03 | 2.662 |
R-HSA-69481 | G2/M Checkpoints | 2.347155e-03 | 2.629 |
R-HSA-9709570 | Impaired BRCA2 binding to RAD51 | 2.634081e-03 | 2.579 |
R-HSA-114452 | Activation of BH3-only proteins | 2.911814e-03 | 2.536 |
R-HSA-6796648 | TP53 Regulates Transcription of DNA Repair Genes | 2.918144e-03 | 2.535 |
R-HSA-9694516 | SARS-CoV-2 Infection | 2.924105e-03 | 2.534 |
R-HSA-9833482 | PKR-mediated signaling | 3.262738e-03 | 2.486 |
R-HSA-72202 | Transport of Mature Transcript to Cytoplasm | 3.636791e-03 | 2.439 |
R-HSA-72203 | Processing of Capped Intron-Containing Pre-mRNA | 3.684394e-03 | 2.434 |
R-HSA-8876725 | Protein methylation | 3.754621e-03 | 2.425 |
R-HSA-446353 | Cell-extracellular matrix interactions | 3.754621e-03 | 2.425 |
R-HSA-9648025 | EML4 and NUDC in mitotic spindle formation | 3.757369e-03 | 2.425 |
R-HSA-9818035 | NFE2L2 regulating ER-stress associated genes | 4.352720e-03 | 2.361 |
R-HSA-9701190 | Defective homologous recombination repair (HRR) due to BRCA2 loss of function | 4.603805e-03 | 2.337 |
R-HSA-9675136 | Diseases of DNA Double-Strand Break Repair | 4.603805e-03 | 2.337 |
R-HSA-162599 | Late Phase of HIV Life Cycle | 4.779820e-03 | 2.321 |
R-HSA-5693616 | Presynaptic phase of homologous DNA pairing and strand exchange | 5.007180e-03 | 2.300 |
R-HSA-68882 | Mitotic Anaphase | 5.375419e-03 | 2.270 |
R-HSA-2028269 | Signaling by Hippo | 5.627087e-03 | 2.250 |
R-HSA-2555396 | Mitotic Metaphase and Anaphase | 5.531112e-03 | 2.257 |
R-HSA-168325 | Viral Messenger RNA Synthesis | 5.508123e-03 | 2.259 |
R-HSA-168255 | Influenza Infection | 5.227076e-03 | 2.282 |
R-HSA-1268020 | Mitochondrial protein import | 5.843640e-03 | 2.233 |
R-HSA-71737 | Pyrophosphate hydrolysis | 5.862358e-03 | 2.232 |
R-HSA-3700989 | Transcriptional Regulation by TP53 | 5.895054e-03 | 2.230 |
R-HSA-9613829 | Chaperone Mediated Autophagy | 6.354930e-03 | 2.197 |
R-HSA-5693579 | Homologous DNA Pairing and Strand Exchange | 6.357810e-03 | 2.197 |
R-HSA-68875 | Mitotic Prophase | 6.453739e-03 | 2.190 |
R-HSA-156842 | Eukaryotic Translation Elongation | 6.583831e-03 | 2.182 |
R-HSA-9709603 | Impaired BRCA2 binding to PALB2 | 7.136360e-03 | 2.147 |
R-HSA-72766 | Translation | 6.789720e-03 | 2.168 |
R-HSA-2500257 | Resolution of Sister Chromatid Cohesion | 6.708596e-03 | 2.173 |
R-HSA-168273 | Influenza Viral RNA Transcription and Replication | 7.493174e-03 | 2.125 |
R-HSA-8935964 | RUNX1 regulates expression of components of tight junctions | 7.576703e-03 | 2.121 |
R-HSA-9701193 | Defective homologous recombination repair (HRR) due to PALB2 loss of function | 7.972288e-03 | 2.098 |
R-HSA-9701192 | Defective homologous recombination repair (HRR) due to BRCA1 loss of function | 7.972288e-03 | 2.098 |
R-HSA-9704646 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 7.972288e-03 | 2.098 |
R-HSA-9704331 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 7.972288e-03 | 2.098 |
R-HSA-162587 | HIV Life Cycle | 7.996576e-03 | 2.097 |
R-HSA-210991 | Basigin interactions | 8.863538e-03 | 2.052 |
R-HSA-8869496 | TFAP2A acts as a transcriptional repressor during retinoic acid induced cell dif... | 9.488890e-03 | 2.023 |
R-HSA-450531 | Regulation of mRNA stability by proteins that bind AU-rich elements | 1.002588e-02 | 1.999 |
R-HSA-5578749 | Transcriptional regulation by small RNAs | 1.002588e-02 | 1.999 |
R-HSA-8949215 | Mitochondrial calcium ion transport | 9.810849e-03 | 2.008 |
R-HSA-1280215 | Cytokine Signaling in Immune system | 1.071423e-02 | 1.970 |
R-HSA-9824446 | Viral Infection Pathways | 1.104544e-02 | 1.957 |
R-HSA-9633012 | Response of EIF2AK4 (GCN2) to amino acid deficiency | 1.140989e-02 | 1.943 |
R-HSA-447041 | CHL1 interactions | 1.159222e-02 | 1.936 |
R-HSA-5336415 | Uptake and function of diphtheria toxin | 1.159222e-02 | 1.936 |
R-HSA-9648895 | Response of EIF2AK1 (HRI) to heme deficiency | 1.187622e-02 | 1.925 |
R-HSA-5693554 | Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD... | 1.417279e-02 | 1.849 |
R-HSA-72706 | GTP hydrolysis and joining of the 60S ribosomal subunit | 1.380033e-02 | 1.860 |
R-HSA-9615933 | Postmitotic nuclear pore complex (NPC) reformation | 1.540882e-02 | 1.812 |
R-HSA-156827 | L13a-mediated translational silencing of Ceruloplasmin expression | 1.380033e-02 | 1.860 |
R-HSA-2995410 | Nuclear Envelope (NE) Reassembly | 1.458281e-02 | 1.836 |
R-HSA-70263 | Gluconeogenesis | 1.331281e-02 | 1.876 |
R-HSA-381119 | Unfolded Protein Response (UPR) | 1.396660e-02 | 1.855 |
R-HSA-9700206 | Signaling by ALK in cancer | 1.329653e-02 | 1.876 |
R-HSA-9725370 | Signaling by ALK fusions and activated point mutants | 1.329653e-02 | 1.876 |
R-HSA-913531 | Interferon Signaling | 1.476889e-02 | 1.831 |
R-HSA-9678108 | SARS-CoV-1 Infection | 1.413022e-02 | 1.850 |
R-HSA-9613354 | Lipophagy | 1.634631e-02 | 1.787 |
R-HSA-5339562 | Uptake and actions of bacterial toxins | 1.670257e-02 | 1.777 |
R-HSA-445355 | Smooth Muscle Contraction | 1.762668e-02 | 1.754 |
R-HSA-1500620 | Meiosis | 1.804133e-02 | 1.744 |
R-HSA-390450 | Folding of actin by CCT/TriC | 1.898446e-02 | 1.722 |
R-HSA-428359 | Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RN... | 1.898446e-02 | 1.722 |
R-HSA-72737 | Cap-dependent Translation Initiation | 1.958959e-02 | 1.708 |
R-HSA-72613 | Eukaryotic Translation Initiation | 1.958959e-02 | 1.708 |
R-HSA-1592230 | Mitochondrial biogenesis | 2.024698e-02 | 1.694 |
R-HSA-109606 | Intrinsic Pathway for Apoptosis | 2.058776e-02 | 1.686 |
R-HSA-156902 | Peptide chain elongation | 2.116888e-02 | 1.674 |
R-HSA-6791312 | TP53 Regulates Transcription of Cell Cycle Genes | 2.163857e-02 | 1.665 |
R-HSA-1852241 | Organelle biogenesis and maintenance | 2.303748e-02 | 1.638 |
R-HSA-2514853 | Condensation of Prometaphase Chromosomes | 2.475262e-02 | 1.606 |
R-HSA-5693537 | Resolution of D-Loop Structures | 2.743137e-02 | 1.562 |
R-HSA-5693568 | Resolution of D-loop Structures through Holliday Junction Intermediates | 2.572041e-02 | 1.590 |
R-HSA-5685938 | HDR through Single Strand Annealing (SSA) | 2.572041e-02 | 1.590 |
R-HSA-418359 | Reduction of cytosolic Ca++ levels | 2.475262e-02 | 1.606 |
R-HSA-379724 | tRNA Aminoacylation | 2.498546e-02 | 1.602 |
R-HSA-9837999 | Mitochondrial protein degradation | 2.745222e-02 | 1.561 |
R-HSA-109581 | Apoptosis | 2.770943e-02 | 1.557 |
R-HSA-2467813 | Separation of Sister Chromatids | 2.916123e-02 | 1.535 |
R-HSA-5357801 | Programmed Cell Death | 3.057568e-02 | 1.515 |
R-HSA-381042 | PERK regulates gene expression | 3.103099e-02 | 1.508 |
R-HSA-187687 | Signalling to ERKs | 3.103099e-02 | 1.508 |
R-HSA-8950505 | Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulati... | 3.122260e-02 | 1.506 |
R-HSA-5619102 | SLC transporter disorders | 3.143405e-02 | 1.503 |
R-HSA-168256 | Immune System | 3.151171e-02 | 1.502 |
R-HSA-5545483 | Defective Mismatch Repair Associated With MLH1 | 3.165797e-02 | 1.500 |
R-HSA-9709275 | Impaired BRCA2 translocation to the nucleus | 3.165797e-02 | 1.500 |
R-HSA-9763198 | Impaired BRCA2 binding to SEM1 (DSS1) | 3.165797e-02 | 1.500 |
R-HSA-5632987 | Defective Mismatch Repair Associated With PMS2 | 3.165797e-02 | 1.500 |
R-HSA-450408 | AUF1 (hnRNP D0) binds and destabilizes mRNA | 3.291923e-02 | 1.483 |
R-HSA-5685942 | HDR through Homologous Recombination (HRR) | 3.395126e-02 | 1.469 |
R-HSA-9933939 | Formation of the polybromo-BAF (pBAF) complex | 3.454782e-02 | 1.462 |
R-HSA-9856872 | Malate-aspartate shuttle | 3.454782e-02 | 1.462 |
R-HSA-72306 | tRNA processing | 3.464535e-02 | 1.460 |
R-HSA-399954 | Sema3A PAK dependent Axon repulsion | 3.809554e-02 | 1.419 |
R-HSA-450385 | Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA | 3.809554e-02 | 1.419 |
R-HSA-450513 | Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA | 3.809554e-02 | 1.419 |
R-HSA-6804114 | TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest | 4.558340e-02 | 1.341 |
R-HSA-5675221 | Negative regulation of MAPK pathway | 4.546786e-02 | 1.342 |
R-HSA-202433 | Generation of second messenger molecules | 4.105520e-02 | 1.387 |
R-HSA-171007 | p38MAPK events | 3.809554e-02 | 1.419 |
R-HSA-199991 | Membrane Trafficking | 4.400570e-02 | 1.356 |
R-HSA-71387 | Metabolism of carbohydrates and carbohydrate derivatives | 4.605051e-02 | 1.337 |
R-HSA-9705671 | SARS-CoV-2 activates/modulates innate and adaptive immune responses | 4.623922e-02 | 1.335 |
R-HSA-9856649 | Transcriptional and post-translational regulation of MITF-M expression and activ... | 3.981307e-02 | 1.400 |
R-HSA-211000 | Gene Silencing by RNA | 4.458876e-02 | 1.351 |
R-HSA-9915355 | Beta-ketothiolase deficiency | 4.711054e-02 | 1.327 |
R-HSA-5619056 | Defective HK1 causes hexokinase deficiency (HK deficiency) | 4.711054e-02 | 1.327 |
R-HSA-163282 | Mitochondrial transcription initiation | 4.711054e-02 | 1.327 |
R-HSA-9636667 | Manipulation of host energy metabolism | 4.711054e-02 | 1.327 |
R-HSA-352238 | Breakdown of the nuclear lamina | 4.711054e-02 | 1.327 |
R-HSA-379716 | Cytosolic tRNA aminoacylation | 4.775884e-02 | 1.321 |
R-HSA-165159 | MTOR signalling | 4.775884e-02 | 1.321 |
R-HSA-9020591 | Interleukin-12 signaling | 4.790081e-02 | 1.320 |
R-HSA-162906 | HIV Infection | 4.816593e-02 | 1.317 |
R-HSA-5210891 | Uptake and function of anthrax toxins | 4.951347e-02 | 1.305 |
R-HSA-1483249 | Inositol phosphate metabolism | 5.145471e-02 | 1.289 |
R-HSA-8864260 | Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors | 5.250759e-02 | 1.280 |
R-HSA-9665230 | Drug resistance in ERBB2 KD mutants | 6.231746e-02 | 1.205 |
R-HSA-9652282 | Drug-mediated inhibition of ERBB2 signaling | 6.231746e-02 | 1.205 |
R-HSA-9665247 | Resistance of ERBB2 KD mutants to osimertinib | 6.231746e-02 | 1.205 |
R-HSA-9665250 | Resistance of ERBB2 KD mutants to AEE788 | 6.231746e-02 | 1.205 |
R-HSA-3656535 | TGFBR1 LBD Mutants in Cancer | 6.231746e-02 | 1.205 |
R-HSA-3645790 | TGFBR2 Kinase Domain Mutants in Cancer | 6.231746e-02 | 1.205 |
R-HSA-9665244 | Resistance of ERBB2 KD mutants to sapitinib | 6.231746e-02 | 1.205 |
R-HSA-9665737 | Drug resistance in ERBB2 TMD/JMD mutants | 6.231746e-02 | 1.205 |
R-HSA-9665245 | Resistance of ERBB2 KD mutants to tesevatinib | 6.231746e-02 | 1.205 |
R-HSA-9665251 | Resistance of ERBB2 KD mutants to lapatinib | 6.231746e-02 | 1.205 |
R-HSA-9665233 | Resistance of ERBB2 KD mutants to trastuzumab | 6.231746e-02 | 1.205 |
R-HSA-9665246 | Resistance of ERBB2 KD mutants to neratinib | 6.231746e-02 | 1.205 |
R-HSA-9665249 | Resistance of ERBB2 KD mutants to afatinib | 6.231746e-02 | 1.205 |
R-HSA-9711097 | Cellular response to starvation | 6.676186e-02 | 1.175 |
R-HSA-3642278 | Loss of Function of TGFBR2 in Cancer | 6.231746e-02 | 1.205 |
R-HSA-446343 | Localization of the PINCH-ILK-PARVIN complex to focal adhesions | 6.231746e-02 | 1.205 |
R-HSA-1839117 | Signaling by cytosolic FGFR1 fusion mutants | 5.356115e-02 | 1.271 |
R-HSA-9612973 | Autophagy | 6.394710e-02 | 1.194 |
R-HSA-75944 | Transcription from mitochondrial promoters | 6.231746e-02 | 1.205 |
R-HSA-4419969 | Depolymerization of the Nuclear Lamina | 5.356115e-02 | 1.271 |
R-HSA-5620922 | BBSome-mediated cargo-targeting to cilium | 6.199052e-02 | 1.208 |
R-HSA-70268 | Pyruvate metabolism | 7.072275e-02 | 1.150 |
R-HSA-445144 | Signal transduction by L1 | 6.199052e-02 | 1.208 |
R-HSA-9679191 | Potential therapeutics for SARS | 5.593130e-02 | 1.252 |
R-HSA-2151201 | Transcriptional activation of mitochondrial biogenesis | 5.683016e-02 | 1.245 |
R-HSA-1912420 | Pre-NOTCH Processing in Golgi | 5.772170e-02 | 1.239 |
R-HSA-5628897 | TP53 Regulates Metabolic Genes | 5.736887e-02 | 1.241 |
R-HSA-167044 | Signalling to RAS | 6.636314e-02 | 1.178 |
R-HSA-6804756 | Regulation of TP53 Activity through Phosphorylation | 6.864025e-02 | 1.163 |
R-HSA-381038 | XBP1(S) activates chaperone genes | 6.864025e-02 | 1.163 |
R-HSA-447115 | Interleukin-12 family signaling | 7.072275e-02 | 1.150 |
R-HSA-450302 | activated TAK1 mediates p38 MAPK activation | 7.083518e-02 | 1.150 |
R-HSA-2995383 | Initiation of Nuclear Envelope (NE) Reformation | 7.083518e-02 | 1.150 |
R-HSA-9663891 | Selective autophagy | 7.283741e-02 | 1.138 |
R-HSA-9938206 | Developmental Lineage of Mammary Stem Cells | 7.540238e-02 | 1.123 |
R-HSA-166208 | mTORC1-mediated signalling | 7.540238e-02 | 1.123 |
R-HSA-6804115 | TP53 regulates transcription of additional cell cycle genes whose exact role in ... | 7.540238e-02 | 1.123 |
R-HSA-1221632 | Meiotic synapsis | 7.651248e-02 | 1.116 |
R-HSA-9673766 | Signaling by cytosolic PDGFRA and PDGFRB fusion proteins | 7.728262e-02 | 1.112 |
R-HSA-9734281 | Defective HPRT1 disrupts guanine and hypoxanthine salvage | 7.728262e-02 | 1.112 |
R-HSA-5660862 | Defective SLC7A7 causes lysinuric protein intolerance (LPI) | 7.728262e-02 | 1.112 |
R-HSA-8875513 | MET interacts with TNS proteins | 7.728262e-02 | 1.112 |
R-HSA-5423599 | Diseases of Mismatch Repair (MMR) | 7.728262e-02 | 1.112 |
R-HSA-72649 | Translation initiation complex formation | 7.943274e-02 | 1.100 |
R-HSA-3000170 | Syndecan interactions | 8.006060e-02 | 1.097 |
R-HSA-389957 | Prefoldin mediated transfer of substrate to CCT/TriC | 8.006060e-02 | 1.097 |
R-HSA-975956 | Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) | 8.161341e-02 | 1.088 |
R-HSA-381070 | IRE1alpha activates chaperones | 8.161341e-02 | 1.088 |
R-HSA-397014 | Muscle contraction | 8.312957e-02 | 1.080 |
R-HSA-389960 | Formation of tubulin folding intermediates by CCT/TriC | 8.480579e-02 | 1.072 |
R-HSA-72702 | Ribosomal scanning and start codon recognition | 8.541649e-02 | 1.068 |
R-HSA-9013957 | TLR3-mediated TICAM1-dependent programmed cell death | 9.200984e-02 | 1.036 |
R-HSA-3656532 | TGFBR1 KD Mutants in Cancer | 9.200984e-02 | 1.036 |
R-HSA-3656534 | Loss of Function of TGFBR1 in Cancer | 1.065029e-01 | 0.973 |
R-HSA-3304356 | SMAD2/3 Phosphorylation Motif Mutants in Cancer | 1.065029e-01 | 0.973 |
R-HSA-164525 | Plus-strand DNA synthesis | 1.207655e-01 | 0.918 |
R-HSA-9645135 | STAT5 Activation | 1.348013e-01 | 0.870 |
R-HSA-9027283 | Erythropoietin activates STAT5 | 1.348013e-01 | 0.870 |
R-HSA-162585 | Uncoating of the HIV Virion | 1.348013e-01 | 0.870 |
R-HSA-2562578 | TRIF-mediated programmed cell death | 1.486139e-01 | 0.828 |
R-HSA-72731 | Recycling of eIF2:GDP | 1.486139e-01 | 0.828 |
R-HSA-9726840 | SHOC2 M1731 mutant abolishes MRAS complex function | 1.486139e-01 | 0.828 |
R-HSA-162589 | Reverse Transcription of HIV RNA | 1.622068e-01 | 0.790 |
R-HSA-164516 | Minus-strand DNA synthesis | 1.622068e-01 | 0.790 |
R-HSA-9660537 | Signaling by MRAS-complex mutants | 1.622068e-01 | 0.790 |
R-HSA-9726842 | Gain-of-function MRAS complexes activate RAF signaling | 1.622068e-01 | 0.790 |
R-HSA-5218900 | CASP8 activity is inhibited | 1.755835e-01 | 0.756 |
R-HSA-9700645 | ALK mutants bind TKIs | 1.755835e-01 | 0.756 |
R-HSA-173107 | Binding and entry of HIV virion | 1.887475e-01 | 0.724 |
R-HSA-933543 | NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 | 2.017020e-01 | 0.695 |
R-HSA-5358493 | Synthesis of diphthamide-EEF2 | 2.144505e-01 | 0.669 |
R-HSA-9931512 | Phosphorylation of CLOCK, acetylation of BMAL1 (ARNTL) at target gene promoters | 2.144505e-01 | 0.669 |
R-HSA-9932451 | SWI/SNF chromatin remodelers | 8.963402e-02 | 1.048 |
R-HSA-9932444 | ATP-dependent chromatin remodelers | 8.963402e-02 | 1.048 |
R-HSA-9820865 | Z-decay: degradation of maternal mRNAs by zygotically expressed factors | 2.269962e-01 | 0.644 |
R-HSA-3656253 | Defective EXT1 causes exostoses 1, TRPS2 and CHDS | 2.269962e-01 | 0.644 |
R-HSA-3656237 | Defective EXT2 causes exostoses 2 | 2.269962e-01 | 0.644 |
R-HSA-3000484 | Scavenging by Class F Receptors | 2.269962e-01 | 0.644 |
R-HSA-8949613 | Cristae formation | 9.952437e-02 | 1.002 |
R-HSA-9933947 | Formation of the non-canonical BAF (ncBAF) complex | 2.393422e-01 | 0.621 |
R-HSA-9927432 | Developmental Lineage of Mammary Gland Myoepithelial Cells | 1.097022e-01 | 0.960 |
R-HSA-9933937 | Formation of the canonical BAF (cBAF) complex | 2.514919e-01 | 0.599 |
R-HSA-2173791 | TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) | 2.634482e-01 | 0.579 |
R-HSA-9933946 | Formation of the embryonic stem cell BAF (esBAF) complex | 2.634482e-01 | 0.579 |
R-HSA-168927 | TICAM1, RIP1-mediated IKK complex recruitment | 2.634482e-01 | 0.579 |
R-HSA-390522 | Striated Muscle Contraction | 1.362245e-01 | 0.866 |
R-HSA-390471 | Association of TriC/CCT with target proteins during biosynthesis | 1.362245e-01 | 0.866 |
R-HSA-6802952 | Signaling by BRAF and RAF1 fusions | 1.145508e-01 | 0.941 |
R-HSA-72689 | Formation of a pool of free 40S subunits | 9.328037e-02 | 1.030 |
R-HSA-9649948 | Signaling downstream of RAS mutants | 2.159453e-01 | 0.666 |
R-HSA-72165 | mRNA Splicing - Minor Pathway | 2.159453e-01 | 0.666 |
R-HSA-72695 | Formation of the ternary complex, and subsequently, the 43S complex | 2.159453e-01 | 0.666 |
R-HSA-927802 | Nonsense-Mediated Decay (NMD) | 1.411678e-01 | 0.850 |
R-HSA-975957 | Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) | 1.411678e-01 | 0.850 |
R-HSA-9954714 | PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA | 2.184961e-01 | 0.661 |
R-HSA-9954716 | ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri... | 2.395576e-01 | 0.621 |
R-HSA-72172 | mRNA Splicing | 1.549134e-01 | 0.810 |
R-HSA-72163 | mRNA Splicing - Major Pathway | 2.599200e-01 | 0.585 |
R-HSA-9656223 | Signaling by RAF1 mutants | 1.868256e-01 | 0.729 |
R-HSA-6802955 | Paradoxical activation of RAF signaling by kinase inactive BRAF | 2.159453e-01 | 0.666 |
R-HSA-6802946 | Signaling by moderate kinase activity BRAF mutants | 2.159453e-01 | 0.666 |
R-HSA-9948299 | Ribosome-associated quality control | 2.404049e-01 | 0.619 |
R-HSA-389958 | Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding | 1.201395e-01 | 0.920 |
R-HSA-72662 | Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub... | 9.158606e-02 | 1.038 |
R-HSA-6802957 | Oncogenic MAPK signaling | 1.897342e-01 | 0.722 |
R-HSA-6802949 | Signaling by RAS mutants | 2.159453e-01 | 0.666 |
R-HSA-9954709 | Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide | 9.328037e-02 | 1.030 |
R-HSA-5213460 | RIPK1-mediated regulated necrosis | 1.639751e-01 | 0.785 |
R-HSA-191650 | Regulation of gap junction activity | 9.200984e-02 | 1.036 |
R-HSA-163680 | AMPK inhibits chREBP transcriptional activation activity | 1.755835e-01 | 0.756 |
R-HSA-5205685 | PINK1-PRKN Mediated Mitophagy | 1.045791e-01 | 0.981 |
R-HSA-6814122 | Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding | 1.416882e-01 | 0.849 |
R-HSA-8857538 | PTK6 promotes HIF1A stabilization | 1.348013e-01 | 0.870 |
R-HSA-180689 | APOBEC3G mediated resistance to HIV-1 infection | 2.144505e-01 | 0.669 |
R-HSA-5675482 | Regulation of necroptotic cell death | 1.308098e-01 | 0.883 |
R-HSA-6802948 | Signaling by high-kinase activity BRAF mutants | 1.583441e-01 | 0.800 |
R-HSA-5674135 | MAP2K and MAPK activation | 1.868256e-01 | 0.729 |
R-HSA-9927418 | Developmental Lineage of Mammary Gland Luminal Epithelial Cells | 1.926077e-01 | 0.715 |
R-HSA-5693567 | HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA) | 1.470029e-01 | 0.833 |
R-HSA-5357905 | Regulation of TNFR1 signaling | 2.159453e-01 | 0.666 |
R-HSA-9692913 | SARS-CoV-1-mediated effects on programmed cell death | 9.200984e-02 | 1.036 |
R-HSA-3134973 | LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production | 1.065029e-01 | 0.973 |
R-HSA-8937144 | Aryl hydrocarbon receptor signalling | 1.207655e-01 | 0.918 |
R-HSA-72764 | Eukaryotic Translation Termination | 2.438117e-01 | 0.613 |
R-HSA-3304351 | Signaling by TGF-beta Receptor Complex in Cancer | 1.348013e-01 | 0.870 |
R-HSA-5693538 | Homology Directed Repair | 1.650500e-01 | 0.782 |
R-HSA-5205647 | Mitophagy | 1.416882e-01 | 0.849 |
R-HSA-9705677 | SARS-CoV-2 targets PDZ proteins in cell-cell junction | 9.200984e-02 | 1.036 |
R-HSA-3304349 | Loss of Function of SMAD2/3 in Cancer | 1.207655e-01 | 0.918 |
R-HSA-351143 | Agmatine biosynthesis | 1.348013e-01 | 0.870 |
R-HSA-446107 | Type I hemidesmosome assembly | 1.622068e-01 | 0.790 |
R-HSA-3371378 | Regulation by c-FLIP | 1.622068e-01 | 0.790 |
R-HSA-176974 | Unwinding of DNA | 1.755835e-01 | 0.756 |
R-HSA-379398 | Enzymatic degradation of Dopamine by monoamine oxidase | 1.755835e-01 | 0.756 |
R-HSA-9693928 | Defective RIPK1-mediated regulated necrosis | 1.887475e-01 | 0.724 |
R-HSA-379397 | Enzymatic degradation of dopamine by COMT | 1.887475e-01 | 0.724 |
R-HSA-2468052 | Establishment of Sister Chromatid Cohesion | 1.887475e-01 | 0.724 |
R-HSA-2151209 | Activation of PPARGC1A (PGC-1alpha) by phosphorylation | 1.887475e-01 | 0.724 |
R-HSA-9634285 | Constitutive Signaling by Overexpressed ERBB2 | 2.269962e-01 | 0.644 |
R-HSA-1810476 | RIP-mediated NFkB activation via ZBP1 | 2.634482e-01 | 0.579 |
R-HSA-9609690 | HCMV Early Events | 1.355427e-01 | 0.868 |
R-HSA-9860927 | Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZ... | 1.471979e-01 | 0.832 |
R-HSA-5693607 | Processing of DNA double-strand break ends | 1.737712e-01 | 0.760 |
R-HSA-170968 | Frs2-mediated activation | 2.393422e-01 | 0.621 |
R-HSA-9686347 | Microbial modulation of RIPK1-mediated regulated necrosis | 1.486139e-01 | 0.828 |
R-HSA-176187 | Activation of ATR in response to replication stress | 1.308098e-01 | 0.883 |
R-HSA-2173789 | TGF-beta receptor signaling activates SMADs | 1.984128e-01 | 0.702 |
R-HSA-9020958 | Interleukin-21 signaling | 1.755835e-01 | 0.756 |
R-HSA-9754560 | SARS-CoV-2 modulates autophagy | 2.017020e-01 | 0.695 |
R-HSA-381183 | ATF6 (ATF6-alpha) activates chaperone genes | 2.144505e-01 | 0.669 |
R-HSA-912446 | Meiotic recombination | 2.454357e-01 | 0.610 |
R-HSA-983189 | Kinesins | 9.793517e-02 | 1.009 |
R-HSA-69416 | Dimerization of procaspase-8 | 1.622068e-01 | 0.790 |
R-HSA-9734207 | Nucleotide salvage defects | 1.622068e-01 | 0.790 |
R-HSA-170984 | ARMS-mediated activation | 1.755835e-01 | 0.756 |
R-HSA-2025928 | Calcineurin activates NFAT | 1.755835e-01 | 0.756 |
R-HSA-1433617 | Regulation of signaling by NODAL | 1.755835e-01 | 0.756 |
R-HSA-77108 | Utilization of Ketone Bodies | 2.017020e-01 | 0.695 |
R-HSA-1483226 | Synthesis of PI | 2.017020e-01 | 0.695 |
R-HSA-168330 | Viral RNP Complexes in the Host Cell Nucleus | 2.144505e-01 | 0.669 |
R-HSA-379401 | Dopamine clearance from the synaptic cleft | 2.634482e-01 | 0.579 |
R-HSA-8985947 | Interleukin-9 signaling | 1.622068e-01 | 0.790 |
R-HSA-1502540 | Signaling by Activin | 2.634482e-01 | 0.579 |
R-HSA-6811438 | Intra-Golgi traffic | 1.868256e-01 | 0.729 |
R-HSA-8983432 | Interleukin-15 signaling | 2.269962e-01 | 0.644 |
R-HSA-5655302 | Signaling by FGFR1 in disease | 1.868256e-01 | 0.729 |
R-HSA-1839124 | FGFR1 mutant receptor activation | 1.308098e-01 | 0.883 |
R-HSA-5663202 | Diseases of signal transduction by growth factor receptors and second messengers | 1.582625e-01 | 0.801 |
R-HSA-5693532 | DNA Double-Strand Break Repair | 1.436559e-01 | 0.843 |
R-HSA-2586552 | Signaling by Leptin | 1.887475e-01 | 0.724 |
R-HSA-9020558 | Interleukin-2 signaling | 2.017020e-01 | 0.695 |
R-HSA-1632852 | Macroautophagy | 2.507897e-01 | 0.601 |
R-HSA-199920 | CREB phosphorylation | 1.348013e-01 | 0.870 |
R-HSA-390696 | Adrenoceptors | 1.622068e-01 | 0.790 |
R-HSA-9820962 | Assembly and release of respiratory syncytial virus (RSV) virions | 1.887475e-01 | 0.724 |
R-HSA-428540 | Activation of RAC1 | 2.144505e-01 | 0.669 |
R-HSA-446205 | Synthesis of GDP-mannose | 2.269962e-01 | 0.644 |
R-HSA-3214841 | PKMTs methylate histone lysines | 1.810690e-01 | 0.742 |
R-HSA-8856688 | Golgi-to-ER retrograde transport | 2.165980e-01 | 0.664 |
R-HSA-5617833 | Cilium Assembly | 2.479227e-01 | 0.606 |
R-HSA-202403 | TCR signaling | 1.354280e-01 | 0.868 |
R-HSA-446388 | Regulation of cytoskeletal remodeling and cell spreading by IPP complex componen... | 1.207655e-01 | 0.918 |
R-HSA-9834752 | Respiratory syncytial virus genome replication | 1.755835e-01 | 0.756 |
R-HSA-381033 | ATF6 (ATF6-alpha) activates chaperones | 2.393422e-01 | 0.621 |
R-HSA-9735804 | Diseases of nucleotide metabolism | 2.393422e-01 | 0.621 |
R-HSA-8939243 | RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not kno... | 1.308098e-01 | 0.883 |
R-HSA-9609507 | Protein localization | 1.436559e-01 | 0.843 |
R-HSA-9861718 | Regulation of pyruvate metabolism | 2.159453e-01 | 0.666 |
R-HSA-1474165 | Reproduction | 8.858029e-02 | 1.053 |
R-HSA-6811434 | COPI-dependent Golgi-to-ER retrograde traffic | 2.480780e-01 | 0.605 |
R-HSA-9840373 | Cellular response to mitochondrial stress | 1.755835e-01 | 0.756 |
R-HSA-389359 | CD28 dependent Vav1 pathway | 2.393422e-01 | 0.621 |
R-HSA-5687128 | MAPK6/MAPK4 signaling | 1.897342e-01 | 0.722 |
R-HSA-373755 | Semaphorin interactions | 1.077813e-01 | 0.967 |
R-HSA-6811442 | Intra-Golgi and retrograde Golgi-to-ER traffic | 1.440042e-01 | 0.842 |
R-HSA-162592 | Integration of provirus | 2.144505e-01 | 0.669 |
R-HSA-1170546 | Prolactin receptor signaling | 2.514919e-01 | 0.599 |
R-HSA-9828642 | Respiratory syncytial virus genome transcription | 2.514919e-01 | 0.599 |
R-HSA-392499 | Metabolism of proteins | 1.728551e-01 | 0.762 |
R-HSA-3214858 | RMTs methylate histone arginines | 2.042389e-01 | 0.690 |
R-HSA-5653656 | Vesicle-mediated transport | 1.229192e-01 | 0.910 |
R-HSA-1643685 | Disease | 1.097176e-01 | 0.960 |
R-HSA-1428517 | Aerobic respiration and respiratory electron transport | 1.310145e-01 | 0.883 |
R-HSA-9839389 | TGFBR3 regulates TGF-beta signaling | 1.486139e-01 | 0.828 |
R-HSA-5685939 | HDR through MMEJ (alt-NHEJ) | 2.393422e-01 | 0.621 |
R-HSA-75892 | Platelet Adhesion to exposed collagen | 2.393422e-01 | 0.621 |
R-HSA-418360 | Platelet calcium homeostasis | 1.097022e-01 | 0.960 |
R-HSA-1650814 | Collagen biosynthesis and modifying enzymes | 1.249965e-01 | 0.903 |
R-HSA-9662834 | CD163 mediating an anti-inflammatory response | 2.017020e-01 | 0.695 |
R-HSA-416700 | Other semaphorin interactions | 2.634482e-01 | 0.579 |
R-HSA-9748787 | Azathioprine ADME | 2.395195e-01 | 0.621 |
R-HSA-162582 | Signal Transduction | 1.194982e-01 | 0.923 |
R-HSA-9610379 | HCMV Late Events | 1.536005e-01 | 0.814 |
R-HSA-5620920 | Cargo trafficking to the periciliary membrane | 1.357715e-01 | 0.867 |
R-HSA-351906 | Apoptotic cleavage of cell adhesion proteins | 1.622068e-01 | 0.790 |
R-HSA-9842663 | Signaling by LTK | 2.269962e-01 | 0.644 |
R-HSA-5689880 | Ub-specific processing proteases | 1.988050e-01 | 0.702 |
R-HSA-9607240 | FLT3 Signaling | 1.810690e-01 | 0.742 |
R-HSA-5663205 | Infectious disease | 1.164919e-01 | 0.934 |
R-HSA-1474290 | Collagen formation | 8.852238e-02 | 1.053 |
R-HSA-2408522 | Selenoamino acid metabolism | 1.716661e-01 | 0.765 |
R-HSA-446728 | Cell junction organization | 2.066365e-01 | 0.685 |
R-HSA-449147 | Signaling by Interleukins | 1.612494e-01 | 0.793 |
R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | 1.273257e-01 | 0.895 |
R-HSA-9768919 | NPAS4 regulates expression of target genes | 1.416882e-01 | 0.849 |
R-HSA-111465 | Apoptotic cleavage of cellular proteins | 1.254471e-01 | 0.902 |
R-HSA-9634815 | Transcriptional Regulation by NPAS4 | 2.513574e-01 | 0.600 |
R-HSA-2132295 | MHC class II antigen presentation | 1.806640e-01 | 0.743 |
R-HSA-75153 | Apoptotic execution phase | 2.159453e-01 | 0.666 |
R-HSA-5619115 | Disorders of transmembrane transporters | 1.418438e-01 | 0.848 |
R-HSA-9692916 | SARS-CoV-1 activates/modulates innate immune responses | 2.513574e-01 | 0.600 |
R-HSA-9725371 | Nuclear events stimulated by ALK signaling in cancer | 2.277107e-01 | 0.643 |
R-HSA-9820965 | Respiratory syncytial virus (RSV) genome replication, transcription and translat... | 1.696413e-01 | 0.770 |
R-HSA-9614085 | FOXO-mediated transcription | 1.031514e-01 | 0.987 |
R-HSA-9609646 | HCMV Infection | 2.695159e-01 | 0.569 |
R-HSA-2408557 | Selenocysteine synthesis | 2.695676e-01 | 0.569 |
R-HSA-75893 | TNF signaling | 2.750665e-01 | 0.561 |
R-HSA-5578775 | Ion homeostasis | 2.750665e-01 | 0.561 |
R-HSA-140534 | Caspase activation via Death Receptors in the presence of ligand | 2.752142e-01 | 0.560 |
R-HSA-169893 | Prolonged ERK activation events | 2.752142e-01 | 0.560 |
R-HSA-9706369 | Negative regulation of FLT3 | 2.752142e-01 | 0.560 |
R-HSA-192823 | Viral mRNA Translation | 2.782242e-01 | 0.556 |
R-HSA-8964616 | G beta:gamma signalling through CDC42 | 2.867930e-01 | 0.542 |
R-HSA-4420332 | Defective B3GALT6 causes EDSP2 and SEMDJL1 | 2.867930e-01 | 0.542 |
R-HSA-3560783 | Defective B4GALT7 causes EDS, progeroid type | 2.867930e-01 | 0.542 |
R-HSA-9702518 | STAT5 activation downstream of FLT3 ITD mutants | 2.867930e-01 | 0.542 |
R-HSA-9931521 | The CRY:PER:kinase complex represses transactivation by the BMAL:CLOCK (ARNTL:CL... | 2.867930e-01 | 0.542 |
R-HSA-1566977 | Fibronectin matrix formation | 2.867930e-01 | 0.542 |
R-HSA-376176 | Signaling by ROBO receptors | 2.873831e-01 | 0.542 |
R-HSA-168164 | Toll Like Receptor 3 (TLR3) Cascade | 2.912573e-01 | 0.536 |
R-HSA-9010553 | Regulation of expression of SLITs and ROBOs | 2.931626e-01 | 0.533 |
R-HSA-1500931 | Cell-Cell communication | 2.979948e-01 | 0.526 |
R-HSA-3560801 | Defective B3GAT3 causes JDSSDHD | 2.981875e-01 | 0.526 |
R-HSA-5637810 | Constitutive Signaling by EGFRvIII | 2.981875e-01 | 0.526 |
R-HSA-5637812 | Signaling by EGFRvIII in Cancer | 2.981875e-01 | 0.526 |
R-HSA-5358565 | Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) | 2.981875e-01 | 0.526 |
R-HSA-5358606 | Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) | 2.981875e-01 | 0.526 |
R-HSA-8873719 | RAB geranylgeranylation | 2.987389e-01 | 0.525 |
R-HSA-9764725 | Negative Regulation of CDH1 Gene Transcription | 2.987389e-01 | 0.525 |
R-HSA-1799339 | SRP-dependent cotranslational protein targeting to membrane | 2.999706e-01 | 0.523 |
R-HSA-450294 | MAP kinase activation | 3.046408e-01 | 0.516 |
R-HSA-5358508 | Mismatch Repair | 3.094007e-01 | 0.509 |
R-HSA-3928664 | Ephrin signaling | 3.094007e-01 | 0.509 |
R-HSA-9665348 | Signaling by ERBB2 ECD mutants | 3.094007e-01 | 0.509 |
R-HSA-1606322 | ZBP1(DAI) mediated induction of type I IFNs | 3.094007e-01 | 0.509 |
R-HSA-9616222 | Transcriptional regulation of granulopoiesis | 3.105336e-01 | 0.508 |
R-HSA-937061 | TRIF (TICAM1)-mediated TLR4 signaling | 3.130649e-01 | 0.504 |
R-HSA-166166 | MyD88-independent TLR4 cascade | 3.130649e-01 | 0.504 |
R-HSA-380284 | Loss of proteins required for interphase microtubule organization from the centr... | 3.164161e-01 | 0.500 |
R-HSA-380259 | Loss of Nlp from mitotic centrosomes | 3.164161e-01 | 0.500 |
R-HSA-937041 | IKK complex recruitment mediated by RIP1 | 3.204354e-01 | 0.494 |
R-HSA-9856532 | Mechanical load activates signaling by PIEZO1 and integrins in osteocytes | 3.204354e-01 | 0.494 |
R-HSA-392517 | Rap1 signalling | 3.204354e-01 | 0.494 |
R-HSA-844456 | The NLRP3 inflammasome | 3.204354e-01 | 0.494 |
R-HSA-449836 | Other interleukin signaling | 3.204354e-01 | 0.494 |
R-HSA-9730414 | MITF-M-regulated melanocyte development | 3.216187e-01 | 0.493 |
R-HSA-5633007 | Regulation of TP53 Activity | 3.219218e-01 | 0.492 |
R-HSA-936837 | Ion transport by P-type ATPases | 3.222873e-01 | 0.492 |
R-HSA-163210 | Formation of ATP by chemiosmotic coupling | 3.312944e-01 | 0.480 |
R-HSA-9934037 | Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) | 3.312944e-01 | 0.480 |
R-HSA-1181150 | Signaling by NODAL | 3.312944e-01 | 0.480 |
R-HSA-5620916 | VxPx cargo-targeting to cilium | 3.312944e-01 | 0.480 |
R-HSA-77111 | Synthesis of Ketone Bodies | 3.312944e-01 | 0.480 |
R-HSA-6807004 | Negative regulation of MET activity | 3.312944e-01 | 0.480 |
R-HSA-8854518 | AURKA Activation by TPX2 | 3.339908e-01 | 0.476 |
R-HSA-168249 | Innate Immune System | 3.348627e-01 | 0.475 |
R-HSA-381426 | Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-l... | 3.349138e-01 | 0.475 |
R-HSA-1474244 | Extracellular matrix organization | 3.363248e-01 | 0.473 |
R-HSA-5357786 | TNFR1-induced proapoptotic signaling | 3.419806e-01 | 0.466 |
R-HSA-5637815 | Signaling by Ligand-Responsive EGFR Variants in Cancer | 3.419806e-01 | 0.466 |
R-HSA-1236382 | Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants | 3.419806e-01 | 0.466 |
R-HSA-162594 | Early Phase of HIV Life Cycle | 3.419806e-01 | 0.466 |
R-HSA-4420097 | VEGFA-VEGFR2 Pathway | 3.436489e-01 | 0.464 |
R-HSA-5218859 | Regulated Necrosis | 3.456354e-01 | 0.461 |
R-HSA-373760 | L1CAM interactions | 3.480133e-01 | 0.458 |
R-HSA-9694614 | Attachment and Entry | 3.524967e-01 | 0.453 |
R-HSA-9705462 | Inactivation of CSF3 (G-CSF) signaling | 3.524967e-01 | 0.453 |
R-HSA-193048 | Androgen biosynthesis | 3.524967e-01 | 0.453 |
R-HSA-9671555 | Signaling by PDGFR in disease | 3.524967e-01 | 0.453 |
R-HSA-175474 | Assembly Of The HIV Virion | 3.524967e-01 | 0.453 |
R-HSA-448424 | Interleukin-17 signaling | 3.572133e-01 | 0.447 |
R-HSA-1834949 | Cytosolic sensors of pathogen-associated DNA | 3.572133e-01 | 0.447 |
R-HSA-9764560 | Regulation of CDH1 Gene Transcription | 3.572133e-01 | 0.447 |
R-HSA-6791226 | Major pathway of rRNA processing in the nucleolus and cytosol | 3.617498e-01 | 0.442 |
R-HSA-8878171 | Transcriptional regulation by RUNX1 | 3.626260e-01 | 0.441 |
R-HSA-2173788 | Downregulation of TGF-beta receptor signaling | 3.628453e-01 | 0.440 |
R-HSA-9670439 | Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT m... | 3.628453e-01 | 0.440 |
R-HSA-9669938 | Signaling by KIT in disease | 3.628453e-01 | 0.440 |
R-HSA-8964038 | LDL clearance | 3.628453e-01 | 0.440 |
R-HSA-9924644 | Developmental Lineages of the Mammary Gland | 3.687170e-01 | 0.433 |
R-HSA-74182 | Ketone body metabolism | 3.730292e-01 | 0.428 |
R-HSA-982772 | Growth hormone receptor signaling | 3.730292e-01 | 0.428 |
R-HSA-9830674 | Formation of the ureteric bud | 3.730292e-01 | 0.428 |
R-HSA-200425 | Carnitine shuttle | 3.730292e-01 | 0.428 |
R-HSA-8854691 | Interleukin-20 family signaling | 3.730292e-01 | 0.428 |
R-HSA-380270 | Recruitment of mitotic centrosome proteins and complexes | 3.744389e-01 | 0.427 |
R-HSA-5683057 | MAPK family signaling cascades | 3.779028e-01 | 0.423 |
R-HSA-983231 | Factors involved in megakaryocyte development and platelet production | 3.798573e-01 | 0.420 |
R-HSA-1226099 | Signaling by FGFR in disease | 3.801396e-01 | 0.420 |
R-HSA-429947 | Deadenylation of mRNA | 3.830509e-01 | 0.417 |
R-HSA-202430 | Translocation of ZAP-70 to Immunological synapse | 3.830509e-01 | 0.417 |
R-HSA-9703648 | Signaling by FLT3 ITD and TKD mutants | 3.830509e-01 | 0.417 |
R-HSA-110314 | Recognition of DNA damage by PCNA-containing replication complex | 3.830509e-01 | 0.417 |
R-HSA-9665686 | Signaling by ERBB2 TMD/JMD mutants | 3.830509e-01 | 0.417 |
R-HSA-9865881 | Complex III assembly | 3.830509e-01 | 0.417 |
R-HSA-9836573 | Mitochondrial RNA degradation | 3.830509e-01 | 0.417 |
R-HSA-5621575 | CD209 (DC-SIGN) signaling | 3.830509e-01 | 0.417 |
R-HSA-8863678 | Neurodegenerative Diseases | 3.830509e-01 | 0.417 |
R-HSA-8862803 | Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's dis... | 3.830509e-01 | 0.417 |
R-HSA-380287 | Centrosome maturation | 3.858185e-01 | 0.414 |
R-HSA-3000171 | Non-integrin membrane-ECM interactions | 3.858185e-01 | 0.414 |
R-HSA-71403 | Citric acid cycle (TCA cycle) | 3.858185e-01 | 0.414 |
R-HSA-3247509 | Chromatin modifying enzymes | 3.879568e-01 | 0.411 |
R-HSA-194138 | Signaling by VEGF | 3.914210e-01 | 0.407 |
R-HSA-1266695 | Interleukin-7 signaling | 3.929131e-01 | 0.406 |
R-HSA-3000157 | Laminin interactions | 3.929131e-01 | 0.406 |
R-HSA-1643713 | Signaling by EGFR in Cancer | 4.026182e-01 | 0.395 |
R-HSA-9931510 | Phosphorylated BMAL1:CLOCK (ARNTL:CLOCK) activates expression of core clock gene... | 4.026182e-01 | 0.395 |
R-HSA-9703465 | Signaling by FLT3 fusion proteins | 4.026182e-01 | 0.395 |
R-HSA-3295583 | TRP channels | 4.026182e-01 | 0.395 |
R-HSA-5357769 | Caspase activation via extrinsic apoptotic signalling pathway | 4.026182e-01 | 0.395 |
R-HSA-8874081 | MET activates PTK2 signaling | 4.026182e-01 | 0.395 |
R-HSA-9865118 | Diseases of branched-chain amino acid catabolism | 4.026182e-01 | 0.395 |
R-HSA-416482 | G alpha (12/13) signalling events | 4.027163e-01 | 0.395 |
R-HSA-187037 | Signaling by NTRK1 (TRKA) | 4.043168e-01 | 0.393 |
R-HSA-73894 | DNA Repair | 4.118737e-01 | 0.385 |
R-HSA-5357956 | TNFR1-induced NF-kappa-B signaling pathway | 4.121687e-01 | 0.385 |
R-HSA-202427 | Phosphorylation of CD3 and TCR zeta chains | 4.121687e-01 | 0.385 |
R-HSA-174414 | Processive synthesis on the C-strand of the telomere | 4.121687e-01 | 0.385 |
R-HSA-264876 | Insulin processing | 4.121687e-01 | 0.385 |
R-HSA-9734009 | Defective Intrinsic Pathway for Apoptosis | 4.121687e-01 | 0.385 |
R-HSA-6806834 | Signaling by MET | 4.138591e-01 | 0.383 |
R-HSA-380994 | ATF4 activates genes in response to endoplasmic reticulum stress | 4.215671e-01 | 0.375 |
R-HSA-9619483 | Activation of AMPK downstream of NMDARs | 4.215671e-01 | 0.375 |
R-HSA-622312 | Inflammasomes | 4.215671e-01 | 0.375 |
R-HSA-8868773 | rRNA processing in the nucleus and cytosol | 4.266112e-01 | 0.370 |
R-HSA-9615710 | Late endosomal microautophagy | 4.308158e-01 | 0.366 |
R-HSA-9674555 | Signaling by CSF3 (G-CSF) | 4.308158e-01 | 0.366 |
R-HSA-1592389 | Activation of Matrix Metalloproteinases | 4.308158e-01 | 0.366 |
R-HSA-9664565 | Signaling by ERBB2 KD Mutants | 4.308158e-01 | 0.366 |
R-HSA-180024 | DARPP-32 events | 4.308158e-01 | 0.366 |
R-HSA-9006335 | Signaling by Erythropoietin | 4.308158e-01 | 0.366 |
R-HSA-450282 | MAPK targets/ Nuclear events mediated by MAP kinases | 4.308158e-01 | 0.366 |
R-HSA-4839726 | Chromatin organization | 4.352241e-01 | 0.361 |
R-HSA-2565942 | Regulation of PLK1 Activity at G2/M Transition | 4.358286e-01 | 0.361 |
R-HSA-68962 | Activation of the pre-replicative complex | 4.399173e-01 | 0.357 |
R-HSA-380972 | Energy dependent regulation of mTOR by LKB1-AMPK | 4.399173e-01 | 0.357 |
R-HSA-1227990 | Signaling by ERBB2 in Cancer | 4.399173e-01 | 0.357 |
R-HSA-888590 | GABA synthesis, release, reuptake and degradation | 4.399173e-01 | 0.357 |
R-HSA-112311 | Neurotransmitter clearance | 4.399173e-01 | 0.357 |
R-HSA-8863795 | Downregulation of ERBB2 signaling | 4.399173e-01 | 0.357 |
R-HSA-9909615 | Regulation of PD-L1(CD274) Post-translational modification | 4.466464e-01 | 0.350 |
R-HSA-162588 | Budding and maturation of HIV virion | 4.488737e-01 | 0.348 |
R-HSA-399719 | Trafficking of AMPA receptors | 4.488737e-01 | 0.348 |
R-HSA-2129379 | Molecules associated with elastic fibres | 4.488737e-01 | 0.348 |
R-HSA-9820960 | Respiratory syncytial virus (RSV) attachment and entry | 4.488737e-01 | 0.348 |
R-HSA-8963693 | Aspartate and asparagine metabolism | 4.488737e-01 | 0.348 |
R-HSA-186763 | Downstream signal transduction | 4.488737e-01 | 0.348 |
R-HSA-182971 | EGFR downregulation | 4.488737e-01 | 0.348 |
R-HSA-9820952 | Respiratory Syncytial Virus Infection Pathway | 4.508456e-01 | 0.346 |
R-HSA-5688426 | Deubiquitination | 4.539341e-01 | 0.343 |
R-HSA-390466 | Chaperonin-mediated protein folding | 4.573476e-01 | 0.340 |
R-HSA-2024096 | HS-GAG degradation | 4.576874e-01 | 0.339 |
R-HSA-69190 | DNA strand elongation | 4.576874e-01 | 0.339 |
R-HSA-380320 | Recruitment of NuMA to mitotic centrosomes | 4.626535e-01 | 0.335 |
R-HSA-9645723 | Diseases of programmed cell death | 4.626535e-01 | 0.335 |
R-HSA-397795 | G-protein beta:gamma signalling | 4.663608e-01 | 0.331 |
R-HSA-399721 | Glutamate binding, activation of AMPA receptors and synaptic plasticity | 4.663608e-01 | 0.331 |
R-HSA-5620912 | Anchoring of the basal body to the plasma membrane | 4.731736e-01 | 0.325 |
R-HSA-5696394 | DNA Damage Recognition in GG-NER | 4.748959e-01 | 0.323 |
R-HSA-9818027 | NFE2L2 regulating anti-oxidant/detoxification enzymes | 4.748959e-01 | 0.323 |
R-HSA-8856828 | Clathrin-mediated endocytosis | 4.796809e-01 | 0.319 |
R-HSA-5696400 | Dual Incision in GG-NER | 4.832951e-01 | 0.316 |
R-HSA-5673000 | RAF activation | 4.832951e-01 | 0.316 |
R-HSA-1971475 | Glycosaminoglycan-protein linkage region biosynthesis | 4.832951e-01 | 0.316 |
R-HSA-9735869 | SARS-CoV-1 modulates host translation machinery | 4.832951e-01 | 0.316 |
R-HSA-9680350 | Signaling by CSF1 (M-CSF) in myeloid cells | 4.832951e-01 | 0.316 |
R-HSA-391251 | Protein folding | 4.887193e-01 | 0.311 |
R-HSA-2682334 | EPH-Ephrin signaling | 4.887193e-01 | 0.311 |
R-HSA-9772755 | Formation of WDR5-containing histone-modifying complexes | 4.915604e-01 | 0.308 |
R-HSA-2022928 | HS-GAG biosynthesis | 4.996940e-01 | 0.301 |
R-HSA-9682385 | FLT3 signaling in disease | 4.996940e-01 | 0.301 |
R-HSA-432720 | Lysosome Vesicle Biogenesis | 4.996940e-01 | 0.301 |
R-HSA-166016 | Toll Like Receptor 4 (TLR4) Cascade | 4.998396e-01 | 0.301 |
R-HSA-166520 | Signaling by NTRKs | 4.998396e-01 | 0.301 |
R-HSA-168928 | DDX58/IFIH1-mediated induction of interferon-alpha/beta | 5.039760e-01 | 0.298 |
R-HSA-5689896 | Ovarian tumor domain proteases | 5.076980e-01 | 0.294 |
R-HSA-381340 | Transcriptional regulation of white adipocyte differentiation | 5.139829e-01 | 0.289 |
R-HSA-1566948 | Elastic fibre formation | 5.155744e-01 | 0.288 |
R-HSA-8875878 | MET promotes cell motility | 5.155744e-01 | 0.288 |
R-HSA-74217 | Purine salvage | 5.155744e-01 | 0.288 |
R-HSA-170834 | Signaling by TGF-beta Receptor Complex | 5.189364e-01 | 0.285 |
R-HSA-9725554 | Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin | 5.233253e-01 | 0.281 |
R-HSA-8964043 | Plasma lipoprotein clearance | 5.233253e-01 | 0.281 |
R-HSA-73887 | Death Receptor Signaling | 5.234991e-01 | 0.281 |
R-HSA-8957275 | Post-translational protein phosphorylation | 5.238562e-01 | 0.281 |
R-HSA-975871 | MyD88 cascade initiated on plasma membrane | 5.238562e-01 | 0.281 |
R-HSA-168142 | Toll Like Receptor 10 (TLR10) Cascade | 5.238562e-01 | 0.281 |
R-HSA-168176 | Toll Like Receptor 5 (TLR5) Cascade | 5.238562e-01 | 0.281 |
R-HSA-5696395 | Formation of Incision Complex in GG-NER | 5.309526e-01 | 0.275 |
R-HSA-451927 | Interleukin-2 family signaling | 5.309526e-01 | 0.275 |
R-HSA-9854311 | Maturation of TCA enzymes and regulation of TCA cycle | 5.309526e-01 | 0.275 |
R-HSA-71240 | Tryptophan catabolism | 5.309526e-01 | 0.275 |
R-HSA-379726 | Mitochondrial tRNA aminoacylation | 5.309526e-01 | 0.275 |
R-HSA-9009391 | Extra-nuclear estrogen signaling | 5.384122e-01 | 0.269 |
R-HSA-5625886 | Activated PKN1 stimulates transcription of AR (androgen receptor) regulated gene... | 5.384584e-01 | 0.269 |
R-HSA-9929491 | SPOP-mediated proteasomal degradation of PD-L1(CD274) | 5.384584e-01 | 0.269 |
R-HSA-9820841 | M-decay: degradation of maternal mRNAs by maternally stored factors | 5.384584e-01 | 0.269 |
R-HSA-5218920 | VEGFR2 mediated vascular permeability | 5.384584e-01 | 0.269 |
R-HSA-73817 | Purine ribonucleoside monophosphate biosynthesis | 5.384584e-01 | 0.269 |
R-HSA-2559580 | Oxidative Stress Induced Senescence | 5.431959e-01 | 0.265 |
R-HSA-174417 | Telomere C-strand (Lagging Strand) Synthesis | 5.458445e-01 | 0.263 |
R-HSA-9006936 | Signaling by TGFB family members | 5.465369e-01 | 0.262 |
R-HSA-1280218 | Adaptive Immune System | 5.515616e-01 | 0.258 |
R-HSA-9860931 | Response of endothelial cells to shear stress | 5.526597e-01 | 0.258 |
R-HSA-512988 | Interleukin-3, Interleukin-5 and GM-CSF signaling | 5.531128e-01 | 0.257 |
R-HSA-1433557 | Signaling by SCF-KIT | 5.602653e-01 | 0.252 |
R-HSA-75876 | Synthesis of very long-chain fatty acyl-CoAs | 5.602653e-01 | 0.252 |
R-HSA-8854214 | TBC/RABGAPs | 5.602653e-01 | 0.252 |
R-HSA-9637690 | Response of Mtb to phagocytosis | 5.602653e-01 | 0.252 |
R-HSA-422475 | Axon guidance | 5.604834e-01 | 0.251 |
R-HSA-418346 | Platelet homeostasis | 5.665953e-01 | 0.247 |
R-HSA-375280 | Amine ligand-binding receptors | 5.673037e-01 | 0.246 |
R-HSA-3928662 | EPHB-mediated forward signaling | 5.673037e-01 | 0.246 |
R-HSA-156581 | Methylation | 5.673037e-01 | 0.246 |
R-HSA-2142691 | Synthesis of Leukotrienes (LT) and Eoxins (EX) | 5.673037e-01 | 0.246 |
R-HSA-9006934 | Signaling by Receptor Tyrosine Kinases | 5.694443e-01 | 0.245 |
R-HSA-3560782 | Diseases associated with glycosaminoglycan metabolism | 5.742299e-01 | 0.241 |
R-HSA-9824585 | Regulation of MITF-M-dependent genes involved in pigmentation | 5.742299e-01 | 0.241 |
R-HSA-6783310 | Fanconi Anemia Pathway | 5.742299e-01 | 0.241 |
R-HSA-9734779 | Developmental Cell Lineages of the Integumentary System | 5.757113e-01 | 0.240 |
R-HSA-975138 | TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation | 5.757113e-01 | 0.240 |
R-HSA-72312 | rRNA processing | 5.784475e-01 | 0.238 |
R-HSA-975155 | MyD88 dependent cascade initiated on endosome | 5.802167e-01 | 0.236 |
R-HSA-6781823 | Formation of TC-NER Pre-Incision Complex | 5.810457e-01 | 0.236 |
R-HSA-9660826 | Purinergic signaling in leishmaniasis infection | 5.810457e-01 | 0.236 |
R-HSA-9664424 | Cell recruitment (pro-inflammatory response) | 5.810457e-01 | 0.236 |
R-HSA-2514859 | Inactivation, recovery and regulation of the phototransduction cascade | 5.810457e-01 | 0.236 |
R-HSA-9839373 | Signaling by TGFBR3 | 5.810457e-01 | 0.236 |
R-HSA-3928665 | EPH-ephrin mediated repulsion of cells | 5.877527e-01 | 0.231 |
R-HSA-8939211 | ESR-mediated signaling | 5.939030e-01 | 0.226 |
R-HSA-202733 | Cell surface interactions at the vascular wall | 5.939030e-01 | 0.226 |
R-HSA-9909648 | Regulation of PD-L1(CD274) expression | 5.941524e-01 | 0.226 |
R-HSA-9634597 | GPER1 signaling | 5.943528e-01 | 0.226 |
R-HSA-389356 | Co-stimulation by CD28 | 5.943528e-01 | 0.226 |
R-HSA-9764265 | Regulation of CDH1 Expression and Function | 5.976789e-01 | 0.224 |
R-HSA-9764274 | Regulation of Expression and Function of Type I Classical Cadherins | 5.976789e-01 | 0.224 |
R-HSA-168181 | Toll Like Receptor 7/8 (TLR7/8) Cascade | 5.978875e-01 | 0.223 |
R-HSA-1912422 | Pre-NOTCH Expression and Processing | 5.978875e-01 | 0.223 |
R-HSA-157858 | Gap junction trafficking and regulation | 6.008477e-01 | 0.221 |
R-HSA-73893 | DNA Damage Bypass | 6.008477e-01 | 0.221 |
R-HSA-9855142 | Cellular responses to mechanical stimuli | 6.022173e-01 | 0.220 |
R-HSA-74160 | Gene expression (Transcription) | 6.035156e-01 | 0.219 |
R-HSA-168138 | Toll Like Receptor 9 (TLR9) Cascade | 6.107716e-01 | 0.214 |
R-HSA-70895 | Branched-chain amino acid catabolism | 6.135282e-01 | 0.212 |
R-HSA-2514856 | The phototransduction cascade | 6.135282e-01 | 0.212 |
R-HSA-611105 | Respiratory electron transport | 6.150108e-01 | 0.211 |
R-HSA-72187 | mRNA 3'-end processing | 6.197171e-01 | 0.208 |
R-HSA-68949 | Orc1 removal from chromatin | 6.197171e-01 | 0.208 |
R-HSA-9931269 | AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) | 6.197171e-01 | 0.208 |
R-HSA-6794361 | Neurexins and neuroligins | 6.197171e-01 | 0.208 |
R-HSA-5250924 | B-WICH complex positively regulates rRNA expression | 6.258074e-01 | 0.204 |
R-HSA-432722 | Golgi Associated Vesicle Biogenesis | 6.258074e-01 | 0.204 |
R-HSA-8956320 | Nucleotide biosynthesis | 6.258074e-01 | 0.204 |
R-HSA-166058 | MyD88:MAL(TIRAP) cascade initiated on plasma membrane | 6.315437e-01 | 0.200 |
R-HSA-168188 | Toll Like Receptor TLR6:TLR2 Cascade | 6.315437e-01 | 0.200 |
R-HSA-9754678 | SARS-CoV-2 modulates host translation machinery | 6.318004e-01 | 0.199 |
R-HSA-9675108 | Nervous system development | 6.361202e-01 | 0.196 |
R-HSA-212436 | Generic Transcription Pathway | 6.376567e-01 | 0.195 |
R-HSA-3214815 | HDACs deacetylate histones | 6.376979e-01 | 0.195 |
R-HSA-6811436 | COPI-independent Golgi-to-ER retrograde traffic | 6.376979e-01 | 0.195 |
R-HSA-9759194 | Nuclear events mediated by NFE2L2 | 6.396081e-01 | 0.194 |
R-HSA-69275 | G2/M Transition | 6.416842e-01 | 0.193 |
R-HSA-6782210 | Gap-filling DNA repair synthesis and ligation in TC-NER | 6.435012e-01 | 0.191 |
R-HSA-193648 | NRAGE signals death through JNK | 6.435012e-01 | 0.191 |
R-HSA-9662361 | Sensory processing of sound by outer hair cells of the cochlea | 6.435012e-01 | 0.191 |
R-HSA-177929 | Signaling by EGFR | 6.435012e-01 | 0.191 |
R-HSA-168179 | Toll Like Receptor TLR1:TLR2 Cascade | 6.435881e-01 | 0.191 |
R-HSA-181438 | Toll Like Receptor 2 (TLR2) Cascade | 6.435881e-01 | 0.191 |
R-HSA-453274 | Mitotic G2-G2/M phases | 6.481469e-01 | 0.188 |
R-HSA-9764561 | Regulation of CDH1 Function | 6.492119e-01 | 0.188 |
R-HSA-388841 | Regulation of T cell activation by CD28 family | 6.494800e-01 | 0.187 |
R-HSA-983712 | Ion channel transport | 6.513472e-01 | 0.186 |
R-HSA-6782135 | Dual incision in TC-NER | 6.548315e-01 | 0.184 |
R-HSA-9772572 | Early SARS-CoV-2 Infection Events | 6.548315e-01 | 0.184 |
R-HSA-168898 | Toll-like Receptor Cascades | 6.576857e-01 | 0.182 |
R-HSA-1638091 | Heparan sulfate/heparin (HS-GAG) metabolism | 6.603615e-01 | 0.180 |
R-HSA-429914 | Deadenylation-dependent mRNA decay | 6.603615e-01 | 0.180 |
R-HSA-352230 | Amino acid transport across the plasma membrane | 6.603615e-01 | 0.180 |
R-HSA-2022090 | Assembly of collagen fibrils and other multimeric structures | 6.603615e-01 | 0.180 |
R-HSA-180786 | Extension of Telomeres | 6.603615e-01 | 0.180 |
R-HSA-5693565 | Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at... | 6.603615e-01 | 0.180 |
R-HSA-9845323 | Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) | 6.658031e-01 | 0.177 |
R-HSA-1227986 | Signaling by ERBB2 | 6.658031e-01 | 0.177 |
R-HSA-8943724 | Regulation of PTEN gene transcription | 6.658031e-01 | 0.177 |
R-HSA-351202 | Metabolism of polyamines | 6.658031e-01 | 0.177 |
R-HSA-114608 | Platelet degranulation | 6.667442e-01 | 0.176 |
R-HSA-73856 | RNA Polymerase II Transcription Termination | 6.711579e-01 | 0.173 |
R-HSA-1442490 | Collagen degradation | 6.711579e-01 | 0.173 |
R-HSA-8956321 | Nucleotide salvage | 6.711579e-01 | 0.173 |
R-HSA-9759476 | Regulation of Homotypic Cell-Cell Adhesion | 6.731692e-01 | 0.172 |
R-HSA-8852276 | The role of GTSE1 in G2/M progression after G2 checkpoint | 6.764273e-01 | 0.170 |
R-HSA-186797 | Signaling by PDGF | 6.764273e-01 | 0.170 |
R-HSA-6799198 | Complex I biogenesis | 6.816125e-01 | 0.166 |
R-HSA-6790901 | rRNA modification in the nucleus and cytosol | 6.816125e-01 | 0.166 |
R-HSA-8848021 | Signaling by PTK6 | 6.816125e-01 | 0.166 |
R-HSA-9006927 | Signaling by Non-Receptor Tyrosine Kinases | 6.816125e-01 | 0.166 |
R-HSA-5576891 | Cardiac conduction | 6.851043e-01 | 0.164 |
R-HSA-9843745 | Adipogenesis | 6.851043e-01 | 0.164 |
R-HSA-389948 | Co-inhibition by PD-1 | 6.851827e-01 | 0.164 |
R-HSA-5690714 | CD22 mediated BCR regulation | 6.867149e-01 | 0.163 |
R-HSA-168643 | Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali... | 6.867149e-01 | 0.163 |
R-HSA-76005 | Response to elevated platelet cytosolic Ca2+ | 6.922138e-01 | 0.160 |
R-HSA-9909649 | Regulation of PD-L1(CD274) transcription | 6.966767e-01 | 0.157 |
R-HSA-6782315 | tRNA modification in the nucleus and cytosol | 6.966767e-01 | 0.157 |
R-HSA-9958863 | SLC-mediated transport of amino acids | 7.015387e-01 | 0.154 |
R-HSA-9830369 | Kidney development | 7.015387e-01 | 0.154 |
R-HSA-196071 | Metabolism of steroid hormones | 7.015387e-01 | 0.154 |
R-HSA-5693606 | DNA Double Strand Break Response | 7.015387e-01 | 0.154 |
R-HSA-71291 | Metabolism of amino acids and derivatives | 7.024672e-01 | 0.153 |
R-HSA-8936459 | RUNX1 regulates genes involved in megakaryocyte differentiation and platelet fun... | 7.063230e-01 | 0.151 |
R-HSA-9662360 | Sensory processing of sound by inner hair cells of the cochlea | 7.063230e-01 | 0.151 |
R-HSA-1168372 | Downstream signaling events of B Cell Receptor (BCR) | 7.156636e-01 | 0.145 |
R-HSA-75105 | Fatty acyl-CoA biosynthesis | 7.156636e-01 | 0.145 |
R-HSA-5250913 | Positive epigenetic regulation of rRNA expression | 7.202223e-01 | 0.143 |
R-HSA-3000178 | ECM proteoglycans | 7.202223e-01 | 0.143 |
R-HSA-975634 | Retinoid metabolism and transport | 7.202223e-01 | 0.143 |
R-HSA-2029482 | Regulation of actin dynamics for phagocytic cup formation | 7.225862e-01 | 0.141 |
R-HSA-199992 | trans-Golgi Network Vesicle Budding | 7.247082e-01 | 0.140 |
R-HSA-198725 | Nuclear Events (kinase and transcription factor activation) | 7.247082e-01 | 0.140 |
R-HSA-73857 | RNA Polymerase II Transcription | 7.273118e-01 | 0.138 |
R-HSA-69052 | Switching of origins to a post-replicative state | 7.291224e-01 | 0.137 |
R-HSA-204998 | Cell death signalling via NRAGE, NRIF and NADE | 7.291224e-01 | 0.137 |
R-HSA-5673001 | RAF/MAP kinase cascade | 7.334392e-01 | 0.135 |
R-HSA-6781827 | Transcription-Coupled Nucleotide Excision Repair (TC-NER) | 7.377405e-01 | 0.132 |
R-HSA-418990 | Adherens junctions interactions | 7.377603e-01 | 0.132 |
R-HSA-5689603 | UCH proteinases | 7.419466e-01 | 0.130 |
R-HSA-2187338 | Visual phototransduction | 7.444328e-01 | 0.128 |
R-HSA-69242 | S Phase | 7.474309e-01 | 0.126 |
R-HSA-5684996 | MAPK1/MAPK3 signaling | 7.491678e-01 | 0.125 |
R-HSA-216083 | Integrin cell surface interactions | 7.501582e-01 | 0.125 |
R-HSA-109582 | Hemostasis | 7.503647e-01 | 0.125 |
R-HSA-9659379 | Sensory processing of sound | 7.541659e-01 | 0.123 |
R-HSA-9755511 | KEAP1-NFE2L2 pathway | 7.562453e-01 | 0.121 |
R-HSA-9856530 | High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR... | 7.581095e-01 | 0.120 |
R-HSA-6806667 | Metabolism of fat-soluble vitamins | 7.619901e-01 | 0.118 |
R-HSA-5696399 | Global Genome Nucleotide Excision Repair (GG-NER) | 7.732637e-01 | 0.112 |
R-HSA-8939236 | RUNX1 regulates transcription of genes involved in differentiation of HSCs | 7.732637e-01 | 0.112 |
R-HSA-983705 | Signaling by the B Cell Receptor (BCR) | 7.757873e-01 | 0.110 |
R-HSA-6794362 | Protein-protein interactions at synapses | 7.769020e-01 | 0.110 |
R-HSA-8876198 | RAB GEFs exchange GTP for GDP on RABs | 7.804823e-01 | 0.108 |
R-HSA-163841 | Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation | 7.840052e-01 | 0.106 |
R-HSA-438064 | Post NMDA receptor activation events | 7.874719e-01 | 0.104 |
R-HSA-9824439 | Bacterial Infection Pathways | 7.920312e-01 | 0.101 |
R-HSA-112310 | Neurotransmitter release cycle | 7.975428e-01 | 0.098 |
R-HSA-373080 | Class B/2 (Secretin family receptors) | 7.975428e-01 | 0.098 |
R-HSA-112315 | Transmission across Chemical Synapses | 8.032368e-01 | 0.095 |
R-HSA-174824 | Plasma lipoprotein assembly, remodeling, and clearance | 8.071383e-01 | 0.093 |
R-HSA-983695 | Antigen activates B Cell Receptor (BCR) leading to generation of second messenge... | 8.102350e-01 | 0.091 |
R-HSA-68867 | Assembly of the pre-replicative complex | 8.102350e-01 | 0.091 |
R-HSA-418555 | G alpha (s) signalling events | 8.108061e-01 | 0.091 |
R-HSA-421270 | Cell-cell junction organization | 8.123270e-01 | 0.090 |
R-HSA-2219530 | Constitutive Signaling by Aberrant PI3K in Cancer | 8.132822e-01 | 0.090 |
R-HSA-2029480 | Fcgamma receptor (FCGR) dependent phagocytosis | 8.176471e-01 | 0.087 |
R-HSA-597592 | Post-translational protein modification | 8.200228e-01 | 0.086 |
R-HSA-5389840 | Mitochondrial translation elongation | 8.221344e-01 | 0.085 |
R-HSA-6807878 | COPI-mediated anterograde transport | 8.221344e-01 | 0.085 |
R-HSA-157579 | Telomere Maintenance | 8.249912e-01 | 0.084 |
R-HSA-193704 | p75 NTR receptor-mediated signalling | 8.305684e-01 | 0.081 |
R-HSA-2559583 | Cellular Senescence | 8.306703e-01 | 0.081 |
R-HSA-382556 | ABC-family proteins mediated transport | 8.332903e-01 | 0.079 |
R-HSA-9842860 | Regulation of endogenous retroelements | 8.386040e-01 | 0.076 |
R-HSA-442755 | Activation of NMDA receptors and postsynaptic events | 8.386040e-01 | 0.076 |
R-HSA-111885 | Opioid Signalling | 8.437490e-01 | 0.074 |
R-HSA-9833110 | RSV-host interactions | 8.462599e-01 | 0.072 |
R-HSA-5696398 | Nucleotide Excision Repair | 8.487306e-01 | 0.071 |
R-HSA-69239 | Synthesis of DNA | 8.535540e-01 | 0.069 |
R-HSA-2672351 | Stimuli-sensing channels | 8.559079e-01 | 0.068 |
R-HSA-69002 | DNA Replication Pre-Initiation | 8.582241e-01 | 0.066 |
R-HSA-2871796 | FCERI mediated MAPK activation | 8.649526e-01 | 0.063 |
R-HSA-9006931 | Signaling by Nuclear Receptors | 8.656384e-01 | 0.063 |
R-HSA-2454202 | Fc epsilon receptor (FCERI) signaling | 8.731774e-01 | 0.059 |
R-HSA-2871809 | FCERI mediated Ca+2 mobilization | 8.754672e-01 | 0.058 |
R-HSA-9007101 | Rab regulation of trafficking | 8.794410e-01 | 0.056 |
R-HSA-2980736 | Peptide hormone metabolism | 8.794410e-01 | 0.056 |
R-HSA-2219528 | PI3K/AKT Signaling in Cancer | 8.813802e-01 | 0.055 |
R-HSA-73886 | Chromosome Maintenance | 8.870136e-01 | 0.052 |
R-HSA-9635486 | Infection with Mycobacterium tuberculosis | 8.870136e-01 | 0.052 |
R-HSA-112314 | Neurotransmitter receptors and postsynaptic signal transmission | 8.884095e-01 | 0.051 |
R-HSA-6811558 | PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling | 8.906202e-01 | 0.050 |
R-HSA-9816359 | Maternal to zygotic transition (MZT) | 8.906202e-01 | 0.050 |
R-HSA-69206 | G1/S Transition | 8.958163e-01 | 0.048 |
R-HSA-9748784 | Drug ADME | 8.967188e-01 | 0.047 |
R-HSA-199418 | Negative regulation of the PI3K/AKT network | 9.039357e-01 | 0.044 |
R-HSA-446219 | Synthesis of substrates in N-glycan biosythesis | 9.070041e-01 | 0.042 |
R-HSA-9909396 | Circadian clock | 9.085015e-01 | 0.042 |
R-HSA-1474228 | Degradation of the extracellular matrix | 9.085015e-01 | 0.042 |
R-HSA-212165 | Epigenetic regulation of gene expression | 9.149526e-01 | 0.039 |
R-HSA-163685 | Integration of energy metabolism | 9.156357e-01 | 0.038 |
R-HSA-9018519 | Estrogen-dependent gene expression | 9.156357e-01 | 0.038 |
R-HSA-15869 | Metabolism of nucleotides | 9.183240e-01 | 0.037 |
R-HSA-5368287 | Mitochondrial translation | 9.183317e-01 | 0.037 |
R-HSA-6807070 | PTEN Regulation | 9.196474e-01 | 0.036 |
R-HSA-157118 | Signaling by NOTCH | 9.225128e-01 | 0.035 |
R-HSA-453279 | Mitotic G1 phase and G1/S transition | 9.294401e-01 | 0.032 |
R-HSA-199977 | ER to Golgi Anterograde Transport | 9.305774e-01 | 0.031 |
R-HSA-2173782 | Binding and Uptake of Ligands by Scavenger Receptors | 9.338810e-01 | 0.030 |
R-HSA-9856651 | MITF-M-dependent gene expression | 9.338810e-01 | 0.030 |
R-HSA-2142753 | Arachidonate metabolism | 9.359959e-01 | 0.029 |
R-HSA-69306 | DNA Replication | 9.370280e-01 | 0.028 |
R-HSA-9917777 | Epigenetic regulation by WDR5-containing histone modifying complexes | 9.380434e-01 | 0.028 |
R-HSA-446193 | Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, L... | 9.409930e-01 | 0.026 |
R-HSA-9734767 | Developmental Cell Lineages | 9.429346e-01 | 0.026 |
R-HSA-9711123 | Cellular response to chemical stress | 9.466425e-01 | 0.024 |
R-HSA-76002 | Platelet activation, signaling and aggregation | 9.507903e-01 | 0.022 |
R-HSA-5621481 | C-type lectin receptors (CLRs) | 9.537699e-01 | 0.021 |
R-HSA-9658195 | Leishmania infection | 9.552417e-01 | 0.020 |
R-HSA-9824443 | Parasitic Infection Pathways | 9.552417e-01 | 0.020 |
R-HSA-9662851 | Anti-inflammatory response favouring Leishmania parasite infection | 9.552506e-01 | 0.020 |
R-HSA-9664433 | Leishmania parasite growth and survival | 9.552506e-01 | 0.020 |
R-HSA-983168 | Antigen processing: Ubiquitination & Proteasome degradation | 9.558454e-01 | 0.020 |
R-HSA-112316 | Neuronal System | 9.558846e-01 | 0.020 |
R-HSA-3781865 | Diseases of glycosylation | 9.625893e-01 | 0.017 |
R-HSA-1257604 | PIP3 activates AKT signaling | 9.630193e-01 | 0.016 |
R-HSA-1630316 | Glycosaminoglycan metabolism | 9.676921e-01 | 0.014 |
R-HSA-8978868 | Fatty acid metabolism | 9.692275e-01 | 0.014 |
R-HSA-948021 | Transport to the Golgi and subsequent modification | 9.721012e-01 | 0.012 |
R-HSA-1483206 | Glycerophospholipid biosynthesis | 9.725525e-01 | 0.012 |
R-HSA-5668914 | Diseases of metabolism | 9.760202e-01 | 0.011 |
R-HSA-8951664 | Neddylation | 9.798698e-01 | 0.009 |
R-HSA-9006925 | Intracellular signaling by second messengers | 9.807297e-01 | 0.008 |
R-HSA-382551 | Transport of small molecules | 9.821601e-01 | 0.008 |
R-HSA-198933 | Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell | 9.823354e-01 | 0.008 |
R-HSA-156580 | Phase II - Conjugation of compounds | 9.849986e-01 | 0.007 |
R-HSA-388396 | GPCR downstream signalling | 9.891662e-01 | 0.005 |
R-HSA-983169 | Class I MHC mediated antigen processing & presentation | 9.893707e-01 | 0.005 |
R-HSA-416476 | G alpha (q) signalling events | 9.900343e-01 | 0.004 |
R-HSA-211945 | Phase I - Functionalization of compounds | 9.920765e-01 | 0.003 |
R-HSA-1266738 | Developmental Biology | 9.925248e-01 | 0.003 |
R-HSA-446203 | Asparagine N-linked glycosylation | 9.939371e-01 | 0.003 |
R-HSA-1483257 | Phospholipid metabolism | 9.940040e-01 | 0.003 |
R-HSA-372790 | Signaling by GPCR | 9.957242e-01 | 0.002 |
R-HSA-8957322 | Metabolism of steroids | 9.962755e-01 | 0.002 |
R-HSA-196854 | Metabolism of vitamins and cofactors | 9.980716e-01 | 0.001 |
R-HSA-211859 | Biological oxidations | 9.986297e-01 | 0.001 |
R-HSA-373076 | Class A/1 (Rhodopsin-like receptors) | 9.988435e-01 | 0.001 |
R-HSA-425407 | SLC-mediated transmembrane transport | 9.988994e-01 | 0.000 |
R-HSA-418594 | G alpha (i) signalling events | 9.990670e-01 | 0.000 |
R-HSA-500792 | GPCR ligand binding | 9.994926e-01 | 0.000 |
R-HSA-1430728 | Metabolism | 9.999000e-01 | 0.000 |
R-HSA-556833 | Metabolism of lipids | 9.999998e-01 | 0.000 |
R-HSA-9709957 | Sensory Perception | 9.999998e-01 | 0.000 |
Download
kinase | JSD_mean | pearson_surrounding | kinase_max_IC_position | max_position_JSD |
---|---|---|---|---|
GAK |
0.896 | 0.074 | 1 | 0.879 |
PKR |
0.888 | 0.077 | 1 | 0.894 |
VRK2 |
0.887 | -0.064 | 1 | 0.919 |
TNIK |
0.886 | 0.094 | 3 | 0.856 |
TAK1 |
0.885 | -0.053 | 1 | 0.856 |
VRK1 |
0.885 | -0.003 | 2 | 0.811 |
MINK |
0.883 | 0.023 | 1 | 0.834 |
BRAF |
0.882 | 0.035 | -4 | 0.886 |
LRRK2 |
0.882 | -0.079 | 2 | 0.808 |
NEK1 |
0.882 | -0.009 | 1 | 0.857 |
GCK |
0.880 | 0.009 | 1 | 0.821 |
EEF2K |
0.880 | 0.036 | 3 | 0.841 |
ASK1 |
0.880 | -0.096 | 1 | 0.807 |
TAO2 |
0.879 | -0.003 | 2 | 0.819 |
HGK |
0.879 | 0.032 | 3 | 0.861 |
MST1 |
0.878 | -0.040 | 1 | 0.831 |
MEKK2 |
0.877 | -0.034 | 2 | 0.775 |
KHS1 |
0.877 | 0.047 | 1 | 0.814 |
NEK5 |
0.877 | 0.018 | 1 | 0.874 |
NIK |
0.877 | 0.016 | -3 | 0.869 |
MST2 |
0.877 | -0.033 | 1 | 0.838 |
TTK |
0.876 | -0.014 | -2 | 0.809 |
TAO3 |
0.876 | 0.069 | 1 | 0.838 |
BMPR2 |
0.876 | -0.080 | -2 | 0.900 |
PDK1 |
0.876 | -0.057 | 1 | 0.840 |
MYO3B |
0.875 | 0.030 | 2 | 0.786 |
OSR1 |
0.875 | 0.011 | 2 | 0.748 |
MYO3A |
0.874 | -0.004 | 1 | 0.831 |
KHS2 |
0.874 | 0.059 | 1 | 0.819 |
MEK1 |
0.873 | -0.194 | 2 | 0.802 |
MST3 |
0.872 | 0.050 | 2 | 0.791 |
MAP3K15 |
0.872 | -0.087 | 1 | 0.818 |
CAMKK2 |
0.872 | -0.086 | -2 | 0.801 |
BIKE |
0.871 | 0.033 | 1 | 0.752 |
CAMKK1 |
0.871 | -0.102 | -2 | 0.802 |
LKB1 |
0.871 | -0.073 | -3 | 0.818 |
MEK5 |
0.871 | -0.247 | 2 | 0.784 |
ANKRD3 |
0.871 | -0.005 | 1 | 0.894 |
DAPK2 |
0.871 | -0.042 | -3 | 0.848 |
ALPHAK3 |
0.870 | -0.048 | -1 | 0.840 |
NEK4 |
0.869 | -0.062 | 1 | 0.839 |
YSK1 |
0.869 | -0.027 | 2 | 0.774 |
HPK1 |
0.869 | -0.034 | 1 | 0.803 |
PRPK |
0.869 | -0.016 | -1 | 0.896 |
NEK8 |
0.869 | -0.082 | 2 | 0.781 |
MEKK1 |
0.869 | -0.070 | 1 | 0.866 |
CAMLCK |
0.868 | -0.034 | -2 | 0.852 |
ALK4 |
0.867 | -0.037 | -2 | 0.817 |
MEKK6 |
0.867 | -0.114 | 1 | 0.842 |
CAMK1B |
0.866 | 0.025 | -3 | 0.851 |
MOS |
0.866 | 0.037 | 1 | 0.890 |
DLK |
0.866 | -0.142 | 1 | 0.874 |
LATS1 |
0.866 | 0.090 | -3 | 0.816 |
ZAK |
0.865 | -0.030 | 1 | 0.839 |
PRP4 |
0.864 | 0.089 | -3 | 0.761 |
PASK |
0.864 | 0.019 | -3 | 0.814 |
STLK3 |
0.864 | -0.179 | 1 | 0.803 |
YSK4 |
0.864 | -0.055 | 1 | 0.812 |
PBK |
0.864 | -0.002 | 1 | 0.803 |
DMPK1 |
0.863 | 0.059 | -3 | 0.769 |
MEKK3 |
0.861 | -0.143 | 1 | 0.839 |
NLK |
0.861 | 0.024 | 1 | 0.867 |
ALK2 |
0.860 | -0.005 | -2 | 0.785 |
NEK11 |
0.860 | -0.189 | 1 | 0.826 |
CDKL1 |
0.860 | 0.019 | -3 | 0.777 |
MPSK1 |
0.860 | -0.015 | 1 | 0.831 |
MEK2 |
0.860 | -0.279 | 2 | 0.774 |
ATR |
0.859 | -0.040 | 1 | 0.851 |
LOK |
0.859 | -0.041 | -2 | 0.801 |
SMMLCK |
0.859 | -0.045 | -3 | 0.806 |
AAK1 |
0.858 | 0.073 | 1 | 0.645 |
DAPK3 |
0.858 | -0.011 | -3 | 0.792 |
TGFBR1 |
0.857 | 0.010 | -2 | 0.784 |
ROCK2 |
0.857 | 0.040 | -3 | 0.779 |
MLK2 |
0.857 | -0.070 | 2 | 0.783 |
CAMK2G |
0.856 | 0.081 | 2 | 0.826 |
TAO1 |
0.855 | -0.036 | 1 | 0.774 |
ICK |
0.855 | 0.004 | -3 | 0.809 |
SKMLCK |
0.855 | 0.056 | -2 | 0.865 |
RAF1 |
0.855 | -0.063 | 1 | 0.871 |
P38A |
0.855 | 0.042 | 1 | 0.731 |
JNK3 |
0.854 | 0.038 | 1 | 0.682 |
NEK9 |
0.853 | -0.038 | 2 | 0.806 |
HRI |
0.853 | -0.133 | -2 | 0.856 |
BMPR1B |
0.853 | 0.056 | 1 | 0.789 |
JNK2 |
0.852 | 0.049 | 1 | 0.640 |
GRK6 |
0.852 | 0.021 | 1 | 0.864 |
CLK3 |
0.852 | 0.270 | 1 | 0.895 |
MLK1 |
0.852 | -0.034 | 2 | 0.780 |
TLK2 |
0.852 | -0.018 | 1 | 0.829 |
PERK |
0.852 | -0.157 | -2 | 0.826 |
CHAK2 |
0.852 | 0.075 | -1 | 0.903 |
WNK1 |
0.851 | 0.119 | -2 | 0.917 |
COT |
0.851 | 0.155 | 2 | 0.840 |
ACVR2B |
0.850 | -0.039 | -2 | 0.783 |
WNK4 |
0.850 | -0.020 | -2 | 0.919 |
TSSK2 |
0.850 | 0.051 | -5 | 0.858 |
GRK5 |
0.849 | -0.067 | -3 | 0.819 |
SLK |
0.849 | -0.040 | -2 | 0.750 |
P38B |
0.849 | 0.046 | 1 | 0.659 |
ERK5 |
0.849 | 0.020 | 1 | 0.830 |
IRAK4 |
0.849 | -0.009 | 1 | 0.864 |
ACVR2A |
0.848 | -0.062 | -2 | 0.774 |
PLK1 |
0.848 | -0.065 | -2 | 0.811 |
DSTYK |
0.848 | 0.090 | 2 | 0.853 |
NEK2 |
0.848 | -0.041 | 2 | 0.776 |
TLK1 |
0.847 | -0.087 | -2 | 0.824 |
PDHK4 |
0.847 | -0.197 | 1 | 0.889 |
PKCD |
0.847 | 0.110 | 2 | 0.767 |
PINK1 |
0.847 | -0.073 | 1 | 0.874 |
PKN3 |
0.847 | 0.030 | -3 | 0.806 |
GRK7 |
0.846 | 0.066 | 1 | 0.798 |
HASPIN |
0.846 | 0.038 | -1 | 0.701 |
PIM1 |
0.846 | 0.091 | -3 | 0.765 |
MLK3 |
0.846 | 0.056 | 2 | 0.720 |
PDHK1 |
0.846 | -0.124 | 1 | 0.888 |
DCAMKL1 |
0.844 | 0.035 | -3 | 0.789 |
DAPK1 |
0.843 | -0.048 | -3 | 0.770 |
MASTL |
0.843 | -0.280 | -2 | 0.853 |
MST4 |
0.843 | 0.088 | 2 | 0.808 |
NEK3 |
0.843 | -0.116 | 1 | 0.820 |
MLK4 |
0.843 | -0.019 | 2 | 0.703 |
AMPKA1 |
0.842 | 0.024 | -3 | 0.843 |
PIM3 |
0.842 | 0.055 | -3 | 0.807 |
BUB1 |
0.842 | 0.062 | -5 | 0.795 |
RIPK1 |
0.842 | -0.169 | 1 | 0.857 |
ROCK1 |
0.842 | -0.002 | -3 | 0.753 |
BMPR1A |
0.841 | 0.018 | 1 | 0.775 |
PKN2 |
0.841 | 0.048 | -3 | 0.833 |
CHK1 |
0.841 | -0.005 | -3 | 0.810 |
CAMK2D |
0.840 | 0.097 | -3 | 0.825 |
RIPK3 |
0.840 | -0.067 | 3 | 0.746 |
NEK7 |
0.840 | 0.001 | -3 | 0.821 |
NUAK2 |
0.839 | 0.028 | -3 | 0.830 |
TSSK1 |
0.839 | 0.073 | -3 | 0.857 |
CDK5 |
0.838 | 0.078 | 1 | 0.720 |
DNAPK |
0.838 | 0.034 | 1 | 0.703 |
MRCKA |
0.838 | 0.007 | -3 | 0.753 |
ULK2 |
0.838 | -0.038 | 2 | 0.761 |
CHAK1 |
0.837 | -0.048 | 2 | 0.717 |
P70S6KB |
0.837 | 0.002 | -3 | 0.788 |
GSK3B |
0.837 | 0.074 | 4 | 0.510 |
DCAMKL2 |
0.837 | -0.010 | -3 | 0.817 |
P38G |
0.837 | 0.039 | 1 | 0.565 |
MTOR |
0.837 | -0.039 | 1 | 0.823 |
ERK2 |
0.837 | -0.021 | 1 | 0.701 |
NEK6 |
0.836 | 0.097 | -2 | 0.892 |
PLK3 |
0.836 | -0.061 | 2 | 0.753 |
CDKL5 |
0.836 | 0.016 | -3 | 0.766 |
MRCKB |
0.836 | 0.004 | -3 | 0.743 |
P38D |
0.836 | 0.065 | 1 | 0.583 |
CDK1 |
0.836 | 0.089 | 1 | 0.651 |
PIM2 |
0.835 | -0.000 | -3 | 0.740 |
GSK3A |
0.835 | 0.114 | 4 | 0.519 |
CDC7 |
0.835 | -0.048 | 1 | 0.847 |
HIPK1 |
0.835 | 0.025 | 1 | 0.745 |
MARK4 |
0.834 | -0.006 | 4 | 0.836 |
WNK3 |
0.834 | -0.137 | 1 | 0.864 |
CAMK2B |
0.833 | 0.148 | 2 | 0.794 |
ERK7 |
0.833 | 0.006 | 2 | 0.520 |
ATM |
0.832 | -0.011 | 1 | 0.777 |
HUNK |
0.832 | -0.157 | 2 | 0.790 |
SGK3 |
0.832 | 0.021 | -3 | 0.756 |
TBK1 |
0.832 | -0.071 | 1 | 0.779 |
IRE1 |
0.832 | -0.027 | 1 | 0.847 |
IRAK1 |
0.832 | -0.205 | -1 | 0.790 |
CDK2 |
0.832 | 0.059 | 1 | 0.741 |
IRE2 |
0.831 | -0.023 | 2 | 0.735 |
GRK2 |
0.831 | -0.067 | -2 | 0.743 |
SMG1 |
0.831 | -0.056 | 1 | 0.797 |
DRAK1 |
0.831 | -0.129 | 1 | 0.752 |
CRIK |
0.831 | -0.028 | -3 | 0.694 |
JNK1 |
0.831 | 0.012 | 1 | 0.628 |
CLK4 |
0.830 | 0.055 | -3 | 0.758 |
DYRK2 |
0.830 | 0.030 | 1 | 0.720 |
PKCZ |
0.830 | 0.029 | 2 | 0.745 |
AMPKA2 |
0.830 | 0.011 | -3 | 0.814 |
ERK1 |
0.830 | 0.015 | 1 | 0.647 |
MAK |
0.829 | 0.042 | -2 | 0.725 |
PKCH |
0.829 | 0.014 | 2 | 0.701 |
CAMK2A |
0.828 | 0.129 | 2 | 0.814 |
PKCA |
0.828 | 0.042 | 2 | 0.703 |
AKT2 |
0.828 | 0.024 | -3 | 0.685 |
TGFBR2 |
0.828 | -0.104 | -2 | 0.765 |
MELK |
0.828 | -0.002 | -3 | 0.803 |
RSK2 |
0.827 | 0.058 | -3 | 0.756 |
IKKE |
0.826 | -0.079 | 1 | 0.774 |
PKCB |
0.826 | 0.072 | 2 | 0.718 |
DYRK1A |
0.826 | -0.003 | 1 | 0.776 |
MYLK4 |
0.826 | -0.057 | -2 | 0.758 |
SRPK1 |
0.826 | 0.089 | -3 | 0.733 |
HIPK3 |
0.826 | -0.017 | 1 | 0.745 |
IKKB |
0.825 | -0.035 | -2 | 0.811 |
MAPKAPK3 |
0.825 | 0.025 | -3 | 0.768 |
SRPK3 |
0.825 | 0.022 | -3 | 0.701 |
TTBK2 |
0.825 | -0.179 | 2 | 0.695 |
CDK6 |
0.824 | 0.020 | 1 | 0.656 |
CAMK1D |
0.824 | 0.002 | -3 | 0.692 |
PAK1 |
0.824 | -0.037 | -2 | 0.769 |
GRK4 |
0.824 | -0.076 | -2 | 0.828 |
PRKD3 |
0.824 | 0.036 | -3 | 0.750 |
HIPK4 |
0.824 | 0.025 | 1 | 0.824 |
CHK2 |
0.824 | -0.020 | -3 | 0.642 |
GRK1 |
0.824 | 0.026 | -2 | 0.768 |
PLK2 |
0.824 | -0.019 | -3 | 0.764 |
MOK |
0.823 | -0.005 | 1 | 0.749 |
P90RSK |
0.823 | 0.008 | -3 | 0.753 |
CAMK4 |
0.823 | -0.095 | -3 | 0.812 |
AKT1 |
0.823 | 0.032 | -3 | 0.705 |
CDK3 |
0.822 | 0.113 | 1 | 0.591 |
PRKD1 |
0.822 | 0.102 | -3 | 0.801 |
PAK2 |
0.822 | -0.124 | -2 | 0.757 |
SSTK |
0.822 | -0.001 | 4 | 0.813 |
IKKA |
0.822 | 0.063 | -2 | 0.802 |
NDR1 |
0.821 | -0.003 | -3 | 0.817 |
RIPK2 |
0.821 | -0.249 | 1 | 0.787 |
CLK1 |
0.821 | 0.087 | -3 | 0.752 |
CDK14 |
0.821 | -0.003 | 1 | 0.677 |
CAMK1G |
0.820 | -0.023 | -3 | 0.755 |
PKCG |
0.820 | 0.020 | 2 | 0.712 |
SGK1 |
0.820 | -0.001 | -3 | 0.599 |
QIK |
0.820 | -0.103 | -3 | 0.822 |
ULK1 |
0.819 | -0.123 | -3 | 0.804 |
STK33 |
0.819 | -0.141 | 2 | 0.583 |
CDK4 |
0.819 | -0.008 | 1 | 0.636 |
CDK8 |
0.819 | 0.019 | 1 | 0.705 |
CDK13 |
0.819 | 0.012 | 1 | 0.674 |
PKCE |
0.818 | 0.041 | 2 | 0.699 |
MARK2 |
0.818 | -0.049 | 4 | 0.738 |
PAK3 |
0.818 | -0.086 | -2 | 0.772 |
PRKD2 |
0.817 | 0.113 | -3 | 0.772 |
GCN2 |
0.817 | -0.107 | 2 | 0.785 |
NIM1 |
0.817 | -0.099 | 3 | 0.754 |
PKCI |
0.816 | -0.019 | 2 | 0.714 |
DYRK1B |
0.816 | 0.001 | 1 | 0.678 |
CDK16 |
0.816 | 0.045 | 1 | 0.595 |
PDHK3_TYR |
0.815 | 0.181 | 4 | 0.905 |
RSK3 |
0.815 | 0.006 | -3 | 0.754 |
CDK17 |
0.815 | 0.014 | 1 | 0.573 |
LATS2 |
0.815 | 0.068 | -5 | 0.769 |
PKCT |
0.815 | -0.007 | 2 | 0.709 |
BCKDK |
0.814 | -0.067 | -1 | 0.874 |
AURB |
0.814 | -0.024 | -2 | 0.639 |
DYRK3 |
0.814 | -0.018 | 1 | 0.746 |
PKACG |
0.814 | -0.004 | -2 | 0.738 |
QSK |
0.814 | -0.021 | 4 | 0.808 |
MSK1 |
0.814 | -0.003 | -3 | 0.728 |
CDK12 |
0.814 | 0.001 | 1 | 0.646 |
MNK2 |
0.813 | 0.037 | -2 | 0.805 |
CDK18 |
0.813 | 0.034 | 1 | 0.631 |
SBK |
0.812 | 0.004 | -3 | 0.574 |
PLK4 |
0.812 | -0.135 | 2 | 0.610 |
NUAK1 |
0.812 | 0.001 | -3 | 0.791 |
NDR2 |
0.812 | 0.067 | -3 | 0.814 |
MNK1 |
0.811 | 0.017 | -2 | 0.808 |
MARK1 |
0.811 | -0.093 | 4 | 0.789 |
MARK3 |
0.811 | -0.030 | 4 | 0.769 |
RSK4 |
0.811 | 0.024 | -3 | 0.717 |
CAMK1A |
0.811 | -0.003 | -3 | 0.669 |
PKG2 |
0.811 | 0.007 | -2 | 0.668 |
MSK2 |
0.811 | -0.046 | -3 | 0.715 |
MAPKAPK2 |
0.810 | 0.066 | -3 | 0.719 |
CDK7 |
0.809 | -0.023 | 1 | 0.701 |
HIPK2 |
0.808 | 0.042 | 1 | 0.628 |
DYRK4 |
0.808 | 0.019 | 1 | 0.643 |
AURA |
0.807 | -0.034 | -2 | 0.601 |
CDK9 |
0.807 | -0.040 | 1 | 0.683 |
FAM20C |
0.807 | 0.153 | 2 | 0.630 |
CLK2 |
0.807 | 0.115 | -3 | 0.741 |
SIK |
0.807 | -0.027 | -3 | 0.759 |
P70S6K |
0.806 | -0.062 | -3 | 0.698 |
BMPR2_TYR |
0.806 | 0.037 | -1 | 0.904 |
MAP2K4_TYR |
0.806 | -0.056 | -1 | 0.913 |
SRPK2 |
0.806 | 0.063 | -3 | 0.654 |
MAP2K6_TYR |
0.805 | -0.017 | -1 | 0.922 |
PHKG1 |
0.805 | -0.040 | -3 | 0.813 |
PKMYT1_TYR |
0.805 | -0.034 | 3 | 0.854 |
PDHK4_TYR |
0.804 | 0.008 | 2 | 0.831 |
TESK1_TYR |
0.804 | -0.077 | 3 | 0.873 |
CDK10 |
0.804 | 0.023 | 1 | 0.659 |
PKACB |
0.804 | 0.036 | -2 | 0.662 |
CK2A2 |
0.804 | 0.086 | 1 | 0.693 |
GRK3 |
0.803 | -0.063 | -2 | 0.687 |
MAP2K7_TYR |
0.803 | -0.182 | 2 | 0.827 |
TTBK1 |
0.803 | -0.177 | 2 | 0.619 |
PDHK1_TYR |
0.802 | -0.038 | -1 | 0.935 |
PAK6 |
0.802 | 0.080 | -2 | 0.700 |
LIMK2_TYR |
0.801 | 0.030 | -3 | 0.877 |
AURC |
0.801 | 0.018 | -2 | 0.640 |
CDK19 |
0.800 | 0.005 | 1 | 0.662 |
PKN1 |
0.800 | -0.021 | -3 | 0.721 |
MAPKAPK5 |
0.800 | -0.091 | -3 | 0.692 |
PINK1_TYR |
0.800 | -0.179 | 1 | 0.881 |
AKT3 |
0.799 | 0.011 | -3 | 0.618 |
EPHA6 |
0.798 | 0.026 | -1 | 0.915 |
CK1D |
0.797 | -0.093 | -3 | 0.434 |
RET |
0.796 | -0.073 | 1 | 0.860 |
EPHB4 |
0.796 | 0.023 | -1 | 0.915 |
PHKG2 |
0.796 | -0.005 | -3 | 0.812 |
LIMK1_TYR |
0.795 | -0.147 | 2 | 0.824 |
CK2A1 |
0.794 | 0.060 | 1 | 0.668 |
PKACA |
0.794 | 0.011 | -2 | 0.610 |
MST1R |
0.794 | -0.077 | 3 | 0.806 |
SNRK |
0.794 | -0.242 | 2 | 0.641 |
TYK2 |
0.794 | -0.117 | 1 | 0.859 |
DDR1 |
0.794 | -0.056 | 4 | 0.846 |
JAK2 |
0.794 | -0.067 | 1 | 0.860 |
YANK3 |
0.793 | -0.110 | 2 | 0.390 |
ROS1 |
0.793 | -0.072 | 3 | 0.765 |
TYRO3 |
0.792 | -0.101 | 3 | 0.795 |
CK1A2 |
0.792 | -0.095 | -3 | 0.434 |
ABL2 |
0.792 | 0.006 | -1 | 0.855 |
CSF1R |
0.792 | -0.061 | 3 | 0.791 |
BRSK2 |
0.791 | -0.108 | -3 | 0.815 |
ABL1 |
0.789 | -0.009 | -1 | 0.842 |
JAK3 |
0.789 | -0.057 | 1 | 0.834 |
FGR |
0.788 | -0.081 | 1 | 0.887 |
BRSK1 |
0.788 | -0.097 | -3 | 0.789 |
FER |
0.788 | -0.117 | 1 | 0.895 |
EPHA4 |
0.788 | -0.035 | 2 | 0.746 |
INSRR |
0.788 | -0.053 | 3 | 0.743 |
PRKX |
0.787 | 0.094 | -3 | 0.679 |
TNNI3K_TYR |
0.787 | 0.039 | 1 | 0.891 |
YES1 |
0.787 | -0.076 | -1 | 0.859 |
EPHB1 |
0.786 | -0.025 | 1 | 0.869 |
EPHB2 |
0.786 | 0.013 | -1 | 0.898 |
PDGFRB |
0.786 | -0.084 | 3 | 0.805 |
CK1E |
0.785 | -0.106 | -3 | 0.483 |
KDR |
0.785 | -0.046 | 3 | 0.748 |
KIT |
0.785 | -0.086 | 3 | 0.797 |
FLT3 |
0.785 | -0.092 | 3 | 0.790 |
YANK2 |
0.785 | -0.126 | 2 | 0.406 |
EPHB3 |
0.785 | -0.024 | -1 | 0.899 |
KIS |
0.784 | 0.033 | 1 | 0.731 |
TXK |
0.784 | -0.015 | 1 | 0.845 |
HCK |
0.784 | -0.081 | -1 | 0.838 |
FGFR2 |
0.783 | -0.124 | 3 | 0.783 |
LCK |
0.783 | -0.018 | -1 | 0.838 |
SRMS |
0.783 | -0.111 | 1 | 0.871 |
TNK2 |
0.782 | -0.077 | 3 | 0.764 |
PAK5 |
0.782 | -0.029 | -2 | 0.627 |
ITK |
0.781 | -0.089 | -1 | 0.825 |
FGFR1 |
0.780 | -0.115 | 3 | 0.755 |
BLK |
0.780 | -0.006 | -1 | 0.845 |
TNK1 |
0.780 | -0.084 | 3 | 0.770 |
JAK1 |
0.780 | -0.069 | 1 | 0.792 |
WEE1_TYR |
0.779 | -0.059 | -1 | 0.805 |
FLT1 |
0.779 | -0.050 | -1 | 0.900 |
LTK |
0.779 | -0.076 | 3 | 0.755 |
MET |
0.778 | -0.098 | 3 | 0.780 |
NEK10_TYR |
0.778 | -0.137 | 1 | 0.728 |
PDGFRA |
0.778 | -0.174 | 3 | 0.808 |
ALK |
0.777 | -0.101 | 3 | 0.737 |
AXL |
0.777 | -0.140 | 3 | 0.757 |
EPHA3 |
0.777 | -0.088 | 2 | 0.725 |
TEK |
0.777 | -0.179 | 3 | 0.733 |
EPHA7 |
0.776 | -0.051 | 2 | 0.748 |
MERTK |
0.776 | -0.107 | 3 | 0.754 |
DDR2 |
0.776 | 0.034 | 3 | 0.746 |
NTRK1 |
0.775 | -0.158 | -1 | 0.892 |
PTK6 |
0.774 | -0.187 | -1 | 0.770 |
BTK |
0.774 | -0.202 | -1 | 0.785 |
NTRK2 |
0.774 | -0.139 | 3 | 0.756 |
INSR |
0.774 | -0.105 | 3 | 0.717 |
BMX |
0.774 | -0.083 | -1 | 0.763 |
PAK4 |
0.773 | -0.013 | -2 | 0.629 |
FGFR3 |
0.773 | -0.137 | 3 | 0.755 |
FYN |
0.772 | -0.045 | -1 | 0.805 |
TEC |
0.772 | -0.129 | -1 | 0.766 |
ERBB2 |
0.772 | -0.166 | 1 | 0.815 |
FLT4 |
0.772 | -0.149 | 3 | 0.748 |
EPHA5 |
0.772 | -0.029 | 2 | 0.734 |
NTRK3 |
0.771 | -0.099 | -1 | 0.852 |
FRK |
0.771 | -0.114 | -1 | 0.856 |
MATK |
0.769 | -0.097 | -1 | 0.809 |
LYN |
0.769 | -0.116 | 3 | 0.724 |
EGFR |
0.768 | -0.054 | 1 | 0.733 |
EPHA1 |
0.768 | -0.138 | 3 | 0.748 |
EPHA8 |
0.768 | -0.077 | -1 | 0.868 |
CSK |
0.767 | -0.126 | 2 | 0.754 |
PTK2B |
0.767 | -0.102 | -1 | 0.805 |
FGFR4 |
0.767 | -0.070 | -1 | 0.848 |
PKG1 |
0.764 | -0.058 | -2 | 0.584 |
SRC |
0.763 | -0.115 | -1 | 0.810 |
PTK2 |
0.762 | -0.036 | -1 | 0.821 |
EPHA2 |
0.761 | -0.050 | -1 | 0.847 |
SYK |
0.761 | -0.037 | -1 | 0.825 |
CK1G1 |
0.759 | -0.114 | -3 | 0.489 |
MUSK |
0.759 | -0.110 | 1 | 0.714 |
IGF1R |
0.757 | -0.132 | 3 | 0.660 |
CK1G3 |
0.751 | -0.110 | -3 | 0.303 |
ERBB4 |
0.750 | -0.093 | 1 | 0.732 |
FES |
0.742 | -0.153 | -1 | 0.745 |
ZAP70 |
0.736 | -0.070 | -1 | 0.754 |
CK1G2 |
0.728 | -0.117 | -3 | 0.403 |
CK1A |
0.724 | -0.113 | -3 | 0.346 |