ID E1B8P9_BOVIN Unreviewed; 456 AA. AC E1B8P9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 2. DT 27-MAR-2024, entry version 94. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|ARBA:ARBA00012411, ECO:0000256|RuleBase:RU361165}; DE EC=2.7.11.24 {ECO:0000256|ARBA:ARBA00012411, ECO:0000256|RuleBase:RU361165}; GN Name=MAPK3 {ECO:0000313|Ensembl:ENSBTAP00000021507.4, GN ECO:0000313|VGNC:VGNC:31219}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000021507.4, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000021507.4, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000021507.4, RC ECO:0000313|Proteomes:UP000009136}; RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A., RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C., RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.; RT "ARS-UCD1.2."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSBTAP00000021507.4} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000021507.4}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CC Evidence={ECO:0000256|ARBA:ARBA00000494}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.24; Evidence={ECO:0000256|ARBA:ARBA00000088, CC ECO:0000256|RuleBase:RU361165}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU361165}; CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine CC phosphorylation. {ECO:0000256|RuleBase:RU361165}. CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion CC {ECO:0000256|ARBA:ARBA00004246}. Membrane, caveola CC {ECO:0000256|ARBA:ARBA00004345}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. MAP kinase subfamily. {ECO:0000256|RuleBase:RU361165}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; E1B8P9; -. DR SMR; E1B8P9; -. DR STRING; 9913.ENSBTAP00000021507; -. DR Ensembl; ENSBTAT00000021507.4; ENSBTAP00000021507.4; ENSBTAG00000016156.5. DR VEuPathDB; HostDB:ENSBTAG00000016156; -. DR VGNC; VGNC:31219; MAPK3. DR eggNOG; KOG0660; Eukaryota. DR GeneTree; ENSGT00940000160691; -. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; E1B8P9; -. DR OMA; CYFLYQM; -. DR TreeFam; TF105097; -. DR Reactome; R-BTA-110056; MAPK3 (ERK1) activation. DR Reactome; R-BTA-112409; RAF-independent MAPK1/3 activation. DR Reactome; R-BTA-1169408; ISG15 antiviral mechanism. DR Reactome; R-BTA-1181150; Signaling by NODAL. DR Reactome; R-BTA-1295596; Spry regulation of FGF signaling. DR Reactome; R-BTA-1502540; Signaling by Activin. DR Reactome; R-BTA-162658; Golgi Cisternae Pericentriolar Stack Reorganization. DR Reactome; R-BTA-170968; Frs2-mediated activation. DR Reactome; R-BTA-198753; ERK/MAPK targets. DR Reactome; R-BTA-202670; ERKs are inactivated. DR Reactome; R-BTA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-BTA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity. DR Reactome; R-BTA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription. DR Reactome; R-BTA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-BTA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-BTA-2559585; Oncogene Induced Senescence. DR Reactome; R-BTA-2871796; FCERI mediated MAPK activation. DR Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-BTA-375165; NCAM signaling for neurite out-growth. DR Reactome; R-BTA-445144; Signal transduction by L1. DR Reactome; R-BTA-450341; Activation of the AP-1 family of transcription factors. DR Reactome; R-BTA-456926; Thrombin signalling through proteinase activated receptors (PARs). DR Reactome; R-BTA-5654726; Negative regulation of FGFR1 signaling. DR Reactome; R-BTA-5654727; Negative regulation of FGFR2 signaling. DR Reactome; R-BTA-5654732; Negative regulation of FGFR3 signaling. DR Reactome; R-BTA-5654733; Negative regulation of FGFR4 signaling. DR Reactome; R-BTA-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-BTA-5668599; RHO GTPases Activate NADPH Oxidases. DR Reactome; R-BTA-5673001; RAF/MAP kinase cascade. DR Reactome; R-BTA-5674135; MAP2K and MAPK activation. DR Reactome; R-BTA-5674499; Negative feedback regulation of MAPK pathway. DR Reactome; R-BTA-5675221; Negative regulation of MAPK pathway. DR Reactome; R-BTA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-BTA-73728; RNA Polymerase I Promoter Opening. DR Reactome; R-BTA-74749; Signal attenuation. DR Reactome; R-BTA-877300; Interferon gamma signaling. DR Reactome; R-BTA-881907; Gastrin-CREB signalling pathway via PKC and MAPK. DR Reactome; R-BTA-8939211; ESR-mediated signaling. DR Reactome; R-BTA-9627069; Regulation of the apoptosome activity. DR Reactome; R-BTA-9732724; IFNG signaling activates MAPKs. DR Reactome; R-BTA-982772; Growth hormone receptor signaling. DR Proteomes; UP000009136; Chromosome 25. DR Bgee; ENSBTAG00000016156; Expressed in temporal cortex and 104 other cell types or tissues. DR ExpressionAtlas; E1B8P9; baseline and differential. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProt. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005769; C:early endosome; IEA:UniProt. DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt. DR GO; GO:0005770; C:late endosome; IEA:UniProt. DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0031143; C:pseudopodium; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0019902; F:phosphatase binding; IEA:Ensembl. DR GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl. DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl. DR GO; GO:0061308; P:cardiac neural crest cell development involved in heart development; IEA:Ensembl. DR GO; GO:0051216; P:cartilage development; IEA:Ensembl. DR GO; GO:0072584; P:caveolin-mediated endocytosis; IEA:UniProt. DR GO; GO:0034198; P:cellular response to amino acid starvation; IEA:Ensembl. DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0006351; P:DNA-templated transcription; IEA:Ensembl. DR GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; IEA:Ensembl. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0060324; P:face development; IEA:Ensembl. DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0042552; P:myelination; IEA:Ensembl. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:Ensembl. DR GO; GO:0042473; P:outer ear morphogenesis; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl. DR GO; GO:0120041; P:positive regulation of macrophage proliferation; IEA:Ensembl. DR GO; GO:1904355; P:positive regulation of telomere capping; IEA:Ensembl. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:1904417; P:positive regulation of xenophagy; IEA:Ensembl. DR GO; GO:0030641; P:regulation of cellular pH; IEA:Ensembl. DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:UniProt. DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; IEA:UniProt. DR GO; GO:0090170; P:regulation of Golgi inheritance; IEA:UniProt. DR GO; GO:0030278; P:regulation of ossification; IEA:Ensembl. DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IEA:UniProt. DR GO; GO:0070849; P:response to epidermal growth factor; IEA:Ensembl. DR GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl. DR GO; GO:0014044; P:Schwann cell development; IEA:Ensembl. DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl. DR GO; GO:0042770; P:signal transduction in response to DNA damage; IEA:Ensembl. DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:Ensembl. DR GO; GO:0048538; P:thymus development; IEA:Ensembl. DR GO; GO:0030878; P:thyroid gland development; IEA:Ensembl. DR GO; GO:0060440; P:trachea formation; IEA:Ensembl. DR GO; GO:0098792; P:xenophagy; IEA:Ensembl. DR CDD; cd07849; STKc_ERK1_2_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR008349; MAPK_ERK1/2. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF393; MITOGEN-ACTIVATED PROTEIN KINASE 3; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01770; ERK1ERK2MAPK. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS01351; MAPK; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361165}; KW Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361165}. FT DOMAIN 119..407 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 149 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 456 AA; 52515 MW; F9F83178E3FCBFA4 CRC64; MPGLSSNQVT FSFHICERGH MCEEATSHGY YEISIVSLSI GPGSRRFHLK PRATPRAEWG QRGHVAWSGS RLQHSFARWL WVRSPGRPTG QHSVRGWGEG LDSLETALGS FYVDWSRRGR QLQYIGEGAY GMVSSAYDHV RKTRVAIKKI SPFEHQTYCQ RTLREIQILL RFRHENVIGI RDILRAPTLE AMRDVYIVQD LMETDLYKLL KSQQLSNDHV CYFLYQILRG LKYIHSANVL HRDLKPSNLL INTTCDLKIC DFGLARIADP EHDHTGFLTE YVATRWYRAP EIMLNSKGYT KSIDIWSVGC ILAEMLSNRP IFPGKHYLDQ LNHILGILGS PSQEDLNCII NMKARNYLQS LPSKTKVAWA KLFPKSDPKA LDLLDRMLTF NPNKRITVEE ALAHPYLEQY YDPTDEPVAE EPFTFDMELD DLPKERLKEL IFQETARFQP GVLEAS //