ID MK14_XENLA Reviewed; 361 AA. AC P47812; Q5D076; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 140. DE RecName: Full=Mitogen-activated protein kinase 14; DE Short=MAP kinase 14; DE Short=MAPK 14; DE EC=2.7.11.24; DE AltName: Full=Mitogen-activated protein kinase 2; DE Short=MAP kinase 2; DE Short=MPK2; GN Name=mapk14; Synonyms=mpk2; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7923353; DOI=10.1016/0092-8674(94)90277-1; RA Rouse J., Cohen P., Trigon S., Morange M., Alonso-Llamazares A., RA Zamanillo D., Hunt T., Nebreda A.R.; RT "A novel kinase cascade triggered by stress and heat shock that stimulates RT MAPKAP kinase-2 and phosphorylation of the small heat shock proteins."; RL Cell 78:1027-1037(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Spleen; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Serine/threonine kinase which acts as an essential component CC of the MAP kinase signal transduction pathway. mapk14a is one of the CC four p38 MAPKs which play an important role in the cascades of cellular CC responses evoked by extracellular stimuli such as pro-inflammatory CC cytokines or physical stress leading to direct activation of CC transcription factors. Accordingly, p38 MAPKs phosphorylate a broad CC range of proteins and it has been estimated that they may have CC approximately 200 to 300 substrates each. Some of the targets are CC downstream kinases which are activated through phosphorylation and CC further phosphorylate additional targets. MPK2 is activated by upstream CC MAPKK/MAPKKK and stimulates MAPKAP kinase 2 to phosphorylate small heat CC shock proteins. Does not phosphorylate myelin basic protein or MAPKAP CC kinase 1. 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 -!- 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine CC phosphorylation. CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues CC whose phosphorylation activates the MAP kinases. CC -!- PTM: Dually phosphorylated on Thr-181 and Tyr-183, which activates the CC enzyme. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. MAP kinase subfamily. {ECO:0000305}. 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 EMBL; X80751; CAA56727.1; -; mRNA. DR EMBL; BC056064; AAH56064.1; -; mRNA. DR PIR; A54805; A54805. DR RefSeq; NP_001080300.1; NM_001086831.1. DR AlphaFoldDB; P47812; -. DR SMR; P47812; -. DR BioGRID; 98234; 1. DR iPTMnet; P47812; -. DR MaxQB; P47812; -. DR DNASU; 379992; -. DR GeneID; 379992; -. DR KEGG; xla:379992; -. DR AGR; Xenbase:XB-GENE-1018624; -. DR CTD; 379992; -. DR Xenbase; XB-GENE-1018624; mapk14.S. DR OMA; PGRDYGH; -. DR OrthoDB; 158564at2759; -. DR BRENDA; 2.7.11.24; 6725. DR Proteomes; UP000186698; Chromosome 2S. DR Bgee; 379992; Expressed in zone of skin and 19 other cell types or tissues. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; ISS:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB. DR GO; GO:0038066; P:p38MAPK cascade; ISS:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB. DR GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB. DR GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR CDD; cd07877; STKc_p38alpha; 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; IPR038784; MAPK14. DR InterPro; IPR008352; MAPK_p38-like. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF110; MITOGEN-ACTIVATED PROTEIN KINASE 14; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01773; P38MAPKINASE. 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. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Stress response; KW Transcription; Transcription regulation; Transferase. FT CHAIN 1..361 FT /note="Mitogen-activated protein kinase 14" FT /id="PRO_0000186299" FT DOMAIN 25..309 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOTIF 181..183 FT /note="TXY" FT ACT_SITE 151 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 31..39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 54 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 181 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 183 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" SQ SEQUENCE 361 AA; 41719 MW; F2B2E6C40800A70D CRC64; MSSNQSYVFY RQELNKTLWE VPDRYQNLTP VGSGAYGSVC SSFDTRTALR IAVKKLSRPF QSIIHAKRTY RELRLLKHMK HENVIGLLDV FSPAKSFEEF NDVYLVTHLM GADLNNIVKC QKLTDDHVQF LIYQILRGLK YIHSAGIIHR DLKPSNLAVN EDCELKILDF GLARHTDEEM TGYVATRWYR APEIMLNWMH YNQTVDIWSV GCIMAELLTG RTLFPGTDHI DQLKLILRLV GTPEPELLQK ISSEAARNYI QSLPYMPKMN FEDVFLGANP QAVDLLEKML VLDTDKRITA AEALAHSYFA QYHDPDDEPI AEPYDQSFES RELDIEEWKR LTYEEVTCFV PPPLDSEEME S //