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}.
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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
//
