MK14B_DANRE
ID MK14B_DANRE Reviewed; 348 AA.
AC Q9DGE1;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Mitogen-activated protein kinase 14B;
DE Short=MAP kinase 14B;
DE Short=MAPK 14B;
DE EC=2.7.11.24;
DE AltName: Full=Mitogen-activated protein kinase p38b;
DE Short=MAP kinase p38b;
DE Short=zp38b;
GN Name=mapk14b; Synonyms=mapk14;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:BAB11808.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], ACTIVITY REGULATION, PHOSPHORYLATION AT THR-181
RP AND TYR-183, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF THR-181 AND TYR-183.
RX PubMed=10995439; DOI=10.1083/jcb.150.6.1335;
RA Fujii R., Yamashita S., Hibi M., Hirano T.;
RT "Asymmetric p38 activation in zebrafish: its possible role in symmetric and
RT synchronous cleavage.";
RL J. Cell Biol. 150:1335-1348(2000).
CC -!- FUNCTION: Serine/threonine kinase which acts as an essential component
CC of the MAP kinase signal transduction pathway. Mapk14b 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 (By similarity).
CC {ECO:0000250}.
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:0000250|UniProtKB:Q90336};
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:0000250|UniProtKB:Q90336};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q90336};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation by the dual specificity kinase, MKK3.
CC {ECO:0000269|PubMed:10995439}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed at very low levels throughout
CC development. {ECO:0000269|PubMed:10995439}.
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:0000269|PubMed:10995439}.
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; AB030898; BAB11808.1; -; mRNA.
DR AlphaFoldDB; Q9DGE1; -.
DR SMR; Q9DGE1; -.
DR STRING; 7955.ENSDARP00000035686; -.
DR iPTMnet; Q9DGE1; -.
DR PaxDb; Q9DGE1; -.
DR ZFIN; ZDB-GENE-021007-1; mapk14b.
DR eggNOG; KOG0660; Eukaryota.
DR InParanoid; Q9DGE1; -.
DR BRENDA; 2.7.11.24; 928.
DR Reactome; R-DRE-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-DRE-171007; p38MAPK events.
DR Reactome; R-DRE-198753; ERK/MAPK targets.
DR Reactome; R-DRE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DRE-376172; DSCAM interactions.
DR Reactome; R-DRE-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-DRE-432142; Platelet sensitization by LDL.
DR Reactome; R-DRE-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DRE-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-DRE-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-DRE-525793; Myogenesis.
DR Reactome; R-DRE-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-6804756; Regulation of TP53 Activity through Phosphorylation.
DR PRO; PR:Q9DGE1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0038066; P:p38MAPK cascade; ISS:UniProtKB.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008352; MAPK_p38-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01773; P38MAPKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Stress response; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..348
FT /note="Mitogen-activated protein kinase 14B"
FT /id="PRO_0000186297"
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 169
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; by MAP2K3"
FT /evidence="ECO:0000269|PubMed:10995439"
FT MOD_RES 183
FT /note="Phosphotyrosine; by MAP2K3"
FT /evidence="ECO:0000269|PubMed:10995439"
FT MUTAGEN 181
FT /note="T->A: Loss of enzyme activation."
FT /evidence="ECO:0000269|PubMed:10995439"
FT MUTAGEN 183
FT /note="Y->F: Loss of enzyme activation."
FT /evidence="ECO:0000269|PubMed:10995439"
SQ SEQUENCE 348 AA; 39998 MW; 9922560377151EEE CRC64;
MSQKARPTFY RQELNKTIWE VPERYQNLSP VGSGAYGSVM SAFDGKAGLR VAVKKLSRPF
QSIIHAKRTY RELRLLKHMK HENVIGLLDV FSPATSLEGF NDVYLVTHLM GADLNNIVKC
QKLTDDHVQF LIYQILRALK YIHSADIIHR DLKPSNLAVN EDCELKILDF GLARLTDDEM
TGYVATRWYR APEIMLNWMH YNMTVDIWSV GCIMAELLTG RTLFPGTDHI NQLQQIMRLT
GTPPASLISR MPSHEARNYI SSLPHMPKRN FADVFIGANP LAVDLLEKML VLDTDKRITA
SQALAHPYFA QYHDPDDEPE ADPYDQSFES RDLEIEEWKS KIYIQNRN
