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 27-MAR-2024, entry version 135. 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}. 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; AB030898; BAB11808.1; -; mRNA. DR AlphaFoldDB; Q9DGE1; -. DR SMR; Q9DGE1; -. DR STRING; 7955.ENSDARP00000035686; -. DR iPTMnet; Q9DGE1; -. DR PaxDb; 7955-ENSDARP00000035686; -. DR AGR; ZFIN:ZDB-GENE-021007-1; -. 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 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: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 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; 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 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 //