MK14B_CYPCA
ID MK14B_CYPCA Reviewed; 361 AA.
AC Q9I958;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=cp38b;
GN Name=mapk14b;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000312|EMBL:BAA96415.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, TISSUE SPECIFICITY, PHOSPHORYLATION
RP AT THR-181 AND TYR-183, AND ACTIVITY REGULATION.
RC TISSUE=Ovary;
RX PubMed=10880959; DOI=10.1046/j.1432-1327.2000.01479.x;
RA Hashimoto H., Fukuda M., Matsuo Y., Yokoyama Y., Nishida E., Toyohara H.,
RA Sakaguchi M.;
RT "Identification of a nuclear export signal in MKK6, an activator of the
RT carp p38 mitogen-activated protein kinases.";
RL Eur. J. Biochem. 267:4362-4371(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:0000269|PubMed:10880959};
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:0000269|PubMed:10880959};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10880959};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation by the dual specificity kinase, MKK6.
CC {ECO:0000269|PubMed:10880959}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the ovary. Lower levels
CC present in brain, gill, heart, spleen, kidney, muscle and gut.
CC {ECO:0000269|PubMed:10880959}.
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:10880959}.
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; AB023481; BAA96415.1; -; mRNA.
DR AlphaFoldDB; Q9I958; -.
DR SMR; Q9I958; -.
DR iPTMnet; Q9I958; -.
DR Ensembl; ENSCCRT00015113040; ENSCCRP00015109567; ENSCCRG00015043456.
DR BRENDA; 2.7.11.24; 1195.
DR Proteomes; UP000694384; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IDA: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; IDA: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..361
FT /note="Mitogen-activated protein kinase 14B"
FT /id="PRO_0000186298"
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; by MAP2K6"
FT /evidence="ECO:0000269|PubMed:10880959"
FT MOD_RES 183
FT /note="Phosphotyrosine; by MAP2K6"
FT /evidence="ECO:0000269|PubMed:10880959"
SQ SEQUENCE 361 AA; 41484 MW; CBE14921A49638BD CRC64;
MSHKERPTFY RQELNKTIWE VPERYQNLSP VGSGAYGSVC SALDTKSGLR VAVKKLSRPF
QSMIHAKRTY RELRLLKHMK HENVIGLLDA FSPATCLAGF NDVYLVTHLM GADLNNIVKC
QKLTDDHVQF LIYQILRGLK YIHSADIIHR DLKPSNLAVN EDCELKILDF GLARLTDDEM
TGYVATRWYR APEIMLNWMH YNMTVDIWSV GCIMAELLTG RTLFPGTDHI NQLQQIMRLT
GTPPASLISR MPSHEARNYI NSLSYMPKRN FADVFVGANP MAVDLLEKML VLDTDKRITA
SQALAHPYFA QYHDPDDEPE ADPYDQSFES RDLDIEEWKR LTYEEVISFE PPVFDGDEME
S
