MK08B_CYPCA
ID MK08B_CYPCA Reviewed; 427 AA.
AC O42099;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Mitogen-activated protein kinase 8B;
DE Short=MAP kinase 8B;
DE Short=MAPK 8B;
DE EC=2.7.11.24;
DE AltName: Full=Stress-activated protein kinase JNKb;
DE AltName: Full=c-Jun N-terminal kinase B;
GN Name=mapk8b;
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:BAA22598.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=9378717; DOI=10.1093/oxfordjournals.jbchem.a021764;
RA Hashimoto H., Matsuo Y., Yokoyama Y., Toyohara H., Sakaguchi M.;
RT "Structure and expression of carp mitogen-activated protein kinases
RT homologous to mammalian JNK/SAPK.";
RL J. Biochem. 122:381-386(1997).
CC -!- FUNCTION: Responds to activation by environmental stress and pro-
CC inflammatory cytokines by phosphorylating a number of transcription
CC factors, primarily components of AP-1 such as c-Jun and ATF2 and thus
CC regulates AP-1 transcriptional activity. May play a role in the
CC regulation of the circadian clock. {ECO:0000250|UniProtKB:P45983,
CC ECO:0000250|UniProtKB:Q91Y86}.
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;
CC Evidence={ECO:0000250|UniProtKB:P45983};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. {ECO:0000250|UniProtKB:P45983}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the ovary and at lower
CC levels in brain, gill, heart, spleen, liver, kidney, muscle, bladder
CC and gut. {ECO:0000269|PubMed:9378717}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-183 and Tyr-185, 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; AB001744; BAA22598.1; -; mRNA.
DR PIR; JC5694; JC5694.
DR AlphaFoldDB; O42099; -.
DR SMR; O42099; -.
DR Ensembl; ENSCCRT00015002500; ENSCCRP00015002368; ENSCCRG00015001463.
DR BRENDA; 2.7.11.24; 1195.
DR Proteomes; UP000694384; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008351; MAPK_JNK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01772; JNKMAPKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Biological rhythms; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..427
FT /note="Mitogen-activated protein kinase 8B"
FT /id="PRO_0000186267"
FT DOMAIN 26..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 372..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 183..185
FT /note="TXY"
FT COMPBIAS 382..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 48295 MW; 9405E55B6F9E6D6F CRC64;
MNKNKREKEF YSVDVGDSTF TVLKRYQNLR PIGSGAQGIV CSAYDHNLER NVAIKKLSRP
FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIQ
MELDHERLSY LLYQMLCGTK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTAATGL
LMTPYVVTRY YRAPEVILGM GYQANVDVWS VGCIMAEMVR GSVLFPGSDH IDQWNKVIEQ
LGTPSQEFMM KLNQSVRTYV ENRPRYTGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK
MLVIDASKRI SVDEALQHPY INVWYDPAEV EAPPPLIIDK QLDEREHTVE EWKELIFKEV
LDWEERMKNG VIRGQPSPIG AAVINGSPQP SSSSSINDVS SMSTEPTVAS DTDSSLEASA
GPLSCCR
