MK08_DANRE
ID MK08_DANRE Reviewed; 384 AA.
AC Q9DGD9;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Mitogen-activated protein kinase 8;
DE Short=MAP kinase 8;
DE Short=MAPK 8;
DE EC=2.7.11.24;
DE AltName: Full=Stress-activated protein kinase JNK1;
DE AltName: Full=c-Jun N-terminal kinase 1;
GN Name=mapk8; Synonyms=jnk1;
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:BAB11810.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
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: 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49185}. Nucleus
CC {ECO:0000250|UniProtKB:Q91Y86}. Synapse {ECO:0000250|UniProtKB:P49185}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the nervous system during embryogenic
CC stage 21. Expression decreases from stage 25 onwards.
CC {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-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; AB030900; BAB11810.1; -; mRNA.
DR RefSeq; NP_571796.1; NM_131721.2.
DR AlphaFoldDB; Q9DGD9; -.
DR SMR; Q9DGD9; -.
DR STRING; 7955.ENSDARP00000111769; -.
DR PaxDb; Q9DGD9; -.
DR Ensembl; ENSDART00000022471; ENSDARP00000012611; ENSDARG00000009870.
DR GeneID; 65236; -.
DR KEGG; dre:65236; -.
DR CTD; 65236; -.
DR ZFIN; ZDB-GENE-010202-1; mapk8b.
DR eggNOG; KOG0665; Eukaryota.
DR GeneTree; ENSGT00940000153692; -.
DR InParanoid; Q9DGD9; -.
DR OMA; HADSEHN; -.
DR PhylomeDB; Q9DGD9; -.
DR TreeFam; TF105100; -.
DR BRENDA; 2.7.11.24; 928.
DR Reactome; R-DRE-139910; Activation of BMF and translocation to mitochondria.
DR Reactome; R-DRE-193648; NRAGE signals death through JNK.
DR Reactome; R-DRE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DRE-2871796; FCERI mediated MAPK activation.
DR Reactome; R-DRE-376172; DSCAM interactions.
DR Reactome; R-DRE-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-DRE-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-DRE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DRE-9007892; Interleukin-38 signaling.
DR SignaLink; Q9DGD9; -.
DR PRO; PR:Q9DGD9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000009870; Expressed in retina and 25 other tissues.
DR ExpressionAtlas; Q9DGD9; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004705; F:JUN kinase activity; IBA:GO_Central.
DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
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:0048263; P:determination of dorsal identity; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007254; P:JNK cascade; IMP:MGI.
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; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..384
FT /note="Mitogen-activated protein kinase 8"
FT /id="PRO_0000186265"
FT DOMAIN 26..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 183..185
FT /note="TXY"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 33..38
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 384 AA; 44140 MW; 9596EE6183D2A6BC CRC64;
MNRNKREKEY YSIDVGDSTF TVLKRYQNLR PIGSGAQGIV CSAYDHVLDR NVAIKKLSRP
FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIQ
MELDHERLSY LLYQMLCGIK HLHAAGIIHR DLKPSNIVVK SDCTLKILDF GLARTAATGL
LMTPYVVTRY YRAPEVILGM GYQANVDVWS IGCIMAEMVR GSVLFPGTDH IDQWNKVIEQ
LGTPSQEFMM KLNQSVRTYV ENRPRYAGYS FEKLFPDVLF PADSDHNKLK ASQARDLLSK
MLVIDASKRI SVDEALQHPY INVWYDPSEV EAPPPAITDK QLDEREHSVE EWKELIYKEV
LEWEERTKNG VIRGQPASLA QVQQ
