MK09_CHICK
ID MK09_CHICK Reviewed; 382 AA.
AC P79996;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Mitogen-activated protein kinase 9;
DE Short=MAP kinase 9;
DE Short=MAPK 9;
DE EC=2.7.11.24;
DE AltName: Full=Stress-activated protein kinase JNK2;
DE AltName: Full=c-Jun N-terminal kinase 2;
GN Name=MAPK9; Synonyms=JNK2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|EMBL:BAA19188.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=9177299; DOI=10.1006/bbrc.1997.6140;
RA Ishikawa T., Nakada-Moriya Y., Ando C., Tanda N., Nishida S.,
RA Minatogawa Y., Nohno T.;
RT "Expression of the JNK2-alpha1 gene in the developing chick brain.";
RL Biochem. Biophys. Res. Commun. 234:489-492(1997).
RN [2]
RP ERRATUM OF PUBMED:9177299.
RA Ishikawa T., Nakada-Moriya Y., Ando C., Tanda N., Nishida S.,
RA Minatogawa Y., Nohno T.;
RL Biochem. Biophys. Res. Commun. 236:538-538(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 JUN and ATF2 and thus
CC regulates AP-1 transcriptional activity (By similarity). May play a
CC role in the development of the central nervous system during
CC embryogenesis. May play a role in the regulation of the circadian clock
CC (By similarity). {ECO:0000250|UniProtKB:Q9WTU6}.
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:P45984};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. {ECO:0000250|UniProtKB:P45984}.
CC -!- TISSUE SPECIFICITY: Expressed in the neuroepithelium of developing
CC brain at stages 16 to 26. {ECO:0000269|PubMed:9177299}.
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; AB000807; BAA19188.1; -; mRNA.
DR PIR; JC5531; JC5531.
DR RefSeq; NP_990426.1; NM_205095.1.
DR AlphaFoldDB; P79996; -.
DR SMR; P79996; -.
DR STRING; 9031.ENSGALP00000022313; -.
DR PaxDb; P79996; -.
DR Ensembl; ENSGALT00000060485; ENSGALP00000050909; ENSGALG00000039099.
DR GeneID; 395983; -.
DR KEGG; gga:395983; -.
DR CTD; 5601; -.
DR VEuPathDB; HostDB:geneid_395983; -.
DR eggNOG; KOG0665; Eukaryota.
DR GeneTree; ENSGT00940000158327; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P79996; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; P79996; -.
DR TreeFam; TF105100; -.
DR Reactome; R-GGA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-GGA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-GGA-437986; Activated TAK1 mediates Jun kinases (JNK) phosphorylation and activation.
DR Reactome; R-GGA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-GGA-450341; Activation of the AP-1 family of transcription factors.
DR PRO; PR:P79996; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000039099; Expressed in skeletal muscle tissue and 12 other tissues.
DR ExpressionAtlas; P79996; baseline and differential.
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: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:0009792; P:embryo development ending in birth or egg hatching; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
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..382
FT /note="Mitogen-activated protein kinase 9"
FT /id="PRO_0000186276"
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 382 AA; 44009 MW; 9A737C925465E54C CRC64;
MSDSKCDSQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP
FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKSLEE FQDVYLVMEL MDANLCQVIH
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF
MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMGELVK GCVIFQGTDH IDQWNKVIEQ
LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESDRDKLK TSQARDLLSK
MLVVDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV
MDWEERSKNG VVKDQPSAQM QQ
