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Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2 7 11 24) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2)

 MK09_MOUSE              Reviewed;         423 AA.
Q9WTU6; Q5NCK9; Q5NCL5; Q8C097; Q8VDD2; Q9WTU4; Q9WTU5;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
05-DEC-2018, entry version 184.
RecName: Full=Mitogen-activated protein kinase 9;
Short=MAP kinase 9;
Short=MAPK 9;
EC=2.7.11.24 {ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:16973441, ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9806643};
AltName: Full=Stress-activated protein kinase JNK2;
AltName: Full=c-Jun N-terminal kinase 2;
Name=Mapk9; Synonyms=Jnk2, Prkm9;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1 AND
BETA-2), FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
PubMed=9806643; DOI=10.1016/S1074-7613(00)80640-8;
Yang D.D., Conze D., Whitmarsh A.J., Barrett T., Davis R.J.,
Rincon M., Flavell R.A.;
"Differentiation of CD4+ T cells to Th1 cells requires MAP kinase
JNK2.";
Immunity 9:575-585(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
TISSUE=Brain;
PubMed=10523642; DOI=10.1128/MCB.19.11.7539;
Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N.,
Sugiyama K., Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
"JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein
that functions as a scaffold factor in the JNK signaling pathway.";
Mol. Cell. Biol. 19:7539-7548(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1
AND BETA-2), AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10674476; DOI=10.1097/00001756-200002070-00017;
Casanova E., Callejo A.I., Calvo P., Chinchetru M.A.;
"Analysis of splicing of four mouse JNK/SAPKalpha variants.";
NeuroReport 11:305-309(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
STRAIN=FVB/N; TISSUE=Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, ACTIVITY REGULATION, AND INDUCTION.
TISSUE=Embryonic stem cell, and T-cell;
PubMed=10811224; DOI=10.1038/35011091;
Dong C., Yang D.D., Tournier C., Whitmarsh A.J., Xu J., Davis R.J.,
Flavell R.A.;
"JNK is required for effector T-cell function but not for T-cell
activation.";
Nature 405:91-94(2000).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
TISSUE=Hippocampus;
PubMed=11562351; DOI=10.1101/gad.922801;
Whitmarsh A.J., Kuan C.-Y., Kennedy N.J., Kelkar N., Haydar T.F.,
Mordes J.P., Appel M., Rossini A.A., Jones S.N., Flavell R.A.,
Rakic P., Davis R.J.;
"Requirement of the JIP1 scaffold protein for stress-induced JNK
activation.";
Genes Dev. 15:2421-2432(2001).
[9]
INTERACTION WITH DCLK2.
PubMed=16628014; DOI=10.4161/cc.5.9.2715;
Coquelle F.M., Levy T., Bergmann S., Wolf S.G., Bar-El D., Sapir T.,
Brody Y., Orr I., Barkai N., Eichele G., Reiner O.;
"Common and divergent roles for members of the mouse DCX
superfamily.";
Cell Cycle 5:976-983(2006).
[10]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=16973441; DOI=10.1016/j.molcel.2006.07.028;
Jaeschke A., Karasarides M., Ventura J.J., Ehrhardt A., Zhang C.,
Flavell R.A., Shokat K.M., Davis R.J.;
"JNK2 is a positive regulator of the cJun transcription factor.";
Mol. Cell 23:899-911(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
FUNCTION IN NEURITE GROWTH.
PubMed=21554942; DOI=10.1016/j.heares.2011.04.011;
Atkinson P.J., Cho C.H., Hansen M.R., Green S.H.;
"Activity of all JNK isoforms contributes to neurite growth in spiral
ganglion neurons.";
Hear. Res. 278:77-85(2011).
[14]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=22441692; DOI=10.1038/embor.2012.37;
Yoshitane H., Honma S., Imamura K., Nakajima H., Nishide S.Y., Ono D.,
Kiyota H., Shinozaki N., Matsuki H., Wada N., Doi H., Hamada T.,
Honma K., Fukada Y.;
"JNK regulates the photic response of the mammalian circadian clock.";
EMBO Rep. 13:455-461(2012).
[15]
IDENTIFICATION IN A COMPLEX WITH SH3RF1; RAC2; MAP3K7; MAPK8IP1;
MAP2K7 AND MAPK8.
PubMed=27084103; DOI=10.4049/jimmunol.1501728;
Cunningham C.A., Cardwell L.N., Guan Y., Teixeiro E., Daniels M.A.;
"POSH regulates CD4+ T cell differentiation and survival.";
J. Immunol. 196:4003-4013(2016).
[16]
FUNCTION, INTERACTION WITH POU5F1, AND SUBCELLULAR LOCATION.
PubMed=29153991; DOI=10.1016/j.stemcr.2017.10.017;
Bae K.B., Yu D.H., Lee K.Y., Yao K., Ryu J., Lim D.Y., Zykova T.A.,
Kim M.O., Bode A.M., Dong Z.;
"Serine 347 Phosphorylation by JNKs Negatively Regulates OCT4 Protein
Stability in Mouse Embryonic Stem Cells.";
Stem Cell Reports 9:2050-2064(2017).
-!- FUNCTION: Serine/threonine-protein kinase involved in various
processes such as cell proliferation, differentiation, migration,
transformation and programmed cell death. Extracellular stimuli
such as proinflammatory cytokines or physical stress stimulate the
stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK)
signaling pathway. In this cascade, two dual specificity kinases
MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2.
In turn, MAPK9/JNK2 phosphorylates a number of transcription
factors, primarily components of AP-1 such as JUN and ATF2 and
thus regulates AP-1 transcriptional activity. In response to
oxidative or ribotoxic stresses, inhibits rRNA synthesis by
phosphorylating and inactivating the RNA polymerase 1-specific
transcription initiation factor RRN3. Promotes stressed cell
apoptosis by phosphorylating key regulatory factors including TP53
and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized
differentiation of T-helper cells into Th1 cells. Upon T-cell
receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7
and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important
role in the osmotic stress-induced epithelial tight-junctions
disruption. When activated, promotes beta-catenin/CTNNB1
degradation and inhibits the canonical Wnt signaling pathway.
Participates also in neurite growth in spiral ganglion neurons.
Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role
in the regulation of the circadian clock (PubMed:22441692).
Phosphorylates POU5F1, which results in the inhibition of POU5F1's
transcriptional activity and enhances its proteosomal degradation
(PubMed:29153991). {ECO:0000269|PubMed:10811224,
ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:16973441,
ECO:0000269|PubMed:21554942, ECO:0000269|PubMed:22441692,
ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9806643}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.24; Evidence={ECO:0000269|PubMed:11562351,
ECO:0000269|PubMed:16973441, ECO:0000269|PubMed:22441692,
ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9806643};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.24; Evidence={ECO:0000269|PubMed:11562351,
ECO:0000269|PubMed:16973441, ECO:0000269|PubMed:22441692,
ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9806643};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P45984};
-!- ACTIVITY REGULATION: Activated by threonine and tyrosine
phosphorylation by either of two dual specificity kinases, MAP2K4
and MAP2K7. MAP2K4 shows a strong preference for Tyr-185 while
MAP2K7 phosphorylates Tyr-183 preferentially. Inhibited by dual
specificity phosphatases, such as DUSP1.
{ECO:0000269|PubMed:10811224}.
-!- SUBUNIT: Interacts with MECOM (By similarity). Binds to at least
four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2,
MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also
bind other components of the JNK signaling pathway
(PubMed:11562351). Interacts with NFATC4 (By similarity).
Interacts with ATF7; the interaction does not phosphorylate ATF7
but acts as a docking site for ATF7-associated partners such as
JUN (By similarity). Interacts with BCL10 (By similarity).
Interacts with CTNNB1 and GSK3B (By similarity). Interacts with
DCLK2 (PubMed:16628014). Interacts with MAPKBP1 (By similarity).
Interacts with POU5F1; phosphorylates POU5F1 at 'Ser-347'
(PubMed:29153991). Found in a complex with SH3RF1, RAC2,
MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1
(PubMed:27084103). {ECO:0000250|UniProtKB:P45984,
ECO:0000250|UniProtKB:P49186, ECO:0000269|PubMed:11562351,
ECO:0000269|PubMed:16628014, ECO:0000269|PubMed:27084103,
ECO:0000269|PubMed:29153991}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P45984}.
Nucleus {ECO:0000269|PubMed:29153991}. Note=Colocalizes with
POU5F1 in the nucleus. {ECO:0000269|PubMed:29153991}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=Alpha-2;
IsoId=Q9WTU6-1; Sequence=Displayed;
Name=Alpha-1;
IsoId=Q9WTU6-2; Sequence=VSP_004837;
Name=Beta-1;
IsoId=Q9WTU6-3; Sequence=VSP_004836, VSP_004837;
Name=Beta-2;
IsoId=Q9WTU6-4; Sequence=VSP_004836;
-!- TISSUE SPECIFICITY: All four isoforms are widely distributed in
brain. Isoforms alpha-1 and alpha-2 are predominantly expressed in
hippocampus, cerebral cortex, caudate-putamen, amygdala and the
granule layer of the cerebellum. Alpha-1 is more abundant than
alpha-2 in the periaqueductal region and the substantia nigra.
{ECO:0000269|PubMed:10674476}.
-!- INDUCTION: In T-cells, following T-cell receptor (TCR) activation.
Levels peak 48 hours after TCR and CD-28 costimulation.
{ECO:0000269|PubMed:10811224, ECO:0000269|PubMed:9806643}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and
MAP2K4, which activates the enzyme. Autophosphorylated in vitro.
{ECO:0000250|UniProtKB:P45984}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
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EMBL; AF052466; AAD22576.1; -; mRNA.
EMBL; AF052467; AAD22577.1; -; mRNA.
EMBL; AF052468; AAD22578.1; -; mRNA.
EMBL; AF052469; AAD22579.1; -; mRNA.
EMBL; AB005664; BAA85876.1; -; mRNA.
EMBL; AJ315339; CAC88132.1; ALT_SEQ; Genomic_DNA.
EMBL; AJ315340; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315341; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315342; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315343; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315344; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315345; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315346; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315347; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315348; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315349; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315350; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AK031959; BAC27623.1; -; mRNA.
EMBL; AL606479; CAI23940.1; -; Genomic_DNA.
EMBL; AL606479; CAI23941.1; -; Genomic_DNA.
EMBL; BC028341; AAH28341.1; -; mRNA.
CCDS; CCDS24623.1; -. [Q9WTU6-4]
CCDS; CCDS24624.1; -. [Q9WTU6-2]
CCDS; CCDS48782.1; -. [Q9WTU6-1]
CCDS; CCDS48783.1; -. [Q9WTU6-3]
RefSeq; NP_001157143.1; NM_001163671.1. [Q9WTU6-1]
RefSeq; NP_001157144.1; NM_001163672.1. [Q9WTU6-3]
RefSeq; NP_058657.1; NM_016961.3. [Q9WTU6-2]
RefSeq; NP_997575.2; NM_207692.2. [Q9WTU6-4]
UniGene; Mm.68933; -.
ProteinModelPortal; Q9WTU6; -.
SMR; Q9WTU6; -.
BioGrid; 204972; 4.
DIP; DIP-31076N; -.
ELM; Q9WTU6; -.
IntAct; Q9WTU6; 6.
MINT; Q9WTU6; -.
STRING; 10090.ENSMUSP00000020634; -.
BindingDB; Q9WTU6; -.
ChEMBL; CHEMBL2034797; -.
iPTMnet; Q9WTU6; -.
PhosphoSitePlus; Q9WTU6; -.
PaxDb; Q9WTU6; -.
PeptideAtlas; Q9WTU6; -.
PRIDE; Q9WTU6; -.
Ensembl; ENSMUST00000020634; ENSMUSP00000020634; ENSMUSG00000020366. [Q9WTU6-4]
Ensembl; ENSMUST00000043321; ENSMUSP00000042744; ENSMUSG00000020366. [Q9WTU6-1]
Ensembl; ENSMUST00000102778; ENSMUSP00000099839; ENSMUSG00000020366. [Q9WTU6-2]
Ensembl; ENSMUST00000109178; ENSMUSP00000104807; ENSMUSG00000020366. [Q9WTU6-3]
Ensembl; ENSMUST00000109179; ENSMUSP00000104808; ENSMUSG00000020366. [Q9WTU6-2]
Ensembl; ENSMUST00000164643; ENSMUSP00000132864; ENSMUSG00000020366. [Q9WTU6-3]
Ensembl; ENSMUST00000178543; ENSMUSP00000136977; ENSMUSG00000020366. [Q9WTU6-1]
GeneID; 26420; -.
KEGG; mmu:26420; -.
UCSC; uc007ird.2; mouse. [Q9WTU6-2]
UCSC; uc007irh.2; mouse. [Q9WTU6-1]
UCSC; uc007iri.2; mouse. [Q9WTU6-3]
CTD; 5601; -.
MGI; MGI:1346862; Mapk9.
eggNOG; KOG0665; Eukaryota.
eggNOG; ENOG410XSHI; LUCA.
GeneTree; ENSGT00940000158327; -.
HOVERGEN; HBG014652; -.
InParanoid; Q9WTU6; -.
KO; K04440; -.
OMA; WEERNKN; -.
OrthoDB; EOG091G09G2; -.
PhylomeDB; Q9WTU6; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 3474.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-MMU-450341; Activation of the AP-1 family of transcription factors.
PRO; PR:Q9WTU6; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020366; Expressed in 286 organ(s), highest expression level in secondary oocyte.
CleanEx; MM_MAPK9; -.
ExpressionAtlas; Q9WTU6; baseline and differential.
Genevisible; Q9WTU6; MM.
GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043204; C:perikaryon; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISO:MGI.
GO; GO:0004705; F:JUN kinase activity; ISS:UniProtKB.
GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IMP:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0034644; P:cellular response to UV; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
GO; GO:0007258; P:JUN phosphorylation; ISO:MGI.
GO; GO:0048666; P:neuron development; IBA:GO_Central.
GO; GO:0031175; P:neuron projection development; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
GO; GO:0010770; P:positive regulation of cell morphogenesis involved in differentiation; ISO:MGI.
GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
GO; GO:0071803; P:positive regulation of podosome assembly; IMP:MGI.
GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; ISO:MGI.
GO; GO:0032308; P:positive regulation of prostaglandin secretion; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
GO; GO:1901485; P:positive regulation of transcription factor catabolic process; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0061833; P:protein localization to tricellular tight junction; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0046328; P:regulation of JNK cascade; ISO:MGI.
GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI.
GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:0046686; P:response to cadmium ion; IGI:MGI.
GO; GO:0042493; P:response to drug; ISO:MGI.
GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008351; MAPK_JNK.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01772; JNKMAPKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Biological rhythms;
Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 423 Mitogen-activated protein kinase 9.
/FTId=PRO_0000186274.
DOMAIN 26 321 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 33 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 183 185 TXY.
ACT_SITE 151 151 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 55 55 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 183 183 Phosphothreonine; by MAP2K7.
{ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079}.
MOD_RES 185 185 Phosphotyrosine; by MAP2K4.
{ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 216 230 AEMVLHKVLFPGRDY -> GELVKGCVIFQGTDH (in
isoform Beta-1 and isoform Beta-2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9806643}.
/FTId=VSP_004836.
VAR_SEQ 377 423 DAAVSSKATPSQSSSINDISSMSTEHTLASDTDSSLDASTG
PLEGCR -> AQMQQ (in isoform Alpha-1 and
isoform Beta-1).
{ECO:0000303|PubMed:10523642,
ECO:0000303|PubMed:9806643}.
/FTId=VSP_004837.
CONFLICT 223 223 V -> C (in Ref. 3). {ECO:0000305}.
CONFLICT 237 237 V -> A (in Ref. 3; CAC88132).
{ECO:0000305}.
CONFLICT 386 386 P -> A (in Ref. 4; BAC27623).
{ECO:0000305}.
SEQUENCE 423 AA; 48189 MW; 0E759B486ABCE20D CRC64;
MSDSKSDGQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP
FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF
MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMAEMVL HKVLFPGRDY IDQWNKVIEQ
LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK
MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV
MDWEERSKNG VKDQPSDAAV SSKATPSQSS SINDISSMST EHTLASDTDS SLDASTGPLE
GCR


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