MK09_MOUSE
ID MK09_MOUSE Reviewed; 423 AA.
AC Q9WTU6; Q5NCK9; Q5NCL5; Q8C097; Q8VDD2; Q9WTU4; Q9WTU5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Mitogen-activated protein kinase 9;
DE Short=MAP kinase 9;
DE Short=MAPK 9;
DE 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};
DE AltName: Full=Stress-activated protein kinase JNK2;
DE AltName: Full=c-Jun N-terminal kinase 2;
GN Name=Mapk9; Synonyms=Jnk2, Prkm9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1 AND BETA-2),
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=9806643; DOI=10.1016/s1074-7613(00)80640-8;
RA Yang D.D., Conze D., Whitmarsh A.J., Barrett T., Davis R.J., Rincon M.,
RA Flavell R.A.;
RT "Differentiation of CD4+ T cells to Th1 cells requires MAP kinase JNK2.";
RL Immunity 9:575-585(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
RC TISSUE=Brain;
RX PubMed=10523642; DOI=10.1128/mcb.19.11.7539;
RA Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N., Sugiyama K.,
RA Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
RT "JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that
RT functions as a scaffold factor in the JNK signaling pathway.";
RL Mol. Cell. Biol. 19:7539-7548(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1 AND
RP BETA-2), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10674476; DOI=10.1097/00001756-200002070-00017;
RA Casanova E., Callejo A.I., Calvo P., Chinchetru M.A.;
RT "Analysis of splicing of four mouse JNK/SAPKalpha variants.";
RL NeuroReport 11:305-309(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, AND INDUCTION.
RC TISSUE=Embryonic stem cell, and T-cell;
RX PubMed=10811224; DOI=10.1038/35011091;
RA Dong C., Yang D.D., Tournier C., Whitmarsh A.J., Xu J., Davis R.J.,
RA Flavell R.A.;
RT "JNK is required for effector T-cell function but not for T-cell
RT activation.";
RL Nature 405:91-94(2000).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC TISSUE=Hippocampus;
RX PubMed=11562351; DOI=10.1101/gad.922801;
RA Whitmarsh A.J., Kuan C.-Y., Kennedy N.J., Kelkar N., Haydar T.F.,
RA Mordes J.P., Appel M., Rossini A.A., Jones S.N., Flavell R.A., Rakic P.,
RA Davis R.J.;
RT "Requirement of the JIP1 scaffold protein for stress-induced JNK
RT activation.";
RL Genes Dev. 15:2421-2432(2001).
RN [9]
RP INTERACTION WITH DCLK2.
RX PubMed=16628014; DOI=10.4161/cc.5.9.2715;
RA Coquelle F.M., Levy T., Bergmann S., Wolf S.G., Bar-El D., Sapir T.,
RA Brody Y., Orr I., Barkai N., Eichele G., Reiner O.;
RT "Common and divergent roles for members of the mouse DCX superfamily.";
RL Cell Cycle 5:976-983(2006).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16973441; DOI=10.1016/j.molcel.2006.07.028;
RA Jaeschke A., Karasarides M., Ventura J.J., Ehrhardt A., Zhang C.,
RA Flavell R.A., Shokat K.M., Davis R.J.;
RT "JNK2 is a positive regulator of the cJun transcription factor.";
RL Mol. Cell 23:899-911(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION IN NEURITE GROWTH.
RX PubMed=21554942; DOI=10.1016/j.heares.2011.04.011;
RA Atkinson P.J., Cho C.H., Hansen M.R., Green S.H.;
RT "Activity of all JNK isoforms contributes to neurite growth in spiral
RT ganglion neurons.";
RL Hear. Res. 278:77-85(2011).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22441692; DOI=10.1038/embor.2012.37;
RA Yoshitane H., Honma S., Imamura K., Nakajima H., Nishide S.Y., Ono D.,
RA Kiyota H., Shinozaki N., Matsuki H., Wada N., Doi H., Hamada T., Honma K.,
RA Fukada Y.;
RT "JNK regulates the photic response of the mammalian circadian clock.";
RL EMBO Rep. 13:455-461(2012).
RN [15]
RP IDENTIFICATION IN A COMPLEX WITH SH3RF1; RAC2; MAP3K7; MAPK8IP1; MAP2K7 AND
RP MAPK8.
RX PubMed=27084103; DOI=10.4049/jimmunol.1501728;
RA Cunningham C.A., Cardwell L.N., Guan Y., Teixeiro E., Daniels M.A.;
RT "POSH regulates CD4+ T cell differentiation and survival.";
RL J. Immunol. 196:4003-4013(2016).
RN [16]
RP FUNCTION, INTERACTION WITH POU5F1, AND SUBCELLULAR LOCATION.
RX PubMed=29153991; DOI=10.1016/j.stemcr.2017.10.017;
RA Bae K.B., Yu D.H., Lee K.Y., Yao K., Ryu J., Lim D.Y., Zykova T.A.,
RA Kim M.O., Bode A.M., Dong Z.;
RT "Serine 347 Phosphorylation by JNKs Negatively Regulates OCT4 Protein
RT Stability in Mouse Embryonic Stem Cells.";
RL Stem Cell Reports 9:2050-2064(2017).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in various processes
CC such as cell proliferation, differentiation, migration, transformation
CC and programmed cell death. Extracellular stimuli such as pro-
CC inflammatory cytokines or physical stress stimulate the stress-
CC activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling
CC pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and
CC MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2
CC phosphorylates a number of transcription factors, primarily components
CC of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional
CC activity. In response to oxidative or ribotoxic stresses, inhibits rRNA
CC synthesis by phosphorylating and inactivating the RNA polymerase 1-
CC specific transcription initiation factor RRN3. Promotes stressed cell
CC apoptosis by phosphorylating key regulatory factors including TP53 and
CC YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized
CC differentiation of T-helper cells into Th1 cells. Upon T-cell receptor
CC (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and
CC MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in
CC the osmotic stress-induced epithelial tight-junctions disruption. When
CC activated, promotes beta-catenin/CTNNB1 degradation and inhibits the
CC canonical Wnt signaling pathway. Participates also in neurite growth in
CC spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1
CC heterodimer and plays a role in the regulation of the circadian clock
CC (PubMed:22441692). Phosphorylates POU5F1, which results in the
CC inhibition of POU5F1's transcriptional activity and enhances its
CC proteosomal degradation (PubMed:29153991).
CC {ECO:0000269|PubMed:10811224, ECO:0000269|PubMed:11562351,
CC ECO:0000269|PubMed:16973441, ECO:0000269|PubMed:21554942,
CC ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:29153991,
CC ECO:0000269|PubMed:9806643}.
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:11562351, ECO:0000269|PubMed:16973441,
CC ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:29153991,
CC ECO:0000269|PubMed:9806643};
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:11562351,
CC ECO:0000269|PubMed:16973441, ECO:0000269|PubMed:22441692,
CC ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9806643};
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 by either of two dual specificity kinases, MAP2K4 and
CC MAP2K7. MAP2K4 shows a strong preference for Tyr-185 while MAP2K7
CC phosphorylates Tyr-183 preferentially. Inhibited by dual specificity
CC phosphatases, such as DUSP1. {ECO:0000269|PubMed:10811224}.
CC -!- SUBUNIT: Interacts with MECOM (By similarity). Binds to at least four
CC scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-
CC 3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also bind other
CC components of the JNK signaling pathway (PubMed:11562351). Interacts
CC with NFATC4 (By similarity). Interacts with ATF7; the interaction does
CC not phosphorylate ATF7 but acts as a docking site for ATF7-associated
CC partners such as JUN (By similarity). Interacts with BCL10 (By
CC similarity). Interacts with CTNNB1 and GSK3B (By similarity). Interacts
CC with DCLK2 (PubMed:16628014). Interacts with MAPKBP1 (By similarity).
CC Interacts with POU5F1; phosphorylates POU5F1 at 'Ser-347'
CC (PubMed:29153991). Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1,
CC MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1 (PubMed:27084103).
CC {ECO:0000250|UniProtKB:P45984, ECO:0000250|UniProtKB:P49186,
CC ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:16628014,
CC ECO:0000269|PubMed:27084103, ECO:0000269|PubMed:29153991}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P45984}. Nucleus
CC {ECO:0000269|PubMed:29153991}. Note=Colocalizes with POU5F1 in the
CC nucleus. {ECO:0000269|PubMed:29153991}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Alpha-2;
CC IsoId=Q9WTU6-1; Sequence=Displayed;
CC Name=Alpha-1;
CC IsoId=Q9WTU6-2; Sequence=VSP_004837;
CC Name=Beta-1;
CC IsoId=Q9WTU6-3; Sequence=VSP_004836, VSP_004837;
CC Name=Beta-2;
CC IsoId=Q9WTU6-4; Sequence=VSP_004836;
CC -!- TISSUE SPECIFICITY: All four isoforms are widely distributed in brain.
CC Isoforms alpha-1 and alpha-2 are predominantly expressed in
CC hippocampus, cerebral cortex, caudate-putamen, amygdala and the granule
CC layer of the cerebellum. Alpha-1 is more abundant than alpha-2 in the
CC periaqueductal region and the substantia nigra.
CC {ECO:0000269|PubMed:10674476}.
CC -!- INDUCTION: In T-cells, following T-cell receptor (TCR) activation.
CC Levels peak 48 hours after TCR and CD-28 costimulation.
CC {ECO:0000269|PubMed:10811224, ECO:0000269|PubMed:9806643}.
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 by MAP2K7 and MAP2K4,
CC which activates the enzyme. Autophosphorylated in vitro.
CC {ECO:0000250|UniProtKB:P45984}.
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; AF052466; AAD22576.1; -; mRNA.
DR EMBL; AF052467; AAD22577.1; -; mRNA.
DR EMBL; AF052468; AAD22578.1; -; mRNA.
DR EMBL; AF052469; AAD22579.1; -; mRNA.
DR EMBL; AB005664; BAA85876.1; -; mRNA.
DR EMBL; AJ315339; CAC88132.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ315340; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AJ315341; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AJ315342; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AJ315343; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AJ315344; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AJ315345; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AJ315346; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AJ315347; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AJ315348; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AJ315349; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AJ315350; CAC88132.1; JOINED; Genomic_DNA.
DR EMBL; AK031959; BAC27623.1; -; mRNA.
DR EMBL; AL606479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028341; AAH28341.1; -; mRNA.
DR CCDS; CCDS24623.1; -. [Q9WTU6-4]
DR CCDS; CCDS24624.1; -. [Q9WTU6-2]
DR CCDS; CCDS48782.1; -. [Q9WTU6-1]
DR CCDS; CCDS48783.1; -. [Q9WTU6-3]
DR RefSeq; NP_001157143.1; NM_001163671.1. [Q9WTU6-1]
DR RefSeq; NP_001157144.1; NM_001163672.1. [Q9WTU6-3]
DR RefSeq; NP_058657.1; NM_016961.3. [Q9WTU6-2]
DR RefSeq; NP_997575.2; NM_207692.2. [Q9WTU6-4]
DR AlphaFoldDB; Q9WTU6; -.
DR SMR; Q9WTU6; -.
DR BioGRID; 204972; 4.
DR DIP; DIP-31076N; -.
DR ELM; Q9WTU6; -.
DR IntAct; Q9WTU6; 6.
DR MINT; Q9WTU6; -.
DR STRING; 10090.ENSMUSP00000020634; -.
DR BindingDB; Q9WTU6; -.
DR ChEMBL; CHEMBL2034797; -.
DR iPTMnet; Q9WTU6; -.
DR PhosphoSitePlus; Q9WTU6; -.
DR EPD; Q9WTU6; -.
DR jPOST; Q9WTU6; -.
DR MaxQB; Q9WTU6; -.
DR PaxDb; Q9WTU6; -.
DR PeptideAtlas; Q9WTU6; -.
DR PRIDE; Q9WTU6; -.
DR ProteomicsDB; 295947; -. [Q9WTU6-1]
DR ProteomicsDB; 295948; -. [Q9WTU6-2]
DR ProteomicsDB; 295949; -. [Q9WTU6-3]
DR ProteomicsDB; 295950; -. [Q9WTU6-4]
DR Antibodypedia; 4557; 916 antibodies from 47 providers.
DR DNASU; 26420; -.
DR Ensembl; ENSMUST00000020634; ENSMUSP00000020634; ENSMUSG00000020366. [Q9WTU6-4]
DR Ensembl; ENSMUST00000043321; ENSMUSP00000042744; ENSMUSG00000020366. [Q9WTU6-1]
DR Ensembl; ENSMUST00000102778; ENSMUSP00000099839; ENSMUSG00000020366. [Q9WTU6-2]
DR Ensembl; ENSMUST00000109178; ENSMUSP00000104807; ENSMUSG00000020366. [Q9WTU6-3]
DR Ensembl; ENSMUST00000109179; ENSMUSP00000104808; ENSMUSG00000020366. [Q9WTU6-2]
DR Ensembl; ENSMUST00000164643; ENSMUSP00000132864; ENSMUSG00000020366. [Q9WTU6-3]
DR Ensembl; ENSMUST00000178543; ENSMUSP00000136977; ENSMUSG00000020366. [Q9WTU6-1]
DR GeneID; 26420; -.
DR KEGG; mmu:26420; -.
DR UCSC; uc007ird.2; mouse. [Q9WTU6-2]
DR UCSC; uc007irh.2; mouse. [Q9WTU6-1]
DR UCSC; uc007iri.2; mouse. [Q9WTU6-3]
DR CTD; 5601; -.
DR MGI; MGI:1346862; Mapk9.
DR VEuPathDB; HostDB:ENSMUSG00000020366; -.
DR eggNOG; KOG0665; Eukaryota.
DR GeneTree; ENSGT00940000158327; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q9WTU6; -.
DR OMA; IESVGNW; -.
DR PhylomeDB; Q9WTU6; -.
DR TreeFam; TF105100; -.
DR BRENDA; 2.7.11.24; 3474.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-MMU-450341; Activation of the AP-1 family of transcription factors.
DR BioGRID-ORCS; 26420; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Mapk9; mouse.
DR PRO; PR:Q9WTU6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WTU6; protein.
DR Bgee; ENSMUSG00000020366; Expressed in dorsomedial nucleus of hypothalamus and 257 other tissues.
DR ExpressionAtlas; Q9WTU6; baseline and differential.
DR Genevisible; Q9WTU6; MM.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0004705; F:JUN kinase activity; ISS:UniProtKB.
DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IMP:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
DR GO; GO:0007258; P:JUN phosphorylation; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0010770; P:positive regulation of cell morphogenesis involved in differentiation; ISO:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IMP:MGI.
DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; ISO:MGI.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:1901485; P:positive regulation of transcription factor catabolic process; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0061833; P:protein localization to tricellular tight junction; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0046328; P:regulation of JNK cascade; ISO:MGI.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0046686; P:response to cadmium ion; IGI:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Biological rhythms; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..423
FT /note="Mitogen-activated protein kinase 9"
FT /id="PRO_0000186274"
FT DOMAIN 26..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 366..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 183..185
FT /note="TXY"
FT COMPBIAS 374..415
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..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; by MAP2K7"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 185
FT /note="Phosphotyrosine; by MAP2K4"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 216..230
FT /note="AEMVLHKVLFPGRDY -> GELVKGCVIFQGTDH (in isoform Beta-
FT 1 and isoform Beta-2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9806643"
FT /id="VSP_004836"
FT VAR_SEQ 377..423
FT /note="DAAVSSKATPSQSSSINDISSMSTEHTLASDTDSSLDASTGPLEGCR -> A
FT QMQQ (in isoform Alpha-1 and isoform Beta-1)"
FT /evidence="ECO:0000303|PubMed:10523642,
FT ECO:0000303|PubMed:9806643"
FT /id="VSP_004837"
FT CONFLICT 223
FT /note="V -> C (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="V -> A (in Ref. 3; CAC88132)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="P -> A (in Ref. 4; BAC27623)"
FT /evidence="ECO:0000305"
SQ 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
