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Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (JNK-55) (Stress-activated protein kinase 1a) (SAPK1a) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2)

 MK09_HUMAN              Reviewed;         424 AA.
P45984; A8K0S3; B5BU66; B5M0B4; D3DWQ8; D3DWQ9; Q15708; Q15710;
Q15711; Q8N5C5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 2.
22-NOV-2017, entry version 192.
RecName: Full=Mitogen-activated protein kinase 9;
Short=MAP kinase 9;
Short=MAPK 9;
EC=2.7.11.24;
AltName: Full=JNK-55;
AltName: Full=Stress-activated protein kinase 1a;
Short=SAPK1a;
AltName: Full=Stress-activated protein kinase JNK2;
AltName: Full=c-Jun N-terminal kinase 2;
Name=MAPK9; Synonyms=JNK2, PRKM9, SAPK1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7969172; DOI=10.1128/MCB.14.12.8376;
Sluss H.K., Barrett T., Derijard B., Davis R.J.;
"Signal transduction by tumor necrosis factor mediated by JNK protein
kinases.";
Mol. Cell. Biol. 14:8376-8384(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8001819; DOI=10.1101/gad.8.24.2996;
Kallunki T., Su B., Tsigelny I., Sluss H.K., Derijard B., Moore G.,
Davis R., Karin M.;
"JNK2 contains a specificity-determining region responsible for
efficient c-Jun binding and phosphorylation.";
Genes Dev. 8:2996-3007(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=8654373;
Gupta S., Barrett T., Whitmarsh A.J., Cavanagh J., Sluss H.K.,
Derijard B., Davis R.J.;
"Selective interaction of JNK protein kinase isoforms with
transcription factors.";
EMBO J. 15:2760-2770(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
PubMed=21110917; DOI=10.5483/BMBRep.2010.43.11.738;
Wang P., Xiong Y., Ma C., Shi T., Ma D.;
"Molecular cloning and characterization of novel human JNK2 (MAPK9)
transcript variants that show different stimulation activities on AP-
1.";
BMB Rep. 43:738-743(2010).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-268.
NIEHS SNPs program;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[12]
INTERACTION WITH ATF7, AND FUNCTION.
PubMed=10376527; DOI=10.1038/sj.onc.1202723;
De Graeve F., Bahr A., Sabapathy K.T., Hauss C., Wagner E.F.,
Kedinger C., Chatton B.;
"Role of the ATFa/JNK2 complex in Jun activation.";
Oncogene 18:3491-3500(1999).
[13]
PHOSPHORYLATION AT THR-183 AND TYR-185, REGULATION BY MAP2K4 AND
MAP2K7, AND COFACTOR.
PubMed=11062067; DOI=10.1042/bj3520145;
Fleming Y., Armstrong C.G., Morrice N., Paterson A., Goedert M.,
Cohen P.;
"Synergistic activation of stress-activated protein kinase 1/c-Jun N-
terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein
kinase kinase 4 (MKK4) and MKK7.";
Biochem. J. 352:145-154(2000).
[14]
INTERACTION WITH SPAG9.
PubMed=15693750; DOI=10.1042/BJ20041577;
Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S.,
Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.;
"Characterization of a novel human sperm-associated antigen 9 (SPAG9)
having structural homology with c-Jun N-terminal kinase-interacting
protein.";
Biochem. J. 389:73-82(2005).
[15]
FUNCTION IN PHOSPHORYLATION OF RRN3.
PubMed=15805466; DOI=10.1101/gad.333205;
Mayer C., Bierhoff H., Grummt I.;
"The nucleolus as a stress sensor: JNK2 inactivates the transcription
factor TIF-IA and down-regulates rRNA synthesis.";
Genes Dev. 19:933-941(2005).
[16]
INTERACTION WITH NFATC4.
PubMed=17875713; DOI=10.1158/0008-5472.CAN-06-4788;
Yao K., Cho Y.-Y., Bergen H.R. III, Madden B.J., Choi B.Y., Ma W.-Y.,
Bode A.M., Dong Z.;
"Nuclear factor of activated T3 is a negative regulator of Ras-JNK1/2-
AP-1 induced cell transformation.";
Cancer Res. 67:8725-8735(2007).
[17]
INTERACTION WITH BCL10.
PubMed=17189706; DOI=10.1016/j.immuni.2006.11.008;
Blonska M., Pappu B.P., Matsumoto R., Li H., Su B., Wang D., Lin X.;
"The CARMA1-Bcl10 signaling complex selectively regulates JNK2 kinase
in the T cell receptor-signaling pathway.";
Immunity 26:55-66(2007).
[18]
FUNCTION IN PHOSPHORYLATION OF TP53.
PubMed=17525747; DOI=10.1038/sj.onc.1210526;
Oleinik N.V., Krupenko N.I., Krupenko S.A.;
"Cooperation between JNK1 and JNK2 in activation of p53 apoptotic
pathway.";
Oncogene 26:7222-7230(2007).
[19]
REVIEW ON FUNCTION.
PubMed=19290929; DOI=10.1111/j.1600-065X.2008.00749.x;
Blonska M., Lin X.;
"CARMA1-mediated NF-kappaB and JNK activation in lymphocytes.";
Immunol. Rev. 228:199-211(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTNNB1.
PubMed=19675674; DOI=10.1371/journal.pone.0006640;
Hu D., Bi X., Fang W., Han A., Yang W.;
"GSK3beta is involved in JNK2-mediated beta-catenin inhibition.";
PLoS ONE 4:E6640-E6640(2009).
[22]
FUNCTION.
PubMed=20595622; DOI=10.1152/ajpgi.00265.2010;
Samak G., Suzuki T., Bhargava A., Rao R.K.;
"c-Jun NH2-terminal kinase-2 mediates osmotic stress-induced tight
junction disruption in the intestinal epithelium.";
Am. J. Physiol. 299:G572-G584(2010).
[23]
FUNCTION IN PHOSPHORYLATION OF YAP1.
PubMed=21364637; DOI=10.1038/cddis.2010.7;
Tomlinson V., Gudmundsdottir K., Luong P., Leung K.Y., Knebel A.,
Basu S.;
"JNK phosphorylates Yes-associated protein (YAP) to regulate
apoptosis.";
Cell Death Dis. 1:E29-E29(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
FUNCTION.
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).
[26]
X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 7-362.
PubMed=18801372; DOI=10.1016/j.jmb.2008.08.086;
Shaw D., Wang S.M., Villasenor A.G., Tsing S., Walter D.,
Browner M.F., Barnett J., Kuglstatter A.;
"The crystal structure of JNK2 reveals conformational flexibility in
the MAP kinase insert and indicates its involvement in the regulation
of catalytic activity.";
J. Mol. Biol. 383:885-893(2008).
[27]
VARIANTS [LARGE SCALE ANALYSIS] MET-13; ASN-56; THR-246 AND ILE-366.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[28]
INTERACTION WITH MAPKBP1.
PubMed=28089251; DOI=10.1016/j.ajhg.2016.12.011;
Macia M.S., Halbritter J., Delous M., Bredrup C., Gutter A.,
Filhol E., Mellgren A.E., Leh S., Bizet A., Braun D.A., Gee H.Y.,
Silbermann F., Henry C., Krug P., Bole-Feysot C., Nitschke P.,
Joly D., Nicoud P., Paget A., Haugland H., Brackmann D., Ahmet N.,
Sandford R., Cengiz N., Knappskog P.M., Boman H., Linghu B., Yang F.,
Oakeley E.J., Saint Mezard P., Sailer A.W., Johansson S., Roedahl E.,
Saunier S., Hildebrandt F., Benmerah A.;
"Mutations in MAPKBP1 cause juvenile or late-onset cilia-independent
nephronophthisis.";
Am. J. Hum. Genet. 100:323-333(2017).
[29]
ERRATUM.
PubMed=28157543; DOI=10.1016/j.ajhg.2017.01.025;
Macia M.S., Halbritter J., Delous M., Bredrup C., Gutter A.,
Filhol E., Mellgren A.E., Leh S., Bizet A., Braun D.A., Gee H.Y.,
Silbermann F., Henry C., Krug P., Bole-Feysot C., Nitschke P.,
Joly D., Nicoud P., Paget A., Haugland H., Brackmann D., Ahmet N.,
Sandford R., Cengiz N., Knappskog P.M., Boman H., Linghu B., Yang F.,
Oakeley E.J., Saint Mezard P., Sailer A.W., Johansson S., Roedahl E.,
Saunier S., Hildebrandt F., Benmerah A.;
Am. J. Hum. Genet. 100:372-372(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).
{ECO:0000269|PubMed:22441692}.
-!- FUNCTION: MAPK9 isoforms display different binding patterns:
alpha-1 and alpha-2 preferentially bind to JUN, whereas beta-1 and
beta-2 bind to ATF2. However, there is no correlation between
binding and phosphorylation, which is achieved at about the same
efficiency by all isoforms. JUNB is not a substrate for JNK2
alpha-2, and JUND binds only weakly to it.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11062067};
-!- ENZYME 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.
-!- SUBUNIT: Interacts with MECOM (By similarity). Interacts with
DCLK2 (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 (By similarity). Interacts with NFATC4
(PubMed:17875713). Interacts with ATF7; the interaction does not
phosphorylate ATF7 but acts as a docking site for ATF7-associated
partners such as JUN (PubMed:10376527). Interacts with BCL10
(PubMed:17189706). Interacts with CTNNB1 and GSK3B
(PubMed:19675674). Interacts with MAPKBP1 (PubMed:28089251).
{ECO:0000250|UniProtKB:P49186, ECO:0000250|UniProtKB:Q9WTU6,
ECO:0000269|PubMed:10376527, ECO:0000269|PubMed:17189706,
ECO:0000269|PubMed:17875713, ECO:0000269|PubMed:19675674,
ECO:0000269|PubMed:28089251}.
-!- INTERACTION:
P49407:ARRB1; NbExp=7; IntAct=EBI-713568, EBI-743313;
P32121:ARRB2; NbExp=7; IntAct=EBI-713568, EBI-714559;
P15336:ATF2; NbExp=5; IntAct=EBI-713568, EBI-1170906;
Q6P1W5:C1orf94; NbExp=3; IntAct=EBI-713568, EBI-946029;
Q13042:CDC16; NbExp=4; IntAct=EBI-713568, EBI-994830;
Q9C0F1:CEP44; NbExp=6; IntAct=EBI-713568, EBI-744115;
Q13363-2:CTBP1; NbExp=3; IntAct=EBI-713568, EBI-10171858;
Q5JST6:EFHC2; NbExp=5; IntAct=EBI-713568, EBI-2349927;
Q96JM7:L3MBTL3; NbExp=3; IntAct=EBI-713568, EBI-2686809;
Q96JM7-2:L3MBTL3; NbExp=4; IntAct=EBI-713568, EBI-11985629;
Q8TBB1:LNX1; NbExp=5; IntAct=EBI-713568, EBI-739832;
P50221:MEOX1; NbExp=5; IntAct=EBI-713568, EBI-2864512;
Q5HYW2:NHSL2; NbExp=4; IntAct=EBI-713568, EBI-2859639;
Q8IYX7:SAXO1; NbExp=4; IntAct=EBI-713568, EBI-3957636;
Q15427:SF3B4; NbExp=6; IntAct=EBI-713568, EBI-348469;
P34896:SHMT1; NbExp=5; IntAct=EBI-713568, EBI-715117;
A2RU48:SMCO3; NbExp=3; IntAct=EBI-713568, EBI-10173195;
P40763:STAT3; NbExp=3; IntAct=EBI-713586, EBI-518675;
Q8IYF3:TEX11; NbExp=3; IntAct=EBI-713568, EBI-742397;
O43379:WDR62; NbExp=4; IntAct=EBI-713568, EBI-714790;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19675674}.
Nucleus {ECO:0000269|PubMed:19675674}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=Alpha-2;
IsoId=P45984-1; Sequence=Displayed;
Name=Alpha-1;
IsoId=P45984-2; Sequence=VSP_004835;
Name=Beta-1;
IsoId=P45984-3; Sequence=VSP_004834, VSP_004835;
Name=Beta-2;
IsoId=P45984-4; Sequence=VSP_004834;
Name=5;
IsoId=P45984-5; Sequence=VSP_041908, VSP_041909;
-!- 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:0000269|PubMed:11062067}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/JNK2ID426.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mapk9/";
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; L31951; AAA56831.1; -; mRNA.
EMBL; U09759; AAA74740.1; -; mRNA.
EMBL; U34821; AAC50606.1; -; mRNA.
EMBL; U35002; AAC50608.1; -; mRNA.
EMBL; U35003; AAC50609.1; -; mRNA.
EMBL; EU927388; ACH57450.1; -; mRNA.
EMBL; CR536580; CAG38817.1; -; mRNA.
EMBL; AK289638; BAF82327.1; -; mRNA.
EMBL; DQ066599; AAY46156.1; -; Genomic_DNA.
EMBL; AB451302; BAG70116.1; -; mRNA.
EMBL; AB451355; BAG70169.1; -; mRNA.
EMBL; AC008610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471165; EAW53759.1; -; Genomic_DNA.
EMBL; CH471165; EAW53757.1; -; Genomic_DNA.
EMBL; CH471165; EAW53758.1; -; Genomic_DNA.
EMBL; CH471165; EAW53762.1; -; Genomic_DNA.
EMBL; BC032539; AAH32539.1; -; mRNA.
CCDS; CCDS43409.1; -. [P45984-2]
CCDS; CCDS43410.1; -. [P45984-3]
CCDS; CCDS4453.1; -. [P45984-1]
CCDS; CCDS4454.1; -. [P45984-4]
CCDS; CCDS47356.1; -. [P45984-5]
PIR; A55480; A55480.
PIR; S71102; S71102.
RefSeq; NP_001128516.1; NM_001135044.1. [P45984-5]
RefSeq; NP_001295173.1; NM_001308244.1.
RefSeq; NP_002743.3; NM_002752.4. [P45984-1]
RefSeq; NP_620707.1; NM_139068.2. [P45984-2]
RefSeq; NP_620708.1; NM_139069.2. [P45984-3]
RefSeq; NP_620709.1; NM_139070.2. [P45984-4]
RefSeq; XP_006714954.1; XM_006714891.2. [P45984-1]
RefSeq; XP_016865127.1; XM_017009638.1. [P45984-4]
RefSeq; XP_016865130.1; XM_017009641.1. [P45984-2]
UniGene; Hs.484371; -.
PDB; 3E7O; X-ray; 2.14 A; A/B=7-362.
PDB; 3NPC; X-ray; 2.35 A; A/B=1-364.
PDBsum; 3E7O; -.
PDBsum; 3NPC; -.
ProteinModelPortal; P45984; -.
SMR; P45984; -.
BioGrid; 111587; 119.
DIP; DIP-270N; -.
ELM; P45984; -.
IntAct; P45984; 82.
MINT; MINT-1400230; -.
STRING; 9606.ENSP00000389338; -.
BindingDB; P45984; -.
ChEMBL; CHEMBL4179; -.
GuidetoPHARMACOLOGY; 1497; -.
iPTMnet; P45984; -.
PhosphoSitePlus; P45984; -.
BioMuta; MAPK9; -.
DMDM; 85700366; -.
REPRODUCTION-2DPAGE; P45984; -.
EPD; P45984; -.
MaxQB; P45984; -.
PaxDb; P45984; -.
PeptideAtlas; P45984; -.
PRIDE; P45984; -.
DNASU; 5601; -.
Ensembl; ENST00000343111; ENSP00000345524; ENSG00000050748. [P45984-3]
Ensembl; ENST00000393360; ENSP00000377028; ENSG00000050748. [P45984-2]
Ensembl; ENST00000425491; ENSP00000397422; ENSG00000050748. [P45984-5]
Ensembl; ENST00000452135; ENSP00000394560; ENSG00000050748. [P45984-1]
Ensembl; ENST00000455781; ENSP00000389338; ENSG00000050748. [P45984-4]
GeneID; 5601; -.
KEGG; hsa:5601; -.
UCSC; uc003mls.5; human. [P45984-1]
CTD; 5601; -.
DisGeNET; 5601; -.
EuPathDB; HostDB:ENSG00000050748.17; -.
GeneCards; MAPK9; -.
HGNC; HGNC:6886; MAPK9.
HPA; CAB008910; -.
MIM; 602896; gene.
neXtProt; NX_P45984; -.
OpenTargets; ENSG00000050748; -.
PharmGKB; PA30630; -.
eggNOG; KOG0665; Eukaryota.
eggNOG; ENOG410XSHI; LUCA.
GeneTree; ENSGT00550000074271; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P45984; -.
KO; K04440; -.
OMA; WEERNKN; -.
OrthoDB; EOG091G09G2; -.
PhylomeDB; P45984; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 2681.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors.
SignaLink; P45984; -.
SIGNOR; P45984; -.
ChiTaRS; MAPK9; human.
EvolutionaryTrace; P45984; -.
GeneWiki; Mitogen-activated_protein_kinase_9; -.
GenomeRNAi; 5601; -.
PRO; PR:P45984; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000050748; -.
CleanEx; HS_MAPK9; -.
ExpressionAtlas; P45984; baseline and differential.
Genevisible; P45984; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004705; F:JUN kinase activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA.
GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:CAFA.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
GO; GO:0048666; P:neuron development; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:CAFA.
GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
GO; GO:0061833; P:protein localization to tricellular tight junction; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; TAS:Reactome.
GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
GO; GO:0006950; P:response to stress; TAS:ProtInc.
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;
3D-structure; Alternative splicing; ATP-binding; Biological rhythms;
Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 424 Mitogen-activated protein kinase 9.
/FTId=PRO_0000186273.
DOMAIN 26 321 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 32 40 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:0000269|PubMed:11062067}.
MOD_RES 185 185 Phosphotyrosine; by MAP2K4.
{ECO:0000269|PubMed:11062067}.
VAR_SEQ 216 230 GELVKGCVIFQGTDH -> AEMVLHKVLFPGRDY (in
isoform Beta-1 and isoform Beta-2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_004834.
VAR_SEQ 230 242 HIDQWNKVIEQLG -> RILPRDLGPAMLS (in
isoform 5).
{ECO:0000303|PubMed:21110917}.
/FTId=VSP_041908.
VAR_SEQ 243 424 Missing (in isoform 5).
{ECO:0000303|PubMed:21110917}.
/FTId=VSP_041909.
VAR_SEQ 378 424 DAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTG
PLEGCR -> AQMQQ (in isoform Alpha-1 and
isoform Beta-1). {ECO:0000305}.
/FTId=VSP_004835.
VARIANT 13 13 V -> M (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042260.
VARIANT 56 56 K -> N (in a head & Neck squamous cell
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042261.
VARIANT 246 246 A -> T (in dbSNP:rs35421153).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042262.
VARIANT 268 268 G -> A (in dbSNP:rs35693958).
{ECO:0000269|Ref.7}.
/FTId=VAR_025175.
VARIANT 366 366 R -> I (in dbSNP:rs55736180).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042263.
CONFLICT 51 51 N -> S (in Ref. 1; AAA56831 and 3;
AAC50606/AAC50608/AAC50609).
{ECO:0000305}.
CONFLICT 377 377 S -> P (in Ref. 2; AAA74740).
{ECO:0000305}.
STRAND 10 15 {ECO:0000244|PDB:3E7O}.
STRAND 18 23 {ECO:0000244|PDB:3E7O}.
STRAND 26 33 {ECO:0000244|PDB:3E7O}.
STRAND 38 45 {ECO:0000244|PDB:3E7O}.
TURN 46 49 {ECO:0000244|PDB:3E7O}.
STRAND 50 58 {ECO:0000244|PDB:3E7O}.
HELIX 64 79 {ECO:0000244|PDB:3E7O}.
STRAND 88 92 {ECO:0000244|PDB:3E7O}.
TURN 98 100 {ECO:0000244|PDB:3E7O}.
STRAND 105 109 {ECO:0000244|PDB:3E7O}.
STRAND 112 114 {ECO:0000244|PDB:3E7O}.
HELIX 115 118 {ECO:0000244|PDB:3E7O}.
HELIX 125 144 {ECO:0000244|PDB:3E7O}.
HELIX 154 156 {ECO:0000244|PDB:3E7O}.
STRAND 157 159 {ECO:0000244|PDB:3E7O}.
STRAND 165 167 {ECO:0000244|PDB:3E7O}.
TURN 176 178 {ECO:0000244|PDB:3NPC}.
STRAND 180 183 {ECO:0000244|PDB:3NPC}.
HELIX 189 191 {ECO:0000244|PDB:3NPC}.
HELIX 194 197 {ECO:0000244|PDB:3E7O}.
HELIX 206 220 {ECO:0000244|PDB:3E7O}.
HELIX 232 241 {ECO:0000244|PDB:3E7O}.
HELIX 246 250 {ECO:0000244|PDB:3E7O}.
HELIX 254 261 {ECO:0000244|PDB:3E7O}.
HELIX 271 274 {ECO:0000244|PDB:3E7O}.
HELIX 277 279 {ECO:0000244|PDB:3E7O}.
HELIX 286 301 {ECO:0000244|PDB:3E7O}.
TURN 306 308 {ECO:0000244|PDB:3NPC}.
HELIX 312 316 {ECO:0000244|PDB:3E7O}.
HELIX 319 322 {ECO:0000244|PDB:3E7O}.
HELIX 327 330 {ECO:0000244|PDB:3NPC}.
TURN 341 343 {ECO:0000244|PDB:3NPC}.
HELIX 349 360 {ECO:0000244|PDB:3E7O}.
SEQUENCE 424 AA; 48139 MW; 9C15DA79981290AF CRC64;
MSDSKCDSQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP
FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF
MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMGELVK GCVIFQGTDH IDQWNKVIEQ
LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK
MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV
MDWEERSKNG VVKDQPSDAA VSSNATPSQS SSINDISSMS TEQTLASDTD SSLDASTGPL
EGCR


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