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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.
17-JUN-2020, entry version 213.
RecName: Full=Mitogen-activated protein kinase 9;
Short=MAP kinase 9;
Short=MAPK 9;
EC=2.7.11.24 {ECO:0000269|PubMed:11062067, ECO:0000269|PubMed:15805466, ECO:0000269|PubMed:17875713, ECO:0000269|PubMed:21110917, ECO:0000269|PubMed:7969172, ECO:0000269|PubMed:8001819, ECO:0000269|PubMed:8654373};
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], AND CATALYTIC ACTIVITY.
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], AND CATALYTIC ACTIVITY.
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], ALTERNATIVE SPLICING, AND CATALYTIC ACTIVITY.
TISSUE=Brain;
PubMed=8654373; DOI=10.1002/j.1460-2075.1996.tb00636.x;
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), AND CATALYTIC ACTIVITY.
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,
CATALYTIC ACTIVITY, 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, AND CATALYTIC ACTIVITY.
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, AND CATALYTIC ACTIVITY.
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, AND CATALYTIC ACTIVITY.
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, AND CATALYTIC ACTIVITY.
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, AND CATALYTIC ACTIVITY.
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, 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).
[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 OF PUBMED:28089251.
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). Phosphorylates POU5F1, which results in the
inhibition of POU5F1's transcriptional activity and enhances its
proteosomal degradation (By similarity). {ECO:0000250|UniProtKB:Q9WTU6,
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:
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:11062067, ECO:0000269|PubMed:15805466,
ECO:0000269|PubMed:17189706, ECO:0000269|PubMed:17525747,
ECO:0000269|PubMed:17875713, ECO:0000269|PubMed:21110917,
ECO:0000269|PubMed:21364637, ECO:0000269|PubMed:22441692,
ECO:0000269|PubMed:7969172, ECO:0000269|PubMed:8001819,
ECO:0000269|PubMed:8654373};
-!- 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:11062067,
ECO:0000269|PubMed:15805466, ECO:0000269|PubMed:17189706,
ECO:0000269|PubMed:17525747, ECO:0000269|PubMed:17875713,
ECO:0000269|PubMed:21110917, ECO:0000269|PubMed:21364637,
ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:7969172,
ECO:0000269|PubMed:8001819, ECO:0000269|PubMed:8654373};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11062067};
-!- 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:11062067}.
-!- 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). Interacts
with POU5F1; phosphorylates POU5F1 at 'Ser-355'. Found in a complex
with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and
MAPK8/JNK1 (By similarity). {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:
P45984; P49407: ARRB1; NbExp=9; IntAct=EBI-713568, EBI-743313;
P45984; P32121: ARRB2; NbExp=9; IntAct=EBI-713568, EBI-714559;
P45984; P15336: ATF2; NbExp=9; IntAct=EBI-713568, EBI-1170906;
P45984; P0C671: BNIP5; NbExp=3; IntAct=EBI-713568, EBI-12806802;
P45984; O95561: C1orf105; NbExp=5; IntAct=EBI-713568, EBI-10191951;
P45984; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-713568, EBI-946029;
P45984; Q8N7E2: CBLL2; NbExp=3; IntAct=EBI-713568, EBI-12196065;
P45984; Q8IYA8: CCDC36; NbExp=3; IntAct=EBI-713568, EBI-8638439;
P45984; Q13042: CDC16; NbExp=3; IntAct=EBI-713568, EBI-994830;
P45984; Q9C0F1: CEP44; NbExp=9; IntAct=EBI-713568, EBI-744115;
P45984; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-713568, EBI-10171858;
P45984; O43602-2: DCX; NbExp=3; IntAct=EBI-713568, EBI-14148644;
P45984; Q8N9I9: DTX3; NbExp=3; IntAct=EBI-713568, EBI-2340258;
P45984; Q9Y6W6: DUSP10; NbExp=4; IntAct=EBI-713568, EBI-3443946;
P45984; Q9BY84: DUSP16; NbExp=5; IntAct=EBI-713568, EBI-3443956;
P45984; Q13115: DUSP4; NbExp=4; IntAct=EBI-713568, EBI-6591081;
P45984; Q5JST6: EFHC2; NbExp=7; IntAct=EBI-713568, EBI-2349927;
P45984; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-713568, EBI-744099;
P45984; P14136: GFAP; NbExp=3; IntAct=EBI-713568, EBI-744302;
P45984; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-713568, EBI-11163335;
P45984; O15499: GSC2; NbExp=3; IntAct=EBI-713568, EBI-19954058;
P45984; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-713568, EBI-712105;
P45984; Q9P2G9-2: KLHL8; NbExp=3; IntAct=EBI-713568, EBI-11959635;
P45984; O00505: KPNA3; NbExp=3; IntAct=EBI-713568, EBI-358297;
P45984; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-713568, EBI-2686809;
P45984; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-713568, EBI-11985629;
P45984; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-713568, EBI-12039345;
P45984; Q8TBB1: LNX1; NbExp=7; IntAct=EBI-713568, EBI-739832;
P45984; Q8N448: LNX2; NbExp=3; IntAct=EBI-713568, EBI-2340947;
P45984; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-713568, EBI-1216080;
P45984; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-713568, EBI-348259;
P45984; Q86YW9: MED12L; NbExp=3; IntAct=EBI-713568, EBI-3957138;
P45984; P50221: MEOX1; NbExp=7; IntAct=EBI-713568, EBI-2864512;
P45984; Q5VWP3-2: MLIP; NbExp=5; IntAct=EBI-713568, EBI-12320785;
P45984; Q5HYW2: NHSL2; NbExp=5; IntAct=EBI-713568, EBI-2859639;
P45984; Q02548: PAX5; NbExp=3; IntAct=EBI-713568, EBI-296331;
P45984; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-713568, EBI-10302990;
P45984; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-713568, EBI-79165;
P45984; P78424: POU6F2; NbExp=3; IntAct=EBI-713568, EBI-12029004;
P45984; P37231: PPARG; NbExp=3; IntAct=EBI-713568, EBI-781384;
P45984; Q96S79: RASL10B; NbExp=3; IntAct=EBI-713568, EBI-3919507;
P45984; Q2I0M5: RSPO4; NbExp=3; IntAct=EBI-713568, EBI-12821217;
P45984; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-713568, EBI-3957636;
P45984; O00560: SDCBP; NbExp=3; IntAct=EBI-713568, EBI-727004;
P45984; Q15427: SF3B4; NbExp=7; IntAct=EBI-713568, EBI-348469;
P45984; P34896: SHMT1; NbExp=7; IntAct=EBI-713568, EBI-715117;
P45984; A2RU48: SMCO3; NbExp=6; IntAct=EBI-713568, EBI-10173195;
P45984; P40763: STAT3; NbExp=2; IntAct=EBI-713568, EBI-518675;
P45984; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-713568, EBI-3923210;
P45984; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-713568, EBI-742397;
P45984; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-713568, EBI-11523345;
P45984; O43379: WDR62; NbExp=4; IntAct=EBI-713568, EBI-714790;
P45984; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-713568, EBI-14104088;
P45984; P52744: ZNF138; NbExp=3; IntAct=EBI-713568, EBI-10746567;
P45984; Q9BR84: ZNF559; NbExp=3; IntAct=EBI-713568, EBI-746605;
P45984; O43257: ZNHIT1; NbExp=3; IntAct=EBI-713568, EBI-347522;
P45984-1; P40763: STAT3; NbExp=3; IntAct=EBI-713586, EBI-518675;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19675674}. Nucleus
{ECO:0000269|PubMed:19675674}. Note=Colocalizes with POU5F1 in the
nucleus. {ECO:0000250|UniProtKB:Q9WTU6}.
-!- 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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Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
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.
RefSeq; XP_016865127.1; XM_017009638.1.
RefSeq; XP_016865130.1; XM_017009641.1.
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; -.
SMR; P45984; -.
BioGRID; 111587; 126.
DIP; DIP-270N; -.
ELM; P45984; -.
IntAct; P45984; 104.
MINT; P45984; -.
STRING; 9606.ENSP00000394560; -.
BindingDB; P45984; -.
ChEMBL; CHEMBL4179; -.
DrugBank; DB12010; Fostamatinib.
DrugBank; DB07020; N-{3-[5-(1H-1,2,4-triazol-3-yl)-1H-indazol-3-yl]phenyl}furan-2-carboxamide.
DrugCentral; P45984; -.
GuidetoPHARMACOLOGY; 1497; -.
GlyConnect; 1515; -.
iPTMnet; P45984; -.
MetOSite; P45984; -.
PhosphoSitePlus; P45984; -.
BioMuta; MAPK9; -.
DMDM; 85700366; -.
REPRODUCTION-2DPAGE; P45984; -.
CPTAC; CPTAC-893; -.
CPTAC; CPTAC-894; -.
EPD; P45984; -.
jPOST; P45984; -.
MassIVE; P45984; -.
MaxQB; P45984; -.
PaxDb; P45984; -.
PeptideAtlas; P45984; -.
PRIDE; P45984; -.
ProteomicsDB; 55698; -. [P45984-1]
ProteomicsDB; 55699; -. [P45984-2]
ProteomicsDB; 55700; -. [P45984-3]
ProteomicsDB; 55701; -. [P45984-4]
ProteomicsDB; 55702; -. [P45984-5]
Antibodypedia; 4557; 831 antibodies.
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; ENSG00000050748; Tissue enhanced (brain).
MIM; 602896; gene.
neXtProt; NX_P45984; -.
OpenTargets; ENSG00000050748; -.
PharmGKB; PA30630; -.
eggNOG; KOG0665; Eukaryota.
eggNOG; ENOG410XSHI; LUCA.
GeneTree; ENSGT00940000158327; -.
HOGENOM; CLU_000288_181_1_1; -.
InParanoid; P45984; -.
KO; K04440; -.
OMA; PSETEHD; -.
OrthoDB; 741207at2759; -.
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; -.
BioGRID-ORCS; 5601; 4 hits in 817 CRISPR screens.
ChiTaRS; MAPK9; human.
EvolutionaryTrace; P45984; -.
GeneWiki; Mitogen-activated_protein_kinase_9; -.
GenomeRNAi; 5601; -.
Pharos; P45984; Tchem.
PRO; PR:P45984; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P45984; protein.
Bgee; ENSG00000050748; Expressed in middle temporal gyrus and 232 other tissues.
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: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:0004707; F:MAP kinase activity; IBA:GO_Central.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:CAFA.
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:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:1901485; P:positive regulation of transcription factor catabolic process; 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 DNA-binding transcription factor activity; TAS:Reactome.
GO; GO:0010468; P:regulation of gene expression; 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;
3D-structure; Alternative splicing; ATP-binding; Biological rhythms;
Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1..424
/note="Mitogen-activated protein kinase 9"
/id="PRO_0000186273"
DOMAIN 26..321
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 32..40
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOTIF 183..185
/note="TXY"
ACT_SITE 151
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 55
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 183
/note="Phosphothreonine; by MAP2K7"
/evidence="ECO:0000269|PubMed:11062067"
MOD_RES 185
/note="Phosphotyrosine; by MAP2K4"
/evidence="ECO:0000269|PubMed:11062067"
VAR_SEQ 216..230
/note="GELVKGCVIFQGTDH -> AEMVLHKVLFPGRDY (in isoform Beta-
1 and isoform Beta-2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_004834"
VAR_SEQ 230..242
/note="HIDQWNKVIEQLG -> RILPRDLGPAMLS (in isoform 5)"
/evidence="ECO:0000303|PubMed:21110917"
/id="VSP_041908"
VAR_SEQ 243..424
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:21110917"
/id="VSP_041909"
VAR_SEQ 378..424
/note="DAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR -> A
QMQQ (in isoform Alpha-1 and isoform Beta-1)"
/evidence="ECO:0000305"
/id="VSP_004835"
VARIANT 13
/note="V -> M (in a colorectal adenocarcinoma sample;
somatic mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042260"
VARIANT 56
/note="K -> N (in a head & Neck squamous cell carcinoma
sample; somatic mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042261"
VARIANT 246
/note="A -> T (in dbSNP:rs35421153)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042262"
VARIANT 268
/note="G -> A (in dbSNP:rs35693958)"
/evidence="ECO:0000269|Ref.7"
/id="VAR_025175"
VARIANT 366
/note="R -> I (in dbSNP:rs55736180)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042263"
CONFLICT 51
/note="N -> S (in Ref. 1; AAA56831 and 3; AAC50606/
AAC50608/AAC50609)"
/evidence="ECO:0000305"
CONFLICT 377
/note="S -> P (in Ref. 2; AAA74740)"
/evidence="ECO:0000305"
STRAND 10..15
/evidence="ECO:0000244|PDB:3E7O"
STRAND 18..23
/evidence="ECO:0000244|PDB:3E7O"
STRAND 26..33
/evidence="ECO:0000244|PDB:3E7O"
STRAND 38..45
/evidence="ECO:0000244|PDB:3E7O"
TURN 46..49
/evidence="ECO:0000244|PDB:3E7O"
STRAND 50..58
/evidence="ECO:0000244|PDB:3E7O"
HELIX 64..79
/evidence="ECO:0000244|PDB:3E7O"
STRAND 88..92
/evidence="ECO:0000244|PDB:3E7O"
TURN 98..100
/evidence="ECO:0000244|PDB:3E7O"
STRAND 105..109
/evidence="ECO:0000244|PDB:3E7O"
STRAND 112..114
/evidence="ECO:0000244|PDB:3E7O"
HELIX 115..118
/evidence="ECO:0000244|PDB:3E7O"
HELIX 125..144
/evidence="ECO:0000244|PDB:3E7O"
HELIX 154..156
/evidence="ECO:0000244|PDB:3E7O"
STRAND 157..159
/evidence="ECO:0000244|PDB:3E7O"
STRAND 165..167
/evidence="ECO:0000244|PDB:3E7O"
TURN 176..178
/evidence="ECO:0000244|PDB:3NPC"
STRAND 180..183
/evidence="ECO:0000244|PDB:3NPC"
HELIX 189..191
/evidence="ECO:0000244|PDB:3NPC"
HELIX 194..197
/evidence="ECO:0000244|PDB:3E7O"
HELIX 206..220
/evidence="ECO:0000244|PDB:3E7O"
HELIX 232..241
/evidence="ECO:0000244|PDB:3E7O"
HELIX 246..250
/evidence="ECO:0000244|PDB:3E7O"
HELIX 254..261
/evidence="ECO:0000244|PDB:3E7O"
HELIX 271..274
/evidence="ECO:0000244|PDB:3E7O"
HELIX 277..279
/evidence="ECO:0000244|PDB:3E7O"
HELIX 286..301
/evidence="ECO:0000244|PDB:3E7O"
TURN 306..308
/evidence="ECO:0000244|PDB:3NPC"
HELIX 312..316
/evidence="ECO:0000244|PDB:3E7O"
HELIX 319..322
/evidence="ECO:0000244|PDB:3E7O"
HELIX 327..330
/evidence="ECO:0000244|PDB:3NPC"
TURN 341..343
/evidence="ECO:0000244|PDB:3NPC"
HELIX 349..360
/evidence="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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EIAAB24855 c-Jun N-terminal kinase 1,Homo sapiens,Human,JNK1,JNK-46,MAP kinase 8,MAPK 8,MAPK8,Mitogen-activated protein kinase 8,PRKM8,SAPK1,Stress-activated protein kinase 1,Stress-activated protein kinase JNK1
EIAAB24858 c-Jun N-terminal kinase 2,Jnk2,MAP kinase 9,MAPK 9,Mapk9,Mitogen-activated protein kinase 9,p54-alpha,Prkm9,Rat,Rattus norvegicus,SAPK-alpha,Stress-activated protein kinase JNK2
EIAAB24859 Chicken,c-Jun N-terminal kinase 2,Gallus gallus,JNK2,MAP kinase 9,MAPK 9,MAPK9,Mitogen-activated protein kinase 9,Stress-activated protein kinase JNK2
EIAAB24861 c-Jun N-terminal kinase 3,Homo sapiens,Human,JNK3,JNK3A,MAP kinase 10,MAP kinase p49 3F12,MAPK 10,MAPK10,Mitogen-activated protein kinase 10,PRKM10,Stress-activated protein kinase JNK3
EIAAB24863 c-Jun N-terminal kinase 3,Jnk3,MAP kinase 10,MAP kinase p49 3F12,MAPK 10,Mapk10,Mitogen-activated protein kinase 10,Mouse,Mus musculus,Prkm10,Serk2,Stress-activated protein kinase JNK3
EIAAB24870 Homo sapiens,Human,MAP kinase 13,MAP kinase p38 delta,MAPK 13,MAPK13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,PRKM13,SAPK4,Stress-activated protein kinase 4
EIAAB24864 Homo sapiens,Human,MAP kinase 11,MAP kinase p38 beta,MAPK 11,MAPK11,Mitogen-activated protein kinase 11,Mitogen-activated protein kinase p38 beta,p38-2,p38b,PRKM11,SAPK2,Stress-activated protein kinas
EIAAB24856 c-Jun N-terminal kinase 1,Jnk1,MAP kinase 8,MAPK 8,Mapk8,Mitogen-activated protein kinase 8,Mouse,Mus musculus,Prkm8,Stress-activated protein kinase JNK1
EIAAB24872 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Mouse,Mus musculus,Serk4,Stress-activated protein kinase 4
15-288-22791 Mitogen-activated protein kinase 9 - EC 2.7.11.24; Stress-activated protein kinase JNK2; c-Jun N-terminal kinase 2; JNK-55 Polyclonal 0.1 mg
15-288-22791 Mitogen-activated protein kinase 9 - EC 2.7.11.24; Stress-activated protein kinase JNK2; c-Jun N-terminal kinase 2; JNK-55 Polyclonal 0.05 mg
EIAAB24869 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Rat,Rattus norvegicus,Stress-activated protein kinase 4
EIAAB24862 c-Jun N-terminal kinase 3,Jnk3,MAP kinase 10,MAPK 10,Mapk10,Mitogen-activated protein kinase 10,p54-beta,Prkm10,Rat,Rattus norvegicus,SAPK-beta,Stress-activated protein kinase JNK3
EIAAB24854 c-Jun N-terminal kinase 1,Jnk1,MAP kinase 8,MAPK 8,Mapk8,Mitogen-activated protein kinase 8,p54 gamma,Prkm8,Rat,Rattus norvegicus,SAPK gamma,Stress-activated protein kinase JNK1
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.005 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.001 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.05 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.01 mg
U1206m CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
U1206r CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
U1206b CLIA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM1 96T