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Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (JNK-46) (Stress-activated protein kinase 1c) (SAPK1c) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)

 MK08_HUMAN              Reviewed;         427 AA.
P45983; B5BTZ5; B7ZLV4; D3DX88; D3DX92; Q15709; Q15712; Q15713;
Q308M2;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 198.
RecName: Full=Mitogen-activated protein kinase 8;
Short=MAP kinase 8;
Short=MAPK 8;
EC=2.7.11.24;
AltName: Full=JNK-46;
AltName: Full=Stress-activated protein kinase 1c;
Short=SAPK1c;
AltName: Full=Stress-activated protein kinase JNK1;
AltName: Full=c-Jun N-terminal kinase 1;
Name=MAPK8; Synonyms=JNK1, PRKM8, SAPK1, SAPK1C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal brain;
PubMed=8137421; DOI=10.1016/0092-8674(94)90380-8;
Derijard B., Hibi M., Wu I.-H., Barrett T., Su B., Deng T., Karin M.,
Davis R.J.;
"JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds
and phosphorylates the c-Jun activation domain.";
Cell 76:1025-1037(1994).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z.,
Liang M., Tang Z., Huang B., Li H., Yang S.;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[8]
MUTAGENESIS.
PubMed=7839144; DOI=10.1126/science.7839144;
Derijard B., Raingeaud J., Barrett T., Wu I.-H., Han J.,
Ulevitch R.J., Davis R.J.;
"Independent human MAP-kinase signal transduction pathways defined by
MEK and MKK isoforms.";
Science 267:682-685(1995).
[9]
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).
[10]
INTERACTION WITH MECOM.
PubMed=10856240; DOI=10.1093/emboj/19.12.2958;
Kurokawa M., Mitani K., Yamagata T., Takahashi T., Izutsu K.,
Ogawa S., Moriguchi T., Nishida E., Yazaki Y., Hirai H.;
"The evi-1 oncoprotein inhibits c-Jun N-terminal kinase and prevents
stress-induced cell death.";
EMBO J. 19:2958-2968(2000).
[11]
FUNCTION IN PHOSPHORYLATION OF HSF1, AND INTERACTION WITH HSF1.
PubMed=10747973; DOI=10.1074/jbc.M000958200;
Dai R., Frejtag W., He B., Zhang Y., Mivechi N.F.;
"c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock
factor-1 suppress its transcriptional activity.";
J. Biol. Chem. 275:18210-18218(2000).
[12]
INTERACTION WITH WWOX AND TP53.
PubMed=12514174; DOI=10.1074/jbc.M208373200;
Chang N.-S., Doherty J., Ensign A.;
"JNK1 physically interacts with WW domain-containing oxidoreductase
(WOX1) and inhibits WOX1-mediated apoptosis.";
J. Biol. Chem. 278:9195-9202(2003).
[13]
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).
[14]
FUNCTION, AND INTERACTION WITH HSF4.
PubMed=16581800; DOI=10.1128/MCB.26.8.3282-3294.2006;
Hu Y., Mivechi N.F.;
"Association and regulation of heat shock transcription factor 4b with
both extracellular signal-regulated kinase mitogen-activated protein
kinase and dual-specificity tyrosine phosphatase DUSP26.";
Mol. Cell. Biol. 26:3282-3294(2006).
[15]
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).
[16]
INTERACTION WITH GRIPAP1, AND PHOSPHORYLATION BY MAP3K1.
PubMed=17761173; DOI=10.1016/j.febslet.2007.08.008;
Ye B., Yu W.P., Thomas G.M., Huganir R.L.;
"GRASP-1 is a neuronal scaffold protein for the JNK signaling
pathway.";
FEBS Lett. 581:4403-4410(2007).
[17]
PHOSPHORYLATION BY TAOK2.
PubMed=17158878; DOI=10.1074/jbc.M608336200;
Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J.,
Morris J.D.;
"Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis.
JNK-and caspase-dependent nuclear localization is a requirement for
membrane blebbing.";
J. Biol. Chem. 282:6484-6493(2007).
[18]
FUNCTION IN PHOSPHORYLATION OF ELK1.
PubMed=17296730; DOI=10.1128/MCB.02276-06;
Zhang L., Yang S.H., Sharrocks A.D.;
"Rev7/MAD2B links c-Jun N-terminal protein kinase pathway signaling to
activation of the transcription factor Elk-1.";
Mol. Cell. Biol. 27:2861-2869(2007).
[19]
FUNCTION IN PHOSPHORYLATION OF JDP2.
PubMed=18307971; DOI=10.1016/j.ab.2008.01.038;
Murata T., Shinozuka Y., Obata Y., Yokoyama K.K.;
"Phosphorylation of two eukaryotic transcription factors, Jun
dimerization protein 2 and activation transcription factor 2, in
Escherichia coli by Jun N-terminal kinase 1.";
Anal. Biochem. 376:115-121(2008).
[20]
FUNCTION IN PHOSPHORYLATION OF BCL2.
PubMed=18570871; DOI=10.1016/j.molcel.2008.06.001;
Wei Y., Pattingre S., Sinha S., Bassik M., Levine B.;
"JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced
autophagy.";
Mol. Cell 30:678-688(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 (ISOFORMS 1 AND 3),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 (ISOFORM 5), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
INTERACTION WITH SERPINB3, AND ENZYME REGULATION.
PubMed=19166818; DOI=10.1016/j.bbrc.2009.01.057;
Zheng B., Matoba Y., Kumagai T., Katagiri C., Hibino T., Sugiyama M.;
"Crystal structure of SCCA1 and insight about the interaction with
JNK1.";
Biochem. Biophys. Res. Commun. 380:143-147(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 (ISOFORMS 1 AND 3),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 (ISOFORM 5), AND
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).
[25]
FUNCTION IN PHOSPHORYLATION OF SIRT1.
PubMed=20027304; DOI=10.1371/journal.pone.0008414;
Nasrin N., Kaushik V.K., Fortier E., Wall D., Pearson K.J.,
de Cabo R., Bordone L.;
"JNK1 phosphorylates SIRT1 and promotes its enzymatic activity.";
PLoS ONE 4:E8414-E8414(2009).
[26]
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).
[27]
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).
[28]
INTERACTION WITH PIN1.
PubMed=21660049; DOI=10.1038/cdd.2011.82;
Park J.E., Lee J.A., Park S.G., Lee D.H., Kim S.J., Kim H.J.,
Uchida C., Uchida T., Park B.C., Cho S.;
"A critical step for JNK activation: isomerization by the prolyl
isomerase Pin1.";
Cell Death Differ. 19:153-161(2012).
[29]
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).
[30]
FUNCTION IN PHOSPHORYLATION OF BAD.
PubMed=21095239; DOI=10.1016/j.biocel.2010.11.011;
Deng H., Zhang J., Yoon T., Song D., Li D., Lin A.;
"Phosphorylation of Bcl-associated death protein (Bad) by
erythropoietin-activated c-Jun N-terminal protein kinase 1 contributes
to survival of erythropoietin-dependent cells.";
Int. J. Biochem. Cell Biol. 43:409-415(2011).
[31]
SUBCELLULAR LOCATION.
PubMed=21148294; DOI=10.1091/mbc.E10-06-0492;
Wang J., Tang R., Lv M., Wang Q., Zhang X., Guo Y., Chang H., Qiao C.,
Xiao H., Li X., Li Y., Shen B., Zhang J.;
"Defective anchoring of JNK1 in the cytoplasm by MKK7 in Jurkat cells
is associated with resistance to Fas-mediated apoptosis.";
Mol. Biol. Cell 22:117-127(2011).
[32]
FUNCTION IN PHOSPHORYLATION OF CDT1.
PubMed=21856198; DOI=10.1016/j.molcel.2011.06.021;
Miotto B., Struhl K.;
"JNK1 phosphorylation of Cdt1 inhibits recruitment of HBO1 histone
acetylase and blocks replication licensing in response to stress.";
Mol. Cell 44:62-71(2011).
[33]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-363.
PubMed=15141161; DOI=10.1038/sj.emboj.7600212;
Heo Y.S., Kim S.K., Seo C.I., Kim Y.K., Sung B.J., Lee H.S., Lee J.I.,
Park S.Y., Kim J.H., Hwang K.Y., Hyun Y.L., Jeon Y.H., Ro S.,
Cho J.M., Lee T.G., Yang C.H.;
"Structural basis for the selective inhibition of JNK1 by the
scaffolding protein JIP1 and SP600125.";
EMBO J. 23:2185-2195(2004).
[34]
VARIANTS [LARGE SCALE ANALYSIS] SER-171 AND ARG-177.
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).
-!- 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 MAPK8/JNK1.
In turn, MAPK8/JNK1 phosphorylates a number of transcription
factors, primarily components of AP-1 such as JUN, JDP2 and ATF2
and thus regulates AP-1 transcriptional activity. Phosphorylates
the replication licensing factor CDT1, inhibiting the interaction
between CDT1 and the histone H4 acetylase HBO1 to replication
origins. Loss of this interaction abrogates the acetylation
required for replication initiation. Promotes stressed cell
apoptosis by phosphorylating key regulatory factors including
p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and
MAPK9 are required for polarized differentiation of T-helper cells
into Th1 cells. Contributes to the survival of erythroid cells by
phosphorylating the antagonist of cell death BAD upon EPO
stimulation. Mediates starvation-induced BCL2 phosphorylation,
BCL2 dissociation from BECN1, and thus activation of autophagy.
Phosphorylates STMN2 and hence regulates microtubule dynamics,
controlling neurite elongation in cortical neurons. In the
developing brain, through its cytoplasmic activity on STMN2,
negatively regulates the rate of exit from multipolar stage and of
radial migration from the ventricular zone. Phosphorylates several
other substrates including heat shock factor protein 4 (HSF4), the
deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the
CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation
of the circadian clock (PubMed:22441692). Phosphorylates the heat
shock transcription factor HSF1, suppressing HSF1-induced
transcriptional activity (PubMed:10747973).
{ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:22441692}.
-!- FUNCTION: JNK1 isoforms display different binding patterns: beta-1
preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-
2 have a similar low level of binding to both c-Jun or ATF2.
However, there is no correlation between binding and
phosphorylation, which is achieved at about the same efficiency by
all isoforms.
-!- 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. Inhibited by SERPINB3.
{ECO:0000269|PubMed:19166818}.
-!- SUBUNIT: Binds to at least four scaffolding proteins,
MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and
SPAG9/MAPK8IP4/JIP-4 (PubMed:15693750). These proteins also bind
other components of the JNK signaling pathway. Interacts with TP53
and WWOX (PubMed:12514174). Interacts with JAMP (By similarity).
Forms a complex with MAPK8IP1 and ARHGEF28 (By similarity).
Interacts with HSF1 (via D domain and preferentially with
hyperphosphorylated form); this interaction occurs under both
normal growth conditions and immediately upon heat shock
(PubMed:10747973). Interacts (phosphorylated form) with NFE2; the
interaction phosphorylates NFE2 in undifferentiated cells (By
similarity). Interacts with NFATC4 (PubMed:17875713). Interacts
with MECOM; regulates JNK signaling (PubMed:10856240). Interacts
with PIN1; this interaction mediates MAPK8 conformational changes
leading to the binding of MAPK8 to its substrates
(PubMed:21660049). Interacts with GRIPAP1 (PubMed:17761173).
{ECO:0000250|UniProtKB:P49185, ECO:0000250|UniProtKB:Q91Y86,
ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:10856240,
ECO:0000269|PubMed:12514174, ECO:0000269|PubMed:15693750,
ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:17761173,
ECO:0000269|PubMed:17875713, ECO:0000269|PubMed:19166818,
ECO:0000269|PubMed:21660049}.
-!- INTERACTION:
Q92934:BAD; NbExp=2; IntAct=EBI-286483, EBI-700771;
P22681:CBL; NbExp=2; IntAct=EBI-286483, EBI-518228;
P60953:CDC42; NbExp=2; IntAct=EBI-286483, EBI-81752;
P46108:CRK; NbExp=2; IntAct=EBI-286483, EBI-886;
P16104:H2AFX; NbExp=3; IntAct=EBI-286483, EBI-494830;
P05412:JUN; NbExp=5; IntAct=EBI-286483, EBI-852823;
O14733:MAP2K7; NbExp=4; IntAct=EBI-286483, EBI-492605;
O14733-2:MAP2K7; NbExp=3; IntAct=EBI-286483, EBI-492627;
Q9UQF2:MAPK8IP1; NbExp=7; IntAct=EBI-286483, EBI-78404;
Q9WVI9-1:Mapk8ip1 (xeno); NbExp=2; IntAct=EBI-286483, EBI-288461;
P27986:PIK3R1; NbExp=6; IntAct=EBI-286483, EBI-79464;
Q8N122:RPTOR; NbExp=6; IntAct=EBI-286483, EBI-1567928;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21148294}.
Nucleus {ECO:0000269|PubMed:21148294}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=2; Synonyms=JNK1-alpha-2;
IsoId=P45983-1; Sequence=Displayed;
Name=1; Synonyms=JNK1-alpha-1;
IsoId=P45983-2; Sequence=VSP_004833;
Note=Contains a phosphoserine at position 377.
{ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19369195};
Name=3; Synonyms=JNK1-beta-1;
IsoId=P45983-3; Sequence=VSP_004831, VSP_004832, VSP_004833;
Note=Contains a phosphoserine at position 377.
{ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19369195};
Name=4; Synonyms=JNK1-beta-2;
IsoId=P45983-4; Sequence=VSP_004831, VSP_004832;
Name=5;
IsoId=P45983-5; Sequence=VSP_054554, VSP_004833;
Note=Contains a phosphoserine at position 301.
{ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19369195};
-!- 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 (PubMed:11062067).
Phosphorylated by TAOK2 (PubMed:17158878). May be phosphorylated
at Thr-183 and Tyr-185 by MAP3K1/MEKK1 (PubMed:17761173).
{ECO:0000269|PubMed:11062067, ECO:0000269|PubMed:17158878,
ECO:0000269|PubMed:17761173}.
-!- 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/JNK1ID196.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=C-Jun N-terminal kinases entry;
URL="https://en.wikipedia.org/wiki/C-Jun_N-terminal_kinases";
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EMBL; L26318; AAA36131.1; -; mRNA.
EMBL; U34822; AAC50607.1; -; mRNA.
EMBL; U35004; AAC50610.1; -; mRNA.
EMBL; U35005; AAC50611.1; -; mRNA.
EMBL; DQ234352; ABB29981.1; -; mRNA.
EMBL; AC016397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC074325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB451231; BAG70045.1; -; mRNA.
EMBL; CH471187; EAW93132.1; -; Genomic_DNA.
EMBL; CH471187; EAW93129.1; -; Genomic_DNA.
EMBL; CH471187; EAW93130.1; -; Genomic_DNA.
EMBL; CH471187; EAW93133.1; -; Genomic_DNA.
EMBL; CH471187; EAW93134.1; -; Genomic_DNA.
EMBL; CH471187; EAW93136.1; -; Genomic_DNA.
EMBL; BC144063; AAI44064.1; -; mRNA.
CCDS; CCDS60527.1; -. [P45983-5]
CCDS; CCDS7223.1; -. [P45983-4]
CCDS; CCDS7224.1; -. [P45983-1]
CCDS; CCDS7225.1; -. [P45983-2]
CCDS; CCDS7226.1; -. [P45983-3]
PIR; S71097; S71097.
PIR; S71099; S71099.
RefSeq; NP_001265476.1; NM_001278547.1. [P45983-4]
RefSeq; NP_001265477.1; NM_001278548.1. [P45983-5]
RefSeq; NP_001310231.1; NM_001323302.1. [P45983-2]
RefSeq; NP_001310250.1; NM_001323321.1. [P45983-3]
RefSeq; NP_001310251.1; NM_001323322.1. [P45983-4]
RefSeq; NP_001310252.1; NM_001323323.1. [P45983-4]
RefSeq; NP_001310253.1; NM_001323324.1. [P45983-2]
RefSeq; NP_001310254.1; NM_001323325.1. [P45983-3]
RefSeq; NP_001310255.1; NM_001323326.1. [P45983-2]
RefSeq; NP_001310256.1; NM_001323327.1. [P45983-2]
RefSeq; NP_001310257.1; NM_001323328.1. [P45983-1]
RefSeq; NP_001310258.1; NM_001323329.1. [P45983-1]
RefSeq; NP_001310259.1; NM_001323330.1. [P45983-4]
RefSeq; NP_001310260.1; NM_001323331.1. [P45983-1]
RefSeq; NP_620634.1; NM_139046.3. [P45983-3]
RefSeq; NP_620637.1; NM_139049.3. [P45983-1]
UniGene; Hs.138211; -.
UniGene; Hs.522924; -.
PDB; 1UKH; X-ray; 2.35 A; A=1-363.
PDB; 1UKI; X-ray; 2.70 A; A=1-363.
PDB; 2G01; X-ray; 3.50 A; A/B=1-364.
PDB; 2GMX; X-ray; 3.50 A; A/B=1-364.
PDB; 2H96; X-ray; 3.00 A; A/B=1-364.
PDB; 2NO3; X-ray; 3.20 A; A/B=1-364.
PDB; 2XRW; X-ray; 1.33 A; A=2-364.
PDB; 2XS0; X-ray; 2.60 A; A=1-379.
PDB; 3ELJ; X-ray; 1.80 A; A=1-364.
PDB; 3O17; X-ray; 3.00 A; A/B=1-364.
PDB; 3O2M; X-ray; 2.70 A; A/B=1-364.
PDB; 3PZE; X-ray; 2.00 A; A=7-364.
PDB; 3V3V; X-ray; 2.70 A; A=1-366.
PDB; 3VUD; X-ray; 3.50 A; A=1-364.
PDB; 3VUG; X-ray; 3.24 A; A=1-364.
PDB; 3VUH; X-ray; 2.70 A; A=1-364.
PDB; 3VUI; X-ray; 2.80 A; A=1-364.
PDB; 3VUK; X-ray; 2.95 A; A=1-364.
PDB; 3VUL; X-ray; 2.81 A; A=1-364.
PDB; 3VUM; X-ray; 2.69 A; A=1-364.
PDB; 4AWI; X-ray; 1.91 A; A=1-364.
PDB; 4E73; X-ray; 2.27 A; A=1-363.
PDB; 4G1W; X-ray; 2.45 A; A=1-363.
PDB; 4HYS; X-ray; 2.42 A; A=1-363.
PDB; 4HYU; X-ray; 2.15 A; A=1-363.
PDB; 4IZY; X-ray; 2.30 A; A=1-363.
PDB; 4L7F; X-ray; 1.95 A; A=7-362.
PDB; 4QTD; X-ray; 1.50 A; A=1-363.
PDB; 4UX9; X-ray; 2.34 A; A/B/C/D=1-364.
PDB; 4YR8; X-ray; 2.40 A; A/C/E/F=1-363.
PDB; 5LEN; X-ray; 2.50 A; B=2-363.
PDBsum; 1UKH; -.
PDBsum; 1UKI; -.
PDBsum; 2G01; -.
PDBsum; 2GMX; -.
PDBsum; 2H96; -.
PDBsum; 2NO3; -.
PDBsum; 2XRW; -.
PDBsum; 2XS0; -.
PDBsum; 3ELJ; -.
PDBsum; 3O17; -.
PDBsum; 3O2M; -.
PDBsum; 3PZE; -.
PDBsum; 3V3V; -.
PDBsum; 3VUD; -.
PDBsum; 3VUG; -.
PDBsum; 3VUH; -.
PDBsum; 3VUI; -.
PDBsum; 3VUK; -.
PDBsum; 3VUL; -.
PDBsum; 3VUM; -.
PDBsum; 4AWI; -.
PDBsum; 4E73; -.
PDBsum; 4G1W; -.
PDBsum; 4HYS; -.
PDBsum; 4HYU; -.
PDBsum; 4IZY; -.
PDBsum; 4L7F; -.
PDBsum; 4QTD; -.
PDBsum; 4UX9; -.
PDBsum; 4YR8; -.
PDBsum; 5LEN; -.
ProteinModelPortal; P45983; -.
SMR; P45983; -.
BioGrid; 111585; 185.
DIP; DIP-249N; -.
ELM; P45983; -.
IntAct; P45983; 90.
MINT; MINT-1211982; -.
STRING; 9606.ENSP00000353483; -.
BindingDB; P45983; -.
ChEMBL; CHEMBL2276; -.
DrugBank; DB07268; 2-({2-[(3-HYDROXYPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)BENZAMIDE.
GuidetoPHARMACOLOGY; 1496; -.
iPTMnet; P45983; -.
PhosphoSitePlus; P45983; -.
BioMuta; MAPK8; -.
DMDM; 2507195; -.
EPD; P45983; -.
MaxQB; P45983; -.
PaxDb; P45983; -.
PeptideAtlas; P45983; -.
PRIDE; P45983; -.
DNASU; 5599; -.
Ensembl; ENST00000360332; ENSP00000353483; ENSG00000107643. [P45983-5]
Ensembl; ENST00000374176; ENSP00000363291; ENSG00000107643. [P45983-4]
Ensembl; ENST00000374179; ENSP00000363294; ENSG00000107643. [P45983-3]
Ensembl; ENST00000374182; ENSP00000363297; ENSG00000107643. [P45983-2]
Ensembl; ENST00000374189; ENSP00000363304; ENSG00000107643. [P45983-1]
Ensembl; ENST00000395611; ENSP00000378974; ENSG00000107643. [P45983-4]
GeneID; 5599; -.
KEGG; hsa:5599; -.
UCSC; uc001jgm.5; human. [P45983-1]
CTD; 5599; -.
DisGeNET; 5599; -.
EuPathDB; HostDB:ENSG00000107643.15; -.
GeneCards; MAPK8; -.
HGNC; HGNC:6881; MAPK8.
HPA; CAB004463; -.
HPA; CAB069396; -.
MIM; 601158; gene.
neXtProt; NX_P45983; -.
OpenTargets; ENSG00000107643; -.
PharmGKB; PA283; -.
eggNOG; KOG0665; Eukaryota.
eggNOG; ENOG410XSHI; LUCA.
GeneTree; ENSGT00550000074271; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P45983; -.
KO; K04440; -.
OMA; YKEVLEW; -.
PhylomeDB; P45983; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 2681.
Reactome; R-HSA-111446; Activation of BIM and translocation to mitochondria.
Reactome; R-HSA-139910; Activation of BMF and translocation to mitochondria.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-376172; DSCAM interactions.
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.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-9007892; Interleukin-38 signaling.
SignaLink; P45983; -.
SIGNOR; P45983; -.
ChiTaRS; MAPK8; human.
EvolutionaryTrace; P45983; -.
GeneWiki; MAPK8; -.
GenomeRNAi; 5599; -.
PRO; PR:P45983; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107643; -.
CleanEx; HS_MAPK8; -.
ExpressionAtlas; P45983; baseline and differential.
Genevisible; P45983; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0035033; F:histone deacetylase regulator activity; IMP:BHF-UCL.
GO; GO:0004705; F:JUN kinase activity; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; IDA:CAFA.
GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
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:0007258; P:JUN phosphorylation; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0048666; P:neuron development; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
GO; GO:0031281; P:positive regulation of cyclase activity; IMP:CACAO.
GO; GO:0090045; P:positive regulation of deacetylase activity; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0051247; P:positive regulation of protein metabolic process; IMP:CACAO.
GO; GO:0006468; P:protein phosphorylation; IDA:CAFA.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:1902595; P:regulation of DNA replication origin binding; IMP:CAFA.
GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; TAS:Reactome.
GO; GO:0006950; P:response to stress; TAS:ProtInc.
GO; GO:0009411; P:response to UV; IDA:MGI.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:CAFA.
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; S-nitrosylation;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 427 Mitogen-activated protein kinase 8.
/FTId=PRO_0000186262.
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 116 116 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P49185}.
MOD_RES 183 183 Phosphothreonine; by MAP2K7.
{ECO:0000269|PubMed:11062067}.
MOD_RES 185 185 Phosphotyrosine; by MAP2K4.
{ECO:0000269|PubMed:11062067}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000250|UniProtKB:Q91Y86}.
VAR_SEQ 206 281 Missing (in isoform 5).
{ECO:0000303|Ref.3}.
/FTId=VSP_054554.
VAR_SEQ 208 208 L -> I (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_004831.
VAR_SEQ 219 230 VCHKILFPGRDY -> IKGGVLFPGTDH (in isoform
3 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_004832.
VAR_SEQ 380 427 GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAA
GPLGCCR -> AQVQQ (in isoform 1, isoform 3
and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:19054851,
ECO:0000303|Ref.3}.
/FTId=VSP_004833.
VARIANT 171 171 G -> S (in a renal clear cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042258.
VARIANT 177 177 G -> R (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042259.
VARIANT 365 365 E -> K (in dbSNP:rs45483593).
/FTId=VAR_050592.
MUTAGEN 183 183 T->A: Phosphorylation blocked.
{ECO:0000269|PubMed:7839144}.
MUTAGEN 185 185 Y->F: Phosphorylation blocked.
{ECO:0000269|PubMed:7839144}.
HELIX 4 9 {ECO:0000244|PDB:2XRW}.
STRAND 10 15 {ECO:0000244|PDB:2XRW}.
STRAND 18 23 {ECO:0000244|PDB:2XRW}.
STRAND 26 34 {ECO:0000244|PDB:2XRW}.
STRAND 36 45 {ECO:0000244|PDB:2XRW}.
TURN 46 49 {ECO:0000244|PDB:2XRW}.
STRAND 50 58 {ECO:0000244|PDB:2XRW}.
HELIX 60 62 {ECO:0000244|PDB:4QTD}.
HELIX 64 79 {ECO:0000244|PDB:2XRW}.
STRAND 83 85 {ECO:0000244|PDB:2GMX}.
STRAND 88 92 {ECO:0000244|PDB:2XRW}.
STRAND 94 97 {ECO:0000244|PDB:3VUM}.
TURN 98 100 {ECO:0000244|PDB:2XRW}.
STRAND 103 109 {ECO:0000244|PDB:2XRW}.
STRAND 112 114 {ECO:0000244|PDB:2XRW}.
HELIX 115 120 {ECO:0000244|PDB:2XRW}.
HELIX 125 144 {ECO:0000244|PDB:2XRW}.
HELIX 154 156 {ECO:0000244|PDB:2XRW}.
STRAND 157 159 {ECO:0000244|PDB:2XRW}.
TURN 161 163 {ECO:0000244|PDB:2H96}.
STRAND 165 167 {ECO:0000244|PDB:2XRW}.
STRAND 174 177 {ECO:0000244|PDB:3O2M}.
STRAND 178 180 {ECO:0000244|PDB:2NO3}.
STRAND 182 184 {ECO:0000244|PDB:3ELJ}.
STRAND 185 187 {ECO:0000244|PDB:2G01}.
HELIX 189 191 {ECO:0000244|PDB:3PZE}.
HELIX 194 197 {ECO:0000244|PDB:2XRW}.
HELIX 206 220 {ECO:0000244|PDB:2XRW}.
HELIX 230 241 {ECO:0000244|PDB:2XRW}.
HELIX 246 249 {ECO:0000244|PDB:2XRW}.
HELIX 254 261 {ECO:0000244|PDB:2XRW}.
HELIX 271 274 {ECO:0000244|PDB:2XRW}.
HELIX 277 279 {ECO:0000244|PDB:2XRW}.
HELIX 285 301 {ECO:0000244|PDB:2XRW}.
HELIX 306 308 {ECO:0000244|PDB:2XRW}.
HELIX 312 317 {ECO:0000244|PDB:2XRW}.
HELIX 319 322 {ECO:0000244|PDB:2XRW}.
HELIX 327 330 {ECO:0000244|PDB:2XRW}.
TURN 339 342 {ECO:0000244|PDB:2XRW}.
HELIX 349 363 {ECO:0000244|PDB:2XRW}.
SEQUENCE 427 AA; 48296 MW; 94FB6BE0358B9B60 CRC64;
MSRSKRDNNF YSVEIGDSTF TVLKRYQNLK PIGSGAQGIV CAAYDAILER NVAIKKLSRP
FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKSLEE FQDVYIVMEL MDANLCQVIQ
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTAGTSF
MMTPYVVTRY YRAPEVILGM GYKENVDLWS VGCIMGEMVC HKILFPGRDY IDQWNKVIEQ
LGTPCPEFMK KLQPTVRTYV ENRPKYAGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK
MLVIDASKRI SVDEALQHPY INVWYDPSEA EAPPPKIPDK QLDEREHTIE EWKELIYKEV
MDLEERTKNG VIRGQPSPLG AAVINGSQHP SSSSSVNDVS SMSTDPTLAS DTDSSLEAAA
GPLGCCR


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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
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
10-782-55060 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
10-782-55060 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
10-782-55059 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
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
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
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
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
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


 

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