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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.
12-AUG-2020, entry version 220.
RecName: Full=Mitogen-activated protein kinase 8;
Short=MAP kinase 8;
Short=MAPK 8;
EC=2.7.11.24 {ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:10856240, ECO:0000269|PubMed:11062067, ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:17296730, ECO:0000269|PubMed:17875713, ECO:0000269|PubMed:8654373};
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], 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).
[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,
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).
[10]
INTERACTION WITH MECOM, AND CATALYTIC ACTIVITY.
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, CATALYTIC ACTIVITY, 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, INTERACTION WITH HSF4, AND CATALYTIC ACTIVITY.
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, 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).
[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, AND CATALYTIC ACTIVITY.
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, AND CATALYTIC ACTIVITY.
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, CATALYTIC ACTIVITY, AND ACTIVITY 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, AND CATALYTIC ACTIVITY.
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, 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).
[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, AND CATALYTIC ACTIVITY.
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, 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).
[30]
FUNCTION IN PHOSPHORYLATION OF BAD, AND CATALYTIC ACTIVITY.
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, AND CATALYTIC ACTIVITY.
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]
FUNCTION.
PubMed=22327296; DOI=10.1038/nature10806;
Huang J., Gurung B., Wan B., Matkar S., Veniaminova N.A., Wan K.,
Merchant J.L., Hua X., Lei M.;
"The same pocket in menin binds both MLL and JUND but has opposite effects
on transcription.";
Nature 482:542-546(2012).
[34]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-363, AND CATALYTIC ACTIVITY.
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).
[35]
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). Phosphorylates POU5F1,
which results in the inhibition of POU5F1's transcriptional activity
and enhances its proteosomal degradation (By similarity).
Phosphorylates JUND and this phosphorylation is inhibited in the
presence of MEN1 (By similarity). In neurons, phosphorylates SYT4 which
captures neuronal dense core vesicles at synapses (By similarity).
{ECO:0000250|UniProtKB:P49185, ECO:0000250|UniProtKB:Q91Y86,
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:
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:10747973, ECO:0000269|PubMed:10856240,
ECO:0000269|PubMed:11062067, ECO:0000269|PubMed:15141161,
ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:17296730,
ECO:0000269|PubMed:17875713, ECO:0000269|PubMed:18307971,
ECO:0000269|PubMed:19166818, ECO:0000269|PubMed:20027304,
ECO:0000269|PubMed:21095239, ECO:0000269|PubMed:21364637,
ECO:0000269|PubMed:21660049, ECO:0000269|PubMed:21856198,
ECO:0000269|PubMed:22441692, 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:10747973,
ECO:0000269|PubMed:10856240, ECO:0000269|PubMed:11062067,
ECO:0000269|PubMed:15141161, ECO:0000269|PubMed:16581800,
ECO:0000269|PubMed:17296730, ECO:0000269|PubMed:17875713,
ECO:0000269|PubMed:18307971, ECO:0000269|PubMed:19166818,
ECO:0000269|PubMed:20027304, ECO:0000269|PubMed:21095239,
ECO:0000269|PubMed:21364637, ECO:0000269|PubMed:21660049,
ECO:0000269|PubMed:21856198, ECO:0000269|PubMed:22441692,
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. 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). Interacts with POU5F1; phosphorylates POU5F1
at 'Ser-355'. Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3,
MAP2K7/MKK7 and MAPK8IP1/JIP1. Found in a complex with SH3RF1, RAC2,
MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK9/JNK2 (By similarity).
{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:
P45983; Q92934: BAD; NbExp=2; IntAct=EBI-286483, EBI-700771;
P45983; P22681: CBL; NbExp=2; IntAct=EBI-286483, EBI-518228;
P45983; P60953: CDC42; NbExp=2; IntAct=EBI-286483, EBI-81752;
P45983; P46108: CRK; NbExp=2; IntAct=EBI-286483, EBI-886;
P45983; P16104: H2AX; NbExp=3; IntAct=EBI-286483, EBI-494830;
P45983; P05412: JUN; NbExp=5; IntAct=EBI-286483, EBI-852823;
P45983; O14733: MAP2K7; NbExp=4; IntAct=EBI-286483, EBI-492605;
P45983; O14733-2: MAP2K7; NbExp=3; IntAct=EBI-286483, EBI-492627;
P45983; Q9UQF2: MAPK8IP1; NbExp=7; IntAct=EBI-286483, EBI-78404;
P45983; P27986: PIK3R1; NbExp=6; IntAct=EBI-286483, EBI-79464;
P45983; Q8N122: RPTOR; NbExp=6; IntAct=EBI-286483, EBI-1567928;
P45983; Q9WVI9-1: Mapk8ip1; Xeno; NbExp=2; IntAct=EBI-286483, EBI-288461;
P45983-1; P05412: JUN; NbExp=2; IntAct=EBI-288687, EBI-852823;
P45983-4; Q9Y6W6: DUSP10; NbExp=3; IntAct=EBI-18121963, EBI-3443946;
P45983-4; Q9BY84: DUSP16; NbExp=3; IntAct=EBI-18121963, EBI-3443956;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21148294}. Nucleus
{ECO:0000269|PubMed:21148294}. Cell junction, synapse
{ECO:0000250|UniProtKB:P49185}. Note=In the cortical neurons,
predominantly cytoplasmic and associated with the Golgi apparatus and
endosomal fraction. Increased neuronal activity increases
phosphorylated form at synapses (By similarity). Colocalizes with
POU5F1 in the nucleus. {ECO:0000250|UniProtKB:P49185,
ECO:0000250|UniProtKB:Q91Y86}.
-!- 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;
Name=3; Synonyms=JNK1-beta-1;
IsoId=P45983-3; Sequence=VSP_004831, VSP_004832, VSP_004833;
Name=4; Synonyms=JNK1-beta-2;
IsoId=P45983-4; Sequence=VSP_004831, VSP_004832;
Name=5;
IsoId=P45983-5; Sequence=VSP_054554, VSP_004833;
-!- 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). Phosphorylated form is more
concentrated at synapses than none-phosphorylated (By similarity).
{ECO:0000250|UniProtKB:P49185, 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]
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; 5LW1; X-ray; 3.20 A; B/E/H=2-363.
PDB; 6F5E; X-ray; 2.70 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; 5LW1; -.
PDBsum; 6F5E; -.
SMR; P45983; -.
BioGRID; 111585; 192.
DIP; DIP-249N; -.
ELM; P45983; -.
IntAct; P45983; 107.
MINT; P45983; -.
STRING; 9606.ENSP00000378974; -.
BindingDB; P45983; -.
ChEMBL; CHEMBL2276; -.
DrugBank; DB07268; 2-({2-[(3-HYDROXYPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)BENZAMIDE.
DrugBank; DB07845; 2-fluoro-6-{[2-({2-methoxy-4-[(methylsulfonyl)methyl]phenyl}amino)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]amino}benzamide.
DrugBank; DB07276; 5-CYANO-N-(2,5-DIMETHOXYBENZYL)-6-ETHOXYPYRIDINE-2-CARBOXAMIDE.
DrugBank; DB07218; 6-CHLORO-9-HYDROXY-1,3-DIMETHYL-1,9-DIHYDRO-4H-PYRAZOLO[3,4-B]QUINOLIN-4-ONE.
DrugBank; DB15624; Halicin.
DrugBank; DB01017; Minocycline.
DrugBank; DB07272; N-(4-AMINO-5-CYANO-6-ETHOXYPYRIDIN-2-YL)-2-(4-BROMO-2,5-DIMETHOXYPHENYL)ACETAMIDE.
DrugBank; DB01782; Pyrazolanthrone.
DrugBank; DB00675; Tamoxifen.
DrugCentral; P45983; -.
GuidetoPHARMACOLOGY; 1496; -.
iPTMnet; P45983; -.
PhosphoSitePlus; P45983; -.
BioMuta; MAPK8; -.
DMDM; 2507195; -.
CPTAC; CPTAC-889; -.
CPTAC; CPTAC-890; -.
CPTAC; CPTAC-891; -.
CPTAC; CPTAC-892; -.
EPD; P45983; -.
jPOST; P45983; -.
MassIVE; P45983; -.
MaxQB; P45983; -.
PaxDb; P45983; -.
PeptideAtlas; P45983; -.
PRIDE; P45983; -.
ProteomicsDB; 55694; -. [P45983-1]
ProteomicsDB; 55695; -. [P45983-2]
ProteomicsDB; 55696; -. [P45983-3]
ProteomicsDB; 55697; -. [P45983-4]
ProteomicsDB; 61569; -.
Antibodypedia; 3846; 1623 antibodies.
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; ENSG00000107643; Low tissue specificity.
MIM; 601158; gene.
neXtProt; NX_P45983; -.
OpenTargets; ENSG00000107643; -.
PharmGKB; PA283; -.
eggNOG; KOG0665; Eukaryota.
GeneTree; ENSGT00940000153692; -.
InParanoid; P45983; -.
KO; K04440; -.
OMA; AMDMWAV; -.
OrthoDB; 741207at2759; -.
PhylomeDB; P45983; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 2681.
PathwayCommons; P45983; -.
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.
Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping.
SignaLink; P45983; -.
SIGNOR; P45983; -.
BioGRID-ORCS; 5599; 11 hits in 905 CRISPR screens.
ChiTaRS; MAPK8; human.
EvolutionaryTrace; P45983; -.
GeneWiki; MAPK8; -.
GenomeRNAi; 5599; -.
Pharos; P45983; Tchem.
PRO; PR:P45983; -.
Proteomes; UP000005640; Chromosome 10.
RNAct; P45983; protein.
Bgee; ENSG00000107643; Expressed in cortical plate and 223 other tissues.
ExpressionAtlas; P45983; baseline and differential.
Genevisible; P45983; HS.
GO; GO:0030424; C:axon; ISS:ARUK-UCL.
GO; GO:0097441; C:basal dendrite; ISS:ARUK-UCL.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
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:0004707; F:MAP kinase activity; IBA:GO_Central.
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:0071345; P:cellular response to cytokine stimulus; TAS:Reactome.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
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: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:0051090; P:regulation of DNA-binding transcription factor activity; TAS:Reactome.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
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.
IDEAL; IID00270; -.
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;
Cell junction; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; S-nitrosylation;
Serine/threonine-protein kinase; Synapse; Transferase.
CHAIN 1..427
/note="Mitogen-activated protein kinase 8"
/id="PRO_0000186262"
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 116
/note="S-nitrosocysteine"
/evidence="ECO:0000250|UniProtKB:P49185"
MOD_RES 183
/note="Phosphothreonine; by MAP2K7"
/evidence="ECO:0000269|PubMed:11062067"
MOD_RES 185
/note="Phosphotyrosine; by MAP2K4"
/evidence="ECO:0000269|PubMed:11062067"
MOD_RES 377
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91Y86"
VAR_SEQ 206..281
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|Ref.3"
/id="VSP_054554"
VAR_SEQ 208
/note="L -> I (in isoform 3 and isoform 4)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_004831"
VAR_SEQ 219..230
/note="VCHKILFPGRDY -> IKGGVLFPGTDH (in isoform 3 and
isoform 4)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_004832"
VAR_SEQ 380..427
/note="GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR ->
AQVQQ (in isoform 1, isoform 3 and isoform 5)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:19054851, ECO:0000303|Ref.3"
/id="VSP_004833"
VARIANT 171
/note="G -> S (in a renal clear cell carcinoma sample;
somatic mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042258"
VARIANT 177
/note="G -> R (in a glioblastoma multiforme sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042259"
VARIANT 365
/note="E -> K (in dbSNP:rs45483593)"
/id="VAR_050592"
MUTAGEN 183
/note="T->A: Phosphorylation blocked."
/evidence="ECO:0000269|PubMed:7839144"
MUTAGEN 185
/note="Y->F: Phosphorylation blocked."
/evidence="ECO:0000269|PubMed:7839144"
HELIX 4..9
/evidence="ECO:0000244|PDB:2XRW"
STRAND 10..15
/evidence="ECO:0000244|PDB:2XRW"
STRAND 18..23
/evidence="ECO:0000244|PDB:2XRW"
STRAND 26..34
/evidence="ECO:0000244|PDB:2XRW"
STRAND 36..45
/evidence="ECO:0000244|PDB:2XRW"
TURN 46..49
/evidence="ECO:0000244|PDB:2XRW"
STRAND 50..58
/evidence="ECO:0000244|PDB:2XRW"
HELIX 60..62
/evidence="ECO:0000244|PDB:4QTD"
HELIX 64..79
/evidence="ECO:0000244|PDB:2XRW"
STRAND 83..85
/evidence="ECO:0000244|PDB:2GMX"
STRAND 88..92
/evidence="ECO:0000244|PDB:2XRW"
STRAND 94..97
/evidence="ECO:0000244|PDB:3VUM"
TURN 98..100
/evidence="ECO:0000244|PDB:2XRW"
STRAND 103..109
/evidence="ECO:0000244|PDB:2XRW"
STRAND 112..114
/evidence="ECO:0000244|PDB:2XRW"
HELIX 115..120
/evidence="ECO:0000244|PDB:2XRW"
HELIX 125..144
/evidence="ECO:0000244|PDB:2XRW"
HELIX 154..156
/evidence="ECO:0000244|PDB:2XRW"
STRAND 157..159
/evidence="ECO:0000244|PDB:2XRW"
TURN 161..163
/evidence="ECO:0000244|PDB:2H96"
STRAND 165..167
/evidence="ECO:0000244|PDB:2XRW"
STRAND 174..177
/evidence="ECO:0000244|PDB:3O2M"
STRAND 178..180
/evidence="ECO:0000244|PDB:2NO3"
STRAND 182..184
/evidence="ECO:0000244|PDB:3ELJ"
STRAND 185..187
/evidence="ECO:0000244|PDB:2G01"
HELIX 189..191
/evidence="ECO:0000244|PDB:3PZE"
HELIX 194..197
/evidence="ECO:0000244|PDB:2XRW"
HELIX 206..220
/evidence="ECO:0000244|PDB:2XRW"
HELIX 230..241
/evidence="ECO:0000244|PDB:2XRW"
HELIX 246..249
/evidence="ECO:0000244|PDB:2XRW"
HELIX 254..261
/evidence="ECO:0000244|PDB:2XRW"
HELIX 271..274
/evidence="ECO:0000244|PDB:2XRW"
HELIX 277..279
/evidence="ECO:0000244|PDB:2XRW"
HELIX 285..301
/evidence="ECO:0000244|PDB:2XRW"
HELIX 306..308
/evidence="ECO:0000244|PDB:2XRW"
HELIX 312..317
/evidence="ECO:0000244|PDB:2XRW"
HELIX 319..322
/evidence="ECO:0000244|PDB:2XRW"
HELIX 327..330
/evidence="ECO:0000244|PDB:2XRW"
TURN 339..342
/evidence="ECO:0000244|PDB:2XRW"
HELIX 349..363
/evidence="ECO:0000244|PDB:2XRW"
MOD_RES P45983-2:377
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195"
MOD_RES P45983-3:377
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195"
MOD_RES P45983-5:301
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195"
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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