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

 MK08_MOUSE              Reviewed;         384 AA.
Q91Y86;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-AUG-2020, entry version 192.
RecName: Full=Mitogen-activated protein kinase 8;
Short=MAP kinase 8;
Short=MAPK 8;
EC=2.7.11.24 {ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:11602244, ECO:0000269|PubMed:16166642, ECO:0000269|PubMed:16618812, ECO:0000269|PubMed:9096336, ECO:0000269|PubMed:9207092, ECO:0000269|PubMed:9393873};
AltName: Full=Stress-activated protein kinase JNK1;
AltName: Full=c-Jun N-terminal kinase 1;
Name=Mapk8; Synonyms=Jnk1, Prkm8;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH MAPK8IP3.
TISSUE=Brain;
PubMed=10523642; DOI=10.1128/mcb.19.11.7539;
Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N., Sugiyama K.,
Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
"JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that
functions as a scaffold factor in the JNK signaling pathway.";
Mol. Cell. Biol. 19:7539-7548(1999).
[2]
FUNCTION IN PHOSPHORYLATION OF TP53, AND CATALYTIC ACTIVITY.
PubMed=9393873; DOI=10.1038/sj.onc.1201401;
Hu M.C., Qiu W.R., Wang Y.P.;
"JNK1, JNK2 and JNK3 are p53 N-terminal serine 34 kinases.";
Oncogene 15:2277-2287(1997).
[3]
CATALYTIC ACTIVITY, AND REGULATION BY MAP2K4.
TISSUE=Embryonic stem cell;
PubMed=9096336; DOI=10.1073/pnas.94.7.3004;
Yang D., Tournier C., Wysk M., Lu H.-T., Xu J., Davis R.J., Flavell R.A.;
"Targeted disruption of the MKK4 gene causes embryonic death, inhibition of
c-Jun NH2-terminal kinase activation, and defects in AP-1 transcriptional
activity.";
Proc. Natl. Acad. Sci. U.S.A. 94:3004-3009(1997).
[4]
CATALYTIC ACTIVITY, COFACTOR, AND REGULATION BY MAP2K7.
PubMed=9207092; DOI=10.1073/pnas.94.14.7337;
Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.;
"Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun
NH2-terminal kinase.";
Proc. Natl. Acad. Sci. U.S.A. 94:7337-7342(1997).
[5]
FUNCTION, ACTIVITY REGULATION, AND INDUCTION.
TISSUE=Embryonic stem cell, and T-cell;
PubMed=10811224; DOI=10.1038/35011091;
Dong C., Yang D.D., Tournier C., Whitmarsh A.J., Xu J., Davis R.J.,
Flavell R.A.;
"JNK is required for effector T-cell function but not for T-cell
activation.";
Nature 405:91-94(2000).
[6]
FUNCTION IN PHOSPHORYLATION OF JDP2, AND CATALYTIC ACTIVITY.
PubMed=11602244; DOI=10.1016/s0014-5793(01)02907-6;
Katz S., Heinrich R., Aronheim A.;
"The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-
terminal kinase.";
FEBS Lett. 506:196-200(2001).
[7]
CATALYTIC ACTIVITY, SUBUNIT, AND PHOSPHORYLATION AT THR-183 AND TYR-185.
TISSUE=Hippocampus;
PubMed=11562351; DOI=10.1101/gad.922801;
Whitmarsh A.J., Kuan C.-Y., Kennedy N.J., Kelkar N., Haydar T.F.,
Mordes J.P., Appel M., Rossini A.A., Jones S.N., Flavell R.A., Rakic P.,
Davis R.J.;
"Requirement of the JIP1 scaffold protein for stress-induced JNK
activation.";
Genes Dev. 15:2421-2432(2001).
[8]
INTERACTION WITH SPAG9.
PubMed=12391307; DOI=10.1073/pnas.232310199;
Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
"JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and
transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
[9]
IDENTIFICATION IN A COMPLEX WITH MAPK8IP1 AND ARHGEF28.
PubMed=14499478; DOI=10.1016/s0169-328x(03)00263-8;
Wu J., Zhai J., Lin H., Nie Z., Ge W.-W., Garcia-Bermejo L., Muschel R.J.,
Schlaepfer W.W., Canete-Soler R.;
"Cytoplasmic retention sites in p190RhoGEF confer anti-apoptotic activity
to an EGFP-tagged protein.";
Brain Res. Mol. Brain Res. 117:27-38(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[11]
CATALYTIC ACTIVITY, AND INTERACTION WITH JAMP.
PubMed=16166642; DOI=10.1128/mcb.25.19.8619-8630.2005;
Kadoya T., Khurana A., Tcherpakov M., Bromberg K.D., Didier C., Broday L.,
Asahara T., Bhoumik A., Ronai Z.;
"JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein,
regulates duration of JNK activity.";
Mol. Cell. Biol. 25:8619-8630(2005).
[12]
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=16618812; DOI=10.1083/jcb.200511055;
Tararuk T., Ostman N., Li W., Bjorkblom B., Padzik A., Zdrojewska J.,
Hongisto V., Herdegen T., Konopka W., Courtney M.J., Coffey E.T.;
"JNK1 phosphorylation of SCG10 determines microtubule dynamics and
axodendritic length.";
J. Cell Biol. 173:265-277(2006).
[13]
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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[15]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH NFE2.
PubMed=19966288; DOI=10.1073/pnas.0909153107;
Lee T.L., Shyu Y.C., Hsu P.H., Chang C.W., Wen S.C., Hsiao W.Y., Tsai M.D.,
Shen C.K.;
"JNK-mediated turnover and stabilization of the transcription factor
p45/NF-E2 during differentiation of murine erythroleukemia cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:52-57(2010).
[16]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
PubMed=21297631; DOI=10.1038/nn.2755;
Westerlund N., Zdrojewska J., Padzik A., Komulainen E., Bjorkblom B.,
Rannikko E., Tararuk T., Garcia-Frigola C., Sandholm J., Nguyen L.,
Kallunki T., Courtney M.J., Coffey E.T.;
"Phosphorylation of SCG10/stathmin-2 determines multipolar stage exit and
neuronal migration rate.";
Nat. Neurosci. 14:305-313(2011).
[17]
FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
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).
[18]
IDENTIFICATION IN A COMPLEX WITH SH3RF1; RAC1; MAP3K11; MAPK8IP1 AND
MAP2K7.
PubMed=23963642; DOI=10.1002/eji.201343635;
Cunningham C.A., Knudson K.M., Peng B.J., Teixeiro E., Daniels M.A.;
"The POSH/JIP-1 scaffold network regulates TCR-mediated JNK1 signals and
effector function in CD8(+) T cells.";
Eur. J. Immunol. 43:3361-3371(2013).
[19]
IDENTIFICATION IN A COMPLEX WITH SH3RF1; RAC2; MAP3K7; MAPK8IP1; MAP2K7 AND
MAPK9.
PubMed=27084103; DOI=10.4049/jimmunol.1501728;
Cunningham C.A., Cardwell L.N., Guan Y., Teixeiro E., Daniels M.A.;
"POSH regulates CD4+ T cell differentiation and survival.";
J. Immunol. 196:4003-4013(2016).
[20]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH POU5F1, AND SUBCELLULAR
LOCATION.
PubMed=29153991; DOI=10.1016/j.stemcr.2017.10.017;
Bae K.B., Yu D.H., Lee K.Y., Yao K., Ryu J., Lim D.Y., Zykova T.A.,
Kim M.O., Bode A.M., Dong Z.;
"Serine 347 Phosphorylation by JNKs Negatively Regulates OCT4 Protein
Stability in Mouse Embryonic Stem Cells.";
Stem Cell Reports 9:2050-2064(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 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 (By
similarity). 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 (By similarity). Phosphorylates
POU5F1, which results in the inhibition of POU5F1's transcriptional
activity and enhances its proteosomal degradation (PubMed:29153991).
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:P45983, ECO:0000250|UniProtKB:P49185,
ECO:0000269|PubMed:10811224, ECO:0000269|PubMed:11602244,
ECO:0000269|PubMed:19966288, ECO:0000269|PubMed:21297631,
ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:29153991,
ECO:0000269|PubMed:9393873}.
-!- 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:11562351, ECO:0000269|PubMed:11602244,
ECO:0000269|PubMed:16166642, ECO:0000269|PubMed:16618812,
ECO:0000269|PubMed:19966288, ECO:0000269|PubMed:21297631,
ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:29153991,
ECO:0000269|PubMed:9096336, ECO:0000269|PubMed:9207092,
ECO:0000269|PubMed:9393873};
-!- 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:11562351,
ECO:0000269|PubMed:11602244, ECO:0000269|PubMed:16166642,
ECO:0000269|PubMed:16618812, ECO:0000269|PubMed:19966288,
ECO:0000269|PubMed:21297631, ECO:0000269|PubMed:22441692,
ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9096336,
ECO:0000269|PubMed:9207092, ECO:0000269|PubMed:9393873};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9207092};
-!- ACTIVITY REGULATION: Inhibited by SERPINB3 (By similarity). 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:0000250|UniProtKB:P45983, ECO:0000269|PubMed:10811224}.
-!- SUBUNIT: Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1,
MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4
(PubMed:10523642, PubMed:12391307, PubMed:11562351). These proteins
also bind other components of the JNK signaling pathway. Forms a
complex with MAPK8IP1 and ARHGEF28 (PubMed:14499478). Interacts with
TP53 and WWOX (By similarity). Interacts with JAMP (PubMed:16166642).
Interacts with NFATC4 (By similarity). Interacts with MECOM; regulates
JNK signaling (By similarity). Interacts with PIN1; this interaction
mediates MAPK8 conformational changes leading to the binding of MAPK8
to its substrates (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 (By similarity). Interacts (phosphorylated form) with NFE2; the
interaction phosphorylates NFE2 in undifferentiated cells
(PubMed:19966288). Interacts with GRIPAP1 (By similarity). Interacts
with POU5F1; phosphorylates POU5F1 at 'Ser-347' (PubMed:29153991).
Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3, MAP2K7/MKK7 and
MAPK8IP1/JIP1 (PubMed:23963642). Found in a complex with SH3RF1, RAC2,
MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK9/JNK2
(PubMed:27084103). {ECO:0000250|UniProtKB:P45983,
ECO:0000250|UniProtKB:P49185, ECO:0000269|PubMed:10523642,
ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:12391307,
ECO:0000269|PubMed:14499478, ECO:0000269|PubMed:16166642,
ECO:0000269|PubMed:19966288, ECO:0000269|PubMed:23963642,
ECO:0000269|PubMed:27084103, ECO:0000269|PubMed:29153991}.
-!- INTERACTION:
Q91Y86; P05627: Jun; NbExp=2; IntAct=EBI-298784, EBI-764369;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16618812}. Nucleus
{ECO:0000269|PubMed:29153991}. 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 (By similarity) (PubMed:29153991).
{ECO:0000250|UniProtKB:P49185, ECO:0000269|PubMed:29153991}.
-!- TISSUE SPECIFICITY: Brain (at protein level).
{ECO:0000269|PubMed:22441692}.
-!- DEVELOPMENTAL STAGE: At 15.5 dpc, mid to low expression throughout the
midbrain, with more prominent levels in the telencephalon, especially
in the intermediate zone, the midbrain roof, the olfactory epithelium,
the inferior colliculus, and the medulla oblongata. telencephalon
revealed concentrated (at protein level).
{ECO:0000269|PubMed:16618812}.
-!- INDUCTION: In T-cells, following T-cell receptor (TCR) activation.
Levels peak 48 hours after TCR and CD-28 costimulation.
{ECO:0000269|PubMed:10811224}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Phosphorylated by TAOK2 (By similarity). Dually phosphorylated on
Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme
(PubMed:11562351). 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:P45983, ECO:0000250|UniProtKB:P49185,
ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:17761173}.
-!- DISRUPTION PHENOTYPE: At 14.5 dpc, brain intermediate zone and cortical
plate are significantly thicker in mutant mice compared to wild type.
The number of neuronal cells is increased in the cortical plate and
intermediate zone. Cell cycle exit is decreased by 13% in the
ventricular and subventricular zones. In 17.5 dpc brains, the
ventricular zone was thinner in mutant mice compared to wild type
animals, consistent with the increased number of neurons in the
cortical plate. TUBB3 is consistently more diffuse and less structured
in mutant telencephalon than in wild type.
{ECO:0000269|PubMed:21297631}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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EMBL; AB005663; BAA85875.1; -; mRNA.
CCDS; CCDS36869.1; -.
RefSeq; NP_057909.1; NM_016700.4.
SMR; Q91Y86; -.
BioGRID; 204971; 24.
DIP; DIP-31075N; -.
ELM; Q91Y86; -.
IntAct; Q91Y86; 8.
MINT; Q91Y86; -.
STRING; 10090.ENSMUSP00000107576; -.
ChEMBL; CHEMBL1795174; -.
iPTMnet; Q91Y86; -.
PhosphoSitePlus; Q91Y86; -.
MaxQB; Q91Y86; -.
PaxDb; Q91Y86; -.
PRIDE; Q91Y86; -.
Antibodypedia; 3846; 1623 antibodies.
Ensembl; ENSMUST00000111945; ENSMUSP00000107576; ENSMUSG00000021936.
GeneID; 26419; -.
KEGG; mmu:26419; -.
UCSC; uc007szt.3; mouse.
CTD; 5599; -.
MGI; MGI:1346861; Mapk8.
eggNOG; KOG0665; Eukaryota.
GeneTree; ENSGT00940000153692; -.
InParanoid; Q91Y86; -.
KO; K04440; -.
PhylomeDB; Q91Y86; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 3474.
Reactome; R-MMU-111446; Activation of BIM and translocation to mitochondria.
Reactome; R-MMU-139910; Activation of BMF and translocation to mitochondria.
Reactome; R-MMU-193648; NRAGE signals death through JNK.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-376172; DSCAM interactions.
Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-MMU-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-9007892; Interleukin-38 signaling.
BioGRID-ORCS; 26419; 0 hits in 18 CRISPR screens.
ChiTaRS; Mapk8; mouse.
PRO; PR:Q91Y86; -.
Proteomes; UP000000589; Chromosome 14.
RNAct; Q91Y86; protein.
Bgee; ENSMUSG00000021936; Expressed in embryo and 306 other tissues.
ExpressionAtlas; Q91Y86; baseline and differential.
Genevisible; Q91Y86; MM.
GO; GO:0030424; C:axon; IMP:ARUK-UCL.
GO; GO:0097441; C:basal dendrite; IMP:ARUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043204; C:perikaryon; ISO:MGI.
GO; GO:0002102; C:podosome; IDA:MGI.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0035033; F:histone deacetylase regulator activity; ISO:MGI.
GO; GO:0004705; F:JUN kinase activity; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0019894; F:kinesin binding; ISO:MGI.
GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IMP:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0071732; P:cellular response to nitric oxide; IMP:MGI.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:CACAO.
GO; GO:0048263; P:determination of dorsal identity; ISO:MGI.
GO; GO:0006954; P:inflammatory response; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
GO; GO:0007258; P:JUN phosphorylation; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:0001764; P:neuron migration; IMP:CACAO.
GO; GO:0031175; P:neuron projection development; ISO:MGI.
GO; GO:0097150; P:neuronal stem cell population maintenance; ISO:MGI.
GO; GO:0001503; P:ossification; IMP:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0031281; P:positive regulation of cyclase activity; ISO:MGI.
GO; GO:0090045; P:positive regulation of deacetylase activity; ISO:MGI.
GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0034352; P:positive regulation of glial cell apoptotic process; ISO:MGI.
GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISO:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
GO; GO:2001224; P:positive regulation of neuron migration; ISO:MGI.
GO; GO:0071803; P:positive regulation of podosome assembly; IMP:MGI.
GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
GO; GO:1901485; P:positive regulation of transcription factor catabolic process; IMP:UniProtKB.
GO; GO:0097300; P:programmed necrotic cell death; IMP:MGI.
GO; GO:0061833; P:protein localization to tricellular tight junction; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0046605; P:regulation of centrosome cycle; ISO:MGI.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:1904809; P:regulation of dense core granule transport; ISO:MGI.
GO; GO:1902595; P:regulation of DNA replication origin binding; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0045664; P:regulation of neuron differentiation; ISO:MGI.
GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0046686; P:response to cadmium ion; IGI:MGI.
GO; GO:0009408; P:response to heat; ISO:MGI.
GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
GO; GO:0006970; P:response to osmotic stress; ISO:MGI.
GO; GO:0009411; P:response to UV; ISO:MGI.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0051403; P:stress-activated MAPK cascade; ISO:MGI.
GO; GO:0097050; P:type B pancreatic cell apoptotic process; ISO:MGI.
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;
ATP-binding; Biological rhythms; Cell junction; Cytoplasm; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
S-nitrosylation; Serine/threonine-protein kinase; Synapse; Transferase.
CHAIN 1..384
/note="Mitogen-activated protein kinase 8"
/id="PRO_0000186263"
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:11562351"
MOD_RES 185
/note="Phosphotyrosine; by MAP2K4"
/evidence="ECO:0000269|PubMed:11562351"
MOD_RES 377
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:15345747"
SEQUENCE 384 AA; 44229 MW; A7320EF933E9CF85 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 VIRGQPSPLA QVQQ


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