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Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (SAPK gamma) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1) (p54 gamma)

 MK08_RAT                Reviewed;         411 AA.
P49185;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
30-AUG-2017, entry version 165.
RecName: Full=Mitogen-activated protein kinase 8;
Short=MAP kinase 8;
Short=MAPK 8;
EC=2.7.11.24;
AltName: Full=SAPK gamma;
AltName: Full=Stress-activated protein kinase JNK1;
AltName: Full=c-Jun N-terminal kinase 1;
AltName: Full=p54 gamma;
Name=Mapk8; Synonyms=Jnk1, Prkm8;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8177321; DOI=10.1038/369156a0;
Kyriakis J.M., Banerjee P., Nikolakaki E., Dai T., Rubie E.A.,
Ahmad M.F., Avruch J., Woodgett J.R.;
"The stress-activated protein kinase subfamily of c-Jun kinases.";
Nature 369:156-160(1994).
[2]
FUNCTION, AND COFACTOR.
TISSUE=Heart;
PubMed=9516415; DOI=10.1074/jbc.273.13.7228;
Clerk A., Fuller S.J., Michael A., Sugden P.H.;
"Stimulation of 'stress-regulated' mitogen-activated protein kinases
(stress-activated protein kinases/c-Jun N-terminal kinases and p38-
mitogen-activated protein kinases) in perfused rat hearts by oxidative
and other stresses.";
J. Biol. Chem. 273:7228-7234(1998).
[3]
S-NITROSYLATION AT CYS-116, AND MUTAGENESIS OF CYS-116.
PubMed=11121042; DOI=10.1073/pnas.97.26.14382;
Park H.S., Huh S.H., Kim M.S., Lee S.H., Choi E.J.;
"Nitric oxide negatively regulates c-Jun N-terminal kinase/stress-
activated protein kinase by means of S-nitrosylation.";
Proc. Natl. Acad. Sci. U.S.A. 97:14382-14387(2000).
[4]
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).
[5]
FUNCTION, INTERACTION WITH MAPK8IP1; STMN2; STMN3 AND STMN4, AND
SUBCELLULAR LOCATION.
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).
[6]
FUNCTION.
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).
-!- 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 (By
similarity). Phosphorylates the heat shock transcription factor
HSF1, suppressing HSF1-induced transcriptional activity (By
similarity). {ECO:0000250|UniProtKB:P45983,
ECO:0000250|UniProtKB:Q91Y86, ECO:0000269|PubMed:16618812,
ECO:0000269|PubMed:21297631, ECO:0000269|PubMed:9516415}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9516415};
-!- 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 (By
similarity). Inhibited by IFN-gamma-induced S-nitrosylation.
{ECO:0000250}.
-!- SUBUNIT: Binds to at least four scaffolding proteins,
MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and
SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of
the JNK signaling pathway. Interacts with TP53, WWOX and JAMP.
Interacts with NFATC4. Interacts (phosphorylated form) with NFE2;
the interaction phosphorylates NFE2 in undifferentiated cells.
Interacts with MECOM; regulates JNK signaling. 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). Forms a complex with MAPK8IP1 and ARHGEF28. Interacts
with STMN2, STMN3 and STMN4. {ECO:0000250,
ECO:0000250|UniProtKB:P45983, ECO:0000269|PubMed:14499478,
ECO:0000269|PubMed:16618812}.
-!- INTERACTION:
P19491-3:Gria2; NbExp=2; IntAct=EBI-7456505, EBI-9118256;
P19493:Gria4; NbExp=2; IntAct=EBI-7456505, EBI-7761834;
P17325:Jun; NbExp=2; IntAct=EBI-7456505, EBI-7709365;
P50232:Syt4; NbExp=5; IntAct=EBI-7456505, EBI-540118;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16618812}.
Nucleus {ECO:0000250}. Note=In the cortical neurons, predominantly
cytoplasmic and associated with the Golgi apparatus and endosomal
fraction.
-!- 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. Phosphorylated by TAOK2 (By
similarity). {ECO:0000250}.
-!- PTM: Nitrosylated upon IFN-gamma-induced endogenous NO production,
which inhibits the enzyme. {ECO:0000269|PubMed:11121042}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; L27129; AAA42111.1; -; mRNA.
PIR; S43970; S43970.
RefSeq; NP_446281.2; NM_053829.2.
UniGene; Rn.4090; -.
ProteinModelPortal; P49185; -.
SMR; P49185; -.
IntAct; P49185; 6.
MINT; MINT-1500743; -.
BindingDB; P49185; -.
ChEMBL; CHEMBL5718; -.
iPTMnet; P49185; -.
PhosphoSitePlus; P49185; -.
PRIDE; P49185; -.
GeneID; 116554; -.
KEGG; rno:116554; -.
UCSC; RGD:621506; rat.
CTD; 5599; -.
RGD; 621506; Mapk8.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P49185; -.
KO; K04440; -.
PhylomeDB; P49185; -.
BRENDA; 2.7.11.24; 5301.
Reactome; R-RNO-193648; NRAGE signals death through JNK.
PRO; PR:P49185; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004705; F:JUN kinase activity; IDA:RGD.
GO; GO:0019894; F:kinesin binding; IPI:RGD.
GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0034349; P:glial cell apoptotic process; IEP:RGD.
GO; GO:0006954; P:inflammatory response; IDA:RGD.
GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:0048666; P:neuron development; IEP:RGD.
GO; GO:0031175; P:neuron projection development; IMP:RGD.
GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IEP:RGD.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IDA:RGD.
GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
GO; GO:0034352; P:positive regulation of glial cell apoptotic process; IMP:RGD.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:RGD.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:2001224; P:positive regulation of neuron migration; IMP:RGD.
GO; GO:0046605; P:regulation of centrosome cycle; IMP:RGD.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0045664; P:regulation of neuron differentiation; IMP:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
GO; GO:0009408; P:response to heat; IDA:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
GO; GO:0006970; P:response to osmotic stress; IDA:RGD.
GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; IDA:RGD.
GO; GO:0097050; P:type B pancreatic cell apoptotic process; IMP:CACAO.
InterPro; IPR011009; Kinase-like_dom.
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; Complete proteome; Cytoplasm; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
S-nitrosylation; Serine/threonine-protein kinase; Transferase.
CHAIN 1 411 Mitogen-activated protein kinase 8.
/FTId=PRO_0000186264.
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; in inhibited form.
{ECO:0000269|PubMed:11121042}.
MOD_RES 183 183 Phosphothreonine; by MAP2K7.
{ECO:0000250|UniProtKB:P45983}.
MOD_RES 185 185 Phosphotyrosine; by MAP2K4.
{ECO:0000250|UniProtKB:P45983}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000250|UniProtKB:Q91Y86}.
MUTAGEN 116 116 C->S: Abolished inhibitory effect of IFN-
gamma on JNK1 activity.
{ECO:0000269|PubMed:11121042}.
SEQUENCE 411 AA; 46807 MW; 04E388B4F94633D4 CRC64;
MSRSKRDNNF YSVEIADSTF TVLKRYQNLK PIGSGAQGIV CAAYDAILER NVAIKKLSRP
FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKSLEE FQDVYIVMEL MDANLCQVIQ
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTAGTSF
MMTPYVVTRY YRAPEVILGM GYKENVDLWS VGCIMGEMVC LKILFPGRDY IDQWNKVIEQ
LGTPCPEFMK KLQPTVRTYV ENRPKYAGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK
MLVIDASKRI SVDEALQHPY INVWYDPSEA EAPPPKIPDK QLDEREHTIE EWKELIYKEV
MDLEERTKNG VIRGQPSPLG AAVINGSQHP VSSPSVNDMS SMSTDPTLAS D


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