MK08_RAT
ID MK08_RAT Reviewed; 411 AA.
AC P49185;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Mitogen-activated protein kinase 8;
DE Short=MAP kinase 8;
DE Short=MAPK 8;
DE EC=2.7.11.24 {ECO:0000269|PubMed:11121042, ECO:0000269|PubMed:16618812, ECO:0000269|PubMed:21297631, ECO:0000269|PubMed:9516415};
DE AltName: Full=SAPK gamma;
DE AltName: Full=Stress-activated protein kinase JNK1;
DE AltName: Full=c-Jun N-terminal kinase 1;
DE AltName: Full=p54 gamma;
GN Name=Mapk8; Synonyms=Jnk1, Prkm8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8177321; DOI=10.1038/369156a0;
RA Kyriakis J.M., Banerjee P., Nikolakaki E., Dai T., Rubie E.A., Ahmad M.F.,
RA Avruch J., Woodgett J.R.;
RT "The stress-activated protein kinase subfamily of c-Jun kinases.";
RL Nature 369:156-160(1994).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC TISSUE=Heart;
RX PubMed=9516415; DOI=10.1074/jbc.273.13.7228;
RA Clerk A., Fuller S.J., Michael A., Sugden P.H.;
RT "Stimulation of 'stress-regulated' mitogen-activated protein kinases
RT (stress-activated protein kinases/c-Jun N-terminal kinases and p38-mitogen-
RT activated protein kinases) in perfused rat hearts by oxidative and other
RT stresses.";
RL J. Biol. Chem. 273:7228-7234(1998).
RN [3]
RP CATALYTIC ACTIVITY, S-NITROSYLATION AT CYS-116, AND MUTAGENESIS OF CYS-116.
RX PubMed=11121042; DOI=10.1073/pnas.97.26.14382;
RA Park H.S., Huh S.H., Kim M.S., Lee S.H., Choi E.J.;
RT "Nitric oxide negatively regulates c-Jun N-terminal kinase/stress-activated
RT protein kinase by means of S-nitrosylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14382-14387(2000).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH MAPK8IP1 AND ARHGEF28.
RX PubMed=14499478; DOI=10.1016/s0169-328x(03)00263-8;
RA Wu J., Zhai J., Lin H., Nie Z., Ge W.-W., Garcia-Bermejo L., Muschel R.J.,
RA Schlaepfer W.W., Canete-Soler R.;
RT "Cytoplasmic retention sites in p190RhoGEF confer anti-apoptotic activity
RT to an EGFP-tagged protein.";
RL Brain Res. Mol. Brain Res. 117:27-38(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MAPK8IP1; STMN2; STMN3 AND
RP STMN4, AND SUBCELLULAR LOCATION.
RX PubMed=16618812; DOI=10.1083/jcb.200511055;
RA Tararuk T., Ostman N., Li W., Bjorkblom B., Padzik A., Zdrojewska J.,
RA Hongisto V., Herdegen T., Konopka W., Courtney M.J., Coffey E.T.;
RT "JNK1 phosphorylation of SCG10 determines microtubule dynamics and
RT axodendritic length.";
RL J. Cell Biol. 173:265-277(2006).
RN [6]
RP INTERACTION WITH GRIPAP1.
RX PubMed=17761173; DOI=10.1016/j.febslet.2007.08.008;
RA Ye B., Yu W.P., Thomas G.M., Huganir R.L.;
RT "GRASP-1 is a neuronal scaffold protein for the JNK signaling pathway.";
RL FEBS Lett. 581:4403-4410(2007).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21297631; DOI=10.1038/nn.2755;
RA Westerlund N., Zdrojewska J., Padzik A., Komulainen E., Bjorkblom B.,
RA Rannikko E., Tararuk T., Garcia-Frigola C., Sandholm J., Nguyen L.,
RA Kallunki T., Courtney M.J., Coffey E.T.;
RT "Phosphorylation of SCG10/stathmin-2 determines multipolar stage exit and
RT neuronal migration rate.";
RL Nat. Neurosci. 14:305-313(2011).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29166604; DOI=10.1016/j.celrep.2017.10.084;
RA Bharat V., Siebrecht M., Burk K., Ahmed S., Reissner C.,
RA Kohansal-Nodehi M., Steubler V., Zweckstetter M., Ting J.T., Dean C.;
RT "Capture of Dense Core Vesicles at Synapses by JNK-Dependent
RT Phosphorylation of Synaptotagmin-4.";
RL Cell Rep. 21:2118-2133(2017).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in various processes
CC such as cell proliferation, differentiation, migration, transformation
CC and programmed cell death (PubMed:9516415, PubMed:16618812).
CC Extracellular stimuli such as pro-inflammatory cytokines or physical
CC stress stimulate the stress-activated protein kinase/c-Jun N-terminal
CC kinase (SAP/JNK) signaling pathway. In this cascade, two dual
CC specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and
CC activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of
CC transcription factors, primarily components of AP-1 such as JUN, JDP2
CC and ATF2 and thus regulates AP-1 transcriptional activity.
CC Phosphorylates the replication licensing factor CDT1, inhibiting the
CC interaction between CDT1 and the histone H4 acetylase HBO1 to
CC replication origins. Loss of this interaction abrogates the acetylation
CC required for replication initiation. Promotes stressed cell apoptosis
CC by phosphorylating key regulatory factors including p53/TP53 and Yes-
CC associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for
CC polarized differentiation of T-helper cells into Th1 cells. Contributes
CC to the survival of erythroid cells by phosphorylating the antagonist of
CC cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2
CC phosphorylation, BCL2 dissociation from BECN1, and thus activation of
CC autophagy. Phosphorylates STMN2 and hence regulates microtubule
CC dynamics, controlling neurite elongation in cortical neurons. In the
CC developing brain, through its cytoplasmic activity on STMN2, negatively
CC regulates the rate of exit from multipolar stage and of radial
CC migration from the ventricular zone (PubMed:21297631). Phosphorylates
CC several other substrates including heat shock factor protein 4 (HSF4),
CC the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the
CC CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the
CC circadian clock (By similarity). Phosphorylates the heat shock
CC transcription factor HSF1, suppressing HSF1-induced transcriptional
CC activity (By similarity). Phosphorylates POU5F1, which results in the
CC inhibition of POU5F1's transcriptional activity and enhances its
CC proteosomal degradation (By similarity). Phosphorylates JUND and this
CC phosphorylation is inhibited in the presence of MEN1 (By similarity).
CC In neurons, phosphorylates SYT4 which captures neuronal dense core
CC vesicles at synapses (PubMed:29166604). Phosphorylates EIF4ENIF1/4-ET
CC in response to oxidative stress, promoting P-body assembly (By
CC similarity). Phosphorylates SIRT6 in response to oxidative stress,
CC stimulating its mono-ADP-ribosyltransferase activity (By similarity).
CC {ECO:0000250|UniProtKB:P45983, ECO:0000250|UniProtKB:Q91Y86,
CC ECO:0000269|PubMed:16618812, ECO:0000269|PubMed:21297631,
CC ECO:0000269|PubMed:29166604, ECO:0000269|PubMed:9516415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC Evidence={ECO:0000269|PubMed:11121042, ECO:0000269|PubMed:16618812,
CC ECO:0000269|PubMed:21297631, ECO:0000269|PubMed:9516415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.24; Evidence={ECO:0000269|PubMed:11121042,
CC ECO:0000269|PubMed:16618812, ECO:0000269|PubMed:21297631,
CC ECO:0000269|PubMed:9516415};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9516415};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation by either of two dual specificity kinases, MAP2K4 and
CC MAP2K7. MAP2K4 shows a strong preference for Tyr-185 while MAP2K7
CC phosphorylates Tyr-183 preferentially. Inhibited by dual specificity
CC phosphatases, such as DUSP1. Inhibited by SERPINB3 (By similarity).
CC Inhibited by IFN-gamma-induced S-nitrosylation.
CC {ECO:0000250|UniProtKB:P45983}.
CC -!- SUBUNIT: Forms a complex with MAPK8IP1 and ARHGEF28 (PubMed:14499478).
CC Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3, MAP2K7/MKK7 and
CC MAPK8IP1/JIP1. Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1,
CC MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK9/JNK2 (By similarity). Binds to at
CC least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2,
CC MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also bind
CC other components of the JNK signaling pathway. Interacts with TP53,
CC WWOX. Interacts with JAMP. Interacts with NFATC4. Interacts
CC (phosphorylated form) with NFE2; the interaction phosphorylates NFE2 in
CC undifferentiated cells. Interacts with MECOM; regulates JNK signaling.
CC Interacts with PIN1; this interaction mediates MAPK8 conformational
CC changes leading to the binding of MAPK8 to its substrates (By
CC similarity). Interacts with HSF1 (via D domain and preferentially with
CC hyperphosphorylated form); this interaction occurs under both normal
CC growth conditions and immediately upon heat shock (By similarity).
CC Interacts with STMN2, STMN3 and STMN4 (PubMed:16618812). Interacts with
CC GRIPAP1 (PubMed:17761173). Interacts with POU5F1; phosphorylates POU5F1
CC at 'Ser-347'. Interacts with HSF4 (By similarity).
CC {ECO:0000250|UniProtKB:P45983, ECO:0000250|UniProtKB:Q91Y86,
CC ECO:0000269|PubMed:14499478, ECO:0000269|PubMed:16618812,
CC ECO:0000269|PubMed:17761173}.
CC -!- INTERACTION:
CC P49185; P19491-3: Gria2; NbExp=2; IntAct=EBI-7456505, EBI-9118256;
CC P49185; P19493: Gria4; NbExp=2; IntAct=EBI-7456505, EBI-7761834;
CC P49185; P17325: Jun; NbExp=2; IntAct=EBI-7456505, EBI-7709365;
CC P49185; P50232: Syt4; NbExp=5; IntAct=EBI-7456505, EBI-540118;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16618812}. Nucleus
CC {ECO:0000250|UniProtKB:Q91Y86}. Synapse {ECO:0000269|PubMed:29166604}.
CC Note=In the cortical neurons, predominantly cytoplasmic and associated
CC with the Golgi apparatus and endosomal fraction (PubMed:16618812).
CC Increased neuronal activity increases phosphorylated form at synapses
CC (PubMed:29166604). Colocalizes with POU5F1 in the nucleus (By
CC similarity). {ECO:0000250|UniProtKB:Q91Y86,
CC ECO:0000269|PubMed:16618812, ECO:0000269|PubMed:29166604}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4,
CC which activates the enzyme. Phosphorylated by TAOK2 (By similarity).
CC Phosphorylated form is more concentrated at synapses than none-
CC phosphorylated (PubMed:29166604). {ECO:0000250,
CC ECO:0000269|PubMed:29166604}.
CC -!- PTM: Nitrosylated upon IFN-gamma-induced endogenous NO production,
CC which inhibits the enzyme (PubMed:11121042). May be phosphorylated at
CC Thr-183 and Tyr-185 by MAP3K1/MEKK1 (By similarity).
CC {ECO:0000250|UniProtKB:P45983, ECO:0000269|PubMed:11121042}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; L27129; AAA42111.1; -; mRNA.
DR PIR; S43970; S43970.
DR RefSeq; NP_446281.2; NM_053829.2.
DR AlphaFoldDB; P49185; -.
DR SMR; P49185; -.
DR IntAct; P49185; 6.
DR MINT; P49185; -.
DR STRING; 10116.ENSRNOP00000062048; -.
DR BindingDB; P49185; -.
DR ChEMBL; CHEMBL5718; -.
DR iPTMnet; P49185; -.
DR PhosphoSitePlus; P49185; -.
DR jPOST; P49185; -.
DR PRIDE; P49185; -.
DR GeneID; 116554; -.
DR KEGG; rno:116554; -.
DR UCSC; RGD:621506; rat.
DR CTD; 5599; -.
DR RGD; 621506; Mapk8.
DR eggNOG; KOG0665; Eukaryota.
DR InParanoid; P49185; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; P49185; -.
DR BRENDA; 2.7.11.24; 5301.
DR Reactome; R-RNO-111446; Activation of BIM and translocation to mitochondria.
DR Reactome; R-RNO-139910; Activation of BMF and translocation to mitochondria.
DR Reactome; R-RNO-193648; NRAGE signals death through JNK.
DR Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-376172; DSCAM interactions.
DR Reactome; R-RNO-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-RNO-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-RNO-9007892; Interleukin-38 signaling.
DR PRO; PR:P49185; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0097441; C:basal dendrite; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0002102; C:podosome; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0035033; F:histone deacetylase regulator activity; ISO:RGD.
DR GO; GO:0004705; F:JUN kinase activity; IDA:RGD.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0019894; F:kinesin binding; IPI:RGD.
DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0120283; F:protein serine/threonine kinase binding; ISO:RGD.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:RGD.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:RGD.
DR GO; GO:0071732; P:cellular response to nitric oxide; ISO:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0034349; P:glial cell apoptotic process; IEP:RGD.
DR GO; GO:0006954; P:inflammatory response; IDA:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
DR GO; GO:0007258; P:JUN phosphorylation; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0048666; P:neuron development; IEP:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IMP:RGD.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:MGI.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEP:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:RGD.
DR GO; GO:0031281; P:positive regulation of cyclase activity; ISO:RGD.
DR GO; GO:0090045; P:positive regulation of deacetylase activity; ISO:RGD.
DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; ISO:RGD.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0034352; P:positive regulation of glial cell apoptotic process; IMP:RGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:RGD.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:RGD.
DR GO; GO:0071803; P:positive regulation of podosome assembly; ISO:RGD.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:RGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:1901485; P:positive regulation of transcription factor catabolic process; ISO:RGD.
DR GO; GO:0097300; P:programmed necrotic cell death; ISO:RGD.
DR GO; GO:0061833; P:protein localization to tricellular tight junction; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0046605; P:regulation of centrosome cycle; IMP:RGD.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:1904809; P:regulation of dense core granule transport; IDA:UniProtKB.
DR GO; GO:1902595; P:regulation of DNA replication origin binding; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0046686; P:response to cadmium ion; ISO:RGD.
DR GO; GO:0009408; P:response to heat; IDA:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IDA:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0009411; P:response to UV; ISO:RGD.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR GO; GO:0051403; P:stress-activated MAPK cascade; ISO:RGD.
DR GO; GO:0097050; P:type B pancreatic cell apoptotic process; IMP:CACAO.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008351; MAPK_JNK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01772; JNKMAPKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Biological rhythms; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; S-nitrosylation;
KW Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..411
FT /note="Mitogen-activated protein kinase 8"
FT /id="PRO_0000186264"
FT DOMAIN 26..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 368..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 183..185
FT /note="TXY"
FT COMPBIAS 386..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 116
FT /note="S-nitrosocysteine; in inhibited form"
FT /evidence="ECO:0000269|PubMed:11121042"
FT MOD_RES 183
FT /note="Phosphothreonine; by MAP2K7"
FT /evidence="ECO:0000250|UniProtKB:P45983"
FT MOD_RES 185
FT /note="Phosphotyrosine; by MAP2K4"
FT /evidence="ECO:0000250|UniProtKB:P45983"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y86"
FT MUTAGEN 116
FT /note="C->S: Abolished inhibitory effect of IFN-gamma on
FT JNK1 activity."
FT /evidence="ECO:0000269|PubMed:11121042"
SQ 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
