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Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (SAPK-alpha) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2) (p54-alpha)

 MK09_RAT                Reviewed;         423 AA.
P49186;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
17-JUN-2020, entry version 171.
RecName: Full=Mitogen-activated protein kinase 9;
Short=MAP kinase 9;
Short=MAPK 9;
EC=2.7.11.24 {ECO:0000269|PubMed:10856240};
AltName: Full=SAPK-alpha;
AltName: Full=Stress-activated protein kinase JNK2;
AltName: Full=c-Jun N-terminal kinase 2;
AltName: Full=p54-alpha;
Name=Mapk9; Synonyms=Jnk2, Prkm9;
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] (ISOFORMS ALPHA-1 AND ALPHA-2), AND PARTIAL
PROTEIN SEQUENCE.
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]
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).
-!- 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 MAPK9/JNK2. In turn, MAPK9/JNK2
phosphorylates a number of transcription factors, primarily components
of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional
activity. In response to oxidative or ribotoxic stresses, inhibits rRNA
synthesis by phosphorylating and inactivating the RNA polymerase 1-
specific transcription initiation factor RRN3. Promotes stressed cell
apoptosis by phosphorylating key regulatory factors including TP53 and
YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized
differentiation of T-helper cells into Th1 cells. Upon T-cell receptor
(TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and
MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in
the osmotic stress-induced epithelial tight-junctions disruption. When
activated, promotes beta-catenin/CTNNB1 degradation and inhibits the
canonical Wnt signaling pathway. Participates also in neurite growth in
spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1
heterodimer and plays a role in the regulation of the circadian clock.
Phosphorylates POU5F1, which results in the inhibition of POU5F1's
transcriptional activity and enhances its proteosomal degradation.
{ECO:0000250|UniProtKB:P45984, ECO:0000250|UniProtKB:Q9WTU6}.
-!- 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:10856240};
-!- 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:10856240};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P45984};
-!- 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. {ECO:0000250|UniProtKB:P45984}.
-!- SUBUNIT: Interacts with MECOM (PubMed:10856240). 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 (By similarity). Interacts with
NFATC4 (By similarity). Interacts with ATF7; the interaction does not
phosphorylate ATF7 but acts as a docking site for ATF7-associated
partners such as JUN (By similarity). Interacts with BCL10 (By
similarity). Interacts with CTNNB1 and GSK3B (By similarity). Interacts
with DCLK2 (By similarity). Interacts with MAPKBP1 (By similarity).
Interacts with POU5F1; phosphorylates POU5F1 at 'Ser-347'. Found in a
complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and
MAPK8/JNK1 (By similarity). {ECO:0000250|UniProtKB:P45984,
ECO:0000250|UniProtKB:Q9WTU6, ECO:0000269|PubMed:10856240}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P45984}. Nucleus
{ECO:0000250|UniProtKB:Q9WTU6}. Note=Colocalizes with POU5F1 in the
nucleus. {ECO:0000250|UniProtKB:Q9WTU6}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha-2;
IsoId=P49186-1; Sequence=Displayed;
Name=Alpha-1;
IsoId=P49186-2; Sequence=VSP_004838;
-!- 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. Autophosphorylated in vitro.
{ECO:0000250|UniProtKB:P45984}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
protein kinase family. MAP kinase subfamily. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; L27112; AAA42109.1; -; mRNA.
EMBL; L27111; AAA42108.1; -; mRNA.
PIR; S43968; S43968.
RefSeq; NP_001257473.1; NM_001270544.1.
RefSeq; NP_059018.1; NM_017322.2. [P49186-1]
SMR; P49186; -.
BioGRID; 248408; 1.
IntAct; P49186; 2.
MINT; P49186; -.
STRING; 10116.ENSRNOP00000003987; -.
iPTMnet; P49186; -.
PhosphoSitePlus; P49186; -.
jPOST; P49186; -.
PaxDb; P49186; -.
PRIDE; P49186; -.
GeneID; 50658; -.
KEGG; rno:50658; -.
UCSC; RGD:628847; rat. [P49186-1]
CTD; 5601; -.
RGD; 628847; Mapk9.
eggNOG; KOG0665; Eukaryota.
eggNOG; ENOG410XSHI; LUCA.
InParanoid; P49186; -.
KO; K04440; -.
OrthoDB; 741207at2759; -.
PhylomeDB; P49186; -.
BRENDA; 2.7.11.24; 5301.
Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
Reactome; R-RNO-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-RNO-450341; Activation of the AP-1 family of transcription factors.
PRO; PR:P49186; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P49186; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IMP:RGD.
GO; GO:0004705; F:JUN kinase activity; IDA:RGD.
GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:RGD.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:RGD.
GO; GO:0008134; F:transcription factor binding; IDA:RGD.
GO; GO:0071474; P:cellular hyperosmotic response; IEP:RGD.
GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:RGD.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0034644; P:cellular response to UV; IMP:RGD.
GO; GO:0007417; P:central nervous system development; IEP:RGD.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007254; P:JNK cascade; IDA:RGD.
GO; GO:0007258; P:JUN phosphorylation; IMP:RGD.
GO; GO:0048666; P:neuron development; IEP:RGD.
GO; GO:0031175; P:neuron projection development; IMP:RGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
GO; GO:0010770; P:positive regulation of cell morphogenesis involved in differentiation; IMP:RGD.
GO; GO:0032722; P:positive regulation of chemokine production; IMP:RGD.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
GO; GO:0071803; P:positive regulation of podosome assembly; ISO:RGD.
GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:RGD.
GO; GO:0032308; P:positive regulation of prostaglandin secretion; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
GO; GO:1901485; P:positive regulation of transcription factor catabolic process; ISO:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:RGD.
GO; GO:0061833; P:protein localization to tricellular tight junction; ISO:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0006626; P:protein targeting to mitochondrion; IEP:RGD.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0046328; P:regulation of JNK cascade; IMP:RGD.
GO; GO:0031396; P:regulation of protein ubiquitination; IMP:RGD.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:RGD.
GO; GO:0014075; P:response to amine; IEP:RGD.
GO; GO:0046686; P:response to cadmium ion; ISO:RGD.
GO; GO:0042493; P:response to drug; IMP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:1990089; P:response to nerve growth factor; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0009414; P:response to water deprivation; IEP:RGD.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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;
Alternative splicing; ATP-binding; Biological rhythms; Cytoplasm;
Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1..423
/note="Mitogen-activated protein kinase 9"
/id="PRO_0000186275"
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 183
/note="Phosphothreonine; by MAP2K7"
/evidence="ECO:0000250|UniProtKB:P45984"
MOD_RES 185
/note="Phosphotyrosine; by MAP2K4"
/evidence="ECO:0000250|UniProtKB:P45984"
VAR_SEQ 216..230
/note="GELVKGCVIFQGTDH -> AEMVLHKSCSPGRDY (in isoform
Alpha-1)"
/evidence="ECO:0000303|PubMed:8177321"
/id="VSP_004838"
SEQUENCE 423 AA; 48017 MW; EE549B9F4F12F421 CRC64;
MSDSKSDGQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP
FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF
MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMGELVK GCVIFQGTDH IDQWNKVIEQ
LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK
MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV
MDWEERSKNG VKDQPSDAAV SSKATPSQSS SINDISSMST EHTLASDTDS SLDASTGPLE
GCR


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