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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.
30-AUG-2017, entry version 157.
RecName: Full=Mitogen-activated protein kinase 9;
Short=MAP kinase 9;
Short=MAPK 9;
EC=2.7.11.24;
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.
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.
{ECO:0000250|UniProtKB:P45984, ECO:0000250|UniProtKB:Q9WTU6}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- 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 (By similarity).
{ECO:0000250}.
-!- 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).
{ECO:0000250|UniProtKB:P45984, ECO:0000250|UniProtKB:Q9WTU6,
ECO:0000269|PubMed:10856240}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- 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
(By similarity). {ECO:0000250}.
-!- 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
-----------------------------------------------------------------------
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]
UniGene; Rn.177202; -.
UniGene; Rn.9910; -.
ProteinModelPortal; P49186; -.
SMR; P49186; -.
BioGrid; 248408; 1.
IntAct; P49186; 2.
MINT; MINT-5027617; -.
STRING; 10116.ENSRNOP00000003987; -.
iPTMnet; P49186; -.
PhosphoSitePlus; 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.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P49186; -.
KO; K04440; -.
PhylomeDB; P49186; -.
BRENDA; 2.7.11.24; 5301.
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:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI: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: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: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: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:0043065; P:positive regulation of apoptotic process; IMP: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: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: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:0045893; P:positive regulation of transcription, DNA-templated; IMP: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: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: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.
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;
Complete proteome; Cytoplasm; Direct protein sequencing; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 423 Mitogen-activated protein kinase 9.
/FTId=PRO_0000186275.
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 183 183 Phosphothreonine; by MAP2K7.
{ECO:0000250|UniProtKB:P45984}.
MOD_RES 185 185 Phosphotyrosine; by MAP2K4.
{ECO:0000250|UniProtKB:P45984}.
VAR_SEQ 216 230 GELVKGCVIFQGTDH -> AEMVLHKSCSPGRDY (in
isoform Alpha-1).
{ECO:0000303|PubMed:8177321}.
/FTId=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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