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Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2 7 11 24) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2)

 MK09_MOUSE              Reviewed;         423 AA.
Q9WTU6; Q5NCK9; Q5NCL5; Q8C097; Q8VDD2; Q9WTU4; Q9WTU5;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
13-FEB-2019, entry version 186.
RecName: Full=Mitogen-activated protein kinase 9;
Short=MAP kinase 9;
Short=MAPK 9;
EC=2.7.11.24 {ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:16973441, ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9806643};
AltName: Full=Stress-activated protein kinase JNK2;
AltName: Full=c-Jun N-terminal kinase 2;
Name=Mapk9; Synonyms=Jnk2, Prkm9;
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] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1 AND
BETA-2), FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
PubMed=9806643; DOI=10.1016/S1074-7613(00)80640-8;
Yang D.D., Conze D., Whitmarsh A.J., Barrett T., Davis R.J.,
Rincon M., Flavell R.A.;
"Differentiation of CD4+ T cells to Th1 cells requires MAP kinase
JNK2.";
Immunity 9:575-585(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1
AND BETA-2), AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10674476; DOI=10.1097/00001756-200002070-00017;
Casanova E., Callejo A.I., Calvo P., Chinchetru M.A.;
"Analysis of splicing of four mouse JNK/SAPKalpha variants.";
NeuroReport 11:305-309(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
STRAIN=FVB/N; TISSUE=Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
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).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
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).
[9]
INTERACTION WITH DCLK2.
PubMed=16628014; DOI=10.4161/cc.5.9.2715;
Coquelle F.M., Levy T., Bergmann S., Wolf S.G., Bar-El D., Sapir T.,
Brody Y., Orr I., Barkai N., Eichele G., Reiner O.;
"Common and divergent roles for members of the mouse DCX
superfamily.";
Cell Cycle 5:976-983(2006).
[10]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=16973441; DOI=10.1016/j.molcel.2006.07.028;
Jaeschke A., Karasarides M., Ventura J.J., Ehrhardt A., Zhang C.,
Flavell R.A., Shokat K.M., Davis R.J.;
"JNK2 is a positive regulator of the cJun transcription factor.";
Mol. Cell 23:899-911(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
Spleen, 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).
[13]
FUNCTION IN NEURITE GROWTH.
PubMed=21554942; DOI=10.1016/j.heares.2011.04.011;
Atkinson P.J., Cho C.H., Hansen M.R., Green S.H.;
"Activity of all JNK isoforms contributes to neurite growth in spiral
ganglion neurons.";
Hear. Res. 278:77-85(2011).
[14]
FUNCTION, AND CATALYTIC ACTIVITY.
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).
[15]
IDENTIFICATION IN A COMPLEX WITH SH3RF1; RAC2; MAP3K7; MAPK8IP1;
MAP2K7 AND MAPK8.
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).
[16]
FUNCTION, 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 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 (PubMed:22441692).
Phosphorylates POU5F1, which results in the inhibition of POU5F1's
transcriptional activity and enhances its proteosomal degradation
(PubMed:29153991). {ECO:0000269|PubMed:10811224,
ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:16973441,
ECO:0000269|PubMed:21554942, ECO:0000269|PubMed:22441692,
ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9806643}.
-!- 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:16973441, ECO:0000269|PubMed:22441692,
ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9806643};
-!- 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:16973441, ECO:0000269|PubMed:22441692,
ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9806643};
-!- 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:0000269|PubMed:10811224}.
-!- SUBUNIT: Interacts with MECOM (By similarity). 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
(PubMed:11562351). 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 (PubMed:16628014). Interacts with MAPKBP1 (By similarity).
Interacts with POU5F1; phosphorylates POU5F1 at 'Ser-347'
(PubMed:29153991). Found in a complex with SH3RF1, RAC2,
MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1
(PubMed:27084103). {ECO:0000250|UniProtKB:P45984,
ECO:0000250|UniProtKB:P49186, ECO:0000269|PubMed:11562351,
ECO:0000269|PubMed:16628014, ECO:0000269|PubMed:27084103,
ECO:0000269|PubMed:29153991}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P45984}.
Nucleus {ECO:0000269|PubMed:29153991}. Note=Colocalizes with
POU5F1 in the nucleus. {ECO:0000269|PubMed:29153991}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=Alpha-2;
IsoId=Q9WTU6-1; Sequence=Displayed;
Name=Alpha-1;
IsoId=Q9WTU6-2; Sequence=VSP_004837;
Name=Beta-1;
IsoId=Q9WTU6-3; Sequence=VSP_004836, VSP_004837;
Name=Beta-2;
IsoId=Q9WTU6-4; Sequence=VSP_004836;
-!- TISSUE SPECIFICITY: All four isoforms are widely distributed in
brain. Isoforms alpha-1 and alpha-2 are predominantly expressed in
hippocampus, cerebral cortex, caudate-putamen, amygdala and the
granule layer of the cerebellum. Alpha-1 is more abundant than
alpha-2 in the periaqueductal region and the substantia nigra.
{ECO:0000269|PubMed:10674476}.
-!- INDUCTION: In T-cells, following T-cell receptor (TCR) activation.
Levels peak 48 hours after TCR and CD-28 costimulation.
{ECO:0000269|PubMed:10811224, ECO:0000269|PubMed:9806643}.
-!- 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; AF052466; AAD22576.1; -; mRNA.
EMBL; AF052467; AAD22577.1; -; mRNA.
EMBL; AF052468; AAD22578.1; -; mRNA.
EMBL; AF052469; AAD22579.1; -; mRNA.
EMBL; AB005664; BAA85876.1; -; mRNA.
EMBL; AJ315339; CAC88132.1; ALT_SEQ; Genomic_DNA.
EMBL; AJ315340; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315341; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315342; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315343; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315344; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315345; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315346; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315347; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315348; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315349; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AJ315350; CAC88132.1; JOINED; Genomic_DNA.
EMBL; AK031959; BAC27623.1; -; mRNA.
EMBL; AL606479; CAI23940.1; -; Genomic_DNA.
EMBL; AL606479; CAI23941.1; -; Genomic_DNA.
EMBL; BC028341; AAH28341.1; -; mRNA.
CCDS; CCDS24623.1; -. [Q9WTU6-4]
CCDS; CCDS24624.1; -. [Q9WTU6-2]
CCDS; CCDS48782.1; -. [Q9WTU6-1]
CCDS; CCDS48783.1; -. [Q9WTU6-3]
RefSeq; NP_001157143.1; NM_001163671.1. [Q9WTU6-1]
RefSeq; NP_001157144.1; NM_001163672.1. [Q9WTU6-3]
RefSeq; NP_058657.1; NM_016961.3. [Q9WTU6-2]
RefSeq; NP_997575.2; NM_207692.2. [Q9WTU6-4]
UniGene; Mm.68933; -.
ProteinModelPortal; Q9WTU6; -.
SMR; Q9WTU6; -.
BioGrid; 204972; 4.
DIP; DIP-31076N; -.
ELM; Q9WTU6; -.
IntAct; Q9WTU6; 6.
MINT; Q9WTU6; -.
STRING; 10090.ENSMUSP00000020634; -.
BindingDB; Q9WTU6; -.
ChEMBL; CHEMBL2034797; -.
iPTMnet; Q9WTU6; -.
PhosphoSitePlus; Q9WTU6; -.
jPOST; Q9WTU6; -.
PaxDb; Q9WTU6; -.
PeptideAtlas; Q9WTU6; -.
PRIDE; Q9WTU6; -.
Ensembl; ENSMUST00000020634; ENSMUSP00000020634; ENSMUSG00000020366. [Q9WTU6-4]
Ensembl; ENSMUST00000043321; ENSMUSP00000042744; ENSMUSG00000020366. [Q9WTU6-1]
Ensembl; ENSMUST00000102778; ENSMUSP00000099839; ENSMUSG00000020366. [Q9WTU6-2]
Ensembl; ENSMUST00000109178; ENSMUSP00000104807; ENSMUSG00000020366. [Q9WTU6-3]
Ensembl; ENSMUST00000109179; ENSMUSP00000104808; ENSMUSG00000020366. [Q9WTU6-2]
Ensembl; ENSMUST00000164643; ENSMUSP00000132864; ENSMUSG00000020366. [Q9WTU6-3]
Ensembl; ENSMUST00000178543; ENSMUSP00000136977; ENSMUSG00000020366. [Q9WTU6-1]
GeneID; 26420; -.
KEGG; mmu:26420; -.
UCSC; uc007ird.2; mouse. [Q9WTU6-2]
UCSC; uc007irh.2; mouse. [Q9WTU6-1]
UCSC; uc007iri.2; mouse. [Q9WTU6-3]
CTD; 5601; -.
MGI; MGI:1346862; Mapk9.
eggNOG; KOG0665; Eukaryota.
eggNOG; ENOG410XSHI; LUCA.
GeneTree; ENSGT00940000158327; -.
HOVERGEN; HBG014652; -.
InParanoid; Q9WTU6; -.
KO; K04440; -.
OMA; WEERNKN; -.
OrthoDB; 741207at2759; -.
PhylomeDB; Q9WTU6; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 3474.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
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.
PRO; PR:Q9WTU6; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020366; Expressed in 286 organ(s), highest expression level in secondary oocyte.
ExpressionAtlas; Q9WTU6; baseline and differential.
Genevisible; Q9WTU6; MM.
GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043204; C:perikaryon; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISO:MGI.
GO; GO:0004705; F:JUN kinase activity; ISS:UniProtKB.
GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IMP:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0034644; P:cellular response to UV; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
GO; GO:0007258; P:JUN phosphorylation; ISO:MGI.
GO; GO:0048666; P:neuron development; IBA:GO_Central.
GO; GO:0031175; P:neuron projection development; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
GO; GO:0010770; P:positive regulation of cell morphogenesis involved in differentiation; ISO:MGI.
GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
GO; GO:0071803; P:positive regulation of podosome assembly; IMP:MGI.
GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; ISO:MGI.
GO; GO:0032308; P:positive regulation of prostaglandin secretion; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; 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:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0061833; P:protein localization to tricellular tight junction; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0046328; P:regulation of JNK cascade; ISO:MGI.
GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI.
GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:0046686; P:response to cadmium ion; IGI:MGI.
GO; GO:0042493; P:response to drug; ISO:MGI.
GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
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;
Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 423 Mitogen-activated protein kinase 9.
/FTId=PRO_0000186274.
DOMAIN 26 321 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 33 38 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:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079}.
MOD_RES 185 185 Phosphotyrosine; by MAP2K4.
{ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 216 230 AEMVLHKVLFPGRDY -> GELVKGCVIFQGTDH (in
isoform Beta-1 and isoform Beta-2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9806643}.
/FTId=VSP_004836.
VAR_SEQ 377 423 DAAVSSKATPSQSSSINDISSMSTEHTLASDTDSSLDASTG
PLEGCR -> AQMQQ (in isoform Alpha-1 and
isoform Beta-1).
{ECO:0000303|PubMed:10523642,
ECO:0000303|PubMed:9806643}.
/FTId=VSP_004837.
CONFLICT 223 223 V -> C (in Ref. 3). {ECO:0000305}.
CONFLICT 237 237 V -> A (in Ref. 3; CAC88132).
{ECO:0000305}.
CONFLICT 386 386 P -> A (in Ref. 4; BAC27623).
{ECO:0000305}.
SEQUENCE 423 AA; 48189 MW; 0E759B486ABCE20D CRC64;
MSDSKSDGQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP
FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF
MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMAEMVL HKVLFPGRDY IDQWNKVIEQ
LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK
MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV
MDWEERSKNG VKDQPSDAAV SSKATPSQSS SINDISSMST EHTLASDTDS SLDASTGPLE
GCR


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1493: Carbon assimilation C4 pathway
WP1567: Glycolysis and Gluconeogenesis
WP1619: Amino sugar and nucleotide sugar metabolism
WP1653: Galactose metabolism
WP1681: Pantothenate and CoA biosynthesis
WP1701: Starch and sucrose metabolism
WP1703: Streptomycin biosynthesis
WP1844: MAP kinase cascade
WP1946: Cori Cycle
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP253: Glycolysis
WP32: Translation Factors
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system

Related Genes :
[MAPK9 JNK2 PRKM9 SAPK1A] Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (JNK-55) (Stress-activated protein kinase 1a) (SAPK1a) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2)
[Mapk9 Jnk2 Prkm9] Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2)
[Mapk9 Jnk2 Prkm9] 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)
[MAPK9 JNK2] Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2)
[MAPK8 JNK1 PRKM8 SAPK1 SAPK1C] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (JNK-46) (Stress-activated protein kinase 1c) (SAPK1c) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)
[Mapk8 Jnk1 Prkm8] 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)
[Mapk8 Jnk1 Prkm8] 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)
[MAPK10 JNK3 JNK3A PRKM10 SAPK1B] Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase 1b) (SAPK1b) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3)
[Mapk8ip1 Ib1 Jip1 Mapk8ip Prkm8ip] C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain-1) (IB-1) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1)
[Mapk8ip1 Ib1 Jip1 Mapk8ip] C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain-1) (IB-1) (JIP-1-related protein) (JRP) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1)
[MAPK8IP1 IB1 JIP1 PRKM8IP] C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain 1) (IB-1) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[Mapk10 Jnk3 Prkm10 Serk2] Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3)
[Mapk10 Jnk3 Prkm10] Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (SAPK-beta) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3) (p54-beta)
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[MAPK1 ERK2 PRKM1 PRKM2] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[MAPK11 PRKM11 SAPK2 SAPK2B] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38b) (Stress-activated protein kinase 2b) (SAPK2b) (p38-2)
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Mapk8ip3 Jip3 Jsap1 Syd2] C-Jun-amino-terminal kinase-interacting protein 3 (JIP-3) (JNK-interacting protein 3) (JNK MAP kinase scaffold protein 3) (JNK/SAPK-associated protein 1) (JSAP1) (Mitogen-activated protein kinase 8-interacting protein 3) (Sunday driver 2)
[MAPK8IP2 IB2 JIP2 PRKM8IPL] C-Jun-amino-terminal kinase-interacting protein 2 (JIP-2) (JNK-interacting protein 2) (Islet-brain-2) (IB-2) (JNK MAP kinase scaffold protein 2) (Mitogen-activated protein kinase 8-interacting protein 2)
[Mapk1 Erk2 Mapk Prkm1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[Mapk1 Erk2 Mapk Prkm1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[MAPK13 PRKM13 SAPK4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[MAPK12 ERK6 SAPK3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk14 Crk1 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[Mapk13] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[MAPK3 ERK1 PRKM3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[Mapk13 Serk4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)

Bibliography :
[30011811] Farrerol Ameliorates TNBS-Induced Colonic Inflammation by Inhibiting ERK1/2, JNK1/2, and NF-κB Signaling Pathway.
[29935949] Uveal melanocytes express high constitutive levels of MMP-8 which can be upregulated by TNF-α via the MAPK pathway.
[29320816] IL-12 and IL-23 Production in Toxoplasma gondii- or LPS-Treated Jurkat T Cells via PI3K and MAPK Signaling Pathways.
[29224011] GLP-1 and Ghrelin Attenuate High Glucose/High Lipid-Induced Apoptosis and Senescence of Human Microvascular Endothelial Cells.
[29080788] l-Theanine prevents ETEC-induced liver damage by reducing intrinsic apoptotic response and inhibiting ERK1/2 and JNK1/2 signaling pathways.
[28680052] Hyperosmolarity-induced AQP5 upregulation promotes inflammation and cell death via JNK1/2 Activation in human corneal epithelial cells.
[28188818] JNK1/2 inhibitor reduces dengue virus-induced liver injury.
[27492456] Extracellular HSP70-peptide complexes promote the proliferation of hepatocellular carcinoma cells via TLR2/4/JNK1/2MAPK pathway.
[26906522] Inhibitor design against JNK1 through e-pharmacophore modeling docking and molecular dynamics simulations.
[26861286] GLP-2 Attenuates LPS-Induced Inflammation in BV-2 Cells by Inhibiting ERK1/2, JNK1/2 and NF-κB Signaling Pathways.
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