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Reviewed, UniProtKB/Swiss-Prot Q9WTU6 (MK09_MOUSE)

Last modified February 9, 2010. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mitogen-activated protein kinase 9
      Short name=MAP kinase 9
      Short name=MAPK 9
    EC=2.7.11.24
Alternative name(s):
    Stress-activated protein kinase JNK2
    c-Jun N-terminal kinase 2
Gene names
Name: Mapk9
Synonyms: Jnk2, Prkm9
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as c-Jun and ATF2 and thus regulates AP-1 transcriptional activity. In T-cells, JNK1 and JNK2 are required for polarized differentiation of T-helper cells into Th1 cells. Ref.1 Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by threonine and tyrosine phosphorylation by either of two dual specificity kinases, MAP2K4 and MAP2K7. Inhibited by dual specificity phosphatases, such as DUSP1. Ref.7

Subunit structure

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. Interacts with NFATC4.

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. Ref.3

Induction

In T-cells, following T-cell receptor (TCR) activation. Levels peak 48 hours after TCR and CD-28 costimulation. Ref.1 Ref.7

Domain

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Post-translational modification

Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme. Ref.9 Ref.10

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Mapk14P478112EBI-432211,EBI-298727

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha-2 (identifier: Q9WTU6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Alpha-1 (identifier: Q9WTU6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     377-423: DAAVSSKATPSQSSSINDISSMSTEHTLASDTDSSLDASTGPLEGCR → AQMQQ
Isoform Beta-1 (identifier: Q9WTU6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     216-230: AEMVLHKVLFPGRDY → GELVKGCVIFQGTDH
     377-423: DAAVSSKATPSQSSSINDISSMSTEHTLASDTDSSLDASTGPLEGCR → AQMQQ
Isoform Beta-2 (identifier: Q9WTU6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     216-230: AEMVLHKVLFPGRDY → GELVKGCVIFQGTDH

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423Mitogen-activated protein kinase 9
PRO_0000186274

Regions

Domain26 – 321296Protein kinase
Nucleotide binding33 – 386ATP By similarity
Motif183 – 1853TXY

Sites

Active site1511Proton acceptor By similarity
Binding site551ATP By similarity

Amino acid modifications

Modified residue1831Phosphothreonine Ref.9
Modified residue1851Phosphotyrosine Ref.9 Ref.10
Modified residue4031Phosphothreonine By similarity

Natural variations

Alternative sequence216 – 23015AEMVL…PGRDY → GELVKGCVIFQGTDH in isoform Beta-1 and isoform Beta-2.
VSP_004836
Alternative sequence377 – 42347DAAVS…LEGCR → AQMQQ in isoform Alpha-1 and isoform Beta-1.
VSP_004837

Experimental info

Sequence conflict2231V → C Ref.3
Sequence conflict2371V → A in CAC88132. Ref.3
Sequence conflict3861P → A in BAC27623. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha-2 [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: 0E759B486ABCE20D

FASTA42348,189
        10         20         30         40         50         60 
MSDSKSDGQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP 

        70         80         90        100        110        120 
FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH 

       130        140        150        160        170        180 
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF 

       190        200        210        220        230        240 
MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMAEMVL HKVLFPGRDY IDQWNKVIEQ 

       250        260        270        280        290        300 
LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK 

       310        320        330        340        350        360 
MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV 

       370        380        390        400        410        420 
MDWEERSKNG VKDQPSDAAV SSKATPSQSS SINDISSMST EHTLASDTDS SLDASTGPLE 


GCR 

« Hide

Isoform Alpha-1.

Checksum: D426C50349A526A4
Show »

FASTA38144,078
Isoform Beta-1.

Checksum: FCCB3C77B7B19C9D
Show »

FASTA38143,906
Isoform Beta-2.

Checksum: EE549B9F4F12F421
Show »

FASTA42348,017

References

« Hide 'large scale' references
[1]"Differentiation of CD4+ T cells to Th1 cells requires MAP kinase JNK2."
Yang D.D., Conze D., Whitmarsh A.J., Barrett T., Davis R.J., Rincon M., Flavell R.A.
Immunity 9:575-585(1998) [PubMed: 9806643] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1 AND BETA-2), FUNCTION, INDUCTION.
[2]"JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a scaffold factor in the JNK signaling pathway."
Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N., Sugiyama K., Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.
Mol. Cell. Biol. 19:7539-7548(1999) [PubMed: 10523642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
Tissue: Brain.
[3]"Analysis of splicing of four mouse JNK/SAPKalpha variants."
Casanova E., Callejo A.I., Calvo P., Chinchetru M.A.
NeuroReport 11:305-309(2000) [PubMed: 10674476] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1 AND BETA-2), TISSUE SPECIFICITY.
Tissue: Liver.
[4]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
Strain: C57BL/6J.
Tissue: Medulla oblongata.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
Strain: FVB/N.
Tissue: Salivary gland.
[7]"JNK is required for effector T-cell function but not for T-cell activation."
Dong C., Yang D.D., Tournier C., Whitmarsh A.J., Xu J., Davis R.J., Flavell R.A.
Nature 405:91-94(2000) [PubMed: 10811224] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, INDUCTION.
Tissue: Embryonic stem cell and T-cell.
[8]"Requirement of the JIP1 scaffold protein for stress-induced JNK activation."
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.
Genes Dev. 15:2421-2432(2001) [PubMed: 11562351] [Abstract]
Cited for: SUBUNIT.
Tissue: Hippocampus.
[9]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY.
Tissue: Brain.
[10]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF052466 mRNA. Translation: AAD22576.1.
AF052467 mRNA. Translation: AAD22577.1.
AF052468 mRNA. Translation: AAD22578.1.
AF052469 mRNA. Translation: AAD22579.1.
AB005664 mRNA. Translation: BAA85876.1.
AJ315339 expand/collapse EMBL AC list , AJ315340, AJ315341, AJ315342, AJ315343, AJ315344, AJ315345, AJ315346, AJ315347, AJ315348, AJ315349, AJ315350 Genomic DNA. Translation: CAC88132.1. Sequence problems.
AK031959 mRNA. Translation: BAC27623.1.
AL606479 Genomic DNA. Translation: CAI23940.1.
AL606479 Genomic DNA. Translation: CAI23941.1.
BC028341 mRNA. Translation: AAH28341.1.
IPIIPI00123875.
IPI00223339.
IPI00223340.
IPI00223342.
RefSeqNP_001157143.1.
NP_001157144.1.
NP_058657.1.
NP_997575.2.
UniGeneMm.68933

3D structure databases

SMRQ9WTU6. Positions 7-362.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9WTU6. 4 interactions.
STRINGQ9WTU6.

PTM databases

PhosphoSiteQ9WTU6.

2-D gel databases

PMMA-2DPAGEQ9WTU6.

Proteomic databases

PRIDEQ9WTU6.

Genome annotation databases

EnsemblENSMUST00000020634; ENSMUSP00000020634; ENSMUSG00000020366; Mus musculus. [Genome view]
ENSMUST00000043321; ENSMUSP00000042744; ENSMUSG00000020366; Mus musculus. [Genome view]
ENSMUST00000109179; ENSMUSP00000104808; ENSMUSG00000020366; Mus musculus. [Genome view]
GeneID26420.
KEGGmmu:26420.
UCSCuc007irf.1. mouse.
uc007irg.1. mouse.
uc007irh.1. mouse.
uc007iri.1. mouse.

Organism-specific databases

CTD26420.
MGIMGI:1346862. Mapk9.

Phylogenomic databases

HOVERGENQ9WTU6.
OMANGVVKDQ.
PhylomeDBQ9WTU6.

Enzyme and pathway databases

BRENDA2.7.11.24. 244.

Gene expression databases

ArrayExpressQ9WTU6.
BgeeQ9WTU6.
CleanExMM_MAPK9.
GenevestigatorQ9WTU6.
GermOnlineENSMUSG00000020366. Mus musculus.

Family and domain databases

InterProIPR008351. JNK_MAPK.
IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_cat_dom.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01772. JNKMAPKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio304437.
SOURCESearch...

Entry information

Entry nameMK09_MOUSE
AccessionPrimary (citable) accession number: Q9WTU6
Secondary accession number(s): Q5NCK9 expand/collapse secondary AC list , Q5NCL5, Q8C097, Q8VDD2, Q9WTU4, Q9WTU5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: February 9, 2010
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents