Q9WTU6 (MK09_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.7 Ref.10 Ref.13
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. MAP2K4 shows a strong preference for Tyr-185 while MAP2K7 phosphorylates Tyr-183 preferentially. Inhibited by dual specificity phosphatases, such as DUSP1. Ref.7
Subunit structure	Interacts with MECOM. 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. Interacts with ATF7; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN. Interacts with BCL10. Interacts with CTNNB1 and GSK3B By similarity. Interacts with DCLK2. Ref.8 Ref.9
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
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 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to UV Inferred from electronic annotation. Source: Compara cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to interleukin-1 Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from electronic annotation. Source: Compara cellular response to tumor necrosis factor Inferred from electronic annotation. Source: Compara central nervous system development Inferred from electronic annotation. Source: Compara neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of apoptotic signaling pathway Inferred from genetic interaction PubMed 16458303. Source: MGI positive regulation of cell morphogenesis involved in differentiation Inferred from electronic annotation. Source: Compara positive regulation of chemokine production Inferred from electronic annotation. Source: Compara positive regulation of macrophage derived foam cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of nitric-oxide synthase biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of prostaglandin biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of prostaglandin secretion Inferred from electronic annotation. Source: Compara positive regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara protein targeting to mitochondrion Inferred from electronic annotation. Source: Compara regulation of JNK cascade Inferred from electronic annotation. Source: Compara regulation of protein ubiquitination Inferred from electronic annotation. Source: Compara release of cytochrome c from mitochondria Inferred from electronic annotation. Source: Compara response to amine stimulus Inferred from electronic annotation. Source: Compara response to cadmium ion Inferred from genetic interaction PubMed 16458303. Source: MGI response to drug Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to toxin Inferred from electronic annotation. Source: Compara
Cellular_component	cytosolic part Inferred from sequence or structural similarity PubMed 18385140. Source: MGI mitochondrion Inferred from direct assay PubMed 11884367. Source: MGI nucleus Inferred by curator Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW JUN kinase activity Inferred from sequence or structural similarity Ref.7. Source: UniProtKB cysteine-type endopeptidase activator activity involved in apoptotic process Inferred from electronic annotation. Source: Compara
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 423	423	Mitogen-activated protein kinase 9		PRO_0000186274
Regions
	Domain	26 – 321	296	Protein kinase
	Nucleotide binding	33 – 38	6	ATP By similarity
	Motif	183 – 185	3	TXY
Sites
	Active site	151	1	Proton acceptor By similarity
	Binding site	55	1	ATP By similarity
Amino acid modifications
	Modified residue	183	1	Phosphothreonine; by MAP2K7 Ref.11
	Modified residue	185	1	Phosphotyrosine; by MAP2K4 Ref.11 Ref.12
Natural variations
	Alternative sequence	216 – 230	15	AEMVL…PGRDY → GELVKGCVIFQGTDH in isoform Beta-1 and isoform Beta-2.		VSP_004836
	Alternative sequence	377 – 423	47	DAAVS…LEGCR → AQMQQ in isoform Alpha-1 and isoform Beta-1.		VSP_004837
Experimental info
	Sequence conflict	223	1	V → C Ref.3
	Sequence conflict	237	1	V → A in CAC88132. Ref.3
	Sequence conflict	386	1	P → A in BAC27623. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha-2 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: 0E759B486ABCE20D	FASTA	423	48,189
	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
	Isoform Alpha-1 [UniParc]. Checksum: D426C50349A526A4	FASTA	381	44,078
	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 MDWEERSKNG VKDQPSAQMQ Q
	Isoform Beta-1 [UniParc]. Checksum: FCCB3C77B7B19C9D	FASTA	381	43,906
	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 VGCIMGELVK GCVIFQGTDH 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 MDWEERSKNG VKDQPSAQMQ Q
	Isoform Beta-2 [UniParc]. Checksum: EE549B9F4F12F421	FASTA	423	48,017
	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 VGCIMGELVK GCVIFQGTDH 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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. , 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] [Europe PMC] [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. , 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: SUBUNIT. Tissue: Hippocampus.
[9]	"Common and divergent roles for members of the mouse DCX superfamily." 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. Cell Cycle 5:976-983(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DCLK2.
[10]	"JNK2 is a positive regulator of the cJun transcription factor." Jaeschke A., Karasarides M., Ventura J.J., Ehrhardt A., Zhang C., Flavell R.A., Shokat K.M., Davis R.J. Mol. Cell 23:899-911(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY. Tissue: Brain.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Activity of all JNK isoforms contributes to neurite growth in spiral ganglion neurons." Atkinson P.J., Cho C.H., Hansen M.R., Green S.H. Hear. Res. 278:77-85(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NEURITE GROWTH.
+	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 , 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.
IPI	IPI00123875. IPI00223339. IPI00223340. IPI00223342.
RefSeq	NP_001157143.1. NM_001163671.1. NP_001157144.1. NM_001163672.1. NP_058657.1. NM_016961.3. NP_997575.2. NM_207692.2.
UniGene	Mm.68933.
3D structure databases
ProteinModelPortal	Q9WTU6.
SMR	Q9WTU6. Positions 7-363.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9WTU6. 4 interactions.
MINT	MINT-1487632.
PTM databases
PhosphoSite	Q9WTU6.
Proteomic databases
PaxDb	Q9WTU6.
PRIDE	Q9WTU6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020634; ENSMUSP00000020634; ENSMUSG00000020366. ENSMUST00000043321; ENSMUSP00000042744; ENSMUSG00000020366. ENSMUST00000102778; ENSMUSP00000099839; ENSMUSG00000020366. ENSMUST00000109178; ENSMUSP00000104807; ENSMUSG00000020366. ENSMUST00000109179; ENSMUSP00000104808; ENSMUSG00000020366. ENSMUST00000164643; ENSMUSP00000132864; ENSMUSG00000020366. ENSMUST00000178543; ENSMUSP00000136977; ENSMUSG00000020366.
GeneID	26420.
KEGG	mmu:26420.
UCSC	uc007ird.2. mouse.
Organism-specific databases
CTD	5601.
MGI	MGI:1346862. Mapk9.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00550000074271.
HOVERGEN	HBG014652.
KO	K04440.
OMA	DWEERNK.
OrthoDB	EOG48SGT3.
Enzyme and pathway databases
BRENDA	2.7.11.24. 3474.
Gene expression databases
ArrayExpress	Q9WTU6.
Bgee	Q9WTU6.
CleanEx	MM_MAPK9.
Genevestigator	Q9WTU6.
GermOnline	ENSMUSG00000020366. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR003527. MAP_kinase_CS. IPR008351. MAPK_JNK. IPR000719. Prot_kinase_cat_dom. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR01772. JNKMAPKINASE.
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	304437.
SOURCE	Search...

Entry information

Entry name

MK09_MOUSE

Accession

Primary (citable) accession number: Q9WTU6
Secondary accession number(s): Q5NCK9 , Q5NCL5, Q8C097, Q8VDD2, Q9WTU4, Q9WTU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	February 21, 2001
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program