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Q9WTU6 (MK09_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Protein existenceEvidence 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.12

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 componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from sequence or structural similarity Ref.7. Source: UniProtKB

cellular response to UV

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of chemokine production

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage derived foam cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of prostaglandin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of prostaglandin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein targeting to mitochondrion

Inferred from electronic annotation. Source: Ensembl

regulation of JNK cascade

Inferred from electronic annotation. Source: Ensembl

regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

response to amine

Inferred from electronic annotation. Source: Ensembl

response to cadmium ion

Inferred from genetic interaction PubMed 16458303. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from direct assay PubMed 11884367. Source: MGI

mitochondrion

Inferred from direct assay PubMed 11884367. Source: MGI

nucleus

Inferred by curator Ref.7. Source: UniProtKB

   Molecular_functionATP 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: Ensembl

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 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; by MAP2K7 Ref.11
Modified residue1851Phosphotyrosine; by MAP2K4 Ref.11

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 [UniParc].

Checksum: D426C50349A526A4
Show »

FASTA38144,078
Isoform Beta-1 [UniParc].

Checksum: FCCB3C77B7B19C9D
Show »

FASTA38143,906
Isoform Beta-2 [UniParc].

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] [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. 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] [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. 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] [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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[12]"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 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.
RefSeqNP_001157143.1. NM_001163671.1.
NP_001157144.1. NM_001163672.1.
NP_058657.1. NM_016961.3.
NP_997575.2. NM_207692.2.
UniGeneMm.68933.

3D structure databases

ProteinModelPortalQ9WTU6.
SMRQ9WTU6. Positions 7-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204972. 3 interactions.
IntActQ9WTU6. 4 interactions.
MINTMINT-1487632.

Chemistry

ChEMBLCHEMBL2034797.

PTM databases

PhosphoSiteQ9WTU6.

Proteomic databases

PaxDbQ9WTU6.
PRIDEQ9WTU6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020634; ENSMUSP00000020634; ENSMUSG00000020366. [Q9WTU6-4]
ENSMUST00000043321; ENSMUSP00000042744; ENSMUSG00000020366. [Q9WTU6-1]
ENSMUST00000102778; ENSMUSP00000099839; ENSMUSG00000020366. [Q9WTU6-2]
ENSMUST00000109178; ENSMUSP00000104807; ENSMUSG00000020366. [Q9WTU6-3]
ENSMUST00000109179; ENSMUSP00000104808; ENSMUSG00000020366. [Q9WTU6-2]
ENSMUST00000164643; ENSMUSP00000132864; ENSMUSG00000020366. [Q9WTU6-3]
ENSMUST00000178543; ENSMUSP00000136977; ENSMUSG00000020366. [Q9WTU6-1]
GeneID26420.
KEGGmmu:26420.
UCSCuc007ird.2. mouse. [Q9WTU6-2]
uc007irh.2. mouse. [Q9WTU6-1]
uc007iri.2. mouse. [Q9WTU6-3]

Organism-specific databases

CTD5601.
MGIMGI:1346862. Mapk9.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074271.
HOVERGENHBG014652.
KOK04440.
OMAWEERNKN.
OrthoDBEOG7PCJGV.
PhylomeDBQ9WTU6.
TreeFamTF105100.

Enzyme and pathway databases

BRENDA2.7.11.24. 3474.

Gene expression databases

ArrayExpressQ9WTU6.
BgeeQ9WTU6.
CleanExMM_MAPK9.
GenevestigatorQ9WTU6.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01772. JNKMAPKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304437.
PROQ9WTU6.
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: April 16, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

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