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Q9WTU6

- MK09_MOUSE

UniProt

Q9WTU6 - MK09_MOUSE

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Protein
Mitogen-activated protein kinase 9
Gene
Mapk9, Jnk2, Prkm9
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium By similarity.

Enzyme regulationi

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 DUSP1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551ATP By similarity
Active sitei151 – 1511Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 386ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. JUN kinase activity Source: UniProtKB
  3. cysteine-type endopeptidase activator activity involved in apoptotic process Source: Ensembl
  4. protein binding Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  1. JNK cascade Source: UniProtKB
  2. cellular response to UV Source: Ensembl
  3. cellular response to growth factor stimulus Source: Ensembl
  4. cellular response to interleukin-1 Source: Ensembl
  5. cellular response to lipopolysaccharide Source: Ensembl
  6. cellular response to tumor necrosis factor Source: Ensembl
  7. central nervous system development Source: Ensembl
  8. neuron projection development Source: Ensembl
  9. positive regulation of apoptotic process Source: Ensembl
  10. positive regulation of apoptotic signaling pathway Source: MGI
  11. positive regulation of cell morphogenesis involved in differentiation Source: Ensembl
  12. positive regulation of chemokine production Source: Ensembl
  13. positive regulation of macrophage derived foam cell differentiation Source: Ensembl
  14. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  15. positive regulation of nitric-oxide synthase biosynthetic process Source: Ensembl
  16. positive regulation of prostaglandin biosynthetic process Source: Ensembl
  17. positive regulation of prostaglandin secretion Source: Ensembl
  18. positive regulation of protein phosphorylation Source: Ensembl
  19. positive regulation of transcription, DNA-templated Source: Ensembl
  20. protein targeting to mitochondrion Source: Ensembl
  21. regulation of JNK cascade Source: Ensembl
  22. regulation of protein ubiquitination Source: Ensembl
  23. release of cytochrome c from mitochondria Source: Ensembl
  24. response to amine Source: Ensembl
  25. response to cadmium ion Source: MGI
  26. response to drug Source: Ensembl
  27. response to mechanical stimulus Source: Ensembl
  28. response to toxic substance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 3474.
ReactomeiREACT_188530. FCERI mediated MAPK activation.
REACT_188970. Oxidative Stress Induced Senescence.
REACT_204811. Activation of the AP-1 family of transcription factors.
REACT_204812. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 9 (EC:2.7.11.24)
Short name:
MAP kinase 9
Short name:
MAPK 9
Alternative name(s):
Stress-activated protein kinase JNK2
c-Jun N-terminal kinase 2
Gene namesi
Name:Mapk9
Synonyms:Jnk2, Prkm9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1346862. Mapk9.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: MGI
  2. mitochondrion Source: MGI
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423Mitogen-activated protein kinase 9
PRO_0000186274Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831Phosphothreonine; by MAP2K71 Publication
Modified residuei185 – 1851Phosphotyrosine; by MAP2K41 Publication

Post-translational modificationi

Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9WTU6.
PaxDbiQ9WTU6.
PRIDEiQ9WTU6.

PTM databases

PhosphoSiteiQ9WTU6.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

In T-cells, following T-cell receptor (TCR) activation. Levels peak 48 hours after TCR and CD-28 costimulation.2 Publications

Gene expression databases

ArrayExpressiQ9WTU6.
BgeeiQ9WTU6.
CleanExiMM_MAPK9.
GenevestigatoriQ9WTU6.

Interactioni

Subunit structurei

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 DCLK2.2 Publications

Protein-protein interaction databases

BioGridi204972. 3 interactions.
IntActiQ9WTU6. 4 interactions.
MINTiMINT-1487632.

Structurei

3D structure databases

ProteinModelPortaliQ9WTU6.
SMRiQ9WTU6. Positions 7-363.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 321296Protein kinase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi183 – 1853TXY

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074271.
HOVERGENiHBG014652.
KOiK04440.
OMAiSSMSTEH.
OrthoDBiEOG7PCJGV.
PhylomeDBiQ9WTU6.
TreeFamiTF105100.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01772. JNKMAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform Alpha-2 (identifier: Q9WTU6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSDSKSDGQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI    50
NVAVKKLSRP FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE 100
FQDVYLVMEL MDANLCQVIH MELDHERMSY LLYQMLCGIK HLHSAGIIHR 150
DLKPSNIVVK SDCTLKILDF GLARTACTNF MMTPYVVTRY YRAPEVILGM 200
GYKENVDIWS VGCIMAEMVL HKVLFPGRDY IDQWNKVIEQ LGTPSAEFMK 250
KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK 300
MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE 350
EWKELIYKEV MDWEERSKNG VKDQPSDAAV SSKATPSQSS SINDISSMST 400
EHTLASDTDS SLDASTGPLE GCR 423
Length:423
Mass (Da):48,189
Last modified:February 21, 2001 - v2
Checksum:i0E759B486ABCE20D
GO
Isoform Alpha-1 (identifier: Q9WTU6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     377-423: DAAVSSKATPSQSSSINDISSMSTEHTLASDTDSSLDASTGPLEGCR → AQMQQ

Show »
Length:381
Mass (Da):44,078
Checksum:iD426C50349A526A4
GO
Isoform Beta-1 (identifier: Q9WTU6-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     216-230: AEMVLHKVLFPGRDY → GELVKGCVIFQGTDH
     377-423: DAAVSSKATPSQSSSINDISSMSTEHTLASDTDSSLDASTGPLEGCR → AQMQQ

Show »
Length:381
Mass (Da):43,906
Checksum:iFCCB3C77B7B19C9D
GO
Isoform Beta-2 (identifier: Q9WTU6-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:423
Mass (Da):48,017
Checksum:iEE549B9F4F12F421
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei216 – 23015AEMVL…PGRDY → GELVKGCVIFQGTDH in isoform Beta-1 and isoform Beta-2.
VSP_004836Add
BLAST
Alternative sequencei377 – 42347DAAVS…LEGCR → AQMQQ in isoform Alpha-1 and isoform Beta-1.
VSP_004837Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2231V → C1 Publication
Sequence conflicti237 – 2371V → A in CAC88132. 1 Publication
Sequence conflicti386 – 3861P → A in BAC27623. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS24623.1. [Q9WTU6-4]
CCDS24624.1. [Q9WTU6-2]
CCDS48782.1. [Q9WTU6-1]
CCDS48783.1. [Q9WTU6-3]
RefSeqiNP_001157143.1. NM_001163671.1. [Q9WTU6-1]
NP_001157144.1. NM_001163672.1. [Q9WTU6-3]
NP_058657.1. NM_016961.3. [Q9WTU6-2]
NP_997575.2. NM_207692.2. [Q9WTU6-4]
UniGeneiMm.68933.

Genome annotation databases

EnsembliENSMUST00000020634; 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]
GeneIDi26420.
KEGGimmu:26420.
UCSCiuc007ird.2. mouse. [Q9WTU6-2]
uc007irh.2. mouse. [Q9WTU6-1]
uc007iri.2. mouse. [Q9WTU6-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS24623.1. [Q9WTU6-4 ]
CCDS24624.1. [Q9WTU6-2 ]
CCDS48782.1. [Q9WTU6-1 ]
CCDS48783.1. [Q9WTU6-3 ]
RefSeqi NP_001157143.1. NM_001163671.1. [Q9WTU6-1 ]
NP_001157144.1. NM_001163672.1. [Q9WTU6-3 ]
NP_058657.1. NM_016961.3. [Q9WTU6-2 ]
NP_997575.2. NM_207692.2. [Q9WTU6-4 ]
UniGenei Mm.68933.

3D structure databases

ProteinModelPortali Q9WTU6.
SMRi Q9WTU6. Positions 7-363.
ModBasei Search...

Protein-protein interaction databases

BioGridi 204972. 3 interactions.
IntActi Q9WTU6. 4 interactions.
MINTi MINT-1487632.

Chemistry

ChEMBLi CHEMBL3038501.

PTM databases

PhosphoSitei Q9WTU6.

Proteomic databases

MaxQBi Q9WTU6.
PaxDbi Q9WTU6.
PRIDEi Q9WTU6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020634 ; 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 ]
GeneIDi 26420.
KEGGi mmu:26420.
UCSCi uc007ird.2. mouse. [Q9WTU6-2 ]
uc007irh.2. mouse. [Q9WTU6-1 ]
uc007iri.2. mouse. [Q9WTU6-3 ]

Organism-specific databases

CTDi 5601.
MGIi MGI:1346862. Mapk9.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074271.
HOVERGENi HBG014652.
KOi K04440.
OMAi SSMSTEH.
OrthoDBi EOG7PCJGV.
PhylomeDBi Q9WTU6.
TreeFami TF105100.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 3474.
Reactomei REACT_188530. FCERI mediated MAPK activation.
REACT_188970. Oxidative Stress Induced Senescence.
REACT_204811. Activation of the AP-1 family of transcription factors.
REACT_204812. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.

Miscellaneous databases

NextBioi 304437.
PROi Q9WTU6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9WTU6.
Bgeei Q9WTU6.
CleanExi MM_MAPK9.
Genevestigatori Q9WTU6.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01772. JNKMAPKINASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiMK09_MOUSE
AccessioniPrimary (citable) accession number: Q9WTU6
Secondary accession number(s): Q5NCK9
, Q5NCL5, Q8C097, Q8VDD2, Q9WTU4, Q9WTU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: September 3, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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