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Q9WTU6

- MK09_MOUSE

UniProt

Q9WTU6 - MK09_MOUSE

Protein

Mitogen-activated protein kinase 9

Gene

Mapk9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (21 Feb 2001)
      Previous versions | rss
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    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 – 551ATPPROSITE-ProRule annotation
    Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi33 – 386ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to growth factor stimulus Source: Ensembl
    2. cellular response to interleukin-1 Source: Ensembl
    3. cellular response to lipopolysaccharide Source: Ensembl
    4. cellular response to tumor necrosis factor Source: Ensembl
    5. cellular response to UV Source: Ensembl
    6. central nervous system development Source: Ensembl
    7. JNK cascade Source: UniProtKB
    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

    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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 423423Mitogen-activated protein kinase 9PRO_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.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.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi204972. 3 interactions.
    IntActiQ9WTU6. 5 interactions.
    MINTiMINT-1487632.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WTU6.
    SMRiQ9WTU6. Positions 7-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 321296Protein kinasePROSITE-ProRule annotationAdd
    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

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231V → C(PubMed:10674476)Curated
    Sequence conflicti237 – 2371V → A in CAC88132. (PubMed:10674476)Curated
    Sequence conflicti386 – 3861P → A in BAC27623. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei216 – 23015AEMVL…PGRDY → GELVKGCVIFQGTDH in isoform Beta-1 and isoform Beta-2. 3 PublicationsVSP_004836Add
    BLAST
    Alternative sequencei377 – 42347DAAVS…LEGCR → AQMQQ in isoform Alpha-1 and isoform Beta-1. 2 PublicationsVSP_004837Add
    BLAST

    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...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204972. 3 interactions.
    IntActi Q9WTU6. 5 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

    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: October 1, 2014
    This is version 148 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