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O54949

- NLK_MOUSE

UniProt

O54949 - NLK_MOUSE

Protein

Serine/threonine-protein kinase NLK

Gene

Nlk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (03 Nov 2009)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Activation of this pathway causes binding to and phosphorylation of the histone methyltransferase SETDB1. The NLK-SETDB1 complex subsequently interacts with PPARG, leading to methylation of PPARG target promoters at histone H3K9 and transcriptional silencing. The resulting loss of PPARG target gene transcription inhibits adipogenesis and promotes osteoblastogenesis in mesenchymal stem cells (MSCs). Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1.16 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.2 Publications

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by the non-canonical Wnt signaling pathway, in which WNT5A leads to activation of MAP3K7/TAK1 and HIPK2, which subsequently phosphorylates and activates this protein. Activated by dimerization and subsequent intermolecular autophosphorylation on Thr-298. Other cytokines such as IL6 may also activate this regulatory circuit.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei167 – 1671ATPCurated
    Active sitei264 – 2641Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi144 – 1529ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. MAP kinase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: MGI
    6. protein serine/threonine kinase activity Source: UniProtKB
    7. SH2 domain binding Source: UniProtKB
    8. transcription factor binding Source: UniProtKB
    9. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. intracellular signal transduction Source: UniProtKB
    2. MAPK cascade Source: GOC
    3. negative regulation of Wnt signaling pathway Source: UniProtKB
    4. peptidyl-threonine phosphorylation Source: UniProtKB
    5. protein autophosphorylation Source: MGI
    6. protein phosphorylation Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB
    8. serine phosphorylation of STAT3 protein Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW
    10. transforming growth factor beta receptor signaling pathway Source: UniProtKB
    11. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation, Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_221970. Ca2+ pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase NLK (EC:2.7.11.24)
    Alternative name(s):
    Nemo-like kinase
    Gene namesi
    Name:NlkImported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1201387. Nlk.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Predominantly nuclear. A smaller fraction is cytoplasmic.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi167 – 1671K → M: Abrogates kinase activity and autophosphorylation. Retains ability to homodimerize. Abrogates ability to induce ubiquitination and degradation of LEF1 and repress canonical Wnt/beta-catenin signaling. Abrogates ability to induce MYB degradation, and reduces ability to repress MYBL1 and MYBL2. 8 Publications
    Mutagenesisi298 – 2981T → D or E: Abrogates autophosphorylation. 3 Publications
    Mutagenesisi298 – 2981T → V: Abrogates autophosphorylation. Retains ability to homodimerize. Abrogates ability to induce MYB degradation. 3 Publications
    Mutagenesisi437 – 4371C → S: Retains kinase activity. 2 Publications
    Mutagenesisi437 – 4371C → Y: Abrogates homodimerization and intermolecular autophosphorylation, with consequent loss of kinase activity. Loss of nuclear localization. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 527527Serine/threonine-protein kinase NLKPRO_0000186337Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei298 – 2981Phosphothreonine; by autocatalysis1 Publication
    Modified residuei522 – 5221PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO54949.
    PRIDEiO54949.

    PTM databases

    PhosphoSiteiO54949.

    Expressioni

    Tissue specificityi

    Expressed at high levels in the brain, and at lower levels in heart, kidney, lung and liver.1 Publication

    Gene expression databases

    ArrayExpressiO54949.
    BgeeiO54949.
    CleanExiMM_NLK.
    GenevestigatoriO54949.

    Interactioni

    Subunit structurei

    Interacts with RNF138/NARF By similarity. Forms a complex with CHD7, PPARG and SETDB1 in response to WNT5A signaling By similarity. Interacts with DAPK3/ZIPK, and this interaction may disrupt interaction with transcription factors such as TCF7L2/TCF4 By similarity. Interacts with FOXO1 and FOXO3 By similarity. Homodimer. Homodimerization is required for intermolecular autophosphorylation, kinase activation and nuclear localization. Interacts with the upstream activating kinases HIPK2 and MAP3K7/TAK1. Interaction with MAP3K7/TAK1 seems to be indirect, and may be mediated by other proteins such as STAT3, TAB1 and TAB2. Interacts with and phosphorylates a number of transcription factors including FOXO4, LEF1, MYB, MYBL1, MYBL2, NOTCH1 and TCF7L2/TCF4. May interact with components of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes. Interacts with MEF2A.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hipk2Q9QZR52EBI-366894,EBI-366905

    Protein-protein interaction databases

    IntActiO54949. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliO54949.
    SMRiO54949. Positions 144-521.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini138 – 427290Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 304304Required for interaction with TAB2Add
    BLAST
    Regioni1 – 125125Sufficient for interaction with DAPK3By similarityAdd
    BLAST
    Regioni124 – 416293Sufficient for interaction with DAPK3By similarityAdd
    BLAST
    Regioni428 – 527100Required for homodimerization and kinase activation and localization to the nucleusAdd
    BLAST
    Regioni434 – 52794Required for interaction with TAB2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi298 – 3003TQE

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi22 – 254Poly-Ala
    Compositional biasi27 – 348Poly-His
    Compositional biasi42 – 487Poly-His
    Compositional biasi71 – 8313Poly-AlaAdd
    BLAST
    Compositional biasi106 – 1116Poly-Ala
    Compositional biasi115 – 1195Poly-Ala

    Domaini

    Contains a TQE activation loop motif in which autophosphorylation of the threonine residue (Thr-298) is sufficient for kinase activation. This mode of activation contrasts with that of classical MAP kinases, which contain a TXY activation loop motif in which phosphorylation of both the threonine and tyrosine residues is required for kinase activation.

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110881.
    HOGENOMiHOG000233024.
    HOVERGENiHBG014652.
    InParanoidiQ5SYE6.
    KOiK04468.
    OMAiCKCCYTT.
    OrthoDBiEOG72RMZ3.
    PhylomeDBiO54949.
    TreeFamiTF315210.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O54949-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLCGTRANA KMMAAYNGGT SAAAAGHHHH HHHHLPHLPP PHLHHHHHPQ    50
    HHLHPGSAAA VHPVQQHTSS AAAAAAAAAA AAAMLNPGQQ QPYFPSPAPG 100
    QAPGPAAAAP AQVQAAAAAT VKAHHHQHSH HPQQQLDIEP DRPIGYGAFG 150
    VVWSVTDPRD GKRVALKKMP NVFQNLVSCK RVFRELKMLC FFKHDNVLSA 200
    LDILQPPHID YFEEIYVVTE LMQSDLHKII VSPQPLSSDH VKVFLYQILR 250
    GLKYLHSAGI LHRDIKPGNL LVNSNCVLKI CDFGLARVEE LDESRHMTQE 300
    VVTQYYRAPE ILMGSRHYSN AIDIWSVGCI FAELLGRRIL FQAQSPIQQL 350
    DLITDLLGTP SLEAMRTACE GAKAHILRGP HKQPSLPVLY TLSSQATHEA 400
    VHLLCRMLVF DPSKRISAKD ALAHPYLDEG RLRYHTCMCK CCFSTSTGRV 450
    YTSDFEPVTN PKFDDTFEKN LSSVRQVKEI IHQFILEQQK GNRVPLCINP 500
    QSAAFKSFIS STVAQPSEMP PSPLVWE 527
    Length:527
    Mass (Da):58,313
    Last modified:November 3, 2009 - v2
    Checksum:iCE6D5DCCB9133989
    GO

    Sequence cautioni

    The sequence AAC24499.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691S → P in AAC24499. (PubMed:9448268)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036332 mRNA. Translation: AAC24499.1. Different initiation.
    AL591177, AL591376 Genomic DNA. Translation: CAI25549.2.
    AL591376, AL591177 Genomic DNA. Translation: CAI25603.2.
    BC057667 mRNA. Translation: AAH57667.2.
    BC058652 mRNA. Translation: AAH58652.2.
    CCDSiCCDS25113.2.
    RefSeqiNP_032728.3. NM_008702.3.
    UniGeneiMm.9001.

    Genome annotation databases

    EnsembliENSMUST00000142739; ENSMUSP00000119345; ENSMUSG00000017376.
    GeneIDi18099.
    KEGGimmu:18099.
    UCSCiuc007kjw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036332 mRNA. Translation: AAC24499.1 . Different initiation.
    AL591177 , AL591376 Genomic DNA. Translation: CAI25549.2 .
    AL591376 , AL591177 Genomic DNA. Translation: CAI25603.2 .
    BC057667 mRNA. Translation: AAH57667.2 .
    BC058652 mRNA. Translation: AAH58652.2 .
    CCDSi CCDS25113.2.
    RefSeqi NP_032728.3. NM_008702.3.
    UniGenei Mm.9001.

    3D structure databases

    ProteinModelPortali O54949.
    SMRi O54949. Positions 144-521.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O54949. 2 interactions.

    PTM databases

    PhosphoSitei O54949.

    Proteomic databases

    PaxDbi O54949.
    PRIDEi O54949.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000142739 ; ENSMUSP00000119345 ; ENSMUSG00000017376 .
    GeneIDi 18099.
    KEGGi mmu:18099.
    UCSCi uc007kjw.1. mouse.

    Organism-specific databases

    CTDi 51701.
    MGIi MGI:1201387. Nlk.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110881.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    InParanoidi Q5SYE6.
    KOi K04468.
    OMAi CKCCYTT.
    OrthoDBi EOG72RMZ3.
    PhylomeDBi O54949.
    TreeFami TF315210.

    Enzyme and pathway databases

    Reactomei REACT_221970. Ca2+ pathway.

    Miscellaneous databases

    ChiTaRSi NLK. mouse.
    NextBioi 293259.
    PROi O54949.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O54949.
    Bgeei O54949.
    CleanExi MM_NLK.
    Genevestigatori O54949.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nlk is a murine protein kinase related to Erk/MAP kinases and localized in the nucleus."
      Brott B.K., Pinsky B.A., Erikson R.L.
      Proc. Natl. Acad. Sci. U.S.A. 95:963-968(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-167 AND THR-298.
      Strain: BALB/cImported.
      Tissue: BrainImported.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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].
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain and Kidney.
    4. "The TAK1-NLK-MAPK-related pathway antagonizes signalling between beta-catenin and transcription factor TCF."
      Ishitani T., Ninomiya-Tsuji J., Nagai S., Nishita M., Meneghini M., Barker N., Waterman M., Bowerman B., Clevers H., Shibuya H., Matsumoto K.
      Nature 399:798-802(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, ENZYME REGULATION, MUTAGENESIS OF LYS-167 AND CYS-437.
    5. "Abnormal bone marrow stroma in mice deficient for nemo-like kinase, Nlk."
      Kortenjann M., Nehls M., Smith A.J., Carsetti R., Schuler J., Kohler G., Boehm T.
      Eur. J. Immunol. 31:3580-3587(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The TAK1-NLK mitogen-activated protein kinase cascade functions in the Wnt-5a/Ca(2+) pathway to antagonize Wnt/beta-catenin signaling."
      Ishitani T., Kishida S., Hyodo-Miura J., Ueno N., Yasuda J., Waterman M., Shibuya H., Moon R.T., Ninomiya-Tsuji J., Matsumoto K.
      Mol. Cell. Biol. 23:131-139(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    7. "Regulation of lymphoid enhancer factor 1/T-cell factor by mitogen-activated protein kinase-related Nemo-like kinase-dependent phosphorylation in Wnt/beta-catenin signaling."
      Ishitani T., Ninomiya-Tsuji J., Matsumoto K.
      Mol. Cell. Biol. 23:1379-1389(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LEF1 AND TCF7L2, MUTAGENESIS OF LYS-167.
    8. "Nemo-like kinase suppresses a wide range of transcription factors, including nuclear factor-kappaB."
      Yasuda J., Yokoo H., Yamada T., Kitabayashi I., Sekiya T., Ichikawa H.
      Cancer Sci. 95:52-57(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Role of the TAK1-NLK-STAT3 pathway in TGF-beta-mediated mesoderm induction."
      Ohkawara B., Shirakabe K., Hyodo-Miura J., Matsuo R., Ueno N., Matsumoto K., Shibuya H.
      Genes Dev. 18:381-386(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH STAT3.
    10. "Wnt-1 signal induces phosphorylation and degradation of c-Myb protein via TAK1, HIPK2, and NLK."
      Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T., Ishitani T., Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E., Kim Y., Matsumoto K., Ishii S.
      Genes Dev. 18:816-829(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYB AND HIPK2, MUTAGENESIS OF LYS-167 AND THR-298.
    11. "Differential sensitivity of v-Myb and c-Myb to Wnt-1-induced protein degradation."
      Kanei-Ishii C., Nomura T., Tanikawa J., Ichikawa-Iwata E., Ishii S.
      J. Biol. Chem. 279:44582-44589(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYB.
    12. "The Wnt-NLK signaling pathway inhibits A-Myb activity by inhibiting the association with coactivator CBP and methylating histone H3."
      Kurahashi T., Nomura T., Kanei-Ishii C., Shinkai Y., Ishii S.
      Mol. Biol. Cell 16:4705-4713(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH MYBL1 AND MYBL2, MUTAGENESIS OF LYS-167.
    13. "Nemo-like kinase-myocyte enhancer factor 2A signaling regulates anterior formation in Xenopus development."
      Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T., Shibuya H.
      Mol. Cell. Biol. 27:7623-7630(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MEF2A.
    14. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    15. "Fbxw7 acts as an E3 ubiquitin ligase that targets c-Myb for nemo-like kinase (NLK)-induced degradation."
      Kanei-Ishii C., Nomura T., Takagi T., Watanabe N., Nakayama K.I., Ishii S.
      J. Biol. Chem. 283:30540-30548(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH E3 UBIQUITIN-PROTEIN LIGASE COMPLEXES.
    16. "TAB2 scaffolds TAK1 and NLK in repressing canonical Wnt signaling."
      Li M., Wang H., Huang T., Wang J., Ding Y., Li Z., Zhang J., Li L.
      J. Biol. Chem. 285:13397-13404(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH MAP3K7 AND TAB2, MUTAGENESIS OF LYS-167.
    17. "Nemo-like kinase suppresses Notch signalling by interfering with formation of the Notch active transcriptional complex."
      Ishitani T., Hirao T., Suzuki M., Isoda M., Ishitani S., Harigaya K., Kitagawa M., Matsumoto K., Itoh M.
      Nat. Cell Biol. 12:278-285(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NOTCH1, MUTAGENESIS OF LYS-167.
    18. "Oxidative stress-dependent regulation of Forkhead box O4 activity by nemo-like kinase."
      Szypowska A.A., de Ruiter H., Meijer L.A.T., Smits L.M.M., Burgering B.M.T.
      Antioxid. Redox Signal. 14:563-578(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FOXO4.
    19. "Homodimerization of Nemo-like kinase is essential for activation and nuclear localization."
      Ishitani S., Inaba K., Matsumoto K., Ishitani T.
      Mol. Biol. Cell 22:266-277(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, ENZYME REGULATION, HOMODIMERIZATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-298, MUTAGENESIS OF LYS-167; THR-298 AND CYS-437.

    Entry informationi

    Entry nameiNLK_MOUSE
    AccessioniPrimary (citable) accession number: O54949
    Secondary accession number(s): Q5SYE6, Q6PF98
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: November 3, 2009
    Last modified: October 1, 2014
    This is version 124 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