Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UBE8

- NLK_HUMAN

UniProt

Q9UBE8 - NLK_HUMAN

Protein

Serine/threonine-protein kinase NLK

Gene

NLK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (03 Nov 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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/TAK1.9 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by dimerization and subsequent intermolecular autophosphorylation on Thr-298 By similarity. Activated by the non-canonical Wnt signaling pathway, in which WNT5A treatment leads to activation of MAP3K7/TAK1 and HIPK2, which subsequently phosphorylates and activates this protein. Other cytokines such as IL6 may also activate this regulatory circuit.By similarity2 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: IntAct
    5. protein kinase activity Source: ProtInc
    6. protein serine/threonine kinase activity Source: Reactome
    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. negative regulation of Wnt signaling pathway Source: UniProtKB
    3. peptidyl-threonine phosphorylation Source: UniProtKB
    4. protein autophosphorylation Source: Ensembl
    5. protein phosphorylation Source: UniProtKB
    6. regulation of transcription, DNA-templated Source: UniProtKB
    7. serine phosphorylation of STAT3 protein Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW
    9. transforming growth factor beta receptor signaling pathway Source: UniProtKB
    10. 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_172761. Ca2+ pathway.
    SignaLinkiQ9UBE8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase NLK (EC:2.7.11.24)
    Alternative name(s):
    Nemo-like kinase
    Protein LAK1
    Gene namesi
    Name:NLK
    Synonyms:LAK1Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:29858. NLK.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi167 – 1671K → N: Abrogates kinase activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA134914500.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 527527Serine/threonine-protein kinase NLKPRO_0000186336Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei298 – 2981Phosphothreonine; by autocatalysis2 Publications
    Modified residuei522 – 5221Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9UBE8.
    PRIDEiQ9UBE8.

    PTM databases

    PhosphoSiteiQ9UBE8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UBE8.
    BgeeiQ9UBE8.
    CleanExiHS_NLK.
    GenevestigatoriQ9UBE8.

    Organism-specific databases

    HPAiHPA018192.
    HPA056511.

    Interactioni

    Subunit structurei

    Homodimer. Homodimerization is required for intermolecular autophosphorylation, kinase activation and nuclear localization By similarity. May interact with components of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes By similarity. Interacts with LEF1, MEF2A, MYBL1 and MYBL2 By similarity. 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 FOXO1, FOXO3, FOXO4, MYB, NOTCH1 and TCF7L2/TCF4. Interacts with DAPK3/ZIPK, and this interaction may disrupt interaction with transcription factors such as TCF7L2/TCF4. Forms a transcriptional repressor complex with CHD7, PPARG and SETDB1. Interacts with RNF138/NARF.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAP3K7O433183EBI-366978,EBI-358684
    RCHY1Q96PM55EBI-366978,EBI-947779
    SMAD4Q134856EBI-366978,EBI-347263
    TFDP1Q141862EBI-366978,EBI-749713

    Protein-protein interaction databases

    BioGridi119685. 53 interactions.
    IntActiQ9UBE8. 33 interactions.
    MINTiMINT-2873487.
    STRINGi9606.ENSP00000384625.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UBE8.
    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 TAB2By similarityAdd
    BLAST
    Regioni1 – 125125Sufficient for interaction with DAPK3Add
    BLAST
    Regioni124 – 416293Sufficient for interaction with DAPK3Add
    BLAST
    Regioni428 – 527100Required for homodimerization and kinase activation and localization to the nucleusBy similarityAdd
    BLAST
    Regioni434 – 52794Required for interaction with TAB2By similarityAdd
    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.
    HOGENOMiHOG000233024.
    HOVERGENiHBG014652.
    InParanoidiQ9UBE8.
    KOiK04468.
    OMAiCKCCYTT.
    OrthoDBiEOG72RMZ3.
    PhylomeDBiQ9UBE8.
    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.

    Q9UBE8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLCGARANA 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):58,283
    Last modified:November 3, 2009 - v2
    Checksum:iCE6AEBA7D8133989
    GO

    Sequence cautioni

    The sequence AAD56013.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAF04857.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence ABC40748.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAG37718.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251A → T in AAH64663. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti177 – 1771V → A.
    Corresponds to variant rs11871287 [ dbSNP | Ensembl ].
    VAR_019549
    Natural varianti343 – 3431A → T in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_042273

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197898 mRNA. Translation: AAF04857.1. Different initiation.
    AF180819 mRNA. Translation: AAD56013.1. Different initiation.
    AK315315 mRNA. Translation: BAG37718.1. Different initiation.
    DQ316259 Genomic DNA. Translation: ABC40748.1. Different initiation.
    BC064663 mRNA. Translation: AAH64663.2.
    CCDSiCCDS11224.2.
    RefSeqiNP_057315.3. NM_016231.4.
    UniGeneiHs.208759.

    Genome annotation databases

    EnsembliENST00000407008; ENSP00000384625; ENSG00000087095.
    GeneIDi51701.
    KEGGihsa:51701.
    UCSCiuc010crj.3. human.

    Polymorphism databases

    DMDMi262527551.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197898 mRNA. Translation: AAF04857.1 . Different initiation.
    AF180819 mRNA. Translation: AAD56013.1 . Different initiation.
    AK315315 mRNA. Translation: BAG37718.1 . Different initiation.
    DQ316259 Genomic DNA. Translation: ABC40748.1 . Different initiation.
    BC064663 mRNA. Translation: AAH64663.2 .
    CCDSi CCDS11224.2.
    RefSeqi NP_057315.3. NM_016231.4.
    UniGenei Hs.208759.

    3D structure databases

    ProteinModelPortali Q9UBE8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119685. 53 interactions.
    IntActi Q9UBE8. 33 interactions.
    MINTi MINT-2873487.
    STRINGi 9606.ENSP00000384625.

    Chemistry

    BindingDBi Q9UBE8.
    ChEMBLi CHEMBL5364.
    GuidetoPHARMACOLOGYi 2125.

    PTM databases

    PhosphoSitei Q9UBE8.

    Polymorphism databases

    DMDMi 262527551.

    Proteomic databases

    PaxDbi Q9UBE8.
    PRIDEi Q9UBE8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000407008 ; ENSP00000384625 ; ENSG00000087095 .
    GeneIDi 51701.
    KEGGi hsa:51701.
    UCSCi uc010crj.3. human.

    Organism-specific databases

    CTDi 51701.
    GeneCardsi GC17P026369.
    HGNCi HGNC:29858. NLK.
    HPAi HPA018192.
    HPA056511.
    MIMi 609476. gene.
    neXtProti NX_Q9UBE8.
    PharmGKBi PA134914500.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    InParanoidi Q9UBE8.
    KOi K04468.
    OMAi CKCCYTT.
    OrthoDBi EOG72RMZ3.
    PhylomeDBi Q9UBE8.
    TreeFami TF315210.

    Enzyme and pathway databases

    Reactomei REACT_172761. Ca2+ pathway.
    SignaLinki Q9UBE8.

    Miscellaneous databases

    GeneWikii NLK.
    GenomeRNAii 51701.
    NextBioi 55724.
    PROi Q9UBE8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBE8.
    Bgeei Q9UBE8.
    CleanExi HS_NLK.
    Genevestigatori Q9UBE8.

    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. "Characterization of the Fugu rubripes NLK and FN5 genes flanking the NF1 (Neurofibromatosis type 1) gene in the 5' direction and mapping of the human counterparts."
      Kehrer-Sawatzki H., Moschgath E., Maier C., Legius E., Elgar G., Krone W.
      Gene 251:63-71(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta1 Publication.
    2. "Cloning of human LAK1 cDNA."
      Wang C., Lo H.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: T-cell.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Amygdala.
    4. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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].
      Tissue: Uterus.
    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. "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, ENZYME REGULATION.
    8. "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: INTERACTION WITH MYB AND HIPK2.
    9. Cited for: FUNCTION.
    10. "STAT3 regulates Nemo-like kinase by mediating its interaction with IL-6-stimulated TGFbeta-activated kinase 1 for STAT3 Ser-727 phosphorylation."
      Kojima H., Sasaki T., Ishitani T., Iemura S., Zhao H., Kaneko S., Kunimoto H., Natsume T., Matsumoto K., Nakajima K.
      Proc. Natl. Acad. Sci. U.S.A. 102:4524-4529(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH MAP3K7 AND STAT3, SUBCELLULAR LOCATION.
    11. "NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF)."
      Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K., Hyodo-Miura J., Kawachi K., Natsume T., Shibuya H.
      J. Biol. Chem. 281:20749-20760(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF138 AND TCF7L2.
    12. Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH CHD7; PPARG AND SETDB1, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-167.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-298 AND SER-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Regulation of FOXO1 by TAK1-Nemo-like kinase pathway."
      Kim S., Kim Y., Lee J., Chung J.
      J. Biol. Chem. 285:8122-8129(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FOXO1, MUTAGENESIS OF LYS-167.
    16. "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.
    17. "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 FOXO1; FOXO3 AND FOXO4.
    18. "Zipper-interacting protein kinase (ZIPK) modulates canonical Wnt/beta-catenin signaling through interaction with Nemo-like kinase and T-cell factor 4 (NLK/TCF4)."
      Togi S., Ikeda O., Kamitani S., Nakasuji M., Sekine Y., Muromoto R., Nanbo A., Oritani K., Kawai T., Akira S., Matsuda T.
      J. Biol. Chem. 286:19170-19177(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DAPK3 AND TCF7L2.
    19. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-343.

    Entry informationi

    Entry nameiNLK_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBE8
    Secondary accession number(s): B2RCX1, Q2PNI9, Q6P2A3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: November 3, 2009
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3