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O54949

- NLK_MOUSE

UniProt

O54949 - NLK_MOUSE

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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

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.2 Publications

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 – 1671ATP Inferred
Active sitei264 – 2641Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi144 – 1529ATP By similarity

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
Complete GO annotation...

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:Nlk
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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB
Complete GO annotation...

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 – 5221Phosphoserine By similarity

Post-translational modificationi

Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme.4 Publications

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.11 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini138 – 427290Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 304304Required for interaction with TAB2Add
BLAST
Regioni1 – 125125Sufficient for interaction with DAPK3 By similarityAdd
BLAST
Regioni124 – 416293Sufficient for interaction with DAPK3 By 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

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

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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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691S → P in AAC24499. 1 Publication

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

« Hide 'large scale' publications
  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/c.
    Tissue: Brain.
  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: September 3, 2014
This is version 123 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

Similar proteinsi