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Q9UBE8

- NLK_HUMAN

UniProt

Q9UBE8 - NLK_HUMAN

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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

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 kinase activity Source: ProtInc
  5. protein serine/threonine kinase activity Source: Reactome
  6. SH2 domain binding Source: UniProtKB
  7. transcription factor binding Source: UniProtKB
  8. 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: Ensembl
  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_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
Complete GO annotation...

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

BgeeiQ9UBE8.
CleanExiHS_NLK.
ExpressionAtlasiQ9UBE8. baseline and differential.
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.
SMRiQ9UBE8. 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 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.
GeneTreeiENSGT00550000074298.
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.
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

        10         20         30         40         50
MSLCGARANA KMMAAYNGGT SAAAAGHHHH HHHHLPHLPP PHLHHHHHPQ
60 70 80 90 100
HHLHPGSAAA VHPVQQHTSS AAAAAAAAAA AAAMLNPGQQ QPYFPSPAPG
110 120 130 140 150
QAPGPAAAAP AQVQAAAAAT VKAHHHQHSH HPQQQLDIEP DRPIGYGAFG
160 170 180 190 200
VVWSVTDPRD GKRVALKKMP NVFQNLVSCK RVFRELKMLC FFKHDNVLSA
210 220 230 240 250
LDILQPPHID YFEEIYVVTE LMQSDLHKII VSPQPLSSDH VKVFLYQILR
260 270 280 290 300
GLKYLHSAGI LHRDIKPGNL LVNSNCVLKI CDFGLARVEE LDESRHMTQE
310 320 330 340 350
VVTQYYRAPE ILMGSRHYSN AIDIWSVGCI FAELLGRRIL FQAQSPIQQL
360 370 380 390 400
DLITDLLGTP SLEAMRTACE GAKAHILRGP HKQPSLPVLY TLSSQATHEA
410 420 430 440 450
VHLLCRMLVF DPSKRISAKD ALAHPYLDEG RLRYHTCMCK CCFSTSTGRV
460 470 480 490 500
YTSDFEPVTN PKFDDTFEKN LSSVRQVKEI IHQFILEQQK GNRVPLCINP
510 520
QSAAFKSFIS STVAQPSEMP PSPLVWE
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.
SMRi Q9UBE8. Positions 144-521.
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.
GeneTreei ENSGT00550000074298.
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

Bgeei Q9UBE8.
CleanExi HS_NLK.
ExpressionAtlasi Q9UBE8. baseline and differential.
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.
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. "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 29, 2014
This is version 136 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