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Q9UBE8 (NLK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase NLK

EC=2.7.11.24
Alternative name(s):
Nemo-like kinase
Protein LAK1
Gene names
Name:NLK
Synonyms:LAK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB O54949

Cofactor

Magnesium By similarity. UniProtKB O54949

Enzyme regulation

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. Ref.6 Ref.7

Subunit structure

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. Ref.8 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Note: Predominantly nuclear. A smaller fraction is cytoplasmic By similarity. Ref.10 Ref.12

Domain

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.

Post-translational modification

Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme. Ref.10

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-threonine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

serine phosphorylation of STAT3 protein

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype Ref.7. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

SH2 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Traceable author statement. Source: Reactome

transcription factor binding

Inferred from physical interaction Ref.11. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527Serine/threonine-protein kinase NLK
PRO_0000186336

Regions

Domain138 – 427290Protein kinase
Nucleotide binding144 – 1529ATP By similarity
Region1 – 304304Required for interaction with TAB2 By similarity
Region1 – 125125Sufficient for interaction with DAPK3
Region124 – 416293Sufficient for interaction with DAPK3
Region428 – 527100Required for homodimerization and kinase activation and localization to the nucleus By similarity
Region434 – 52794Required for interaction with TAB2 By similarity
Motif298 – 3003TQE
Compositional bias22 – 254Poly-Ala
Compositional bias27 – 348Poly-His
Compositional bias42 – 487Poly-His
Compositional bias71 – 8313Poly-Ala
Compositional bias106 – 1116Poly-Ala
Compositional bias115 – 1195Poly-Ala

Sites

Active site2641Proton acceptor By similarity
Binding site1671ATP Probable

Amino acid modifications

Modified residue2981Phosphothreonine; by autocatalysis Ref.13 Ref.14
Modified residue5221Phosphoserine Ref.13

Natural variations

Natural variant1771V → A.
Corresponds to variant rs11871287 [ dbSNP | Ensembl ].
VAR_019549
Natural variant3431A → T in a glioblastoma multiforme sample; somatic mutation. Ref.19
VAR_042273

Experimental info

Mutagenesis1671K → N: Abrogates kinase activity. Ref.12 Ref.15
Sequence conflict251A → T in AAH64663. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9UBE8 [UniParc].

Last modified November 3, 2009. Version 2.
Checksum: CE6AEBA7D8133989

FASTA52758,283
        10         20         30         40         50         60 
MSLCGARANA KMMAAYNGGT SAAAAGHHHH HHHHLPHLPP PHLHHHHHPQ HHLHPGSAAA 

        70         80         90        100        110        120 
VHPVQQHTSS AAAAAAAAAA AAAMLNPGQQ QPYFPSPAPG QAPGPAAAAP AQVQAAAAAT 

       130        140        150        160        170        180 
VKAHHHQHSH HPQQQLDIEP DRPIGYGAFG VVWSVTDPRD GKRVALKKMP NVFQNLVSCK 

       190        200        210        220        230        240 
RVFRELKMLC FFKHDNVLSA LDILQPPHID YFEEIYVVTE LMQSDLHKII VSPQPLSSDH 

       250        260        270        280        290        300 
VKVFLYQILR GLKYLHSAGI LHRDIKPGNL LVNSNCVLKI CDFGLARVEE LDESRHMTQE 

       310        320        330        340        350        360 
VVTQYYRAPE ILMGSRHYSN AIDIWSVGCI FAELLGRRIL FQAQSPIQQL DLITDLLGTP 

       370        380        390        400        410        420 
SLEAMRTACE GAKAHILRGP HKQPSLPVLY TLSSQATHEA VHLLCRMLVF DPSKRISAKD 

       430        440        450        460        470        480 
ALAHPYLDEG RLRYHTCMCK CCFSTSTGRV YTSDFEPVTN PKFDDTFEKN LSSVRQVKEI 

       490        500        510        520 
IHQFILEQQK GNRVPLCINP QSAAFKSFIS STVAQPSEMP PSPLVWE 

« Hide

References

« Hide 'large scale' references
[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: Placenta.
[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. expand/collapse author list , 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]"Wnt activates the Tak1/Nemo-like kinase pathway."
Smit L., Baas A., Kuipers J., Korswagen H., van de Wetering M., Clevers H.
J. Biol. Chem. 279:17232-17240(2004) [PubMed] [Europe PMC] [Abstract]
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]"A histone lysine methyltransferase activated by non-canonical Wnt signalling suppresses PPAR-gamma transactivation."
Takada I., Mihara M., Suzawa M., Ohtake F., Kobayashi S., Igarashi M., Youn M.Y., Takeyama K., Nakamura T., Mezaki Y., Takezawa S., Yogiashi Y., Kitagawa H., Yamada G., Takada S., Minami Y., Shibuya H., Matsumoto K., Kato S.
Nat. Cell Biol. 9:1273-1285(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH CHD7; PPARG AND SETDB1, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-167.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_057315.3. NM_016231.4.
UniGeneHs.208759.

3D structure databases

ProteinModelPortalQ9UBE8.
SMRQ9UBE8. Positions 135-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119685. 50 interactions.
IntActQ9UBE8. 33 interactions.
MINTMINT-2873487.
STRING9606.ENSP00000384625.

Chemistry

BindingDBQ9UBE8.
ChEMBLCHEMBL5364.
GuidetoPHARMACOLOGY2125.

PTM databases

PhosphoSiteQ9UBE8.

Polymorphism databases

DMDM262527551.

Proteomic databases

PaxDbQ9UBE8.
PRIDEQ9UBE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000407008; ENSP00000384625; ENSG00000087095.
GeneID51701.
KEGGhsa:51701.
UCSCuc010crj.3. human.

Organism-specific databases

CTD51701.
GeneCardsGC17P026369.
HGNCHGNC:29858. NLK.
HPAHPA018192.
HPA056511.
MIM609476. gene.
neXtProtNX_Q9UBE8.
PharmGKBPA134914500.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidQ9UBE8.
KOK04468.
OMACKCCYTT.
OrthoDBEOG72RMZ3.
PhylomeDBQ9UBE8.
TreeFamTF315210.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ9UBE8.

Gene expression databases

ArrayExpressQ9UBE8.
BgeeQ9UBE8.
CleanExHS_NLK.
GenevestigatorQ9UBE8.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNLK.
GenomeRNAi51701.
NextBio55724.
PROQ9UBE8.
SOURCESearch...

Entry information

Entry nameNLK_HUMAN
AccessionPrimary (citable) accession number: Q9UBE8
Secondary accession number(s): B2RCX1, Q2PNI9, Q6P2A3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 3, 2009
Last modified: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM