Q9UBE8 (NLK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation Wnt signaling pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of Wnt receptor 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: Compara regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB serine phosphorylation of STAT3 protein Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype Ref.7. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-366978,EBI-366978
RCHY1	Q96PM5	5	EBI-366978,EBI-947779
SMAD4	Q13485	5	EBI-366978,EBI-347263

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 527	527	Serine/threonine-protein kinase NLK		PRO_0000186336
Regions
	Domain	138 – 427	290	Protein kinase
	Nucleotide binding	144 – 152	9	ATP By similarity
	Region	1 – 304	304	Required for interaction with TAB2 By similarity
	Region	1 – 125	125	Sufficient for interaction with DAPK3
	Region	124 – 416	293	Sufficient for interaction with DAPK3
	Region	428 – 527	100	Required for homodimerization and kinase activation and localization to the nucleus By similarity
	Region	434 – 527	94	Required for interaction with TAB2 By similarity
	Motif	298 – 300	3	TQE
	Compositional bias	22 – 25	4	Poly-Ala
	Compositional bias	27 – 34	8	Poly-His
	Compositional bias	42 – 48	7	Poly-His
	Compositional bias	71 – 83	13	Poly-Ala
	Compositional bias	106 – 111	6	Poly-Ala
	Compositional bias	115 – 119	5	Poly-Ala
Sites
	Active site	264	1	Proton acceptor By similarity
	Binding site	167	1	ATP Probable
Amino acid modifications
	Modified residue	298	1	Phosphothreonine; by autocatalysis Ref.13 Ref.14
	Modified residue	522	1	Phosphoserine Ref.13
Natural variations
	Natural variant	177	1	V → A. Corresponds to variant rs11871287 [ dbSNP | Ensembl ].		VAR_019549
	Natural variant	343	1	A → T in a glioblastoma multiforme sample; somatic mutation. Ref.19		VAR_042273
Experimental info
	Mutagenesis	167	1	K → N: Abrogates kinase activity. Ref.12 Ref.15
	Sequence conflict	25	1	A → T in AAH64663. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9UBE8 [UniParc]. Last modified November 3, 2009. Version 2. Checksum: CE6AEBA7D8133989	FASTA	527	58,283
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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.
+	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.
IPI	IPI00936281.
RefSeq	NP_057315.3. NM_016231.4.
UniGene	Hs.208759.
3D structure databases
ProteinModelPortal	Q9UBE8.
SMR	Q9UBE8. Positions 143-468.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UBE8. 9 interactions.
MINT	MINT-2873487.
STRING	9606.ENSP00000384625.
PTM databases
PhosphoSite	Q9UBE8.
Polymorphism databases
DMDM	262527551.
Proteomic databases
PaxDb	Q9UBE8.
PRIDE	Q9UBE8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000407008; ENSP00000384625; ENSG00000087095.
GeneID	51701.
KEGG	hsa:51701.
UCSC	uc010crj.3. human.
Organism-specific databases
CTD	51701.
GeneCards	GC17P026369.
HGNC	HGNC:29858. NLK.
HPA	HPA018192.
MIM	609476. gene.
neXtProt	NX_Q9UBE8.
PharmGKB	PA134914500.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233024.
HOVERGEN	HBG014652.
InParanoid	Q9UBE8.
KO	K04468.
OMA	CKCCYTT.
OrthoDB	EOG4QFWD8.
Enzyme and pathway databases
Pathway_Interaction_DB	wnt_canonical_pathway. Canonical Wnt signaling pathway. wnt_calcium_pathway. Noncanonical Wnt signaling pathway. ps1pathway. Presenilin action in Notch and Wnt signaling.
SignaLink	Q9UBE8.
Gene expression databases
ArrayExpress	Q9UBE8.
Bgee	Q9UBE8.
CleanEx	HS_NLK.
Genevestigator	Q9UBE8.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR003527. MAP_kinase_CS. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9UBE8.
ChEMBL	CHEMBL5364.
GenomeRNAi	51701.
NextBio	55724.
SOURCE	Search...

Entry information

Entry name

NLK_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.