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Q8QGV6 (NLK2_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase NLK2

EC=2.7.11.24
Alternative name(s):
Nemo-like kinase 2
Short name=Nlk.2
Short name=xNLK
Gene names
Name:nlk.2
Synonyms:nlk
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Negatively regulates Wnt/beta-catenin-signaling during development. Plays a role together with sox11 in neural induction during early embryogenesis. Involved in TGFbeta-mediated mesoderm induction in early embryos, acting downstream of map3k7/tak1 to phosphorylate stat3.1. Augments the rnf138/narf-directed ubiquitination and degradation of tcf/lef by enhancing the association of rnf138/narf and tcf/lef. Phosphorylates mef2a to play a role in anterior neural development, including eye formation. Ref.1 Ref.4 Ref.5 Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.6

Cofactor

Magnesium By similarity. UniProtKB O54949

Enzyme regulation

Activated by tyrosine and threonine phosphorylation By similarity. UniProtKB Q63844

Subunit structure

Interacts with sox11, hmgxb4/hmg2l1, rnf138/narf, stat3.1 and mef2a. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6

Subcellular location

Nucleus By similarity. Cytoplasm By similarity UniProtKB O54949.

Tissue specificity

Expressed widely in the ectoderm during early gastrula stage when neural induction is taking place. Expressed in the head region of neurula stage embryos. At the end of neurulation, expression becomes localized to the nervous system, and is restricted to the central nervous system, eye and head neural crest cells by the early tadpole stages. Ref.1 Ref.6

Developmental stage

Expressed maternally and throughout embryonic development through to the tadpole stage. Ref.1

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 AAH77759.1 differs from that shown. Reason: Frameshift at position 128.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
Wnt signaling pathway
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

anterior/posterior pattern specification

Inferred from mutant phenotype Ref.1Ref.6. Source: UniProtKB

mesoderm formation

Inferred from mutant phenotype Ref.4. Source: UniProtKB

nervous system development

Inferred from genetic interaction Ref.1. Source: UniProtKB

peptidyl-serine phosphorylation

Inferred from direct assay Ref.6. Source: UniProtKB

peptidyl-threonine phosphorylation

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of protein ubiquitination

Inferred from physical interaction Ref.5. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

serine phosphorylation of STAT3 protein

Inferred from mutant phenotype Ref.4. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype Ref.4. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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 electronic annotation. Source: UniProtKB-EC

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1Ref.3Ref.4. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.6. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.6. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Serine/threonine-protein kinase NLK2
PRO_0000370235

Regions

Domain60 – 349290Protein kinase
Nucleotide binding66 – 749ATP By similarity UniProtKB P53779

Sites

Active site1861Proton acceptor By similarity UniProtKB P53779
Binding site891ATP Probable UniProtKB P53779

Experimental info

Mutagenesis891K → R: Kinase inactive. Does not enhance rnf138/narf-mediated ubiquitination or association of rnf138/narf and tcf/lef. Ref.5
Sequence conflict201S → G in AAH77759. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8QGV6 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: F05DE96445D0FAE9

FASTA44750,138
        10         20         30         40         50         60 
MAFPGSGRSI PGQLCAGVFS GLIQPPLGQK FYCPNGGGAV PSPLPQALSA PQCNGEGRDP 

        70         80         90        100        110        120 
EPDRPIGYGA FGVVWSVTDP RDGKRVALKK MPNVFQNLVS CKRVFRELKM LCFFKHDNVL 

       130        140        150        160        170        180 
SALDILQPPQ IDCFEEIYVI TELMQTDLHK VIVSPQPLSS DHIKVFLYQI LRGLKYLHSA 

       190        200        210        220        230        240 
GILHRDIKPG NLLVNSNCVL KICDFGLARV EELDESQHMT QEVVTQYYRA PEILMGSRHY 

       250        260        270        280        290        300 
RSAIDIWSVG CIFAELLGRR ILFQAQSPIQ QLDLITDLLG TPPLTAMRSA CEGARAHILR 

       310        320        330        340        350        360 
GPHKPPSLSV LYMLSGEATH EAVHLLCRML LFDPLKRISA KDALAHPYLE EGRLRYHTCM 

       370        380        390        400        410        420 
CHCCYSVSSG RVYTADFEPT ATNRFDDSYE KSLTSVWQVK ELVHRFITDQ HQGKRPPLCI 

       430        440 
NPHSAAFKTF IRSTAWHSSK VSKKEER 

« Hide

References

« Hide 'large scale' references
[1]"Involvement of NLK and Sox11 in neural induction in Xenopus development."
Hyodo-Miura J., Urushiyama S., Nagai S., Nishita M., Ueno N., Shibuya H.
Genes Cells 7:487-496(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SOX11, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Oocyte.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[3]"Negative regulation of Wnt signalling by HMG2L1, a novel NLK-binding protein."
Yamada M., Ohkawara B., Ichimura N., Hyodo-Miura J., Urushiyama S., Shirakabe K., Shibuya H.
Genes Cells 8:677-684(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HMGXB4.
[4]"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, INTERACTION WITH STAT3.1.
[5]"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: FUNCTION, INTERACTION WITH RNF138, MUTAGENESIS OF LYS-89.
[6]"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, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB071285 mRNA. Translation: BAB85870.1.
BC077759 mRNA. Translation: AAH77759.1. Frameshift.
RefSeqNP_001082214.1. NM_001088745.1.
UniGeneXl.7148.

3D structure databases

ProteinModelPortalQ8QGV6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid99628. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID398295.
KEGGxla:398295.

Organism-specific databases

CTD398295.
XenbaseXB-GENE-1218927. nlk.2.

Phylogenomic databases

KOK04468.

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...

Entry information

Entry nameNLK2_XENLA
AccessionPrimary (citable) accession number: Q8QGV6
Secondary accession number(s): Q6DD67
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families