Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8QGV6

- NLK2_XENLA

UniProt

Q8QGV6 - NLK2_XENLA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein kinase NLK2

Gene

nlk.2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium.By similarity

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891ATPCurated
Active sitei186 – 1861Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 749ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. MAP kinase activity Source: UniProtKB-EC
  4. protein serine/threonine kinase activity Source: UniProtKB
  5. transcription factor binding Source: UniProtKB
  6. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. anterior/posterior pattern specification Source: UniProtKB
  2. mesoderm formation Source: UniProtKB
  3. nervous system development Source: UniProtKB
  4. peptidyl-serine phosphorylation Source: UniProtKB
  5. peptidyl-threonine phosphorylation Source: UniProtKB
  6. positive regulation of protein ubiquitination Source: UniProtKB
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  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

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway, Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase NLK2 (EC:2.7.11.24)
Alternative name(s):
Nemo-like kinase 2
Short name:
Nlk.2
Short name:
xNLK3 Publications
Gene namesi
Name:nlk.2
Synonyms:nlk4 Publications
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-1218927. nlk.2.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891K → R: Kinase inactive. Does not enhance rnf138/narf-mediated ubiquitination or association of rnf138/narf and tcf/lef. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Serine/threonine-protein kinase NLK2PRO_0000370235Add
BLAST

Keywords - PTMi

Phosphoprotein

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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

Interactioni

Subunit structurei

Interacts with sox11, hmgxb4/hmg2l1, rnf138/narf, stat3.1 and mef2a.5 Publications

Protein-protein interaction databases

BioGridi99628. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8QGV6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 349290Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK04468.

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.

Q8QGV6 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFPGSGRSI PGQLCAGVFS GLIQPPLGQK FYCPNGGGAV PSPLPQALSA
60 70 80 90 100
PQCNGEGRDP EPDRPIGYGA FGVVWSVTDP RDGKRVALKK MPNVFQNLVS
110 120 130 140 150
CKRVFRELKM LCFFKHDNVL SALDILQPPQ IDCFEEIYVI TELMQTDLHK
160 170 180 190 200
VIVSPQPLSS DHIKVFLYQI LRGLKYLHSA GILHRDIKPG NLLVNSNCVL
210 220 230 240 250
KICDFGLARV EELDESQHMT QEVVTQYYRA PEILMGSRHY RSAIDIWSVG
260 270 280 290 300
CIFAELLGRR ILFQAQSPIQ QLDLITDLLG TPPLTAMRSA CEGARAHILR
310 320 330 340 350
GPHKPPSLSV LYMLSGEATH EAVHLLCRML LFDPLKRISA KDALAHPYLE
360 370 380 390 400
EGRLRYHTCM CHCCYSVSSG RVYTADFEPT ATNRFDDSYE KSLTSVWQVK
410 420 430 440
ELVHRFITDQ HQGKRPPLCI NPHSAAFKTF IRSTAWHSSK VSKKEER
Length:447
Mass (Da):50,138
Last modified:June 1, 2002 - v1
Checksum:iF05DE96445D0FAE9
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201S → G in AAH77759. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB071285 mRNA. Translation: BAB85870.1.
BC077759 mRNA. Translation: AAH77759.1. Frameshift.
RefSeqiNP_001082214.1. NM_001088745.1.
UniGeneiXl.7148.

Genome annotation databases

GeneIDi398295.
KEGGixla:398295.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB071285 mRNA. Translation: BAB85870.1 .
BC077759 mRNA. Translation: AAH77759.1 . Frameshift.
RefSeqi NP_001082214.1. NM_001088745.1.
UniGenei Xl.7148.

3D structure databases

ProteinModelPortali Q8QGV6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 99628. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 398295.
KEGGi xla:398295.

Organism-specific databases

CTDi 398295.
Xenbasei XB-GENE-1218927. nlk.2.

Phylogenomic databases

KOi K04468.

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. "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: Oocyte1 Publication.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: EmbryoImported.
  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.

Entry informationi

Entry nameiNLK2_XENLA
AccessioniPrimary (citable) accession number: Q8QGV6
Secondary accession number(s): Q6DD67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3