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Q9U2Q9 (GSK3_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Glycogen synthase kinase-3

EC=2.7.11.26
Gene names
Name:gsk-3
Synonyms:sgg-1
ORF Names:Y18D10A.5
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates oma-1, a regulator of the oocyte-to-embryo transition, enabling its degradation. Phosphorylates skn-1, preventing it from accumulating in nuclei and thus inhibiting phase II gene expression in the oxidative stress defense. Involved in mesendoderm specification and mitotic spindle orientation in EMS blastomeres. Thought to be a branch point in these processes as proteins downstream are not required. Negatively regulates Wnt signaling in vulval precursor cells and acts as a Wnt-independent repressor of med-1 and med-2 in the C lineage inhibiting mesoderm development. Required for normal lifespan and LiCl-induced lifespan extension. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10

Catalytic activity

ATP + [tau protein] = ADP + [tau protein] phosphate. Ref.10

Subunit structure

Monomer By similarity. Interacts with axl-1. Ref.8 Ref.9

Disruption phenotype

Worms exhibit defects in endoderm specification and mitotic spindle alignment. Mutants show reduced degradation of oma-1 and have shortened lifespan. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.

Contains 1 protein kinase domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362Glycogen synthase kinase-3
PRO_0000349136

Regions

Domain36 – 320285Protein kinase
Nucleotide binding42 – 509ATP By similarity

Sites

Active site1611Proton acceptor By similarity
Binding site651ATP By similarity

Experimental info

Sequence conflict3501V → I in AAD45354. Ref.1
Sequence conflict3521T → P in AAD45354. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9U2Q9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: ABDD2F49CC475BF5

FASTA36240,882
        10         20         30         40         50         60 
MNKQLLSCSL KSGKQVTMVV ASVATDGVDQ QVEISYYDQK VIGNGSFGVV FLAKLSTTNE 

        70         80         90        100        110        120 
MVAIKKVLQD KRFKNRELQI MRKLNHPNIV KLKYFFYSSG EKKDELYLNL ILEYVPETVY 

       130        140        150        160        170        180 
RVARHYSKQR QQIPMIYVKL YMYQLLRSLA YIHSIGICHR DIKPQNLLID PESGVLKLCD 

       190        200        210        220        230        240 
FGSAKYLVRN EPNVSYICSR YYRAPELIFG ATNYTNSIDV WSAGTVMAEL LLGQPIFPGD 

       250        260        270        280        290        300 
SGVDQLVEII KVLGTPTREQ IQSMNPNYKE FKFPQIKAHP WNKVFRVHTP AEAIDLISKI 

       310        320        330        340        350        360 
IEYTPTSRPT PQAACQHAFF DELRNPDARL PSGRPLPTLE MDGPMGTGEV STTSGDVAGP 


SA 

« Hide

References

« Hide 'large scale' references
[1]"Wnt pathway components orient a mitotic spindle in the early Caenorhabditis elegans embryo without requiring gene transcription in the responding cell."
Schlesinger A., Shelton C.A., Maloof J.N., Meneghini M.D., Bowerman B.
Genes Dev. 13:2028-2038(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Restriction of mesendoderm to a single blastomere by the combined action of SKN-1 and a GSK-3beta homolog is mediated by MED-1 and -2 in C. elegans."
Maduro M.F., Meneghini M.D., Bowerman B., Broitman-Maduro G., Rothman J.H.
Mol. Cell 7:475-485(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Multiple Wnt signaling pathways converge to orient the mitotic spindle in early C. elegans embryos."
Walston T., Tuskey C., Edgar L., Hawkins N., Ellis G., Bowerman B., Wood W., Hardin J.
Dev. Cell 7:831-841(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"DYRK2 and GSK-3 phosphorylate and promote the timely degradation of OMA-1, a key regulator of the oocyte-to-embryo transition in C. elegans."
Nishi Y., Lin R.
Dev. Biol. 288:139-149(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Regulation of the Caenorhabditis elegans oxidative stress defense protein SKN-1 by glycogen synthase kinase-3."
An J.H., Vranas K., Lucke M., Inoue H., Hisamoto N., Matsumoto K., Blackwell T.K.
Proc. Natl. Acad. Sci. U.S.A. 102:16275-16280(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The conserved kinases CDK-1, GSK-3, KIN-19, and MBK-2 promote OMA-1 destruction to regulate the oocyte-to-embryo transition in C. elegans."
Shirayama M., Soto M.C., Ishidate T., Kim S., Nakamura K., Bei Y., van den Heuvel S., Mello C.C.
Curr. Biol. 16:47-55(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Multiple redundant Wnt signaling components function in two processes during C. elegans vulval development."
Gleason J.E., Szyleyko E.A., Eisenmann D.M.
Dev. Biol. 298:442-457(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Two functionally distinct axin-like proteins regulate canonical Wnt signaling in C. elegans."
Oosterveen T., Coudreuse D.Y.M., Yang P.-T., Fraser E., Bergsma J., Dale T.C., Korswagen H.C.
Dev. Biol. 308:438-448(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXL-1.
[10]"Pharmacogenetic analysis of lithium-induced delayed aging in Caenorhabditis elegans."
McColl G., Killilea D.W., Hubbard A.E., Vantipalli M.C., Melov S., Lithgow G.J.
J. Biol. Chem. 283:350-357(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF159950 mRNA. Translation: AAD45354.1.
AL034393 Genomic DNA. Translation: CAA22311.1.
PIRT26520.
RefSeqNP_493243.1. NM_060842.5.
UniGeneCel.7399.

3D structure databases

ProteinModelPortalQ9U2Q9.
SMRQ9U2Q9. Positions 15-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid38546. 20 interactions.
DIPDIP-25216N.
IntActQ9U2Q9. 12 interactions.
MINTMINT-1073589.
STRING6239.Y18D10A.5.

Proteomic databases

PaxDbQ9U2Q9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaY18D10A.5.1; Y18D10A.5.1; Y18D10A.5.
Y18D10A.5.2; Y18D10A.5.2; Y18D10A.5.
GeneID173149.
KEGGcel:CELE_Y18D10A.5.
UCSCY18D10A.5. c. elegans.

Organism-specific databases

CTD173149.
WormBaseY18D10A.5; CE21401; WBGene00001746; gsk-3.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233017.
InParanoidQ9U2Q9.
KOK03083.
OMADELRCHG.
PhylomeDBQ9U2Q9.

Enzyme and pathway databases

SignaLinkQ9U2Q9.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
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.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio878473.

Entry information

Entry nameGSK3_CAEEL
AccessionPrimary (citable) accession number: Q9U2Q9
Secondary accession number(s): Q9Y0C2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase