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Protein

Glycogen synthase kinase-3

Gene

gsk-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

Catalytic activityi

ATP + [tau protein] = ADP + [tau protein] phosphate.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651ATPPROSITE-ProRule annotation
Active sitei161 – 1611Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 509ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: WormBase
  • tau-protein kinase activity Source: UniProtKB-EC

GO - Biological processi

  • engulfment of apoptotic cell Source: WormBase
  • germ cell development Source: WormBase
  • multicellular organismal development Source: UniProtKB-KW
  • negative regulation of Wnt signaling pathway Source: UniProtKB
  • peptidyl-threonine phosphorylation Source: WormBase
  • Wnt signaling pathway, regulating spindle positioning Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Stress response, Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_297277. Degradation of beta-catenin by the destruction complex.
REACT_308298. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_319084. Regulation of HSF1-mediated heat shock response.
REACT_333609. Beta-catenin phosphorylation cascade.
REACT_338256. AKT phosphorylates targets in the cytosol.
REACT_351918. CRMPs in Sema3A signaling.
SignaLinkiQ9U2Q9.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen synthase kinase-31 Publication (EC:2.7.11.26)
Gene namesi
Name:gsk-3Imported
Synonyms:sgg-11 Publication
ORF Names:Y18D10A.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiY18D10A.5; CE21401; WBGene00001746; gsk-3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: WormBase
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362Glycogen synthase kinase-3PRO_0000349136Add
BLAST

Proteomic databases

PaxDbiQ9U2Q9.

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with axl-1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
axl-1Q3LRZ34EBI-330089,EBI-327368
mac-1Q9NAG43EBI-330089,EBI-2005767
pry-1O620903EBI-330089,EBI-2917690

Protein-protein interaction databases

BioGridi38546. 22 interactions.
DIPiDIP-25216N.
IntActiQ9U2Q9. 12 interactions.
MINTiMINT-1073589.
STRINGi6239.Y18D10A.5.2.

Structurei

3D structure databases

ProteinModelPortaliQ9U2Q9.
SMRiQ9U2Q9. Positions 15-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 320285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00520000055635.
HOGENOMiHOG000233017.
InParanoidiQ9U2Q9.
KOiK03083.
OMAiQSMNPNY.
PhylomeDBiQ9U2Q9.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
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.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9U2Q9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKQLLSCSL KSGKQVTMVV ASVATDGVDQ QVEISYYDQK VIGNGSFGVV
60 70 80 90 100
FLAKLSTTNE MVAIKKVLQD KRFKNRELQI MRKLNHPNIV KLKYFFYSSG
110 120 130 140 150
EKKDELYLNL ILEYVPETVY RVARHYSKQR QQIPMIYVKL YMYQLLRSLA
160 170 180 190 200
YIHSIGICHR DIKPQNLLID PESGVLKLCD FGSAKYLVRN EPNVSYICSR
210 220 230 240 250
YYRAPELIFG ATNYTNSIDV WSAGTVMAEL LLGQPIFPGD SGVDQLVEII
260 270 280 290 300
KVLGTPTREQ IQSMNPNYKE FKFPQIKAHP WNKVFRVHTP AEAIDLISKI
310 320 330 340 350
IEYTPTSRPT PQAACQHAFF DELRNPDARL PSGRPLPTLE MDGPMGTGEV
360
STTSGDVAGP SA
Length:362
Mass (Da):40,882
Last modified:May 1, 2000 - v1
Checksum:iABDD2F49CC475BF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti350 – 3501V → I in AAD45354 (PubMed:10444600).Curated
Sequence conflicti352 – 3521T → P in AAD45354 (PubMed:10444600).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159950 mRNA. Translation: AAD45354.1.
AL034393 Genomic DNA. Translation: CAA22311.1.
PIRiT26520.
RefSeqiNP_493243.1. NM_060842.5.
UniGeneiCel.7399.

Genome annotation databases

EnsemblMetazoaiY18D10A.5; Y18D10A.5; WBGene00001746.
GeneIDi173149.
KEGGicel:CELE_Y18D10A.5.
UCSCiY18D10A.5. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159950 mRNA. Translation: AAD45354.1.
AL034393 Genomic DNA. Translation: CAA22311.1.
PIRiT26520.
RefSeqiNP_493243.1. NM_060842.5.
UniGeneiCel.7399.

3D structure databases

ProteinModelPortaliQ9U2Q9.
SMRiQ9U2Q9. Positions 15-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi38546. 22 interactions.
DIPiDIP-25216N.
IntActiQ9U2Q9. 12 interactions.
MINTiMINT-1073589.
STRINGi6239.Y18D10A.5.2.

Proteomic databases

PaxDbiQ9U2Q9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY18D10A.5; Y18D10A.5; WBGene00001746.
GeneIDi173149.
KEGGicel:CELE_Y18D10A.5.
UCSCiY18D10A.5. c. elegans.

Organism-specific databases

CTDi173149.
WormBaseiY18D10A.5; CE21401; WBGene00001746; gsk-3.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00520000055635.
HOGENOMiHOG000233017.
InParanoidiQ9U2Q9.
KOiK03083.
OMAiQSMNPNY.
PhylomeDBiQ9U2Q9.

Enzyme and pathway databases

ReactomeiREACT_297277. Degradation of beta-catenin by the destruction complex.
REACT_308298. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_319084. Regulation of HSF1-mediated heat shock response.
REACT_333609. Beta-catenin phosphorylation cascade.
REACT_338256. AKT phosphorylates targets in the cytosol.
REACT_351918. CRMPs in Sema3A signaling.
SignaLinkiQ9U2Q9.

Miscellaneous databases

NextBioi878473.
PROiQ9U2Q9.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
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.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiGSK3_CAEEL
AccessioniPrimary (citable) accession number: Q9U2Q9
Secondary accession number(s): Q9Y0C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.