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Q9U2Q9

- GSK3_CAEEL

UniProt

Q9U2Q9 - GSK3_CAEEL

Protein

Glycogen synthase kinase-3

Gene

gsk-3

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein serine/threonine kinase activity Source: WormBase
    4. tau-protein kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. engulfment of apoptotic cell Source: WormBase
    2. germ cell development Source: WormBase
    3. multicellular organismal development Source: UniProtKB-KW
    4. negative regulation of Wnt signaling pathway Source: UniProtKB
    5. response to stress Source: UniProtKB-KW
    6. Wnt signaling pathway, regulating spindle positioning Source: WormBase

    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

    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: Chromosome I

    Organism-specific databases

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

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: WormBase

    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.

    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.
    OMAiKIIEYTP.
    PhylomeDBiQ9U2Q9.

    Family and domain databases

    InterProiIPR011009. 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]
    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

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    MNKQLLSCSL KSGKQVTMVV ASVATDGVDQ QVEISYYDQK VIGNGSFGVV    50
    FLAKLSTTNE MVAIKKVLQD KRFKNRELQI MRKLNHPNIV KLKYFFYSSG 100
    EKKDELYLNL ILEYVPETVY RVARHYSKQR QQIPMIYVKL YMYQLLRSLA 150
    YIHSIGICHR DIKPQNLLID PESGVLKLCD FGSAKYLVRN EPNVSYICSR 200
    YYRAPELIFG ATNYTNSIDV WSAGTVMAEL LLGQPIFPGD SGVDQLVEII 250
    KVLGTPTREQ IQSMNPNYKE FKFPQIKAHP WNKVFRVHTP AEAIDLISKI 300
    IEYTPTSRPT PQAACQHAFF DELRNPDARL PSGRPLPTLE MDGPMGTGEV 350
    STTSGDVAGP SA 362
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF159950 mRNA. Translation: AAD45354.1 .
    AL034393 Genomic DNA. Translation: CAA22311.1 .
    PIRi T26520.
    RefSeqi NP_493243.1. NM_060842.5.
    UniGenei Cel.7399.

    3D structure databases

    ProteinModelPortali Q9U2Q9.
    SMRi Q9U2Q9. Positions 15-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 38546. 22 interactions.
    DIPi DIP-25216N.
    IntActi Q9U2Q9. 12 interactions.
    MINTi MINT-1073589.
    STRINGi 6239.Y18D10A.5.

    Proteomic databases

    PaxDbi Q9U2Q9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai Y18D10A.5 ; Y18D10A.5 ; WBGene00001746 .
    GeneIDi 173149.
    KEGGi cel:CELE_Y18D10A.5.
    UCSCi Y18D10A.5. c. elegans.

    Organism-specific databases

    CTDi 173149.
    WormBasei Y18D10A.5 ; CE21401 ; WBGene00001746 ; gsk-3.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00520000055635.
    HOGENOMi HOG000233017.
    InParanoidi Q9U2Q9.
    KOi K03083.
    OMAi KIIEYTP.
    PhylomeDBi Q9U2Q9.

    Enzyme and pathway databases

    SignaLinki Q9U2Q9.

    Miscellaneous databases

    NextBioi 878473.

    Family and domain databases

    InterProi IPR011009. 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 ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 118 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