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P51136

- GSK3_DICDI

UniProt

P51136 - GSK3_DICDI

Protein

Glycogen synthase kinase-3

Gene

gskA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
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    Functioni

    During cellular differentiation, may mediate an extracellular cyclic AMP stimulated signal transduction pathway that regulates prespore and prestalk B-cell proportions through inhibition of stalk cell formation and induction of prespore cell differentiation. The cAMP receptor carC appears to activate gskA via the tyrosine kinases zakA and zak2, to stimulate prespore differentiation, while carD appears to negatively regulate gskA, to promote prestalk formation.7 Publications

    Catalytic activityi

    ATP + [tau protein] = ADP + [tau protein] phosphate.3 Publications

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Inhibited by lithium. Lithium inhibition is competitive with respect to magnesium but non-competitive with respect to the peptide substrate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei85 – 851ATP
    Active sitei179 – 1791Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi62 – 709ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell differentiation Source: dictyBase
    2. culmination involved in sorocarp development Source: UniProtKB
    3. mitotic cytokinesis Source: dictyBase
    4. multicellular organismal development Source: UniProtKB
    5. peptidyl-threonine phosphorylation Source: dictyBase
    6. positive regulation of protein export from nucleus Source: dictyBase
    7. protein phosphorylation Source: UniProtKB
    8. regulation of aggregation involved in sorocarp development Source: dictyBase
    9. regulation of cell adhesion Source: dictyBase
    10. regulation of positive chemotaxis to cAMP Source: dictyBase
    11. signal transduction Source: dictyBase
    12. sorocarp morphogenesis Source: dictyBase
    13. spindle elongation Source: dictyBase
    14. sporulation resulting in formation of a cellular spore Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.26. 1939.
    ReactomeiREACT_218739. XBP1(S) activates chaperone genes.
    REACT_227492. Regulation of HSF1-mediated heat shock response.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycogen synthase kinase-3 (EC:2.7.11.26)
    Short name:
    GSK-3
    Gene namesi
    Name:gskA
    Synonyms:gsk3
    ORF Names:DDB_G0272110
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 2, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0272110. gskA.

    Subcellular locationi

    GO - Cellular componenti

    1. mitotic spindle Source: dictyBase

    Pathology & Biotechi

    Disruption phenotypei

    Cells grow normally in both axenic medium and with bacteria. Under starvation conditions, mutants lacking gskA aggregate more quickly and form smaller mounds than wild type, fail to form slugs and take longer than wild type to reach culmination. At culmination, mutants lacking gskA form abnormal fruiting bodies characterized by an unusually large mound-like basal disk. Prestalk B (pstB) cells are formed at the expense of prespore cells, and the proportion of gskA null cells that differentiate into spores is greatly reduced when compared to wild-type cells.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851K → M: Inactive kinase. 1 Publication
    Mutagenesisi86 – 861K → M: Inactive kinase. 1 Publication
    Mutagenesisi214 – 2141Y → F: Not phosphorylated or activated by zakA. 1 Publication
    Mutagenesisi220 – 2201Y → F: Not phosphorylated or activated by zakA. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 467467Glycogen synthase kinase-3PRO_0000085983Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei214 – 2141Phosphotyrosine; by zakA1 Publication
    Modified residuei220 – 2201Phosphotyrosine; by zakA1 Publication

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Developmental stagei

    Expressed in growing cells and throughout development. Levels increase during mound formation (12 hours) and peak at approximately twice the level seen in growing cells before decreasing again at the start of culmination (16 hours).1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDB_0185150.

    Structurei

    3D structure databases

    ProteinModelPortaliP51136.
    SMRiP51136. Positions 54-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 339284Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi28 – 4114Ser-richAdd
    BLAST
    Compositional biasi399 – 45052Ser-richAdd
    BLAST
    Compositional biasi444 – 46421Thr-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    KOiK03083.
    OMAiMELCAHE.
    PhylomeDBiP51136.

    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.

    P51136-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSKDQILEK DKKETDDNGN KKTTTTTSSS SSSSSSSKPR SNKFDKVIIK    50
    SNGVCYITEG VIGNGSFGVV TQAIVADTKE VVAIKKVLQD QRYKNRELQI 100
    MKMLNHINIV SLKNSFYTSD NDEVYLNLVL EYVPDTVYRV SRHYSMSKQP 150
    VPNIFVKLYI YQLCRSINYI HSLGICHRDI KPQNLLLDTS TSTLKLCDFG 200
    SAKILIKGET NVSYICSRHY RAPELIFGST NYTTTIDVWS LGCVLAELLL 250
    GQPLFPGENG IDQLVEIIKV LGTPTKEQIH AMNPYYTSFK FPEIKANPWP 300
    RVFKAKDVPA ESIDLISKIL LYDPSSRLKP VEICAHPFFD ELRDPKTCLP 350
    DGKPLPPLFN FTIAEQTSIG PKLAKTLIPS HAMNQIELPS PLFPNLAISS 400
    SNQSSSSNSN ANVSSNLNSH SASPSTTSSS SSTPNSIPVQ SPSTTNTTSS 450
    TTNNTTTTTT TTTTSNH 467
    Length:467
    Mass (Da):51,483
    Last modified:May 10, 2004 - v2
    Checksum:iEF6C00122B90C61D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34674 mRNA. Translation: AAA65968.2.
    AAFI02000008 Genomic DNA. Translation: EAL71207.1.
    PIRiA55476.
    RefSeqiXP_645156.1. XM_640064.1.

    Genome annotation databases

    EnsemblProtistsiDDB0185150; DDB0185150; DDB_G0272110.
    GeneIDi8618327.
    KEGGiddi:DDB_G0272110.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34674 mRNA. Translation: AAA65968.2 .
    AAFI02000008 Genomic DNA. Translation: EAL71207.1 .
    PIRi A55476.
    RefSeqi XP_645156.1. XM_640064.1.

    3D structure databases

    ProteinModelPortali P51136.
    SMRi P51136. Positions 54-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0185150.

    Chemistry

    ChEMBLi CHEMBL2311226.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0185150 ; DDB0185150 ; DDB_G0272110 .
    GeneIDi 8618327.
    KEGGi ddi:DDB_G0272110.

    Organism-specific databases

    dictyBasei DDB_G0272110. gskA.

    Phylogenomic databases

    eggNOGi COG0515.
    KOi K03083.
    OMAi MELCAHE.
    PhylomeDBi P51136.

    Enzyme and pathway databases

    BRENDAi 2.7.11.26. 1939.
    Reactomei REACT_218739. XBP1(S) activates chaperone genes.
    REACT_227492. Regulation of HSF1-mediated heat shock response.

    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. "Glycogen synthase kinase 3 regulates cell fate in Dictyostelium."
      Harwood A.J., Plyte S.E., Woodgett J., Strutt H., Kay R.R.
      Cell 80:139-148(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
      Strain: AX2.
    2. Harwood A.J., Plyte S.E., Woodgett J., Strutt H., Kay R.R.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    4. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    5. "Activation of the Wnt signaling pathway: a molecular mechanism for lithium action."
      Hedgepeth C.M., Conrad L.J., Zhang J., Huang H.-C., Lee V.M.Y., Klein P.S.
      Dev. Biol. 185:82-91(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, INHIBITION BY LITHIUM.
    6. "Autonomous and nonautonomous regulation of axis formation by antagonistic signaling via 7-span cAMP receptors and GSK3 in Dictyostelium."
      Ginsburg G.T., Kimmel A.R.
      Genes Dev. 11:2112-2123(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "An assay for glycogen synthase kinase 3 (GSK-3) for use in crude cell extracts."
      Ryves W.J., Fryer L., Dale T., Harwood A.J.
      Anal. Biochem. 264:124-127(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, INHIBITION BY LITHIUM.
    8. "The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate specification."
      Kim L., Liu J., Kimmel A.R.
      Cell 99:399-408(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Glycogen synthase kinase-3 (GSK-3) is regulated during Dictyostelium development via the serpentine receptor cAR3."
      Plyte S.E., O'Donovan E., Woodgett J.R., Harwood A.J.
      Development 126:325-333(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    10. "Lithium inhibits glycogen synthase kinase-3 by competition for magnesium."
      Ryves W.J., Harwood A.J.
      Biochem. Biophys. Res. Commun. 280:720-725(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, COFACTOR REQUIREMENT, INHIBITION BY LITHIUM.
    11. "Receptor-dependent and tyrosine phosphatase-mediated inhibition of GSK3 regulates cell fate choice."
      Kim L., Harwood A.J., Kimmel A.R.
      Dev. Cell 3:523-532(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-85; LYS-86; TYR-214 AND TYR-220, PHOSPHORYLATION AT TYR-214 AND TYR-220.
    12. "GSK3 is a multifunctional regulator of Dictyostelium development."
      Schilde C., Araki T., Williams H., Harwood A.J., Williams J.G.
      Development 131:4555-4565(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    13. "Combinatorial cell-specific regulation of GSK3 directs cell differentiation and polarity in Dictyostelium."
      Kim L., Brzostowski J., Majithia A., Lee N.S., McMains V., Kimmel A.R.
      Development 138:421-430(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiGSK3_DICDI
    AccessioniPrimary (citable) accession number: P51136
    Secondary accession number(s): Q55A28, Q86KY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3