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http://purl.uniprot.org/citations/8382613http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8382613http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8382613http://www.w3.org/2000/01/rdf-schema#comment"Glycogen synthase kinase-3 (GSK-3) is a protein serine kinase implicated in the cellular response to insulin. The enzyme is the mammalian homologue of the zeste-white3 (shaggy) homeotic gene of Drosophila melanogaster and has been implicated in the regulation of the c-Jun/AP-1 transcription factor. In mammals this protein serine kinase is encoded by two related genes termed GSK-3 alpha and beta. Here, we demonstrate that these two proteins and the fruit fly protein are phosphorylated on tyrosine in vivo. Moreover, GSK-3 beta activity and function are shown to be dependent on tyrosine phosphorylation. The modified tyrosine residue is conserved in all members of the GSK-3 family and is equivalent to that required for activity by mitogen-activated protein (MAP) kinases. However, unlike MAP kinases, GSK-3 is highly phosphorylated on tyrosine and thus active in resting cells."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1993.tb05715.x"xsd:string
http://purl.uniprot.org/citations/8382613http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1993.tb05715.x"xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/author"Hughes K."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/author"Hughes K."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/author"Plyte S.E."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/author"Plyte S.E."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/author"Woodgett J.R."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/author"Woodgett J.R."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/author"Totty N.F."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/author"Totty N.F."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/author"Nikolakaki E."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/author"Nikolakaki E."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/pages"803-808"xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/pages"803-808"xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/title"Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/title"Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation."xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/8382613http://purl.uniprot.org/core/volume"12"xsd:string