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http://purl.uniprot.org/citations/1846781http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1846781http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1846781http://www.w3.org/2000/01/rdf-schema#comment"In resting human epithelial and fibroblastic cells, c-Jun is phosphorylated on serine and threonine at five sites, three of which are phosphorylated in vitro by glycogen synthase kinase 3 (GSK-3). These three sites are nested within a single tryptic peptide located just upstream of the basic region of the c-Jun DNA-binding domain (residues 227-252). Activation of protein kinase C results in rapid, site-specific dephosphorylation of c-Jun at one or more of these three sites and is coincident with increased AP-1-binding activity. Phosphorylation of recombinant human c-Jun proteins in vitro by GSK-3 decreases their DNA-binding activity. Mutation of serine 243 to phenylalanine blocks phosphorylation of all three sites in vivo and increases the inherent trans-activation ability of c-Jun at least 10-fold. We propose that c-Jun is present in resting cells in a latent, phosphorylated form that can be activated by site-specific dephosphorylation in response to protein kinase C activation."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(91)90241-p"xsd:string
http://purl.uniprot.org/citations/1846781http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(91)90241-p"xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Hunter T."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Hunter T."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Karin M."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Karin M."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Woodgett J.R."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Woodgett J.R."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Angel P."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Angel P."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Smeal T."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Smeal T."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Boyle W.J."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Boyle W.J."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Defize L.H."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/author"Defize L.H."xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/pages"573-584"xsd:string
http://purl.uniprot.org/citations/1846781http://purl.uniprot.org/core/pages"573-584"xsd:string