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http://purl.uniprot.org/citations/8464713http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8464713http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8464713http://www.w3.org/2000/01/rdf-schema#comment"The DNA-dependent protein kinase (DNA-PK) phosphorylates a number of transcription factors. Here, we show that the DNA-PK modifies c-Jun in vitro and that serine residue 249 (Ser-249) is required for phosphorylation to occur. This residue corresponds to one of three sites of c-Jun that are phosphorylated in vivo and which negatively regulate c-Jun DNA binding in vitro. However, we find that phosphorylation of c-Jun by the DNA-PK does not interfere with DNA binding, indicating that phosphorylation at other sites is required for this effect. Mutagenesis of the phosphorylated region of c-Jun reveals that the primary amino acid sequence recognised by the DNA-PK consists of the sequence Ser-Gln, and that adjacent acidic residues potentiate kinase activity. Furthermore, when this site is placed within the context of a second protein, it confers DNA-PK directed phosphorylation upon that protein. Our findings will facilitate identification of DNA-PK phosphorylation sites in other transcription factors."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.org/dc/terms/identifier"doi:10.1093/nar/21.5.1289"xsd:string
http://purl.uniprot.org/citations/8464713http://purl.org/dc/terms/identifier"doi:10.1093/nar/21.5.1289"xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/author"Jackson S.P."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/author"Jackson S.P."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/author"Kouzarides T."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/author"Kouzarides T."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/author"Bannister A.J."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/author"Bannister A.J."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/author"Gottlieb T.M."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/author"Gottlieb T.M."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/pages"1289-1295"xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/pages"1289-1295"xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/title"c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro; definition of the minimal kinase recognition motif."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/title"c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro; definition of the minimal kinase recognition motif."xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/8464713http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/8464713http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8464713
http://purl.uniprot.org/citations/8464713http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8464713