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http://purl.uniprot.org/citations/16818604http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16818604http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16818604http://www.w3.org/2000/01/rdf-schema#comment"BRCA1 (Breast Cancer Susceptibility Gene 1) possesses an N-terminal Ring domain and tandem C-terminal BRCT motifs. While the Ring domain has E3 ubiquitin ligase activity, the BRCA1 BRCT domains specifically recognize phospho-serine motifs. Here, we demonstrate that BRCA1 Ring domain catalyzes CtIP ubiquitination in a manner that depends on a phosphorylation-mediated interaction between CtIP and BRCA1 BRCT domains. The BRCA1-dependent ubiquitination of CtIP does not target CtIP for degradation. Instead, ubiquitinated CtIP associates with chromatin following DNA damage and participates in G2/M checkpoint control. Thus, we propose that BRCA1 can regulate the functions of its substrates through nonproteasomal pathways that do not involve substrate degradation."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.org/dc/terms/identifier"doi:10.1101/gad.1431006"xsd:string
http://purl.uniprot.org/citations/16818604http://purl.org/dc/terms/identifier"doi:10.1101/gad.1431006"xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/author"Baer R."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/author"Baer R."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/author"Fu S."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/author"Fu S."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/author"Yu X."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/author"Yu X."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/author"Lai M."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/author"Lai M."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/pages"1721-1726"xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/pages"1721-1726"xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/title"BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/title"BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP."xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/16818604http://purl.uniprot.org/core/volume"20"xsd:string