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http://purl.uniprot.org/citations/17873885http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17873885http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17873885http://www.w3.org/2000/01/rdf-schema#comment"An E3 ubiquitin ligase mediates the transfer of activated ubiquitin from an E2 ubiquitin-conjugating enzyme to its substrate lysine residues. Using a structure-based, yeast two-hybrid strategy, we discovered six previously unidentified interactions between the human heterodimeric RING E3 BRCA1-BARD1 and the human E2s UbcH6, Ube2e2, UbcM2, Ubc13, Ube2k and Ube2w. All six E2s bind directly to the BRCA1 RING motif and are active with BRCA1-BARD1 for autoubiquitination in vitro. Four of the E2s direct monoubiquitination of BRCA1. Ubc13-Mms2 and Ube2k direct the synthesis of Lys63- or Lys48-linked ubiquitin chains on BRCA1 and require an acceptor ubiquitin attached to BRCA1. Differences between the mono- and polyubiquitination activities of the BRCA1-interacting E2s correlate with their ability to bind ubiquitin noncovalently at a site distal to the active site. Thus, BRCA1 has the ability to direct the synthesis of specific polyubiquitin chain linkages, depending on the E2 bound to its RING."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.org/dc/terms/identifier"doi:10.1038/nsmb1295"xsd:string
http://purl.uniprot.org/citations/17873885http://purl.org/dc/terms/identifier"doi:10.1038/nsmb1295"xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/author"Klevit R.E."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/author"Klevit R.E."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/author"Brzovic P.S."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/author"Brzovic P.S."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/author"Christensen D.E."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/author"Christensen D.E."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/pages"941-948"xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/pages"941-948"xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/title"E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/title"E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages."xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/17873885http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/17873885http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17873885
http://purl.uniprot.org/citations/17873885http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17873885
http://purl.uniprot.org/citations/17873885http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17873885
http://purl.uniprot.org/citations/17873885http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17873885