| http://purl.uniprot.org/citations/12485996 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12485996 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12485996 | http://www.w3.org/2000/01/rdf-schema#comment | "Loss of the tumour suppressor BRCA1 results in profound chromosomal instability. The fundamental defect underlying this catastrophic phenotype is not yet known. In vivo, BRCA1 forms a heterodimeric complex with BARD1. Both proteins contain an N-terminal zinc RING-finger domain which confers E3 ubiquitin ligase activity. We have isolated full-length human BRCA1/BARD1 complex and have shown that it has a dual E3 ubiquitin ligase activity. First, it mediates the monoubiquitylation of nucleosome core histones in vitro, including the variant histone H2AX that co-localizes with BRCA1 at sites of DNA damage. Secondly, BRCA1/BARD1 catalyses the formation of multiple polyubiquitin chains on itself. Remarkably, this auto-polyubiquitylation potentiates the E3 ubiquitin ligase activity of the BRCA1/BARD1 complex >20-fold. Even though BRCA1 has been reported to associate with a C-terminal ubiquitin hydrolase, BAP1, this enzyme does not appear to function in the deubiquitylation of the BRCA1/BARD1 complex."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/cdf691"xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/cdf691"xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/author | "Hiom K."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/author | "Hiom K."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/author | "Mallery D.L."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/author | "Mallery D.L."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/author | "Vandenberg C.J."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/author | "Vandenberg C.J."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/pages | "6755-6762"xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/pages | "6755-6762"xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/title | "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/title | "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains."xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/volume | "21"xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://purl.uniprot.org/core/volume | "21"xsd:string |
| http://purl.uniprot.org/citations/12485996 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12485996 |
| http://purl.uniprot.org/citations/12485996 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12485996 |
| http://purl.uniprot.org/citations/12485996 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12485996 |
| http://purl.uniprot.org/citations/12485996 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12485996 |