| http://purl.uniprot.org/citations/14576433 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14576433 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14576433 | http://www.w3.org/2000/01/rdf-schema#comment | "The carboxyl-terminal domain (BRCT) of the Breast Cancer Gene 1 (BRCA1) protein is an evolutionarily conserved module that exists in a large number of proteins from prokaryotes to eukaryotes. Although most BRCT domain-containing proteins participate in DNA-damage checkpoint or DNA-repair pathways, or both, the function of the BRCT domain is not fully understood. We show that the BRCA1 BRCT domain directly interacts with phosphorylated BRCA1-Associated Carboxyl-terminal Helicase (BACH1). This specific interaction between BRCA1 and phosphorylated BACH1 is cell cycle regulated and is required for DNA damage-induced checkpoint control during the transition from G2 to M phase of the cell cycle. Further, we show that two other BRCT domains interact with their respective physiological partners in a phosphorylation-dependent manner. Thirteen additional BRCT domains also preferentially bind phospho-peptides rather than nonphosphorylated control peptides. These data imply that the BRCT domain is a phospho-protein binding domain involved in cell cycle control."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1088753"xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1088753"xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/author | "Chen J."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/author | "Chen J."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/author | "He M."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/author | "He M."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/author | "Yu X."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/author | "Yu X."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/author | "Chini C.C.S."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/author | "Chini C.C.S."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/author | "Mer G."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/author | "Mer G."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/name | "Science"xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/name | "Science"xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/pages | "639-642"xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/pages | "639-642"xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/title | "The BRCT domain is a phospho-protein binding domain."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/title | "The BRCT domain is a phospho-protein binding domain."xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/volume | "302"xsd:string |
| http://purl.uniprot.org/citations/14576433 | http://purl.uniprot.org/core/volume | "302"xsd:string |