| http://purl.uniprot.org/citations/11285227 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11285227 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11285227 | http://www.w3.org/2000/01/rdf-schema#comment | "In higher eukaryotic cells, the p53 protein is degraded by the ubiquitin-26S proteasome system mediated by Mdm2 or the human papilloma virus E6 protein. Here we show that COP9 signalosome (CSN)-specific phosphorylation targets human p53 to ubiquitin-26S proteasome-dependent degradation. As visualized by electron microscopy, p53 binds with high affinity to the native CSN complex. p53 interacts via its N-terminus with CSN subunit 5/Jab1 as shown by far-western and pull-down assays. The CSN-specific phosphorylation sites were mapped to the core domain of p53 including Thr155. A phosphorylated peptide, Deltap53(145-164), specifically inhibits CSN-mediated phosphorylation and p53 degradation. Curcumin, a CSN kinase inhibitor, blocks E6-dependent p53 degradation in reticulocyte lysates. Mutation of Thr155 to valine is sufficient to stabilize p53 against E6-dependent degradation in reticulocyte lysates and to reduce binding to Mdm2. The p53T155V mutant accumulates in both HeLa and HL 60 cells and exhibits a mutant (PAb 240+) conformation. It induces the cyclin-dependent inhibitor p21. In HeLa and MCF-7 cells, inhibition of CSN kinase by curcumin or Deltap53(145-164) results in accumulation of endogenous p53."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/20.7.1630"xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/20.7.1630"xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Huang X."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Huang X."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Kraft R."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Kraft R."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Henklein P."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Henklein P."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Pollmann C."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Pollmann C."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Dubiel W."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Dubiel W."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Bech-Otschir D."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Bech-Otschir D."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Kapelari B."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/author | "Kapelari B."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/pages | "1630-1639"xsd:string |
| http://purl.uniprot.org/citations/11285227 | http://purl.uniprot.org/core/pages | "1630-1639"xsd:string |