http://purl.uniprot.org/citations/12402045 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12402045 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12402045 | http://www.w3.org/2000/01/rdf-schema#comment | "Ubiquitin-mediated proteolysis of securin and mitotic cyclins is essential for exit from mitosis. The final step in ubiquitination of these and other proteins is catalysed by the anaphase-promoting complex (APC), a multi-subunit ubiquitin-protein ligase (E3). Little is known about the molecular reaction resulting in APC-dependent substrate ubiquitination or the role of individual APC subunits in the reaction. Using a well-defined in vitro system, we show that highly purified APC from Saccharomyces cerevisiae ubiquitinates a model cyclin substrate in a processive manner. Analysis of mutant APC lacking the Doc1/Apc10 subunit (APC(doc1 Delta)) indicates that Doc1 is required for processivity. The specific molecular defect in APC(doc1 Delta) is identified by a large increase in apparent K(M) for the cyclin substrate relative to the wild-type enzyme. This suggests that Doc1 stimulates processivity by limiting substrate dissociation. Addition of recombinant Doc1 to APC(doc1 Delta) fully restores enzyme function. Doc1-related domains are found in mechanistically distinct ubiquitin-ligase enzymes and may generally stimulate ubiquitination by contributing to substrate-enzyme affinity."xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb871"xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb871"xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/author | "Morgan D.O."xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/author | "Morgan D.O."xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/author | "Carroll C.W."xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/author | "Carroll C.W."xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/pages | "880-887"xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/pages | "880-887"xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/title | "The Doc1 subunit is a processivity factor for the anaphase-promoting complex."xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/title | "The Doc1 subunit is a processivity factor for the anaphase-promoting complex."xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/volume | "4"xsd:string |
http://purl.uniprot.org/citations/12402045 | http://purl.uniprot.org/core/volume | "4"xsd:string |
http://purl.uniprot.org/citations/12402045 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12402045 |
http://purl.uniprot.org/citations/12402045 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12402045 |
http://purl.uniprot.org/citations/12402045 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12402045 |
http://purl.uniprot.org/citations/12402045 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12402045 |
http://purl.uniprot.org/uniprot/P53068 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12402045 |
http://purl.uniprot.org/uniprot/P53068#attribution-2913960051F704A28107982C2E6AF739 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/12402045 |