| http://purl.uniprot.org/citations/18206966 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18206966 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/18206966 | http://www.w3.org/2000/01/rdf-schema#comment | "Cullin-based E3 ubiquitin ligases are activated through modification of the cullin subunit with the ubiquitin-like protein Nedd8. Dcn1 regulates cullin neddylation and thus ubiquitin ligase activity. Here we describe the 1.9 A X-ray crystal structure of yeast Dcn1 encompassing an N-terminal ubiquitin-binding (UBA) domain and a C-terminal domain of unique architecture, which we termed PONY domain. A conserved surface on Dcn1 is required for direct binding to cullins and for neddylation. The reciprocal binding site for Dcn1 on Cdc53 is located approximately 18 A from the site of neddylation. Dcn1 does not require cysteine residues for catalytic function, and directly interacts with the Nedd8 E2 Ubc12 on a surface that overlaps with the E1-binding site. We show that Dcn1 is necessary and sufficient for cullin neddylation in a purified recombinant system. Taken together, these data demonstrate that Dcn1 is a scaffold-like E3 ligase for cullin neddylation."xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2007.12.012"xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/author | "Peter M."xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/author | "Sicheri F."xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/author | "Kurz T."xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/author | "Chou Y.C."xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/author | "Tyers M."xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/author | "Willems A.R."xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/author | "Meyer-Schaller N."xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/author | "Hecht M.L."xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/name | "Mol Cell"xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/pages | "23-35"xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/title | "Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation."xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://purl.uniprot.org/core/volume | "29"xsd:string |
| http://purl.uniprot.org/citations/18206966 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18206966 |
| http://purl.uniprot.org/citations/18206966 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18206966 |
| http://purl.uniprot.org/citations/18206966 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18206966 |
| http://purl.uniprot.org/citations/18206966 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18206966 |
| http://purl.uniprot.org/enzyme/2.3.2.32 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18206966 |
| http://purl.uniprot.org/uniprot/Q12395#attribution-0A1DA78C910290CBDA5E12CE27849DCD | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/18206966 |
| http://purl.uniprot.org/uniprot/Q12395#attribution-4F1115727B2E095C36729A2941478453 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/18206966 |
| http://purl.uniprot.org/uniprot/#_Q14145-mappedCitation-18206966 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18206966 |