| http://purl.uniprot.org/citations/17452440 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17452440 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17452440 | http://www.w3.org/2000/01/rdf-schema#comment | "DET1 (de-etiolated 1) is an essential negative regulator of plant light responses, and it is a component of the Arabidopsis thaliana CDD complex containing DDB1 and COP10 ubiquitin E2 variant. Human DET1 has recently been isolated as one of the DDB1- and Cul4A-associated factors, along with an array of WD40-containing substrate receptors of the Cul4A-DDB1 ubiquitin ligase. However, DET1 differs from conventional substrate receptors of cullin E3 ligases in both biochemical behavior and activity. Here we report that mammalian DET1 forms stable DDD-E2 complexes, consisting of DDB1, DDA1 (DET1, DDB1 associated 1), and a member of the UBE2E group of canonical ubiquitin-conjugating enzymes. DDD-E2 complexes interact with multiple ubiquitin E3 ligases. We show that the E2 component cannot maintain the ubiquitin thioester linkage once bound to the DDD core, rendering mammalian DDD-E2 equivalent to the Arabidopsis CDD complex. While free UBE2E-3 is active and able to enhance UbcH5/Cul4A activity, the DDD core specifically inhibits Cul4A-dependent polyubiquitin chain assembly in vitro. Overexpression of DET1 inhibits UV-induced CDT1 degradation in cultured cells. These findings demonstrate that the conserved DET1 complex modulates Cul4A functions by a novel mechanism."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.02432-06"xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.02432-06"xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Deng X.W."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Deng X.W."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Tong Y."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Tong Y."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Tsuge T."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Tsuge T."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Menon S."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Menon S."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Dohmae N."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Dohmae N."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Wei N."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Wei N."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Lau O.-S."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Lau O.-S."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Pick E."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Pick E."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Plafker S.M."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/author | "Plafker S.M."xsd:string |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17452440 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |