| http://purl.uniprot.org/citations/12186903 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12186903 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12186903 | http://www.w3.org/2000/01/rdf-schema#comment | "During the early phase of infection, the E1B-55K protein of adenovirus type 5 (Ad5) counters the E1A-induced stabilization of p53, whereas in the late phase, E1B-55K modulates the preferential nucleocytoplasmic transport and translation of the late viral mRNAs. The mechanism(s) by which E1B-55K performs these functions has not yet been clearly elucidated. In this study, we have taken a proteomics-based approach to identify and characterize novel E1B-55K-associated proteins. A multiprotein E1B-55K-containing complex was immunopurified from Ad5-infected HeLa cells and found to contain E4-orf6, as well as several cellular factors previously implicated in the ubiquitin-proteasome-mediated destruction of proteins, including Cullin-5, Rbx1/ROC1/Hrt1, and Elongins B and C. We further demonstrate that a complex containing these as well as other proteins is capable of directing the polyubiquitination of p53 in vitro. These ubiquitin ligase components were found in a high-molecular-mass complex of 800 to 900 kDa. We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation. We further suggest that E1B-55K functions as the principal substrate recognition component of this SCF-type ubiquitin ligase, whereas E4-orf6 may serve to nucleate the assembly of the complex. Lastly, we describe the identification and characterization of two novel E1B-55K interacting factors, importin-alpha 1 and pp32, that may also participate in the functions previously ascribed to E1B-55K and E4-orf6."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.76.18.9194-9206.2002"xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.76.18.9194-9206.2002"xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/author | "Pallas D.C."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/author | "Pallas D.C."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/author | "Shevchenko A."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/author | "Shevchenko A."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/author | "Berk A.J."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/author | "Berk A.J."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/author | "Shevchenko A.'"xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/author | "Shevchenko A.'"xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/author | "Harada J.N."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/author | "Harada J.N."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/name | "J. Virol."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/name | "J. Virol."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/pages | "9194-9206"xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/pages | "9194-9206"xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/title | "Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/title | "Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery."xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/volume | "76"xsd:string |
| http://purl.uniprot.org/citations/12186903 | http://purl.uniprot.org/core/volume | "76"xsd:string |