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http://purl.uniprot.org/citations/17023019http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17023019http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17023019http://www.w3.org/2000/01/rdf-schema#comment"The cellular E3 ubiquitin ligase E6AP (UBE3A) interacts with the cancer-associated HPV E6 oncoproteins, where together with the viral E6 oncoprotein it binds and targets the degradation of the p53 tumor suppressor. We find that the HPV-11E6 protein also associates with E6AP in vivo, and thereby can target the degradation of an E6-associated protein. Mutation of an E6-binding LXXLL peptide motif on E6AP eliminated the association, revealing a common mode of interaction between high- and low-risk E6 proteins and E6AP. E6AP was required for the in vivo degradation of DLG1 by both HVP-18 E6 and a chimeric HPV-11E6. The common functional interaction of both cancer-associated and non-cancer-associated E6 proteins with E6AP establishes a common mechanism for E6 proteins trophic to mucosal squamous epithelium."xsd:string
http://purl.uniprot.org/citations/17023019http://purl.org/dc/terms/identifier"doi:10.1016/j.virol.2006.08.038"xsd:string
http://purl.uniprot.org/citations/17023019http://purl.org/dc/terms/identifier"doi:10.1016/j.virol.2006.08.038"xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/author"Lyons C."xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/author"Lyons C."xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/author"Brimer N."xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/author"Brimer N."xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/author"Vande Pol S.B."xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/author"Vande Pol S.B."xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/name"Virology"xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/name"Virology"xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/pages"303-310"xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/pages"303-310"xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/title"Association of E6AP (UBE3A) with human papillomavirus type 11 E6 protein."xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/title"Association of E6AP (UBE3A) with human papillomavirus type 11 E6 protein."xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/volume"358"xsd:string
http://purl.uniprot.org/citations/17023019http://purl.uniprot.org/core/volume"358"xsd:string
http://purl.uniprot.org/citations/17023019http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17023019
http://purl.uniprot.org/citations/17023019http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17023019
http://purl.uniprot.org/citations/17023019http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17023019
http://purl.uniprot.org/citations/17023019http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17023019