RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/17721809http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17721809http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17721809http://www.w3.org/2000/01/rdf-schema#comment"Ubiquitylation appears to be involved in the membrane trafficking system including endocytosis, exocytosis, and ER-to-Golgi transport. We found that PIRH2, which was identified as an interacting protein for androgen receptor or p53, interacts with and ubiquitylates the epsilon-subunit of coatmer complex, epsilon-COP. PIRH2 promotes the ubiquitylation of epsilon-COP in vitro and in vivo and consequently promotes the degradation of epsilon-COP. The interaction between PIRH2 and epsilon-COP is affected by the presence of androgen, and PIRH2 in the presence of androgen promotes ubiquitylation of epsilon-COP in vivo. Furthermore, overexpression of the wild type of PIRH2 in prostate cancer cells causes downregulation of the secretion of prostate-specific antigen (PSA), a secretory protein in prostate epithelial cells and one of diagnostic markers for prostate cancer. Our results indicate that PIRH2 functions as a regulator for COP I complex."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.org/dc/terms/identifier"doi:10.1007/s11010-007-9586-3"xsd:string
http://purl.uniprot.org/citations/17721809http://purl.org/dc/terms/identifier"doi:10.1007/s11010-007-9586-3"xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Maruyama S."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Maruyama S."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Miyajima N."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Miyajima N."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Tsukiyama T."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Tsukiyama T."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Bohgaki M."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Bohgaki M."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Hatakeyama S."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Hatakeyama S."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Nonomura K."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Nonomura K."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Shigemura M."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/author"Shigemura M."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/name"Mol. Cell. Biochem."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/name"Mol. Cell. Biochem."xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/pages"73-82"xsd:string
http://purl.uniprot.org/citations/17721809http://purl.uniprot.org/core/pages"73-82"xsd:string