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http://purl.uniprot.org/citations/12778054http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12778054http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12778054http://www.w3.org/2000/01/rdf-schema#comment"Ubiquitination is important for a broad array of cellular functions. Although reversal of this process, de-ubiquitination, most probably represents an important regulatory step contributing to cellular homeostasis, the specificity and properties of de-ubiquitination enzymes remain poorly understood. Here, we show that the Saccharomyces cerevisiae ubiquitin protease Ubp3 requires an additional protein, Bre5, to form an active de-ubiquitination complex that cleaves ubiquitin from specific substrates. In particular, this complex rescues Sec23p, a COPII subunit essential for the transport between the endoplasmic reticulum and the Golgi apparatus, from degradation by the proteasome. This probably contributes to maintaining and adapting a Sec23 expression level that is compatible with an efficient secretion pathway, and consequently with cell growth and viability."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.org/dc/terms/identifier"doi:10.1038/ncb1003"xsd:string
http://purl.uniprot.org/citations/12778054http://purl.org/dc/terms/identifier"doi:10.1038/ncb1003"xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/author"Cohen M."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/author"Cohen M."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/author"Stutz F."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/author"Stutz F."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/author"Haguenauer-Tsapis R."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/author"Haguenauer-Tsapis R."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/author"Belgareh N."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/author"Belgareh N."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/author"Dargemont C."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/author"Dargemont C."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/pages"661-667"xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/pages"661-667"xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/title"Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/title"Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23."xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/12778054http://purl.uniprot.org/core/volume"5"xsd:string