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http://purl.uniprot.org/citations/2000150http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2000150http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2000150http://www.w3.org/2000/01/rdf-schema#comment"Secretory-protein translocation into the endoplasmic reticulum (ER) is thought to be catalysed by integral membrane proteins. Genetic selections uncovered three Saccharomyces cerevisiae genes (SEC61, SEC62 and SEC63), mutations in which block import of precursor proteins into the ER lumen in vivo and in vitro. The DNA sequences of SEC62 and SEC63 predict multispanning membrane proteins, and biochemical characterization of the SEC62 protein (Sec62) confirms that it is an integral ER membrane protein. Here we show that Sec61, Sec62 and Sec63 are assembled with two additional proteins into a multisubunit membrane-associated complex. These results confirm previous predictions, based upon genetic interactions between the SEC genes, that Sec61, Sec62 and Sec63 act together to facilitate protein translocation into the ER."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.org/dc/terms/identifier"doi:10.1038/349806a0"xsd:string
http://purl.uniprot.org/citations/2000150http://purl.org/dc/terms/identifier"doi:10.1038/349806a0"xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/author"Schekman R."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/author"Schekman R."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/author"Deshaies R.J."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/author"Deshaies R.J."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/author"Sanders S.L."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/author"Sanders S.L."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/author"Feldheim D.A."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/author"Feldheim D.A."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/pages"806-808"xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/pages"806-808"xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/title"Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/title"Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex."xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/volume"349"xsd:string
http://purl.uniprot.org/citations/2000150http://purl.uniprot.org/core/volume"349"xsd:string
http://purl.uniprot.org/citations/2000150http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2000150
http://purl.uniprot.org/citations/2000150http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2000150