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http://purl.uniprot.org/citations/9559540http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9559540http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9559540http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9559540http://www.w3.org/2000/01/rdf-schema#comment"Saccharomyces cerevisiae mutants lacking Scs7p fail to accumulate the inositolphosphorylceramide (IPC) species. IPC-C, which is the predominant form found in wild-type cells. Instead scs7 mutants accumulate an IPC-B species believed to be unhydroxylated on the amide-linked C26-fatty acid. Elimination of the SCS7 gene suppresses the Ca(2+)-sensitive phenotype of csg1 and csg2 mutants. The CSG1 and CSG2 genes are required for mannosylation of IPC-C and accumulation of IPC-C by the csg mutants renders them Ca(2+)-sensitive. The SCS7 gene encodes a protein that contains both a cytochrome b5-like domain and a domain that resembles the family of cytochrome b5-dependent enzymes that use iron and oxygen to catalyse desaturation or hydroxylation of fatty acids and sterols. Scs7p is therefore likely to be the enzyme that hydroxylates the C26-fatty acid of IPC-C."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.org/dc/terms/identifier"doi:10.1002/(sici)1097-0061(19980315)14:4<311::aid-yea220>3.0.co;2-b"xsd:string
http://purl.uniprot.org/citations/9559540http://purl.org/dc/terms/identifier"doi:10.1002/(sici)1097-0061(19980315)14:4<311::aid-yea220>3.0.co;2-b"xsd:string
http://purl.uniprot.org/citations/9559540http://purl.org/dc/terms/identifier"doi:10.1002/(sici)1097-0061(19980315)14:4<311::aid-yea220>3.0.co;2-b"xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/author"Beeler T.J."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/author"Beeler T.J."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/author"Dunn T.M."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/author"Dunn T.M."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/author"Monaghan E."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/author"Monaghan E."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/author"Haak D."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/author"Haak D."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/name"Yeast"xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/name"Yeast"xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/pages"311-321"xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/pages"311-321"xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/title"Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/title"Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain."xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/9559540http://purl.uniprot.org/core/volume"14"xsd:string