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http://purl.uniprot.org/citations/11226175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11226175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11226175http://www.w3.org/2000/01/rdf-schema#comment"Glycosylphosphatidylinositol (GPI) acts as a membrane anchor of many cell surface proteins. Its structure and biosynthetic pathway are generally conserved among eukaryotic organisms, with a number of differences. In particular, mammalian and protozoan mannosyltransferases needed for addition of the first mannose (GPI-MT-I) have different substrate specificities and are targets of species-specific inhibitors of GPI biosynthesis. GPI-MT-I, however, has not been molecularly characterized. Characterization of GPI-MT-I would also help to clarify the topology of GPI biosynthesis. Here, we report a human cell line defective in GPI-MT-I and the gene responsible, PIG-M. PIG-M encodes a new type of mannosyltransferase of 423 amino acids, bearing multiple transmembrane domains. PIG-M has a functionally important DXD motif, a characteristic of many glycosyltransferases, within a domain facing the lumen of the endoplasmic reticulum (ER), indicating that transfer of the first mannose to GPI occurs on the lumenal side of the ER membrane."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.org/dc/terms/identifier"doi:10.1093/emboj/20.1.250"xsd:string
http://purl.uniprot.org/citations/11226175http://purl.org/dc/terms/identifier"doi:10.1093/emboj/20.1.250"xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Hong Y."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Hong Y."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Maeda Y."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Maeda Y."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Harris C.L."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Harris C.L."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Kinoshita K."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Kinoshita K."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Ohishi K."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Ohishi K."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Watanabe R."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/author"Watanabe R."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/pages"250-261"xsd:string
http://purl.uniprot.org/citations/11226175http://purl.uniprot.org/core/pages"250-261"xsd:string