RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/15635094http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15635094http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15635094http://www.w3.org/2000/01/rdf-schema#comment"Within the endoplasmic reticulum (ER), mannoses and glucoses, donated from dolichol-phosphate-mannose and -glucose, are transferred to N-glycan and GPI-anchor precursors, and serine/threonine residues in many proteins. Glycosyltransferases that mediate these reactions are ER-resident multitransmembrane proteins with common characteristics, forming a superfamily of >10 enzymes. Here, we report an essential component of glycosylphosphatidylinositol-mannosyltransferase I (GPI-MT-I), which transfers the first of the four mannoses in the GPI-anchor precursors. We isolated a Chinese hamster ovary (CHO) cell mutant defective in GPI-MT-I but not its catalytic component PIG-M. The mutant gene, termed phosphatidylinositolglycan-class X (PIG-X), encoded a 252-amino acid ER-resident type I transmembrane protein with a large lumenal domain. PIG-X and PIG-M formed a complex, and PIG-M expression was <10% in the absence of PIG-X, indicating that PIG-X stabilizes PIG-M. We found that Saccharomyces cerevisiae Pbn1p/YCL052Cp, which was previously reported to be involved in autoprocessing of proproteinase B, is the functional homologue of PIG-X; Pbn1p is critical for Gpi14p/YJR013Wp function, the yeast homologue of PIG-M. This is the first report of an essential subcomponent of glycosyltransferases using dolichol-phosphate-monosaccharide."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e04-09-0802"xsd:string
http://purl.uniprot.org/citations/15635094http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e04-09-0802"xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Hong Y."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Hong Y."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Murakami Y."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Murakami Y."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Maeda Y."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Maeda Y."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Sugimoto N."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Sugimoto N."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Ashida H."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Ashida H."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Shishioh N."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Shishioh N."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Kim Y.U."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/author"Kim Y.U."xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/15635094http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string