http://purl.uniprot.org/citations/9463366 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9463366 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9463366 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
http://purl.uniprot.org/citations/9463366 | http://www.w3.org/2000/01/rdf-schema#comment | "Biosynthesis of glycosylphosphatidylinositol (GPI) is initiated by transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to phosphatidylinositol (PI). This chemically simple step is genetically complex because three genes are required in both mammals and yeast. Mammalian PIG-A and PIG-C are homologous to yeast GPI3 and GPI2, respectively; however, mammalian PIG-H is not homologous to yeast GPI1. Here, we report cloning of a human homolog of GPI1 (hGPI1) and demonstrate that four mammalian gene products form a protein complex in the endoplasmic reticulum membrane. PIG-L, which is involved in the second step in GPI synthesis, GlcNAc-PI de-N-acetylation, did not associate with the isolated complex. The protein complex had GPI-GlcNAc transferase (GPI-GnT) activity in vitro, but did not mediate the second reaction. Bovine PI was utilized approximately 100-fold more efficiently than soybean PI as a substrate, and lyso PI was a very inefficient substrate. These results suggest that GPI-GnT recognizes the fatty acyl chains of PI. The unusually complex organization of GPI-GnT may be relevant to selective usage of PI and/or regulation."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/17.4.877"xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/17.4.877"xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Inoue N."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Inoue N."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Takeda J."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Takeda J."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Kinoshita T."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Kinoshita T."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Watanabe R."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Watanabe R."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Taron C.H."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Taron C.H."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Orlean P."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Orlean P."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Westfall B."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/author | "Westfall B."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
http://purl.uniprot.org/citations/9463366 | http://purl.uniprot.org/core/pages | "877-885"xsd:string |