Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-10-22
pubmed:databankReference
pubmed:abstractText
Glycosylphosphatidylinositol (GPI) protein anchors are ubiquitous in eukaryotic cells. GPI anchors are synthesized in the endoplasmic reticulum by actions of ten or more gene products. The first step of the biosynthesis, the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, is mediated by at least three genes in mammalian cells (PIG-A, PIG-H and PIG-C) and in yeast (GPI1, GPI2 and GPI3/SPT14/CWH6). PIG-A is homologous to GPI3/SPTI4/CWH6. However, PIG-H has no homology with GPI1 or GPI2. Here we cloned a human homologue of GPI2 and showed that it is PIG-C. PIG-C protein is a 297 amino-acid membrane protein in the endoplasmic reticulum that has 20% amino acid identity with GPI2. Since there are several human EST sequences that have homology to GPI1, our results suggest that four genes are involved in the first step of GPI anchor synthesis in mammalian cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
226
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2.
pubmed:affiliation
Department of Immunoregulation, Osaka University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't