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Phosphatidylinositol glycan anchor biosynthesis, class H

This gene encodes an endoplasmic reticulum associated protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI anchor is a glycolipid found on many blood cells and which serves to anchor proteins to the cell surface. The protein encoded by this gene is a subunit of the GPI N-acetylglucosaminyl (GlcNAc) transferase that transfers GlcNAc to phosphatidylinositol (PI) on the cytoplasmic side of the endoplasmic reticulum. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: GPI2, STEP, DSCR5, CAN, SIMPLE
Papers on PIG-H
Genome-wide next-generation DNA and RNA sequencing reveals a mutation that perturbs splicing of the phosphatidylinositol glycan anchor biosynthesis class H gene (PIGH) and causes arthrogryposis in Belgian Blue cattle.
Charlier et al., Liège, Belgium. In Bmc Genomics, 2014
By analyzing RNA-Seq data from a carrier fetus, we observe skipping of the second exon of the PIGH gene, which we confirm by RT-PCR to be fully penetrant in tissues from affected calves.
Challenging single- and multi-probesets gene expression signatures of pathological complete response to neoadjuvant chemotherapy in breast cancer: experience of the REMAGUS 02 phase II trial.
Asselain et al., Paris, France. In Breast, 2013
Models including probesets associated with ESR1, MAPT, CA12 or PIGH presented good classification performances.
Two populations of double minute chromosomes harbor distinct amplicons, the MYC locus at 8q24.2 and a 0.43-Mb region at 14q24.1, in the SW613-S human carcinoma cell line.
Bernheim et al., Villejuif, France. In Cytogenet Genome Res, 2008
The 0.43-Mb amplified and overexpressed region contains the PLEK2, PIGH, ARG2, VTI1B, RDH11, and ZFYVE26 genes.
Gpi19, the Saccharomyces cerevisiae homologue of mammalian PIG-P, is a subunit of the initial enzyme for glycosylphosphatidylinositol anchor biosynthesis.
Levin et al., Baltimore, United States. In Eukaryot Cell, 2005
The human enzyme has six known subunits, at least four of which, GPI1, PIG-A, PIG-C, and PIG-H, have functional homologs in the budding yeast Saccharomyces cerevisiae.
The human GPI1 gene is required for efficient glycosylphosphatidylinositol biosynthesis.
Schubert et al., Hannover, Germany. In Gene, 2001
Six human genes encode subunits of this enzyme, namely PIG-A, PIG-C, PIG-H, PIG-P, GPI1, and DPM2.
Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2.
Kinoshita et al., Suita, Japan. In Embo J, 2000
Biosynthesis of GPI is initiated by GPI-N-acetylglucosaminyltransferase (GPI-GnT), which transfers N-acetylglucosamine from UDP- N-acetylglucosamine to phosphatidylinositol. GPI-GnT is a uniquely complex glycosyltransferase, consisting of at least four proteins, PIG-A, PIG-H, PIG-C and GPI1.
Characterisation of the enzymatic complex for the first step in glycosylphosphatidylinositol biosynthesis.
Schmidt et al., Hannover, Germany. In Int J Biochem Cell Biol, 2000
The mammalian N-acetylglucosaminyl transferase for the first step in glycosylphosphatidylinositol biosynthesis has been shown to consist of at least four components: PIG-A, PIG-C, PIG-H and GPI1.
GPI1 stabilizes an enzyme essential in the first step of glycosylphosphatidylinositol biosynthesis.
Kinoshita et al., Ōsaka, Japan. In J Biol Chem, 1999
In mammalian cells, this reaction is mediated by a complex of PIG-A, PIG-H, PIG-C, and GPI1.
Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol membrane anchor biosynthesis in yeast mutants.
Schmidt et al., Hannover, Germany. In Biochem J, 1998
The products of three mammalian genes, PIG-A, PIG-C and PIG-H, have previously been shown to be involved in the putative enzymic complex.
The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1.
Kinoshita et al., Ōsaka, Japan. In Embo J, 1998
Mammalian PIG-A and PIG-C are homologous to yeast GPI3 and GPI2, respectively; however, mammalian PIG-H is not homologous to yeast GPI1.
Structures and chromosomal localizations of the glycosylphosphatidylinositol synthesis gene PIGC and its pseudogene PIGCP1.
Kinoshita et al., Ōsaka, Japan. In Genomics, 1997
Consistent with this notion, three other genes, PIGB, PIGF, and PIGH, are autosomal.
PIG-A and PIG-H, which participate in glycosylphosphatidylinositol anchor biosynthesis, form a protein complex in the endoplasmic reticulum.
Inoue et al., Suita, Japan. In J Biol Chem, 1996
To clarify this complexity, we analyzed the products of two cloned human genes, PIG-A and PIG-H.
PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2.
Kinoshita et al., Ōsaka, Japan. In Biochem Biophys Res Commun, 1996
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).
Chromosomal assignment of genes involved in glycosylphosphatidylinositol anchor biosynthesis: implications for the pathogenesis of paroxysmal nocturnal hemoglobinuria.
Seldin et al., Durham, United States. In Blood, 1994
In the current study, the chromosomal assignment of Piga, as well as of Pigf and Pigh, two additional genes involved in GPI-anchor biosynthesis, has been established using a mouse interspecific backcross mapping technique.
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