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edit Phosphatidylinositol glycan anchor biosynthesis, class H Identifiers Symbols PIGH; GPI-H External IDs OMIM: 600154 MGI: 99463 HomoloGene: 3361 GeneCards: PIGH Gene Gene Ontology Molecular function • transferase activity, transferring glycosyl groups • phosphatidylinositol N-acetylglucosaminyltransferase activity Cellular component • endoplasmic reticulum Biological process • protein modification process • GPI anchor biosynthetic process Sources: Amigo / QuickGO RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 5283 110417 Ensembl ENSG00000100564 ENSMUSG00000021120 UniProt Q14442 n/a RefSeq (mRNA) NM_004569 NM_029988 RefSeq (protein) NP_004560 NP_084264 Location (UCSC) Chr 14: 67.13 - 67.14 Mb Chr 12: 80 - 80.01 Mb PubMed search [1] [2] Phosphatidylinositol N-acetylglucosaminyltransferase subunit H is an enzyme that in humans is encoded by the PIGH gene.[1][2] 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.[2] Interactions PIGH has been shown to interact with PIGQ.[3] References ^ Ware RE, Howard TA, Kamitani T, Change HM, Yeh ET, Seldin MF (Jul 1994). "Chromosomal assignment of genes involved in glycosylphosphatidylinositol anchor biosynthesis: implications for the pathogenesis of paroxysmal nocturnal hemoglobinuria". Blood 83 (12): 3753–7. PMID 8204896.  ^ a b "Entrez Gene: PIGH phosphatidylinositol glycan anchor biosynthesis, class H". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5283.  ^ Watanabe, R; Inoue N, Westfall B, Taron C H, Orlean P, Takeda J, Kinoshita T (Feb. 1998). "The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1". EMBO J. (ENGLAND) 17 (4): 877–85. doi:10.1093/emboj/17.4.877. ISSN 0261-4189. PMID 9463366.  Further reading Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.  Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.  Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions.". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMID 15342556.  Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.  Watanabe R, Inoue N, Westfall B, et al. (1998). "The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1.". EMBO J. 17 (4): 877–85. doi:10.1093/emboj/17.4.877. PMID 9463366.  Watanabe R, Kinoshita T, Masaki R, et al. (1996). "PIG-A and PIG-H, which participate in glycosylphosphatidylinositol anchor biosynthesis, form a protein complex in the endoplasmic reticulum.". J. Biol. Chem. 271 (43): 26868–75. doi:10.1074/jbc.271.43.26868. PMID 8900170.  Kamitani T, Chang HM, Rollins C, et al. (1993). "Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk- cells by a human cDNA clone.". J. Biol. Chem. 268 (28): 20733–6. PMID 8407896.  This article on a gene on chromosome 14 is a stub. You can help Wikipedia by expanding it. v • d • e