PIGK

Phosphatidylinositol glycan anchor biosynthesis, class K
Identifiers
Symbols	PIGK ; GPI8; MGC22559
External IDs	Template:OMIM5 Template:MGI HomoloGene: 4002
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE PIGK 209707 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Phosphatidylinositol glycan anchor biosynthesis, class K, also known as PIGK, is a human gene.

This gene encodes a member of the cysteine protease family C13 that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is a member of the multisubunit enzyme, GPI transamidase and is thought to be its enzymatic component. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins.

Further reading

• Benghezal M, Benachour A, Rusconi S; et al. (1997). "Yeast Gpi8p is essential for GPI anchor attachment onto proteins". EMBO J. 15 (23): 6575–83. PMID 8978684.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yu J, Nagarajan S, Knez JJ; et al. (1997). "The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase". Proc. Natl. Acad. Sci. U.S.A. 94 (23): 12580–5. PMID 9356492.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Meyer U, Benghezal M, Imhof I, Conzelmann A (2000). "Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins". Biochemistry. 39 (12): 3461–71. PMID 10727241.CS1 maint: Multiple names: authors list (link)
• Ohishi K, Inoue N, Maeda Y; et al. (2000). "Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins". Mol. Biol. Cell. 11 (5): 1523–33. PMID 10793132.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Spurway TD, Dalley JA, High S, Bulleid NJ (2001). "Early events in glycosylphosphatidylinositol anchor addition. substrate proteins associate with the transamidase subunit gpi8p". J. Biol. Chem. 276 (19): 15975–82. doi:10.1074/jbc.M010128200. PMID 11278620.CS1 maint: Multiple names: authors list (link)
• Ohishi K, Inoue N, Kinoshita T (2001). "PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8". EMBO J. 20 (15): 4088–98. doi:10.1093/emboj/20.15.4088. PMID 11483512.CS1 maint: Multiple names: authors list (link)
• Vainauskas S, Maeda Y, Kurniawan H; et al. (2002). "Structural requirements for the recruitment of Gaa1 into a functional glycosylphosphatidylinositol transamidase complex". J. Biol. Chem. 277 (34): 30535–42. doi:10.1074/jbc.M205402200. PMID 12052837.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ohishi K, Nagamune K, Maeda Y, Kinoshita T (2003). "Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge". J. Biol. Chem. 278 (16): 13959–67. doi:10.1074/jbc.M300586200. PMID 12582175.CS1 maint: Multiple names: authors list (link)
• Chen R, Anderson V, Hiroi Y, Medof ME (2003). "Proprotein interaction with the GPI transamidase". J. Cell. Biochem. 88 (5): 1025–37. doi:10.1002/jcb.10439. PMID 12616539.CS1 maint: Multiple names: authors list (link)
• Hong Y, Ohishi K, Kang JY; et al. (2004). "Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins". Mol. Biol. Cell. 14 (5): 1780–9. doi:10.1091/mbc.E02-12-0794. PMID 12802054.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kimura K, Wakamatsu A, Suzuki Y; et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)