PIGS (genetics)

PIGS (genetics)

Phosphatidylinositol glycan anchor biosynthesis, class S, also known as PIGS, is a human gene.cite web | title = Entrez Gene: PIGS phosphatidylinositol glycan anchor biosynthesis, class S| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=94005| accessdate = ] PBB_Summary
section_title =
summary_text = This gene encodes a protein that is involved in GPI-anchor biosynthesis. The glycosylphosphatidylinositol (GPI) anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This gene encodes an essential component of the multisubunit enzyme, GPI transamidase. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins.cite web | title = Entrez Gene: PIGS phosphatidylinositol glycan anchor biosynthesis, class S| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=94005| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Ohishi K, Inoue N, Kinoshita T |title=PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. |journal=EMBO J. |volume=20 |issue= 15 |pages= 4088-98 |year= 2001 |pmid= 11483512 |doi= 10.1093/emboj/20.15.4088
*cite journal | author=Vainauskas S, Maeda Y, Kurniawan H, "et al." |title=Structural requirements for the recruitment of Gaa1 into a functional glycosylphosphatidylinositol transamidase complex. |journal=J. Biol. Chem. |volume=277 |issue= 34 |pages= 30535-42 |year= 2002 |pmid= 12052837 |doi= 10.1074/jbc.M205402200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ohishi K, Nagamune K, Maeda Y, Kinoshita T |title=Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge. |journal=J. Biol. Chem. |volume=278 |issue= 16 |pages= 13959-67 |year= 2003 |pmid= 12582175 |doi= 10.1074/jbc.M300586200
*cite journal | author=Hong Y, Ohishi K, Kang JY, "et al." |title=Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins. |journal=Mol. Biol. Cell |volume=14 |issue= 5 |pages= 1780-9 |year= 2004 |pmid= 12802054 |doi= 10.1091/mbc.E02-12-0794
*cite journal | author=Clark HF, Gurney AL, Abaya E, "et al." |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Vainauskas S, Menon AK |title=Endoplasmic reticulum localization of Gaa1 and PIG-T, subunits of the glycosylphosphatidylinositol transamidase complex. |journal=J. Biol. Chem. |volume=280 |issue= 16 |pages= 16402-9 |year= 2005 |pmid= 15713669 |doi= 10.1074/jbc.M414253200
*cite journal | author=Otsuki T, Ota T, Nishikawa T, "et al." |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117-26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117

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