PIGK

Phosphatidylinositol glycan anchor biosynthesis, class K, also known as PIGK, is a human gene.cite web | title = Entrez Gene: PIGK phosphatidylinositol glycan anchor biosynthesis, class K| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10026| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: PIGK phosphatidylinositol glycan anchor biosynthesis, class K| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10026| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Benghezal M, Benachour A, Rusconi S, "et al." |title=Yeast Gpi8p is essential for GPI anchor attachment onto proteins. |journal=EMBO J. |volume=15 |issue= 23 |pages= 6575–83 |year= 1997 |pmid= 8978684 |doi=
*cite journal | author=Yu J, Nagarajan S, Knez JJ, "et al." |title=The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 23 |pages= 12580–5 |year= 1997 |pmid= 9356492 |doi=
*cite journal | author=Meyer U, Benghezal M, Imhof I, Conzelmann A |title=Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins. |journal=Biochemistry |volume=39 |issue= 12 |pages= 3461–71 |year= 2000 |pmid= 10727241 |doi=
*cite journal | author=Ohishi K, Inoue N, Maeda Y, "et al." |title=Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins. |journal=Mol. Biol. Cell |volume=11 |issue= 5 |pages= 1523–33 |year= 2000 |pmid= 10793132 |doi=
*cite journal | author=Spurway TD, Dalley JA, High S, Bulleid NJ |title=Early events in glycosylphosphatidylinositol anchor addition. substrate proteins associate with the transamidase subunit gpi8p. |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 15975–82 |year= 2001 |pmid= 11278620 |doi= 10.1074/jbc.M010128200
*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=Chen R, Anderson V, Hiroi Y, Medof ME |title=Proprotein interaction with the GPI transamidase. |journal=J. Cell. Biochem. |volume=88 |issue= 5 |pages= 1025–37 |year= 2003 |pmid= 12616539 |doi= 10.1002/jcb.10439
*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=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=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, "et al." |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406
*cite journal | author=Gregory SG, Barlow KF, McLay KE, "et al." |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727

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