PIGK: Difference between revisions

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{{Infobox_gene}}
{{Infobox_gene}}
'''GPI-anchor transamidase''' is an [[enzyme]] that in humans is encoded by the ''PIGK'' [[gene]].<ref name="pmid9356492">{{cite journal |vauthors=Yu J, Nagarajan S, Knez JJ, Udenfriend S, Chen R, Medof ME | 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 |date=December 1997 | pmid = 9356492 | pmc = 25045 | doi =10.1073/pnas.94.23.12580  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PIGK phosphatidylinositol glycan anchor biosynthesis, class K| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10026| accessdate = }}</ref>
'''GPI-anchor transamidase''' is an [[enzyme]] that in humans is encoded by the ''PIGK'' [[gene]].<ref name="pmid9356492">{{cite journal |vauthors=Yu J, Nagarajan S, Knez JJ, Udenfriend S, Chen R, Medof ME | 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 |date=December 1997 | pmid = 9356492 | pmc = 25045 | doi =10.1073/pnas.94.23.12580  | bibcode =1997PNAS...9412580Y }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PIGK phosphatidylinositol glycan anchor biosynthesis, class K| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10026| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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.<ref name="entrez"/>
| 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.<ref name="entrez"/>
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*{{cite journal  |vauthors=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  | pmc=149153 }}
*{{cite journal  |vauthors=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  | pmc=149153 }}
*{{cite journal  |vauthors=Vainauskas S, Maeda Y, Kurniawan H, etal |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  |vauthors=Vainauskas S, Maeda Y, Kurniawan H, etal |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  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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  | pmc=139241 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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  | pmc=139241 |bibcode=2002PNAS...9916899M }}
*{{cite journal  |vauthors=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  |vauthors=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  |vauthors=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  |vauthors=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  |vauthors=Hong Y, Ohishi K, Kang JY, etal |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  | pmc=165076 }}
*{{cite journal  |vauthors=Hong Y, Ohishi K, Kang JY, etal |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  | pmc=165076 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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  | pmc=528928 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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  | pmc=528928 }}
*{{cite journal  |vauthors=Rual JF, Venkatesan K, Hao T, etal |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  |vauthors=Rual JF, Venkatesan K, Hao T, etal |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 |bibcode=2005Natur.437.1173R }}
*{{cite journal  |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |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  | pmc=1356129 }}
*{{cite journal  |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |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  | pmc=1356129 }}
*{{cite journal  |vauthors=Gregory SG, Barlow KF, McLay KE, etal |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 }}
*{{cite journal  |vauthors=Gregory SG, Barlow KF, McLay KE, etal |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 |bibcode=2006Natur.441..315G }}
}}
}}
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Latest revision as of 00:12, 19 July 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

GPI-anchor transamidase is an enzyme that in humans is encoded by the PIGK gene.[1][2]

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.[2]

Interactions

PIGK has been shown to interact with PIGT[3] and GPAA1.[4][5]

References

  1. ↑ Yu J, Nagarajan S, Knez JJ, Udenfriend S, Chen R, Medof ME (December 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. Bibcode:1997PNAS...9412580Y. doi:10.1073/pnas.94.23.12580. PMC 25045. PMID 9356492.
  2. ↑ 2.0 2.1 "Entrez Gene: PIGK phosphatidylinositol glycan anchor biosynthesis, class K".
  3. ↑ Ohishi, Kazuhito; Nagamune Kisaburo; Maeda Yusuke; Kinoshita Taroh (April 2003). "Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge". J. Biol. Chem. United States. 278 (16): 13959–67. doi:10.1074/jbc.M300586200. ISSN 0021-9258. PMID 12582175.
  4. ↑ Ohishi, K; Inoue N; Maeda Y; Takeda J; Riezman H; Kinoshita T (May 2000). "Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins". Mol. Biol. Cell. UNITED STATES. 11 (5): 1523–33. doi:10.1091/mbc.11.5.1523. ISSN 1059-1524. PMC 14864. PMID 10793132.
  5. ↑ Vainauskas, Saulius; Maeda Yusuke; Kurniawan Henry; Kinoshita Taroh; Menon Anant K (August 2002). "Structural requirements for the recruitment of Gaa1 into a functional glycosylphosphatidylinositol transamidase complex". J. Biol. Chem. United States. 277 (34): 30535–42. doi:10.1074/jbc.M205402200. ISSN 0021-9258. PMID 12052837.

Further reading

External links



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