PIGQ

Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q is an enzyme that in humans is encoded by the PIGQ gene.[5][6][7]

PIGQ
Identifiers
Aliases	PIGQ, GPI1, c407A10.1, phosphatidylinositol glycan anchor biosynthesis class Q, EIEE77
External IDs	OMIM: 605754 MGI: 1333114 HomoloGene: 31228 GeneCards: PIGQ
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 566,995 bp[1] End 584,136 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 A3.3 Start 25,926,421 bp[2] End 25,944,936 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • phosphatidylinositol N-acetylglucosaminyltransferase activity • transferase activity, transferring glycosyl groups Cellular component • integral component of membrane • endoplasmic reticulum membrane • glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex • membrane Biological process • GPI anchor biosynthetic process • preassembly of GPI anchor in ER membrane • carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9091	14755
Ensembl	ENSG00000007541	ENSMUSG00000025728
UniProt	Q9BRB3	Q9QYT7
RefSeq (mRNA)	NM_148920 NM_004204	NM_001291025 NM_011822 NM_001357592
RefSeq (protein)	NP_004195 NP_683721	NP_001277954 NP_035952 NP_001344521
Location (UCSC)	Chr 16: 0.57 – 0.58 Mb	Chr 17: 25.93 – 25.94 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

This gene is involved in the first step 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 gene encodes a N-acetylglucosaminyl transferase component that is part of the complex that catalyzes transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to phosphatidylinositol (PI).[7]

Interactions

PIGQ has been shown to interact with PIGH,[5] PIGA[5] and PIGC.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000007541 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025728 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T (Mar 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. PMC 1170437. PMID 9463366.
6. Tiede A, Schubert J, Nischan C, Jensen I, Westfall B, Taron CH, Orlean P, Schmidt RE (Nov 1998). "Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol membrane anchor biosynthesis in yeast mutants". Biochem J. 334 (3): 609–16. doi:10.1042/bj3340609. PMC 1219730. PMID 9729469.
7. "Entrez Gene: PIGQ phosphatidylinositol glycan anchor biosynthesis, class Q".

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. S2CID 4427026.
• Martin J, Han C, Gordon LA, et al. (2005). "The sequence and analysis of duplication-rich human chromosome 16". Nature. 432 (7020): 988–94. doi:10.1038/nature03187. PMID 15616553.
• 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. PMC 528928. PMID 15489334.
• Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• 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. PMC 139241. PMID 12477932.
• Tiede A, Daniels RJ, Higgs DR, et al. (2001). "The human GPI1 gene is required for efficient glycosylphosphatidylinositol biosynthesis". Gene. 271 (2): 247–54. doi:10.1016/S0378-1119(01)00510-8. PMID 11418246.
• Daniels RJ, Peden JF, Lloyd C, et al. (2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16". Hum. Mol. Genet. 10 (4): 339–52. doi:10.1093/hmg/10.4.339. PMID 11157797.
• Watanabe R, Murakami Y, Marmor MD, et al. (2000). "Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2". EMBO J. 19 (16): 4402–11. doi:10.1093/emboj/19.16.4402. PMC 302040. PMID 10944123.
• Hong Y, Ohishi K, Watanabe R, et al. (1999). "GPI1 stabilizes an enzyme essential in the first step of glycosylphosphatidylinositol biosynthesis". J. Biol. Chem. 274 (26): 18582–8. doi:10.1074/jbc.274.26.18582. PMID 10373468.
• 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.