PIGQ

Protein-coding gene in the species Homo sapiens
PIGQ
Identifiers
AliasesPIGQ, GPI1, c407A10.1, phosphatidylinositol glycan anchor biosynthesis class Q, EIEE77, DEE77, MCAHS4, GPIBD19
External IDsOMIM: 605754; MGI: 1333114; HomoloGene: 31228; GeneCards: PIGQ; OMA:PIGQ - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for PIGQ
Genomic location for PIGQ
Band16p13.3Start566,995 bp[1]
End584,109 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for PIGQ
Genomic location for PIGQ
Band17|17 A3.3Start26,145,395 bp[2]
End26,163,910 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of thyroid gland

  • right uterine tube

  • left lobe of thyroid gland

  • right testis

  • anterior pituitary

  • left testis

  • right frontal lobe

  • body of pancreas

  • right hemisphere of cerebellum

  • right adrenal cortex
Top expressed in
  • fetal liver hematopoietic progenitor cell

  • motor neuron

  • substantia nigra

  • fossa

  • ciliary body

  • endocardial cushion

  • barrel cortex

  • medullary collecting duct

  • ascending aorta

  • crypt of lieberkuhn of small intestine
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • phosphatidylinositol N-acetylglucosaminyltransferase activity
  • glycosyltransferase activity
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
SpeciesHumanMouse
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 MbChr 17: 26.15 – 26.16 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000007541 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b c d 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. ^ a b "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. Bibcode:2005Natur.437.1173R. 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. Bibcode:2004Natur.432..988M. 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. Bibcode:2002PNAS...9916899M. 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.


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