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ALG8

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase is an enzyme encoded in humans by the ALG8 gene.{{cite web | title = Entrez Gene: ALG8 asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79053}}

This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation of proteins. Mutations in this gene are associated with congenital disorder of glycosylation type Ih (CDG-Ih). Alternatively spliced transcript variants encoding different isoforms have been identified.

References

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Further reading

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  • {{cite journal | author=Jaeken J |title=Congenital disorders of glycosylation (CDG): update and new developments. |journal=J. Inherit. Metab. Dis. |volume=27 |issue= 3 |pages= 423–6 |year= 2005 |pmid= 15272470 |doi=10.1023/B:BOLI.0000031221.44647.9e |s2cid=7608163 }}
  • {{cite journal | vauthors=Jaeken J, Carchon H |title=Congenital disorders of glycosylation: a booming chapter of pediatrics. |journal=Curr. Opin. Pediatr. |volume=16 |issue= 4 |pages= 434–9 |year= 2004 |pmid= 15273506 |doi=10.1097/01.mop.0000133636.56790.4a }}
  • {{cite journal | vauthors=Adams MD, Kerlavage AR, Fleischmann RD |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3–174 |year= 1995 |pmid= 7566098 |url=http://www.columbia.edu/itc/biology/pollack/w4065/client_edit/readings/nature377_3.pdf |display-authors=etal}}
  • {{cite journal | vauthors=Stanchi F, Bertocco E, Toppo S |title=Characterization of 16 novel human genes showing high similarity to yeast sequences. |journal=Yeast |volume=18 |issue= 1 |pages= 69–80 |year= 2001 |pmid= 11124703 |doi= 10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H |s2cid=21397515 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Oriol R, Martinez-Duncker I, Chantret I |title=Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate. |journal=Mol. Biol. Evol. |volume=19 |issue= 9 |pages= 1451–63 |year= 2003 |pmid= 12200473 |doi= 10.1093/oxfordjournals.molbev.a004208|display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Chantret I, Dancourt J, Dupré T |title=A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9962–71 |year= 2003 |pmid= 12480927 |doi= 10.1074/jbc.M211950200 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |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 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Schollen E, Frank CG, Keldermans L |title=Clinical and molecular features of three patients with congenital disorders of glycosylation type Ih (CDG-Ih) (ALG8 deficiency). |journal=J. Med. Genet. |volume=41 |issue= 7 |pages= 550–6 |year= 2004 |pmid= 15235028 |doi=10.1136/jmg.2003.016923 | pmc=1735831 |display-authors=etal}}
  • {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |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 |display-authors=etal}}
  • {{cite journal | vauthors=Otsuki T, Ota T, Nishikawa T |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 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Kimura K, Wakamatsu A, Suzuki Y |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 |display-authors=etal}}

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External links

  • [https://www.ncbi.nlm.nih.gov/books/NBK1332/ GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview]
  • {{UCSC gene info|ALG8}}

{{Glycosyltransferases}}

{{gene-11-stub}}