DDOST: Difference between revisions

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{{Underlinked|date=May 2016}}
 
{{Infobox_gene}}
{{Infobox_gene}}
'''Dolichyl-diphosphooligosaccharide—protein glycosyltransferase 48 kDa subunit''' is an [[enzyme]] that in humans is encoded by the ''DDOST'' [[gene]].<ref name="pmid9367678">{{cite journal | vauthors = Yamagata T, Tsuru T, Momoi MY, Suwa K, Nozaki Y, Mukasa T, Ohashi H, Fukushima Y, Momoi T | title = Genome organization of human 48-kDa oligosaccharyltransferase (DDOST) | journal = Genomics | volume = 45 | issue = 3 | pages = 535–40 |date=Jan 1998 | pmid = 9367678 | pmc =  | doi = 10.1006/geno.1997.4966 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DDOST dolichyl-diphosphooligosaccharide-protein glycosyltransferase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1650| accessdate = }}</ref>
'''Dolichyl-diphosphooligosaccharide—protein glycosyltransferase 48 kDa subunit''' is an [[enzyme]] that in humans is encoded by the ''DDOST'' [[gene]].<ref name="pmid9367678">{{cite journal | vauthors = Yamagata T, Tsuru T, Momoi MY, Suwa K, Nozaki Y, Mukasa T, Ohashi H, Fukushima Y, Momoi T | title = Genome organization of human 48-kDa oligosaccharyltransferase (DDOST) | journal = Genomics | volume = 45 | issue = 3 | pages = 535–40 |date=Jan 1998 | pmid = 9367678 | pmc =  | doi = 10.1006/geno.1997.4966 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DDOST dolichyl-diphosphooligosaccharide-protein glycosyltransferase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1650| accessdate = }}</ref>
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a component of the oligosaccharyltransferase complex which catalyzes the transfer of high-mannose oligosaccharides to asparagine residues on nascent polypeptides in the lumen of the rough endoplasmic reticulum. The protein complex co-purifies with ribosomes. The product of this gene is also implicated in the processing of advanced glycation endproducts (AGEs), which form from non-enzymatic reactions between sugars and proteins or lipids and are associated with aging and hyperglycemia.<ref name="entrez" />
| summary_text = This gene encodes a component of the [[oligosaccharyltransferase]] complex which catalyzes the transfer of high-mannose [[oligosaccharides]] to [[asparagine]] residues on nascent [[polypeptides]] in the [[Lumen (anatomy)|lumen]] of the [[rough endoplasmic reticulum]]. The protein complex co-purifies with [[ribosomes]]. The product of this gene is also implicated in the processing of [[advanced glycation endproducts]] (AGEs), which form from non-enzymatic reactions between sugars and proteins or lipids and are associated with [[aging]] and [[hyperglycemia]].<ref name="entrez" />
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Latest revision as of 11:57, 18 February 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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

Dolichyl-diphosphooligosaccharide—protein glycosyltransferase 48 kDa subunit is an enzyme that in humans is encoded by the DDOST gene.[1][2]

This gene encodes a component of the oligosaccharyltransferase complex which catalyzes the transfer of high-mannose oligosaccharides to asparagine residues on nascent polypeptides in the lumen of the rough endoplasmic reticulum. The protein complex co-purifies with ribosomes. The product of this gene is also implicated in the processing of advanced glycation endproducts (AGEs), which form from non-enzymatic reactions between sugars and proteins or lipids and are associated with aging and hyperglycemia.[2]

References

  1. Yamagata T, Tsuru T, Momoi MY, Suwa K, Nozaki Y, Mukasa T, Ohashi H, Fukushima Y, Momoi T (Jan 1998). "Genome organization of human 48-kDa oligosaccharyltransferase (DDOST)". Genomics. 45 (3): 535–40. doi:10.1006/geno.1997.4966. PMID 9367678.
  2. 2.0 2.1 "Entrez Gene: DDOST dolichyl-diphosphooligosaccharide-protein glycosyltransferase".

Further reading