ALG14
{{Short description|Protein-coding gene in the species Homo sapiens}}
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UDP-N-acetylglucosamine transferase subunit ALG14 homolog is a protein that in humans is encoded by the ALG14 gene.{{cite web | title = Entrez Gene: asparagine-linked glycosylation 14 homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=199857}}{{cite journal |vauthors=Chantret I, Dancourt J, Barbat A, Moore SE | title = Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae | journal = J. Biol. Chem. | volume = 280 | issue = 10 | pages = 9236–42 |date=March 2005 | pmid = 15615718 | doi = 10.1074/jbc.M413941200 | doi-access = free }}
Asparagine (N)-glycosylation is an essential modification that regulates protein folding and stability. ALG13 and ALG14 (this protein) constitute the UDP-GlcNAc transferase, which catalyzes a key step in endoplasmic reticulum N-linked glycosylation.{{cite journal |vauthors=Averbeck N, Keppler-Ross S, Dean N | title = Membrane topology of the Alg14 endoplasmic reticulum UDP-GlcNAc transferase subunit | journal = J. Biol. Chem. | volume= 282 | issue = 40 | pages = 29081–8 |date=October 2007 | pmid = 17686769 | doi = 10.1074/jbc.M704410200 | doi-access = free }}
See also
References
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External links
- {{UCSC gene info|ALG14}}
Further reading
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- {{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= 2002 |pmid= 12477932 |doi= 10.1073/pnas.242603899 |pmc=139241|bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
- {{cite journal |vauthors=Gao XD, Tachikawa H, Sato T |title=Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation. |journal=J. Biol. Chem. |volume=280 |issue= 43 |pages= 36254–62 |year= 2005 |pmid= 16100110 |doi= 10.1074/jbc.M507569200 |display-authors=etal|doi-access=free }}
- {{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}}
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