Biology:ALG14
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 Generic protein structure example |
UDP-N-acetylglucosamine transferase subunit ALG14 homolog is a protein that in humans is encoded by the ALG14 gene.[1][2]
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.[3]
See also
- Congenital disorder of glycosylation
References
- ↑ "Entrez Gene: asparagine-linked glycosylation 14 homolog (S. cerevisiae)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=199857.
- ↑ "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". J. Biol. Chem. 280 (10): 9236–42. March 2005. doi:10.1074/jbc.M413941200. PMID 15615718.
- ↑ "Membrane topology of the Alg14 endoplasmic reticulum UDP-GlcNAc transferase subunit". J. Biol. Chem. 282 (40): 29081–8. October 2007. doi:10.1074/jbc.M704410200. PMID 17686769.
External links
- Human ALG14 genome location and ALG14 gene details page in the UCSC Genome Browser.
Further reading
- "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. 2002. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "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.". J. Biol. Chem. 280 (43): 36254–62. 2005. doi:10.1074/jbc.M507569200. PMID 16100110.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
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