ALG14
ALG14 | |||||||||||||||||
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Identifiers | |||||||||||||||||
Aliases | ALG14, CMS15, UDP-N-acetylglucosaminyltransferase subunit | ||||||||||||||||
External IDs | MGI: 1914039 HomoloGene: 49751 GeneCards: ALG14 | ||||||||||||||||
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Orthologs | |||||||||||||||||
Species | Human | Mouse | |||||||||||||||
Entrez | |||||||||||||||||
Ensembl | |||||||||||||||||
UniProt | |||||||||||||||||
RefSeq (mRNA) | |||||||||||||||||
RefSeq (protein) | |||||||||||||||||
Location (UCSC) | Chr 1: 94.97 – 95.07 Mb | Chr 3: 121.29 – 121.36 Mb | |||||||||||||||
PubMed search | [1] | [2] | |||||||||||||||
Wikidata |
View/Edit Human | View/Edit Mouse |
UDP-N-acetylglucosamine transferase subunit ALG14 homolog is a protein that in humans is encoded by the ALG14 gene.[3][4]
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.[5]
See also
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ "Entrez Gene: asparagine-linked glycosylation 14 homolog (S. cerevisiae)".
- ↑ Chantret I, Dancourt J, Barbat A, Moore SE (March 2005). "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. doi:10.1074/jbc.M413941200. PMID 15615718.
- ↑ Averbeck N, Keppler-Ross S, Dean N (October 2007). "Membrane topology of the Alg14 endoplasmic reticulum UDP-GlcNAc transferase subunit". J. Biol. Chem. 282 (40): 29081–8. doi:10.1074/jbc.M704410200. PMID 17686769.
Further reading
- Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Gao XD, Tachikawa H, Sato T, et al. (2005). "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. doi:10.1074/jbc.M507569200. PMID 16100110.
- 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.
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