ALG14

ALG14, UDP-N-acetylglucosaminyltransferase subunit
Identifiers
Symbols	ALG14 ; CMS15
External IDs	OMIM: 612866 MGI: 1914039 HomoloGene: 49751 GeneCards: ALG14 Gene
Gene ontology Molecular function • N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity • protein anchor Cellular component • endoplasmic reticulum membrane • integral component of endoplasmic reticulum membrane • UDP-N-acetylglucosamine transferase complex Biological process • dolichol-linked oligosaccharide biosynthetic process • protein N-linked glycosylation via asparagine • post-translational protein modification • cellular protein metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	199857	66789
Ensembl	ENSG00000172339	ENSMUSG00000039887
UniProt	Q96F25	Q9D081
RefSeq (mRNA)	NM_001305242	NM_024178
RefSeq (protein)	NP_001292171	NP_077140
Location (UCSC)	Chr 1: 94.97 – 95.07 Mb	Chr 3: 121.29 – 121.36 Mb
PubMed search

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

1. "Entrez Gene: asparagine-linked glycosylation 14 homolog (S. cerevisiae)".
2. 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.
3. 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.