ALG14 explained

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]

Further reading

• Strausberg RL, Feingold EA, Grouse LH . 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 . 12477932 . 10.1073/pnas.242603899 . 139241. 2002PNAS...9916899M . etal. free .
• Gao XD, Tachikawa H, Sato T . 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 . 16100110 . 10.1074/jbc.M507569200 . etal. free .
• Gerhard DS, Wagner L, Feingold EA . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928. etal.

Notes and References

1. Web site: Entrez Gene: asparagine-linked glycosylation 14 homolog (S. cerevisiae).
2. Chantret I, Dancourt J, Barbat A, Moore SE . 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 . 15615718 . 10.1074/jbc.M413941200 . free .
3. Averbeck N, Keppler-Ross S, Dean N . Membrane topology of the Alg14 endoplasmic reticulum UDP-GlcNAc transferase subunit . J. Biol. Chem. . 282 . 40 . 29081–8 . October 2007 . 17686769 . 10.1074/jbc.M704410200 . free .