ALG13

UDP-N-acetylglucosamine transferase subunit ALG13 homolog, also known as asparagine-linked glycosylation 13 homolog, is an enzyme that in humans is encoded by the ALG13 gene.[3][4]

ALG13
Identifiers
Aliases	ALG13, CDG1S, CXorf45, GLT28D1, MDS031, TDRD13, YGL047W, EIEE36, UDP-N-acetylglucosaminyltransferase subunit, ALG13 UDP-N-acetylglucosaminyltransferase subunit
External IDs	OMIM: 300776 HomoloGene: 78772 GeneCards: ALG13
Gene location (Human) Chr. X chromosome (human)[1] Band Xq23 Start 111,665,811 bp[1] End 111,760,649 bp[1]
Gene ontology Molecular function • thiol-dependent ubiquitinyl hydrolase activity • transferase activity • peptidase activity • cysteine-type peptidase activity • transferase activity, transferring hexosyl groups • GO:0001948 protein binding • catalytic activity • hydrolase activity • transferase activity, transferring glycosyl groups • N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity • RNA binding Cellular component • endoplasmic reticulum membrane • endoplasmic reticulum • UDP-N-acetylglucosamine transferase complex Biological process • metabolism • proteolysis • dolichol-linked oligosaccharide biosynthetic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	79868	n/a
Ensembl	ENSG00000101901	n/a
UniProt	Q9NP73	n/a
RefSeq (mRNA)	NM_001039210 NM_001099922 NM_001168385 NM_001257230 NM_001257231 NM_001257234 NM_001257235 NM_001257237 NM_001257239 NM_001257240 NM_001257241 NM_018466 NM_001324290 NM_001324291 NM_001324292 NM_001324293 NM_001324294	n/a
RefSeq (protein)	NP_001034299 NP_001093392 NP_001161857 NP_001244159 NP_001244160 NP_001244163 NP_001244164 NP_001244166 NP_001244168 NP_001244169 NP_001244170 NP_001311219 NP_001311220 NP_001311221 NP_001311222 NP_001311223 NP_060936	n/a
Location (UCSC)	Chr X: 111.67 – 111.76 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

Function

The protein encoded by this gene is a subunit of a bipartite UDP-N-acetylglucosamine transferase. It heterodimerizes with asparagine-linked glycosylation 14 (ALG14) homolog to form a functional UDP-GlcNAc glycosyltransferase that catalyzes the second sugar addition of the highly conserved oligosaccharide precursor in endoplasmic reticulum N-linked glycosylation.[3][5]

See also

• Congenital disorder of glycosylation

References

1. GRCh38: Ensembl release 89: ENSG00000101901 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Entrez Gene: asparagine-linked glycosylation 13 homolog (S. cerevisiae)".
4. Gao XD, Tachikawa H, Sato T, Jigami Y, Dean N (October 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.
5. 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.

External links

• Human ALG13 genome location and ALG13 gene details page in the UCSC Genome Browser.

Further reading

• Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. Bibcode:2005Natur.434..325R. doi:10.1038/nature03440. PMC 2665286. PMID 15772651.
• Mizuochi T, Matthews TJ, Kato M, et al. (1990). "Diversity of oligosaccharide structures on the envelope glycoprotein gp 120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N-acetylglucosamine residues". J. Biol. Chem. 265 (15): 8519–24. PMID 2341393.
• Shimizu H, Tsuchie H, Honma H, et al. (1990). "Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins". Jpn. J. Med. Sci. Biol. 43 (3): 75–87. doi:10.7883/yoken1952.43.75. PMID 2283726.
• Yeh JC, Seals JR, Murphy CI, et al. (1993). "Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system". Biochemistry. 32 (41): 11087–99. doi:10.1021/bi00092a019. PMID 8218172.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• 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.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Oh JH, Yang JO, Hahn Y, et al. (2005). "Transcriptome analysis of human gastric cancer". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Epplen C, Epplen JT (1994). "Expression of (cac)n/(gtg)n simple repetitive sequences in mRNA of human lymphocytes". Hum. Genet. 93 (1): 35–41. doi:10.1007/BF00218910. PMID 7505766.
• Venter JC, Adams MD, Myers EW, et al. (2001). "The sequence of the human genome". Science. 291 (5507): 1304–51. Bibcode:2001Sci...291.1304V. doi:10.1126/science.1058040. PMID 11181995.
• Kozarsky K, Penman M, Basiripour L, et al. (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". J. Acquir. Immune Defic. Syndr. 2 (2): 163–9. PMID 2649653.