ALG2

Asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)
Identifiers
Symbols	ALG2 ; CDGIi; FLJ14511; hALPG2
External IDs	Template:OMIM5 Template:MGI HomoloGene: 5930
Gene ontology Molecular function Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase), also known as ALG2, is a human gene.

This gene encodes a member of the glycosyltransferase 1 family. The encoded protein acts as an alpha 1,3 mannosyltransferase, mannosylating Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. Defects in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ii).

Further reading

• Jaeken J (2005). "Congenital disorders of glycosylation (CDG): update and new developments". J. Inherit. Metab. Dis. 27 (3): 423–6. PMID 15272470.
• Jaeken J, Carchon H (2004). "Congenital disorders of glycosylation: a booming chapter of pediatrics". Curr. Opin. Pediatr. 16 (4): 434–9. PMID 15273506.
• Satoh H, Shibata H, Nakano Y; et al. (2002). "ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner". Biochem. Biophys. Res. Commun. 291 (5): 1166–72. doi:10.1006/bbrc.2002.6600. PMID 11883939.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Satoh H, Nakano Y, Shibata H, Maki M (2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner". Biochim. Biophys. Acta. 1600 (1–2): 61–7. PMID 12445460.CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "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. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Thiel C, Schwarz M, Peng J; et al. (2003). "A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis". J. Biol. Chem. 278 (25): 22498–505. doi:10.1074/jbc.M302850200. PMID 12684507.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hansen C, Tarabykina S, la Cour JM; et al. (2003). "The PEF family proteins sorcin and grancalcin interact in vivo and in vitro". FEBS Lett. 545 (2–3): 151–4. PMID 12804766.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Clark HF, Gurney AL, Abaya E; et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMID 12975309.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Shibata H, Yamada K, Mizuno T; et al. (2004). "The penta-EF-hand protein ALG-2 interacts with a region containing PxY repeats in Alix/AIP1, which is required for the subcellular punctate distribution of the amino-terminal truncation form of Alix/AIP1". J. Biochem. 135 (1): 117–28. PMID 14999017.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Humphray SJ, Oliver K, Hunt AR; et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. doi:10.1038/nature02465. PMID 15164053.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Katoh K, Suzuki H, Terasawa Y; et al. (2006). "The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B". Biochem. J. 391 (Pt 3): 677–85. doi:10.1042/BJ20050398. PMID 16004603.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Otsuki T, Ota T, Nishikawa T; et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 16344560.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Draeby I, Woods YL, la Cour JM; et al. (2007). "The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane". Arch. Biochem. Biophys. 467 (1): 87–94. doi:10.1016/j.abb.2007.07.028. PMID 17889823.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)