ALG2

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ALG2
Identifiers
Aliases ALG2, CDGIi, NET38, hALPG2, CMS14, CMSTA3, alpha-1,3/1,6-mannosyltransferase
External IDs MGI: 1914731 HomoloGene: 5930 GeneCards: 85365
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_033087
NM_197973

NM_019998

RefSeq (protein)

NP_149078.1

NP_064382.3

Location (UCSC) Chr 9: 99.22 – 99.22 Mb Chr 4: 47.47 – 47.47 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Alpha-1,3-mannosyltransferase ALG2 is an enzyme that is encoded by the ALG2 gene.[1] Mutations in the human gene are associated with congenital defects in glycosylation [2][3]

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).[3]

Interactions[edit]

ALG2 has been shown to interact with ANXA7[4] and ANXA11.[4]

References[edit]

  1. ^ Jackson BJ, Kukuruzinska MA, Robbins P (Jun 1993). "Biosynthesis of asparagine-linked oligosaccharides in Saccharomyces cerevisiae: the alg2 mutation.". Glycobiology 3 (4): 357–64. doi:10.1093/glycob/3.4.357. PMID 8400550. 
  2. ^ Thiel, C.; Schwarz, M.; Peng, J.; Grzmil, M.; Hasilik, M.; Braulke, T.; Kohlschutter, A.; von Figura, K.; Lehle, L.; Korner, C. (2003). "A New Type of Congenital Disorders of Glycosylation (CDG-Ii) Provides New Insights into the Early Steps of Dolichol-linked Oligosaccharide Biosynthesis". Journal of Biological Chemistry 278 (25): 22498–22505. doi:10.1074/jbc.M302850200. ISSN 0021-9258. PMID 12684507. 
  3. ^ a b "Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)". 
  4. ^ a b Satoh, Hirokazu; Nakano Yoshimi; Shibata Hideki; Maki Masatoshi (Nov 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 (Netherlands) 1600 (1–2): 61–7. doi:10.1016/S1570-9639(02)00445-4. ISSN 0006-3002. PMID 12445460. 

Further reading[edit]

External links[edit]