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Gene Review

ALG6  -  ALG6, alpha-1,3-glucosyltransferase

Homo sapiens

Synonyms: Asparagine-linked glycosylation protein 6 homolog, Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase, Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase, Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase, My046
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Disease relevance of ALG6


High impact information on ALG6


Biological context of ALG6

  • The genomic organization of the human ALG6 gene was determined, revealing 14 exons spread over 55 kb [5].
  • Haplotype analysis of CDG-Ic patients revealed a founder effect for the ALG6 allele bearing the A333 V mutation [5].

Anatomical context of ALG6

  • Wildtype hALG6, delivered by a lentiviral vector into patient's fibroblasts, clearly improves the biochemical phenotype, which confirms that the mutations are disease-causing [6].

Other interactions of ALG6

  • New mutations were identified in MPI (Y129C) and ALG6 (G227E) [7].
  • By polymerase chain reaction amplification and sequencing of ALG6 exons, three mutations, in addition to the previously described A333 V substitution, were detected in CDG-Ic patients [5].
  • Identification of a frequent variant in ALG6, the cause of Congenital Disorder of Glycosylation-Ic [8].


  1. A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic. Imbach, T., Burda, P., Kuhnert, P., Wevers, R.A., Aebi, M., Berger, E.G., Hennet, T. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  2. Carbohydrate-deficient glycoprotein syndrome type V: deficiency of dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase. Körner, C., Knauer, R., Holzbach, U., Hanefeld, F., Lehle, L., von Figura, K. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  3. A frequent mild mutation in ALG6 may exacerbate the clinical severity of patients with congenital disorder of glycosylation Ia (CDG-Ia) caused by phosphomannomutase deficiency. Westphal, V., Kjaergaard, S., Schollen, E., Martens, K., Grunewald, S., Schwartz, M., Matthijs, G., Freeze, H.H. Hum. Mol. Genet. (2002) [Pubmed]
  4. Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation. Westphal, V., Murch, S., Kim, S., Srikrishna, G., Winchester, B., Day, R., Freeze, H.H. Am. J. Pathol. (2000) [Pubmed]
  5. Multi-allelic origin of congenital disorder of glycosylation (CDG)-Ic. Imbach, T., Grünewald, S., Schenk, B., Burda, P., Schollen, E., Wevers, R.A., Jaeken, J., de Klerk, J.B., Berger, E.G., Matthijs, G., Aebi, M., Hennet, T. Hum. Genet. (2000) [Pubmed]
  6. Clinical and molecular characterization of the first adult congenital disorder of glycosylation (CDG) type Ic patient. Sun, L., Eklund, E.A., Van Hove, J.L., Freeze, H.H., Thomas, J.A. Am. J. Med. Genet. A (2005) [Pubmed]
  7. DHPLC analysis as a platform for molecular diagnosis of congenital disorders of glycosylation (CDG). Schollen, E., Martens, K., Geuzens, E., Matthijs, G. Eur. J. Hum. Genet. (2002) [Pubmed]
  8. Identification of a frequent variant in ALG6, the cause of Congenital Disorder of Glycosylation-Ic. Westphal, V., Xiao, M., Kwok, P.Y., Freeze, H.H. Hum. Mutat. (2003) [Pubmed]
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