ALG6

From Wikipedia, the free encyclopedia

Asparagine-linked glycosylation 6 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)

Identifiers

External IDs

OMIM: 604566 MGI: 2444031 HomoloGene: 6920

Gene ontology
Molecular Function:	• oligosaccharyl transferase activity • transferase activity, transferring glycosyl groups • glucosyltransferase activity
Cellular Component:	• endoplasmic reticulum • membrane • integral to membrane
Biological Process:	• protein amino acid N-linked glycosylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_013339 (mRNA)
NP_037471 (protein)

XM_620085 (mRNA)
XP_620085 (protein)

Location

Chr 1: 63.61 - 63.68 Mb

Chr 4: 99.21 - 99.26 Mb

Pubmed search

[1]

[2]

Asparagine-linked glycosylation 6 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase), also known as ALG6, is a human gene.^[1]

This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the first glucose residue to the growing lipid-linked oligosaccharide precursor of N-linked glycosylation. Mutations in this gene are associated with congenital disorders of glycosylation type Ic.^[1]

[edit] References

^ ^a ^b Entrez Gene: ALG6 asparagine-linked glycosylation 6 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase).

[edit] Further reading

Burda P, Borsig L, de Rijk-van Andel J, et al. (1998). "A novel carbohydrate-deficient glycoprotein syndrome characterized by a deficiency in glucosylation of the dolichol-linked oligosaccharide.". J. Clin. Invest. 102 (4): 647-52. PMID 9710431.
Körner C, Knauer R, Holzbach U, et al. (1998). "Carbohydrate-deficient glycoprotein syndrome type V: deficiency of dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase.". Proc. Natl. Acad. Sci. U.S.A. 95 (22): 13200-5. PMID 9789065.
Imbach T, Burda P, Kuhnert P, et al. (1999). "A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic.". Proc. Natl. Acad. Sci. U.S.A. 96 (12): 6982-7. PMID 10359825.
Imbach T, Grünewald S, Schenk B, et al. (2000). "Multi-allelic origin of congenital disorder of glycosylation (CDG)-Ic.". Hum. Genet. 106 (5): 538-45. PMID 10914684.
Westphal V, Schottstädt C, Marquardt T, Freeze HH (2000). "Analysis of multiple mutations in the hALG6 gene in a patient with congenital disorder of glycosylation Ic.". Mol. Genet. Metab. 70 (3): 219-23. doi:10.1006/mgme.2000.3017. PMID 10924277.
Westphal V, Murch S, Kim S, et al. (2001). "Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation.". Am. J. Pathol. 157 (6): 1917-25. PMID 11106564.
de Lonlay P, Seta N, Barrot S, et al. (2001). "A broad spectrum of clinical presentations in congenital disorders of glycosylation I: a series of 26 cases.". J. Med. Genet. 38 (1): 14-9. PMID 11134235.
Vuillaumier-Barrot S, Le Bizec C, Durand G, Seta N (2001). "The T911C (F304S) substitution in the human ALG6 gene is a common polymorphism and not a causal mutation of CDG-Ic.". J. Hum. Genet. 46 (9): 547-8. PMID 11558905.
Westphal V, Kjaergaard S, Schollen E, et al. (2002). "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.". Hum. Mol. Genet. 11 (5): 599-604. PMID 11875054.
Oriol R, Martinez-Duncker I, Chantret I, et al. (2003). "Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate.". Mol. Biol. Evol. 19 (9): 1451-63. PMID 12200473.
Schollen E, Martens K, Geuzens E, Matthijs G (2003). "DHPLC analysis as a platform for molecular diagnosis of congenital disorders of glycosylation (CDG).". Eur. J. Hum. Genet. 10 (10): 643-8. doi:10.1038/sj.ejhg.5200858. PMID 12357336.
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.
Imabayashi H, Mori T, Gojo S, et al. (2003). "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis.". Exp. Cell Res. 288 (1): 35-50. PMID 12878157.
Westphal V, Xiao M, Kwok PY, Freeze HH (2004). "Identification of a frequent variant in ALG6, the cause of Congenital Disorder of Glycosylation-Ic.". Hum. Mutat. 22 (5): 420-1. doi:10.1002/humu.9195. PMID 14517965.
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.
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.
Eklund EA, Sun L, Yang SP, et al. (2006). "Congenital disorder of glycosylation Ic due to a de novo deletion and an hALG-6 mutation.". Biochem. Biophys. Res. Commun. 339 (3): 755-60. doi:10.1016/j.bbrc.2005.11.073. PMID 16321363.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315-21. doi:10.1038/nature04727. PMID 16710414.