ALG6

Jump to: navigation, search


Asparagine-linked glycosylation 6 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)
Identifiers
Symbol(s) ALG6;
External IDs OMIM: 604566 MGI2444031 Homologene6920
RNA expression pattern

PBB GE ALG6 219649 at tn.png

More reference expression data

Orthologs
Human Mouse
Entrez 29929 320438
Ensembl ENSG00000088035 ENSMUSG00000073792
Uniprot Q9Y672 na
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]


References

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. PMID 10924277. doi:10.1006/mgme.2000.3017. 
  • 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. PMID 12357336. doi:10.1038/sj.ejhg.5200858. 
  • 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. PMID 12477932. doi:10.1073/pnas.242603899. 
  • 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. PMID 14517965. doi:10.1002/humu.9195. 
  • 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. PMID 14702039. doi:10.1038/ng1285. 
  • 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. PMID 15489334. doi:10.1101/gr.2596504. 
  • 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. PMID 16321363. doi:10.1016/j.bbrc.2005.11.073. 
  • Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature. 441 (7091): 315–21. PMID 16710414. doi:10.1038/nature04727. 
</dl>

Linked-in.jpg