ALG8/YOR067C Summary Help

Standard Name ALG8 1, 2
Systematic Name YOR067C
Alias YOR29-18
Feature Type ORF, Verified
Description Glucosyl transferase; involved in N-linked glycosylation; adds glucose to the dolichol-linked oligosaccharide precursor prior to transfer to protein during lipid-linked oligosaccharide biosynthesis; similar to Alg6p (1, 2 and see Summary Paragraph)
Name Description Asparagine-Linked Glycosylation 3
Chromosomal Location
ChrXV:453462 to 451729 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All ALG8 GO evidence and references
  View Computational GO annotations for ALG8
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 122 genes
Classical genetics
Large-scale survey
278 total interaction(s) for 144 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • PCA: 1

Genetic Interactions
  • Negative Genetic: 158
  • Phenotypic Suppression: 67
  • Positive Genetic: 25
  • Synthetic Growth Defect: 19
  • Synthetic Lethality: 5
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 577
Molecular Weight (Da) 67,384
Isoelectric Point (pI) 10.31
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXV:453462 to 451729 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1734 453462..451729 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005593

During N-linked glycosylation of proteins, oligosaccharide chains are assembled on the carrier molecule dolichyl pyrophosphate in the following order: 2 molecules of N-acetylglucosamine (GlcNAc), 9 molecules of mannose, and 3 molecules of glucose. These 14-residue oligosaccharide cores are then transferred to asparagine residues on nascent polypeptide chains in the endoplasmic reticulum (ER). As proteins progress through the Golgi apparatus, the oligosaccharide cores are modified by trimming and extension to generate a diverse array of glycosylated proteins (reviewed in 4, 5).

ALG8 encodes an ER-membrane-bound alpha 1,3 glucosyltransferase that catalyzes the addition of the second of three glucose moieties (2) to growing lipid-linked oligosaccharides (LLO's) in the lumen of the endoplasmic reticulum. The first and third glucose residues are added by Alg6p (a close homolog of Alg8p) and Die2p (also known as Alg10p), respectively. Mutants lacking Alg8p produce truncated LLO's with only one glucose residue (6) that are able to be transferred to proteins with reduced efficiency (2). Mutations in human ALG8 (OMIM) have been implicated in the congenital disorder of glycosylation CDG-Ih (OMIM) (7, 8).

Last updated: 2005-07-12 Contact SGD

References cited on this page View Complete Literature Guide for ALG8
1) Stagljar I, et al.  (1994) New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc Natl Acad Sci U S A 91(13):5977-81
2) Runge KW and Robbins PW  (1986) A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues. J Biol Chem 261(33):15582-90
3) Huffaker TC and Robbins PW  (1982) Temperature-sensitive yeast mutants deficient in asparagine-linked glycosylation. J Biol Chem 257(6):3203-10
4) Herscovics A and Orlean P  (1993) Glycoprotein biosynthesis in yeast. FASEB J 7(6):540-50
5) Burda P and Aebi M  (1999) The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta 1426(2):239-57
6) Munoz MD, et al.  (1994) Glycosylation of yeast exoglucanase sequons in alg mutants deficient in the glucosylation steps of the lipid-linked oligosaccharide. Presence of glucotriose unit in Dol-PP-GlcNAc2Man9Glc3 influences both glycosylation efficiency and selection of N-linked sites. Biochim Biophys Acta 1201(3):361-6
7) Chantret I, et al.  (2003) A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. J Biol Chem 278(11):9962-71
8) Schollen E, et al.  (2004) Clinical and molecular features of three patients with congenital disorders of glycosylation type Ih (CDG-Ih) (ALG8 deficiency). J Med Genet 41(7):550-6