ALG9/YNL219C Summary Help

ALG9 BASIC INFORMATION

Standard Name ALG9 1
Systematic Name YNL219C
Feature Type ORF, Verified
Description Mannosyltransferase, involved in N-linked glycosylation; catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides; mutation of the human ortholog causes type 1 congenital disorders of glycosylation (1, 2 and see Summary Paragraph)
Name Description Asparagine-Linked Glycosylation 1
GO Annotations All ALG9 GO evidence and references
    View Computational GO annotations for ALG9
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Pathways
Mutant Phenotype All ALG9 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions ALG9 All interactions details and references
44 total interaction(s) for 26 unique genes/features.
Physical Interactions
  • Affinity Capture-RNA: 1
  • Two-hybrid: 5
Genetic Interactions
  • Phenotypic Enhancement: 30
  • Phenotypic Suppression: 6
  • Synthetic Lethality: 2
Sequence Information
ChrXIV:237664 to 235997 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 2005-11-07 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1668 237664..235997 2005-11-07 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000005163

ALG9 RESOURCES

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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for ALG9

SUMMARY PARAGRAPH for ALG9

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 3, 4).

Alg9p, which is an alpha 1,2 mannosyltransferase, catalyzes two steps in lipid-linked oligosaccharide (LLO) assembly: the addition of the seventh and ninth mannose moieties to the growing oligosaccharide (1, 2) in the lumen of the endoplasmic reticulum. The sixth and eighth mannose moieties are added by Alg3p and Alg12p, respectively. Disruption of ALG9 causes accumulation of lipid-linked oligosaccharides with six mannose residues and hypoglycosylation of secreted proteins (1).

Human ALG9 (OMIM) cDNA complements the deletion of yeast ALG9 in a delta-alg9 wbp1-2 background (2) and has been found to be mutated in the congenital disorder of glycosylation CDG-1L (OMIM).

Last updated: 2010-01-19

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for ALG9]

1) Burda P, et al.  (1996) Stepwise assembly of the lipid-linked oligosaccharide in the endoplasmic reticulum of Saccharomyces cerevisiae: identification of the ALG9 gene encoding a putative mannosyl transferase. Proc Natl Acad Sci U S A 93(14):7160-5
2) Frank CG, et al.  (2004) Identification and functional analysis of a defect in the human ALG9 gene: definition of congenital disorder of glycosylation type IL. Am J Hum Genet 75(1):146-50
3) Herscovics A and Orlean P  (1993) Glycoprotein biosynthesis in yeast. FASEB J 7(6):540-50
4) Burda P and Aebi M  (1999) The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta 1426(2):239-57