DIE2/YGR227W Summary Help

Standard Name DIE2 1
Systematic Name YGR227W
Alias ALG10 2
Feature Type ORF, Verified
Description Dolichyl-phosphoglucose-dependent alpha-1,2 glucosyltransferase; located in the ER; functions in the pathway that synthesizes the dolichol-linked oligosaccharide precursor for N-linked protein glycosylation; has a role in regulation of ITR1 and INO1 (1, 2, 3 and see Summary Paragraph)
Name Description Derepression of ITR1 Expression 1
Chromosomal Location
ChrVII:947420 to 948997 | ORF Map | GBrowse
Gene Ontology Annotations All DIE2 GO evidence and references
  View Computational GO annotations for DIE2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 1 genes
Classical genetics
Large-scale survey
155 total interaction(s) for 82 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 1
  • Affinity Capture-RNA: 1
  • Two-hybrid: 4

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 67
  • Phenotypic Enhancement: 16
  • Phenotypic Suppression: 22
  • Positive Genetic: 30
  • Synthetic Growth Defect: 6
  • Synthetic Lethality: 6
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 525
Molecular Weight (Da) 61,793
Isoelectric Point (pI) 9.7
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:947420 to 948997 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 2011-02-03
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1578 947420..948997 2011-02-03 2011-02-03
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 SGDIDS000003459

The name DIE2, for Derepression of ITR1 Expression, comes from a screen for genes involved in regulation of an inositol transporter gene (1). The name ALG10 was assigned after it was determined that the gene plays a role in asparagine-linked glycosylation (4).

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 5, 6).

Die2p is an alpha-1,2 glucosyltransferase that catalyzes the addition of the third glucose moiety during lipid-linked oligosaccharide (LLO) assembly (2) in the lumen of the endoplasmic reticulum. This is the final sugar added to an LLO before it is transferred as a whole to asparagine; Alg8p adds the second glucose. The human (OMIM) and rat homologs of DIE2 are called KCR1, for potassium channel regulator.

Last updated: 2005-07-01 Contact SGD

References cited on this page View Complete Literature Guide for DIE2
1) Nikawa J and Hosaka K  (1995) Isolation and characterization of genes that promote the expression of inositol transporter gene ITR1 in Saccharomyces cerevisiae. Mol Microbiol 16(2):301-8
2) Burda P and Aebi M  (1998) The ALG10 locus of Saccharomyces cerevisiae encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology 8(5):455-62
3) Ni L and Snyder M  (2001) A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae. Mol Biol Cell 12(7):2147-70
4) Zufferey R, et al.  (1995) STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo. EMBO J 14(20):4949-60
5) Herscovics A and Orlean P  (1993) Glycoprotein biosynthesis in yeast. FASEB J 7(6):540-50
6) Burda P and Aebi M  (1999) The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta 1426(2):239-57