ERG2/YMR202W Summary Help

Standard Name ERG2 1
Systematic Name YMR202W
Alias END11
Feature Type ORF, Verified
Description C-8 sterol isomerase; catalyzes the isomerization of the delta-8 double bond to the delta-7 position at an intermediate step in ergosterol biosynthesis (1, 2, 3 and see Summary Paragraph)
Name Description ERGosterol biosynthesis 1
Chromosomal Location
ChrXIII:667537 to 668205 | ORF Map | GBrowse
Gene Ontology Annotations All ERG2 GO evidence and references
  View Computational GO annotations for ERG2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 9 genes
Classical genetics
Large-scale survey
436 total interaction(s) for 303 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 14
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 1
  • Co-purification: 1
  • PCA: 8

Genetic Interactions
  • Negative Genetic: 205
  • Phenotypic Enhancement: 10
  • Phenotypic Suppression: 59
  • Positive Genetic: 77
  • Synthetic Growth Defect: 27
  • Synthetic Lethality: 24
  • Synthetic Rescue: 9

Expression Summary
Length (a.a.) 222
Molecular Weight (Da) 24,895
Isoelectric Point (pI) 5.83
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIII:667537 to 668205 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..669 667537..668205 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 SGDIDS000004815

ERG2 encodes C-8 sterol isomerase, an enzyme that catalyzes the isomerization of the delta-8 double bond to the delta-7 position in an intermedate in ergosterol biosynthesis (2, 1, 3, 4, 5). The erg2 null mutant has been reported to be viable (2); erg2 null mutant cells are ergosterol auxotrophs, accumulate aberrant sterols, and show a competitive growth disadvantage compared to wild type cells (6, 7). The immunosuppressant drug SR 31747 causes yeast cells to accumulate the same aberrant sterols seen in erg2 mutants, and overproduction of Erg2p causes resistance to SR 31747 (6). Erg2p also binds a class of drugs known as sigma ligands, as does a related protein from guinea pig liver (8, 9). Expression of ERG2 increases several fold upon ergosterol depletion by starvation or SR 31747 treatment (10). Production of the human or murine emopamil-binding protein, or a related Arabidopsis protein, restores the ability of erg2 mutants to convert delta-8 sterols to delta-7 isomers (11, 12).

Last updated: 2000-09-05 Contact SGD

References cited on this page View Complete Literature Guide for ERG2
1) Arthington BA, et al.  (1991) Nucleotide sequence of the gene encoding yeast C-8 sterol isomerase. Gene 107(1):173-4
2) Ashman WH, et al.  (1991) Cloning and disruption of the yeast C-8 sterol isomerase gene. Lipids 26(8):628-32
3) Paltauf F, et al.  (1992) "Regulation and compartmentalization of lipid synthesis in yeast." Pp. 415-500 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
4) Lees ND, et al.  (1995) Cloning of the late genes in the ergosterol biosynthetic pathway of Saccharomyces cerevisiae--a review. Lipids 30(3):221-6
5) Parks LW, et al.  (1995) Biochemical and physiological effects of sterol alterations in yeast--a review. Lipids 30(3):227-30
6) Silve S, et al.  (1996) The immunosuppressant SR 31747 blocks cell proliferation by inhibiting a steroid isomerase in Saccharomyces cerevisiae. Mol Cell Biol 16(6):2719-27
7) Palermo LM, et al.  (1997) Assessment of the essentiality of ERG genes late in ergosterol biosynthesis in Saccharomyces cerevisiae. Curr Genet 32(2):93-9
8) Moebius FF, et al.  (1996) Yeast sterol C8-C7 isomerase: identification and characterization of a high-affinity binding site for enzyme inhibitors. Biochemistry 35(51):16871-8
9) Moebius FF, et al.  (1997) High affinity of sigma 1-binding sites for sterol isomerization inhibitors: evidence for a pharmacological relationship with the yeast sterol C8-C7 isomerase. Br J Pharmacol 121(1):1-6
10) Soustre I, et al.  (2000) Sterol metabolism and ERG2 gene regulation in the yeast Saccharomyces cerevisiae. FEBS Lett 470(2):102-6
11) Silve S, et al.  (1996) Emopamil-binding protein, a mammalian protein that binds a series of structurally diverse neuroprotective agents, exhibits delta8-delta7 sterol isomerase activity in yeast. J Biol Chem 271(37):22434-40
12) Grebenok RJ, et al.  (1998) Isolation and characterization of an Arabidopsis thaliana C-8,7 sterol isomerase: functional and structural similarities to mammalian C-8,7 sterol isomerase/emopamil-binding protein. Plant Mol Biol 38(5):807-15