ERG7/YHR072W Summary Help

Standard Name ERG7 1, 2
Systematic Name YHR072W
Feature Type ORF, Verified
Description Lanosterol synthase; an essential enzyme that catalyzes the cyclization of squalene 2,3-epoxide, a step in ergosterol biosynthesis (3, 4, 5, 6, 7 and see Summary Paragraph)
Name Description ERGosterol biosynthesis 1
Chromosomal Location
ChrVIII:239098 to 241293 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All ERG7 GO evidence and references
  View Computational GO annotations for ERG7
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 3 genes
Resources
Pathways
Classical genetics
gain of function
null
Large-scale survey
null
repressible
Resources
46 total interaction(s) for 33 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 3
  • Co-fractionation: 1
  • Co-purification: 1
  • PCA: 23

Genetic Interactions
  • Dosage Lethality: 1
  • Negative Genetic: 4
  • Positive Genetic: 3
  • Synthetic Growth Defect: 3
  • Synthetic Lethality: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 731
Molecular Weight (Da) 83,460
Isoelectric Point (pI) 6.59
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVIII:239098 to 241293 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 2011-02-03
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2196 239098..241293 2011-02-03 2011-02-03
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001114
SUMMARY PARAGRAPH for ERG7

ERG7 encodes lanosterol synthase, which catalyzes the cyclization of squalene 2,3-epoxide, a step in the biosynthesis of ergosterol (6, 5, 7, 3, 4). Deletion of ERG7 is lethal; an erg7 hem1 (heme-deficient) mutant is auxotrophic for sterols (8). The erg7 null phenotype can be suppressed by expression of the Candida albicans ERG7 gene(9). Expression of ERG9, which encodes farnesyl-diphosphate farnesy l transferase, is increased in erg7 mutants (10).

Last updated: 2005-06-29 Contact SGD

References cited on this page View Complete Literature Guide for ERG7
1) Karst F and Lacroute F  (1977) Ertosterol biosynthesis in Saccharomyces cerevisiae: mutants deficient in the early steps of the pathway. Mol Gen Genet 154(3):269-77
2) Griffin, J.H. et al.  (1996) Mutations in the Oxidosqualene-Lanosterol Cyclase gene of Saccharomyces cerevisiae. Unpublished
3) 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
4) Parks LW, et al.  (1995) Biochemical and physiological effects of sterol alterations in yeast--a review. Lipids 30(3):227-30
5) Shi Z, et al.  (1994) Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 91(15):7370-4
6) Corey EJ, et al.  (1994) Molecular cloning, characterization, and overexpression of ERG7, the Saccharomyces cerevisiae gene encoding lanosterol synthase. Proc Natl Acad Sci U S A 91(6):2211-5
7) 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
8) Lewis TA, et al.  (1985) Involvement of heme biosynthesis in control of sterol uptake by Saccharomyces cerevisiae. J Bacteriol 163(1):199-207
9) Kelly R, et al.  (1990) Cloning and characterization of the 2,3-oxidosqualene cyclase-coding gene of Candida albicans. Gene 87(2):177-83
10) Kennedy MA, et al.  (1999) Transcriptional regulation of the squalene synthase gene (ERG9) in the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1445(1):110-22