ERG4/YGL012W Summary Help

Standard Name ERG4 1
Systematic Name YGL012W
Feature Type ORF, Verified
Description C-24(28) sterol reductase; catalyzes the final step in ergosterol biosynthesis; mutants are viable, but lack ergosterol (2, 3, 4, 5 and see Summary Paragraph)
Name Description ERGosterol biosynthesis 1
Chromosomal Location
ChrVII:472855 to 474276 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All ERG4 GO evidence and references
  View Computational GO annotations for ERG4
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 12 genes
Resources
Pathways
Classical genetics
null
Large-scale survey
null
overexpression
Resources
207 total interaction(s) for 119 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 10
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 1
  • PCA: 16

Genetic Interactions
  • Dosage Lethality: 1
  • Dosage Rescue: 2
  • Negative Genetic: 136
  • Phenotypic Enhancement: 2
  • Phenotypic Suppression: 1
  • Positive Genetic: 29
  • Synthetic Growth Defect: 4
  • Synthetic Lethality: 1
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 473
Molecular Weight (Da) 56,039
Isoelectric Point (pI) 8.77
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVII:472855 to 474276 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1422 472855..474276 2011-02-03 1996-07-31
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 SGDIDS000002980
SUMMARY PARAGRAPH for ERG4

ERG4 encodes sterol C-24(28) reductase, which catalyzes the final step in ergosterol biosynthesis (4, 5, 2, 3). Cells lacking ERG4 are viable, but lack ergosterol and are sensitive to several drugs (4, 6, 7). A mutation in ERG4 increases expression of ERG3, which encodes another enzyme involved in ergosterol biosynthesis (8). The S. pombe gene sts1 encodes a protein similar to Erg4p (9).

Last updated: 2000-09-06 Contact SGD

References cited on this page View Complete Literature Guide for ERG4
1) Lai MH, et al.  (1994) The identification of a gene family in the Saccharomyces cerevisiae ergosterol biosynthesis pathway. Gene 140(1):41-9
2) 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
3) Parks LW, et al.  (1995) Biochemical and physiological effects of sterol alterations in yeast--a review. Lipids 30(3):227-30
4) Zweytick D, et al.  (2000) Biochemical characterization and subcellular localization of the sterol C-24(28) reductase, erg4p, from the yeast saccharomyces cerevisiae. FEBS Lett 470(1):83-7
5) 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
6) Sauer B  (1992) Identification of cryptic lox sites in the yeast genome by selection for Cre-mediated chromosome translocations that confer multiple drug resistance. J Mol Biol 223(4):911-28
7) Kaur R and Bachhawat AK  (1999) The yeast multidrug resistance pump, Pdr5p, confers reduced drug resistance in erg mutants of Saccharomyces cerevisiae. Microbiology 145 ( Pt 4)():809-18
8) Arthington-Skaggs BA, et al.  (1996) Positive and negative regulation of a sterol biosynthetic gene (ERG3) in the post-squalene portion of the yeast ergosterol pathway. FEBS Lett 392(2):161-5
9) Shimanuki M, et al.  (1992) Fission yeast sts1+ gene encodes a protein similar to the chicken lamin B receptor and is implicated in pleiotropic drug-sensitivity, divalent cation-sensitivity, and osmoregulation. Mol Biol Cell 3(3):263-73