ERG20/YJL167W Summary Help

Standard Name ERG20 1
Systematic Name YJL167W
Alias BOT3 , FDS1 , FPP1
Feature Type ORF, Verified
Description Farnesyl pyrophosphate synthetase; has both dimethylallyltranstransferase and geranyltranstransferase activities; catalyzes the formation of C15 farnesyl pyrophosphate units for isoprenoid and sterol biosynthesis (2, 3 and see Summary Paragraph)
Name Description ERGosterol biosynthesis 1
Chromosomal Location
ChrX:105014 to 106072 | ORF Map | GBrowse
Gene Ontology Annotations All ERG20 GO evidence and references
  View Computational GO annotations for ERG20
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 5 genes
Classical genetics
Large-scale survey
reduction of function
62 total interaction(s) for 53 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 15
  • Affinity Capture-RNA: 2
  • Biochemical Activity: 3
  • Co-fractionation: 1
  • Co-purification: 1
  • Protein-peptide: 2
  • Reconstituted Complex: 1
  • Two-hybrid: 5

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 24
  • Phenotypic Enhancement: 3
  • Positive Genetic: 4

Expression Summary
Length (a.a.) 352
Molecular Weight (Da) 40,483
Isoelectric Point (pI) 5.21
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrX:105014 to 106072 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1059 105014..106072 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 SGDIDS000003703

ERG20 encodes farnesyl pyrophosphate synthetase (FPP synthase), a cytosolic enzyme that has dimethylallyltranstransferase and geranyltranstransferase activities (3, 2, 4). FPP synthase catalyzes the sequential 1'-4 coupling of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate and geranyl diphosphate, forming C15 farnesyl pyrophosphate units for isoprenoid and sterol biosynthesis; in yeast ergosterol is the end product of the sterol biosynthetic pathway (3, 5, 4).

ERG20 is essential; erg20 mutations cause ergosterol auxotrophy, and erg20 mutant cells excrete prenyl alcohols (3, 6). FPP synthases have been identified in many organisms (3, 7, 4); the Arabidopsis gene FPS1 can complement the yeast erg20 null phenotype (8).

Last updated: 2000-08-28 Contact SGD

References cited on this page View Complete Literature Guide for ERG20
1) Chambon C, et al.  (1991) Sterol pathway in yeast. Identification and properties of mutant strains defective in mevalonate diphosphate decarboxylase and farnesyl diphosphate synthetase. Lipids 26(8):633-6
2) Parks LW, et al.  (1995) Biochemical and physiological effects of sterol alterations in yeast--a review. Lipids 30(3):227-30
3) Anderson MS, et al.  (1989) Farnesyl diphosphate synthetase. Molecular cloning, sequence, and expression of an essential gene from Saccharomyces cerevisiae. J Biol Chem 264(32):19176-84
4) Stryer L  (1995) Biochemistry (4th ed.). New York: W. H. Freeman and Company
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) Chambon C, et al.  (1990) Isolation and properties of yeast mutants affected in farnesyl diphosphate synthetase. Curr Genet 18(1):41-6
7) Ohnuma Si, et al.  (1997) Conversion from archaeal geranylgeranyl diphosphate synthase to farnesyl diphosphate synthase. Two amino acids before the first aspartate-rich motif solely determine eukaryotic farnesyl diphosphate synthase activity. J Biol Chem 272(8):5192-8
8) Cunillera N, et al.  (1996) Arabidopsis thaliana contains two differentially expressed farnesyl-diphosphate synthase genes. J Biol Chem 271(13):7774-80