---

• Site Map |
• Search Options |
• Help |
• Home |
•   |
•  

•  
• Community Info
• Submit Data
• BLAST
• Primers
• PatMatch
• Gene/Seq Resources
• Advanced Search
• Community Wiki

---

ERG5/YMR015C Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrXIII: 302484 to 300868 CDS: 302484 - 300868 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
ERG5	YMR015C	CYP61	ORF, Verified	S000004617
Description
C-22 sterol desaturase, a cytochrome P450 enzyme that catalyzes the formation of the C-22(23) double bond in the sterol side chain in ergosterol biosynthesis; may be a target of azole antifungal drugs

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By C-22 sterol desaturase activity 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    TAS : Traceable Author Statement Assigned on 2001-01-19 SGD electron carrier activity DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001128 Assigned on 2008-04-01 UniProtKB heme binding DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001128 , EBI:IPR002403 Assigned on 2007-05-23 UniProtKB iron ion binding DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001128 , EBI:IPR002403 Assigned on 2007-05-23 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0408 Assigned on 2007-05-23 UniProtKB metal ion binding GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0479 Assigned on 2007-05-23 UniProtKB monooxygenase activity DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001128 , EBI:IPR002403 Assigned on 2007-05-23 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0503 Assigned on 2007-05-23 UniProtKB oxidoreductase activity GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0560 Assigned on 2007-05-23 UniProtKB
Biological Process Annotation(s) Reference(s) Evidence Assigned By alcohol metabolic process Huttenhower C and Troyanskaya OG (2009) Prediction of Gene Ontology annotations by integrating high-throughput datasets    RCA : Reviewed Computational Analysis Assigned on 2009-08-06 bioPIXIE_MEFIT cellular lipid metabolic process Huttenhower C and Troyanskaya OG (2009) Prediction of Gene Ontology annotations by integrating high-throughput datasets    RCA : Reviewed Computational Analysis Assigned on 2009-08-06 bioPIXIE_MEFIT cellular metabolic compound salvage Huttenhower C and Troyanskaya OG (2009) Prediction of Gene Ontology annotations by integrating high-throughput datasets    RCA : Reviewed Computational Analysis Assigned on 2009-08-06 bioPIXIE_MEFIT ergosterol biosynthetic process 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    TAS : Traceable Author Statement Assigned on 2001-01-19 SGD lipid biosynthetic process GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0444 Assigned on 2007-05-23 UniProtKB oxidation reduction GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0560 Assigned on 2008-05-21 UniProtKB steroid biosynthetic process GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0752 Assigned on 2007-05-23 UniProtKB sterol biosynthetic process GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0756 Assigned on 2007-05-23 UniProtKB
Cellular Component Annotation(s) Reference(s) Evidence Assigned By endoplasmic reticulum 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    TAS : Traceable Author Statement Assigned on 2001-01-19 SGD

Pathways [TOP] [NEXT]
ergosterol biosynthesis

Summary Paragraph [TOP] [NEXT]

SUMMARY PARAGRAPH for ERG5/YMR015C for ERG5 ERG5 encodes C-22 sterol desaturase, a cytochrome P-450 enzyme that catalyzes the formation of the C-22(23) double bond in the sterol side chain in ergosterol biosynthesis (1, 2, 3, 4, 5). Cells lacking ERG5 are viable (2); an erg5 mutation increases ERG3 expression (6). Erg5p binds, and may be a target of, azole antifungal drugs (7). An ERG5 homolog has been identified in Candida glabrata (8). Last Updated: 2000-09-06

Basic References [TOP]

BASIC INFORMATION REFERENCES forERG5/YMR015C for ERG5 1) Kelly SL, et al. (1995) Purification and reconstitution of activity of Saccharomyces cerevisiae P450 61, a sterol delta 22-desaturase. FEBS Lett 377(2):217-20        2) Skaggs BA, et al. (1996) Cloning and characterization of the Saccharomyces cerevisiae C-22 sterol desaturase gene, encoding a second cytochrome P-450 involved in ergosterol biosynthesis. Gene 169(1):105-9        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) 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        7) Kelly SL, et al. (1997) Characterization of Saccharomyces cerevisiae CYP61, sterol delta22-desaturase, and inhibition by azole antifungal agents. J Biol Chem 272(15):9986-8        8) Lamb DC, et al. (1999) Purification, reconstitution, and inhibition of cytochrome P-450 sterol delta22-desaturase from the pathogenic fungus Candida glabrata. Antimicrob Agents Chemother 43(7):1725-8

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for ERG5/YMR015C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for ERG5/YMR015C

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Candida Homologs (CGD) Candida Homologs (CandidaDB) Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]

Protein Sequence Calculations from Predicted Full length Translation N-term MSSVAEN C-term ITGEVFE Length(aa) 538 MW(Da) 61,334 pI 7.88 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.388   Codon Adaptation Index 0.363   Frequency of Optimal Codons 0.641   Hydropathicity of Protein -0.061   Aromaticity Score 0.115

10 20 30 40 50 | | | | | MSSVAENIIQHATHNSTLHQLAKDQPSVGVTTAFSILDTLKSMSYLKIFA TLICILLVWDQVAYQIKKGSIAGPKFKFWPIIGPFLESLDPKFEEYKAKW ASGPLSCVSIFHKFVVIASTRDLARKILQSSKFVKPCVVDVAVKILRPCN WVFLDGKAHTDYRKSLNGLFTKQALAQYLPSLEQIMDKYMDKFVRLSKEN NYEPQVFFHEMREILCALSLNSFCGNYITEDQVRKIADDYYLVTAALELV NFPIIIPYTKTWYGKKTADMAMKIFENCAQMAKDHIAAGGKPVCVMDAWC KLMHDAKNSNDDDSRIYHREFTNKEISEAVFTFLFASQDASSSLACWLFQ IVADRPDVLAKIREEQLAVRNNDMSTELNLDLIEKMKYTNMVIKETLRYR PPVLMVPYVVKKNFPVSPNYTAPKGAMLIPTLYPALHDPEVYENPDEFIP ERWVEGSKASEAKKNWLVFGCGPHVCLGQTYVMITFAALLGKFALYTDFH HTVTPLSEKIKVFATIFPKDDLLLTFKKRDPITGEVFE*

Protein Structures from PDB: proteins of known structure with sequence similarity to ERG5/YMR015C, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to ERG5 Homolog Source (per PDB) Protein Alignment: ERG5 vs. Homolog External Links P-Value %Identical %Similar Alignment 2v0m ( Chain: C, B, D, A) Crystal structure of human p450 3a4 in complex with ketoconazole PDB_Info PDB_Structure Homo sapiens Chain C = 2.8e-17 25 32 View alignment SCOP MMDB CATH Chain B = 2.8e-17 25 32 View alignment Chain D = 2.8e-17 25 32 View alignment Chain A = 2.8e-17 25 32 View alignment 2j0d ( Chain: B, A) Crystal structure of human p450 3a4 in complex with erythromycin PDB_Info PDB_Structure Homo sapiens Chain B = 2.8e-17 25 32 View alignment SCOP MMDB CATH Chain A = 2.8e-17 25 32 View alignment 1tqn ( Chain: A) Crystal structure of human microsomal p450 3a4 PDB_Info PDB_Structure Homo sapiens 2.8e-17 25 32 View alignment SCOP MMDB CATH 1w0f ( Chain: A) Crystal structure of human cytochrome p450 3a4 PDB_Info PDB_Structure Homo sapiens 2.8e-17 25 32 View alignment SCOP MMDB CATH 1w0e ( Chain: A) Crystal structure of human cytochrome p450 3a4 PDB_Info PDB_Structure Homo sapiens 2.8e-17 25 32 View alignment SCOP MMDB CATH 1w0g ( Chain: A) Crystal structure of human cytochrome p450 3a4 PDB_Info PDB_Structure Homo sapiens 2.8e-17 25 32 View alignment SCOP MMDB CATH 2ve4 ( Chain: B, A) Substrate free cyanobacterial cyp120a1 PDB_Info PDB_Structure Synechocystis sp. Chain B = 9.4e-17 23 32 View alignment SCOP MMDB CATH Chain A = 9.4e-17 23 32 View alignment 2ve3 ( Chain: B, A) Retinoic acid bound cyanobacterial cyp120a1 PDB_Info PDB_Structure Synechocystis sp. Chain B = 9.4e-17 23 32 View alignment SCOP MMDB CATH Chain A = 9.4e-17 23 32 View alignment 3g93 ( Chain: A, B, C, D) Cytochrome P450 2B4 PDB_Info PDB_Structure Unknown Chain A = 1.9e-12 23 32 View alignment SCOP MMDB CATH Chain B = 1.9e-12 23 32 View alignment Chain C = 1.9e-12 23 32 View alignment Chain D = 1.9e-12 23 32 View alignment 3el3 ( Chain: A, B) Putative cytochrome P45 PDB_Info PDB_Structure Unknown Chain A = 1.9e-12 23 28 View alignment SCOP MMDB CATH Chain B = 1.9e-12 23 28 View alignment 2bdm ( Chain: A) Structure of cytochrome p450 2b4 with bound bifonazole PDB_Info PDB_Structure Oryctolagus cuniculus 1.9e-12 23 32 View alignment SCOP MMDB CATH 3g5n ( Chain: D, B, A, C) Cytochrome P450 2B4 PDB_Info PDB_Structure Unknown Chain D = 1.9e-12 23 32 View alignment SCOP MMDB CATH Chain B = 1.9e-12 23 32 View alignment Chain A = 1.9e-12 23 32 View alignment Chain C = 1.9e-12 23 32 View alignment 1suo ( Chain: A) Structure of mammalian cytochrome p450 2b4 with bound 4-(4- chlorophenyl)imidazole PDB_Info PDB_Structure Oryctolagus cuniculus 1.9e-12 23 32 View alignment SCOP MMDB CATH 2q6n ( Chain: B, A, D, C, G, F, E) Structure of cytochrome p450 2b4 with bound 1-(4- cholorophenyl)imidazole PDB_Info PDB_Structure Oryctolagus cuniculus Chain B = 1.9e-12 23 32 View alignment SCOP MMDB CATH Chain A = 1.9e-12 23 32 View alignment Chain D = 1.9e-12 23 32 View alignment Chain C = 1.9e-12 23 32 View alignment Chain G = 1.9e-12 23 32 View alignment Chain F = 1.9e-12 23 32 View alignment Chain E = 1.9e-12 23 32 View alignment 1po5 ( Chain: A) Structure of mammalian cytochrome p450 2b4 PDB_Info PDB_Structure Oryctolagus cuniculus 1.9e-12 23 32 View alignment SCOP MMDB CATH 3dbg ( Chain: B, A) Putative cytochrome P45 PDB_Info PDB_Structure Unknown Chain B = 1.9e-12 23 28 View alignment SCOP MMDB CATH Chain A = 1.9e-12 23 28 View alignment 1fah ( Chain: A, B) Structure of cytochrome p450 PDB_Info PDB_Structure Bacillus megaterium Chain A = 7.5e-12 24 31 View alignment SCOP MMDB CATH Chain B = 7.5e-12 24 31 View alignment 1zoa ( Chain: B, A) Crystal structure of a328v mutant of the heme domain of p450bm-3 with n-palmitoylglycine PDB_Info PDB_Structure Bacillus megaterium Chain B = 7.5e-12 24 31 View alignment SCOP MMDB CATH Chain A = 7.5e-12 24 31 View alignment 2uwh ( Chain: E, B, C, A, D, F) Cytochrome p450 bm3 mutant in complex with palmitic acid PDB_Info PDB_Structure Bacillus megaterium Chain E = 1.6e-11 23 32 View alignment SCOP MMDB CATH Chain B = 1.6e-11 23 32 View alignment Chain C = 1.6e-11 23 32 View alignment Chain A = 1.6e-11 23 32 View alignment Chain D = 1.6e-11 23 32 View alignment Chain F = 1.6e-11 23 32 View alignment 3dgi ( Chain: A, B) Bifunctional P-450/NADP PDB_Info PDB_Structure Unknown Chain A = 1.6e-11 24 31 View alignment SCOP MMDB CATH Chain B = 1.6e-11 24 31 View alignment 1bvy ( Chain: B, A) Complex of the heme and fmn-binding domains of the cytochrome p450(bm-3) PDB_Info PDB_Structure Bacillus megaterium Chain B = 1.6e-11 23 32 View alignment SCOP MMDB CATH Chain A = 1.6e-11 23 32 View alignment 2ij2 ( Chain: A, B) Atomic structure of the heme domain of flavocytochrome p450- bm3 PDB_Info PDB_Structure Bacillus megaterium Chain A = 1.6e-11 23 32 View alignment SCOP MMDB CATH Chain B = 1.6e-11 23 32 View alignment 3ben ( Chain: A, B) Structure of n-(12-imidazolyl-dodecanoyl)-l-leucine inhibitor bound to the heme domain of cytochrome p450-bm3 PDB_Info PDB_Structure Bacillus megaterium Chain A = 1.6e-11 23 32 View alignment SCOP MMDB CATH Chain B = 1.6e-11 23 32 View alignment 1fag ( Chain: C, A, D, B) Structure of cytochrome p450 PDB_Info PDB_Structure Bacillus megaterium Chain C = 1.6e-11 23 32 View alignment SCOP MMDB CATH Chain A = 1.6e-11 23 32 View alignment Chain D = 1.6e-11 23 32 View alignment Chain B = 1.6e-11 23 32 View alignment 2hpd ( Chain: A, B) Crystal structure of hemoprotein domain of p450bm-3, a prototype for microsomal p450's PDB_Info PDB_Structure Bacillus megaterium Chain A = 1.6e-11 23 32 View alignment SCOP MMDB CATH Chain B = 1.6e-11 23 32 View alignment 1jpz ( Chain: B, A) Crystal structure of a complex of the heme domain of p450bm- 3 with n-palmitoylglycine PDB_Info PDB_Structure Bacillus megaterium Chain B = 1.6e-11 23 32 View alignment SCOP MMDB CATH Chain A = 1.6e-11 23 32 View alignment 1zo9 ( Chain: A, B) Crystal structure of the wild type heme domain of p450bm-3 with n-palmitoylmethionine PDB_Info PDB_Structure Bacillus megaterium Chain A = 1.6e-11 23 32 View alignment SCOP MMDB CATH Chain B = 1.6e-11 23 32 View alignment 1yqo ( Chain: A, B) T268a mutant heme domain of flavocytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain A = 2.0e-11 24 31 View alignment SCOP MMDB CATH Chain B = 2.0e-11 24 31 View alignment 1p0w ( Chain: A, B) F393w mutant heme domain of flavocytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain A = 2.2e-11 24 31 View alignment SCOP MMDB CATH Chain B = 2.2e-11 24 31 View alignment 3cbd ( Chain: A, B) Directed evolution of cytochrome p450 bm3, to octane monoxygenase 139-3 PDB_Info PDB_Structure Bacillus megaterium Chain A = 2.2e-11 23 32 View alignment SCOP MMDB CATH Chain B = 2.2e-11 23 32 View alignment 1zo4 ( Chain: A, B) Crystal structure of a328s mutant of the heme domain of p450bm-3 PDB_Info PDB_Structure Bacillus megaterium Chain A = 2.3e-11 23 32 View alignment SCOP MMDB CATH Chain B = 2.3e-11 23 32 View alignment 2nnb ( Chain: A, B) The q403k mutnat heme domain of flavocytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain A = 4.0e-11 23 32 View alignment SCOP MMDB CATH Chain B = 4.0e-11 23 32 View alignment 2bmh ( Chain: A, B) Modeling protein-substrate interactions in the heme domain of cytochrome p450bm-3 PDB_Info PDB_Structure Bacillus megaterium Chain A = 4.5e-11 23 32 View alignment SCOP MMDB CATH Chain B = 4.5e-11 23 32 View alignment 2j4s ( Chain: B, A) P450 bm3 heme domain in complex with dmso PDB_Info PDB_Structure Bacillus megaterium Chain B = 4.5e-11 23 32 View alignment SCOP MMDB CATH Chain A = 4.5e-11 23 32 View alignment 2j1m ( Chain: B, A) P450 bm3 heme domain in complex with dmso PDB_Info PDB_Structure Bacillus megaterium Chain B = 4.5e-11 23 32 View alignment SCOP MMDB CATH Chain A = 4.5e-11 23 32 View alignment 1bu7 ( Chain: A, B) Cryogenic structure of cytochrome p450bm-3 heme domain PDB_Info PDB_Structure Bacillus megaterium Chain A = 4.5e-11 23 32 View alignment SCOP MMDB CATH Chain B = 4.5e-11 23 32 View alignment 3ekb ( Chain: B, A) Crystal structure of the a264c mutant heme domain of cytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain B = 4.6e-11 23 32 View alignment SCOP MMDB CATH Chain A = 4.6e-11 23 32 View alignment 2ij4 ( Chain: A, B) Structure of the a264k mutant of cytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain A = 4.6e-11 23 32 View alignment SCOP MMDB CATH Chain B = 4.6e-11 23 32 View alignment 1smj ( Chain: D, C, B, A) Structure of the a264e mutant of cytochrome p450 bm3 complexed with palmitoleate PDB_Info PDB_Structure Bacillus megaterium Chain D = 4.6e-11 23 32 View alignment SCOP MMDB CATH Chain C = 4.6e-11 23 32 View alignment Chain B = 4.6e-11 23 32 View alignment Chain A = 4.6e-11 23 32 View alignment 3ekd ( Chain: A, B) Crystal structure of the a264m heme domain of cytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain A = 4.6e-11 23 32 View alignment SCOP MMDB CATH Chain B = 4.6e-11 23 32 View alignment 3ekf ( Chain: B, A) Crystal structure of the a264q heme domain of cytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain B = 4.6e-11 23 32 View alignment SCOP MMDB CATH Chain A = 4.6e-11 23 32 View alignment 1smi ( Chain: A, B) A single mutation of p450 bm3 induces the conformational rearrangement seen upon substrate-binding in wild-type enzyme PDB_Info PDB_Structure Bacillus megaterium Chain A = 4.6e-11 23 32 View alignment SCOP MMDB CATH Chain B = 4.6e-11 23 32 View alignment 3hf2 ( Chain: A, B) Bifunctional P-450/NADP PDB_Info PDB_Structure Unknown Chain A = 4.9e-11 23 32 View alignment SCOP MMDB CATH Chain B = 4.9e-11 23 32 View alignment 1yqp ( Chain: B, A) T268n mutant cytochrome domain of flavocytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain B = 5.4e-11 23 32 View alignment SCOP MMDB CATH Chain A = 5.4e-11 23 32 View alignment 2ij3 ( Chain: B, A) Structure of the a264h mutant of cytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain B = 5.5e-11 23 32 View alignment SCOP MMDB CATH Chain A = 5.5e-11 23 32 View alignment 1p0x ( Chain: B, A) F393y mutant heme domain of flavocytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain B = 8.7e-11 23 32 View alignment SCOP MMDB CATH Chain A = 8.7e-11 23 32 View alignment 3i3k ( Chain: B, A) Lanosterol 14-alpha dem PDB_Info PDB_Structure Unknown Chain B = 1.5e-10 21 29 View alignment SCOP MMDB CATH Chain A = 1.5e-10 21 29 View alignment 1og2 ( Chain: B, A) Structure of human cytochrome p450 cyp2c9 PDB_Info PDB_Structure Homo sapiens Chain B = 1.8e-10 21 32 View alignment SCOP MMDB CATH Chain A = 1.8e-10 21 32 View alignment 1og5 ( Chain: B, A) Structure of human cytochrome p450 cyp2c9 PDB_Info PDB_Structure Homo sapiens Chain B = 1.8e-10 21 32 View alignment SCOP MMDB CATH Chain A = 1.8e-10 21 32 View alignment 1jme ( Chain: B, A) Crystal structure of phe393his cytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain B = 1.9e-10 23 32 View alignment SCOP MMDB CATH Chain A = 1.9e-10 23 32 View alignment 1p0v ( Chain: B, A) F393a mutant heme domain of flavocytochrome p450 bm3 PDB_Info PDB_Structure Bacillus megaterium Chain B = 2.9e-10 23 32 View alignment SCOP MMDB CATH Chain A = 2.9e-10 23 32 View alignment 3c6g ( Chain: B, A) Crystal structure of cyp2r1 in complex with vitamin d3 PDB_Info PDB_Structure Homo sapiens Chain B = 3.0e-10 24 31 View alignment SCOP MMDB CATH Chain A = 3.0e-10 24 31 View alignment 3dl9 ( Chain: B, A) Crystal structure of cyp2r1 in complex with 1-alpha-hydroxy- vitamin d2 PDB_Info PDB_Structure Homo sapiens Chain B = 3.0e-10 24 31 View alignment SCOP MMDB CATH Chain A = 3.0e-10 24 31 View alignment 3czh ( Chain: A, B) Crystal structure of cyp2r1 in complex with vitamin d2 PDB_Info PDB_Structure Homo sapiens Chain A = 3.1e-10 24 31 View alignment SCOP MMDB CATH Chain B = 3.1e-10 24 31 View alignment 2bz9 ( Chain: B, A) Ligand-free structure of sterol 14alpha-demethylase from mycobacterium tuberculosis in p2(1) space group PDB_Info PDB_Structure Mycobacterium tuberculosis Chain B = 1.0e-09 24 38 View alignment SCOP MMDB CATH Chain A = 1.0e-09 24 38 View alignment 1u13 ( Chain: A) Crystal structure analysis of the c37l/c151t/c442a-triple mutant of cyp51 from mycobacterium tuberculosis PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 2w0b ( Chain: A) Cyp51 of m. tuberculosis bound to an inhibitor 3-{[(4- methylphenyl)sulfonyl]amino}propyl pyridin-4-ylcarbamate PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 2vku ( Chain: A) ,4'-dihydroxybenzophenone mimics sterol substrate in the binding site of sterol 14alpha-demethylase (cyp51) in the x-ray structure of the complex PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 2w09 ( Chain: A) Cyp51 of m. tuberculosis bound to an inhibitor cis-4- methyl-n-[(1s)-3-(methylsulfanyl)-1-(pyridin-4- ylcarbamoyl)propyl]cyclohexanecarboxamide PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 2w0a ( Chain: A) Cyp51 of m. tuberculosis bound to an inhibitor n-[(1s)-2-methyl-1-(pyridin-4-ylcarbamoyl)propyl] cyclohexanecarboxamide PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 2ci0 ( Chain: A) High throughput screening and x-ray crystallography assisted evaluation of small molecule scaffolds for cyp51 inhibitors PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 2cib ( Chain: A) High throughput screening and x-ray crystallography assisted evaluation of small molecule scaffolds for cyp51 inhibitors PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 1x8v ( Chain: A) Estriol-bound and ligand-free structures of sterol 14alpha- demethylase (cyp51) PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 1ea1 ( Chain: A) Cytochrome p450 14 alpha-sterol demethylase (cyp51) from mycobacterium tuberculosis in complex with fluconazole PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 1h5z ( Chain: A) Cytochrome p450 14 alpha-sterol demethylase (cyp51) from mycobacterium tuberculosis in ferric low-spin state PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 1e9x ( Chain: A) Cytochrome p450 14 alpha-sterol demethylase (cyp51) from mycobacterium tuberculosis in complex with 4-phenylimidazole PDB_Info PDB_Structure Mycobacterium tuberculosis 1.0e-09 24 38 View alignment SCOP MMDB CATH 1r9o ( Chain: A) Crystal structure of p4502c9 with flurbiprofen bound PDB_Info PDB_Structure Homo sapiens 1.9e-09 21 32 View alignment SCOP MMDB CATH 3e4e ( Chain: B, A) Human cytochrome p450 2e1 in complex with the inhibitor 4- methylpyrazole PDB_Info PDB_Structure Homo sapiens Chain B = 1.9e-08 21 29 View alignment SCOP MMDB CATH Chain A = 1.9e-08 21 29 View alignment 3e6i ( Chain: A, B) Human cytochrome p450 2e1 in complex with the inhibitor indazole PDB_Info PDB_Structure Homo sapiens Chain A = 1.9e-08 21 29 View alignment SCOP MMDB CATH Chain B = 1.9e-08 21 29 View alignment 1nr6 ( Chain: A) Microsomal cytochrome p450 2c5/3lvdh complex with diclofenac PDB_Info PDB_Structure Oryctolagus cuniculus 3.7e-08 22 32 View alignment SCOP MMDB CATH 1n6b ( Chain: A) Microsomal cytochrome p450 2c5/3lvdh complex with a dimethyl derivative of sulfaphenazole PDB_Info PDB_Structure Oryctolagus cuniculus 3.7e-08 22 32 View alignment SCOP MMDB CATH 1dt6 ( Chain: A) Structure of mammalian cytochrome p450 2c5 PDB_Info PDB_Structure Oryctolagus cuniculus 3.7e-08 22 32 View alignment SCOP MMDB CATH 2q9f ( Chain: A) Crystal structure of human cytochrome p450 46a1 in complex with cholesterol-3-sulphate PDB_Info PDB_Structure Homo sapiens 5.1e-08 18 38 View alignment SCOP MMDB CATH 2q9g ( Chain: A) Crystal structure of human cytochrome p450 46a1 PDB_Info PDB_Structure Homo sapiens 5.1e-08 18 38 View alignment SCOP MMDB CATH 3g1q ( Chain: D, A, B, C) Sterol 14-alpha-demethy PDB_Info PDB_Structure Unknown Chain D = 5.8e-08 20 35 View alignment SCOP MMDB CATH Chain A = 5.8e-08 20 35 View alignment Chain B = 5.8e-08 20 35 View alignment Chain C = 5.8e-08 20 35 View alignment 3eqm ( Chain: A) Crystal structure of human placental aromatase cytochrome p450 in complex with androstenedione PDB_Info PDB_Structure Homo sapiens 2.1e-07 23 28 View alignment SCOP MMDB CATH 1pq2 ( Chain: A, B) Crystal structure of human drug metabolizing cytochrome p450 2c8 PDB_Info PDB_Structure Homo sapiens Chain A = 3.9e-07 20 32 View alignment SCOP MMDB CATH Chain B = 3.9e-07 20 32 View alignment 2nnh ( Chain: B, A) Cyp2c8dh complexed with 2 molecules of 9-cis retinoic acid PDB_Info PDB_Structure Homo sapiens Chain B = 3.9e-07 20 32 View alignment SCOP MMDB CATH Chain A = 3.9e-07 20 32 View alignment 2nnj ( Chain: A) Cyp2c8dh complexed with felodipine PDB_Info PDB_Structure Homo sapiens 3.9e-07 20 32 View alignment SCOP MMDB CATH 2vn0 ( Chain: A) Cyp2c8dh complexed with troglitazone PDB_Info PDB_Structure Homo sapiens 3.9e-07 20 32 View alignment SCOP MMDB CATH 2nni ( Chain: A) Cyp2c8dh complexed with montelukast PDB_Info PDB_Structure Homo sapiens 3.9e-07 20 32 View alignment SCOP MMDB CATH 2p85 ( Chain: B, A, E, F, D, C) Structure of human lung cytochrome p450 2a13 with indole bound in two alternate conformations PDB_Info PDB_Structure Homo sapiens Chain B = 4.6e-07 26 34 View alignment SCOP MMDB CATH Chain A = 4.6e-07 26 34 View alignment Chain E = 4.6e-07 26 34 View alignment Chain F = 4.6e-07 26 34 View alignment Chain D = 4.6e-07 26 34 View alignment Chain C = 4.6e-07 26 34 View alignment 3ebs ( Chain: D, A, B, C) Human cytochrome p450 2a6 i208s/i300f/g301a/s369g in complex with phenacetin PDB_Info PDB_Structure Homo sapiens Chain D = 4.6e-07 21 30 View alignment SCOP MMDB CATH Chain A = 4.6e-07 21 30 View alignment Chain B = 4.6e-07 21 30 View alignment Chain C = 4.6e-07 21 30 View alignment 2zqj ( Chain: A, B, C) Cytochrome P450 152A1 PDB_Info PDB_Structure Unknown Chain A = 4.9e-06 26 25 View alignment SCOP MMDB CATH Chain B = 4.9e-06 26 25 View alignment Chain C = 4.9e-06 26 25 View alignment 1izo ( Chain: B, A, C) Cytochrome p450 bs beta complexed with fatty acid PDB_Info PDB_Structure Bacillus subtilis Chain B = 4.9e-06 26 25 View alignment SCOP MMDB CATH Chain A = 4.9e-06 26 25 View alignment Chain C = 4.9e-06 26 25 View alignment 2zqx ( Chain: C, A, B) Cytochrome P450 152A1 PDB_Info PDB_Structure Unknown Chain C = 4.9e-06 26 25 View alignment SCOP MMDB CATH Chain A = 4.9e-06 26 25 View alignment Chain B = 4.9e-06 26 25 View alignment 2fdw ( Chain: C, D, B, A) Crystal structure of human microsomal p450 2a6 with the inhibitor (5-(pyridin-3-yl)furan-2-yl)methanamine bound PDB_Info PDB_Structure Homo sapiens Chain C = 4.9e-06 26 33 View alignment SCOP MMDB CATH Chain D = 4.9e-06 26 33 View alignment Chain B = 4.9e-06 26 33 View alignment Chain A = 4.9e-06 26 33 View alignment 2fdy ( Chain: C, B, D, A) Microsomal p450 2a6 with the inhibitor adrithiol bound PDB_Info PDB_Structure Homo sapiens Chain C = 4.9e-06 26 33 View alignment SCOP MMDB CATH Chain B = 4.9e-06 26 33 View alignment Chain D = 4.9e-06 26 33 View alignment Chain A = 4.9e-06 26 33 View alignment 2fdu ( Chain: D, B, C, A) Microsomal p450 2a6 with the inhibitor n,n-dimethyl(5- (pyridin-3-yl)furan-2-yl)methanamine bound PDB_Info PDB_Structure Homo sapiens Chain D = 4.9e-06 26 33 View alignment SCOP MMDB CATH Chain B = 4.9e-06 26 33 View alignment Chain C = 4.9e-06 26 33 View alignment Chain A = 4.9e-06 26 33 View alignment 1z11 ( Chain: A, B, C, D) Crystal structure of human microsomal p450 2a6 with methoxsalen bound PDB_Info PDB_Structure Homo sapiens Chain A = 4.9e-06 26 33 View alignment SCOP MMDB CATH Chain B = 4.9e-06 26 33 View alignment Chain C = 4.9e-06 26 33 View alignment Chain D = 4.9e-06 26 33 View alignment 1z10 ( Chain: B, D, C, A) Crystal structure of human microsomal p450 2a6 with coumarin bound PDB_Info PDB_Structure Homo sapiens Chain B = 4.9e-06 26 33 View alignment SCOP MMDB CATH Chain D = 4.9e-06 26 33 View alignment Chain C = 4.9e-06 26 33 View alignment Chain A = 4.9e-06 26 33 View alignment 2fdv ( Chain: A, B, D, C) Microsomal p450 2a6 with the inhibitor n-methyl(5-(pyridin- 3-yl)furan-2-yl)methanamine bound PDB_Info PDB_Structure Homo sapiens Chain A = 4.9e-06 26 33 View alignment SCOP MMDB CATH Chain B = 4.9e-06 26 33 View alignment Chain D = 4.9e-06 26 33 View alignment Chain C = 4.9e-06 26 33 View alignment 2pg5 ( Chain: A, C, B, D) Crystal structure of human microsomal p450 2a6 n297q PDB_Info PDB_Structure Homo sapiens Chain A = 5.7e-06 26 32 View alignment SCOP MMDB CATH Chain C = 5.7e-06 26 32 View alignment Chain B = 5.7e-06 26 32 View alignment Chain D = 5.7e-06 26 32 View alignment 2pg6 ( Chain: D, C, B, A) Crystal structure of human microsomal p450 2a6 l240c/n297q PDB_Info PDB_Structure Homo sapiens Chain D = 5.7e-06 26 32 View alignment SCOP MMDB CATH Chain C = 5.7e-06 26 32 View alignment Chain B = 5.7e-06 26 32 View alignment Chain A = 5.7e-06 26 32 View alignment 2pg7 ( Chain: A, B, D, C) Crystal structure of human microsomal p450 2a6 n297q/i300v PDB_Info PDB_Structure Homo sapiens Chain A = 6.8e-06 26 32 View alignment SCOP MMDB CATH Chain B = 6.8e-06 26 32 View alignment Chain D = 6.8e-06 26 32 View alignment Chain C = 6.8e-06 26 32 View alignment 2f9q ( Chain: C, D, A, B) Crystal structure of human cytochrome p450 2d6 PDB_Info PDB_Structure Homo sapiens Chain C = 8.2e-06 25 36 View alignment SCOP MMDB CATH Chain D = 8.2e-06 25 36 View alignment Chain A = 8.2e-06 25 36 View alignment Chain B = 8.2e-06 25 36 View alignment 2hi4 ( Chain: A) Crystal structure of human microsomal p450 1a2 in complex with alpha-naphthoflavone PDB_Info PDB_Structure Homo sapiens 1.7e-05 20 31 View alignment SCOP MMDB CATH 3dsj ( Chain: B, A) Crystal structure of arabidopsis thaliana allene oxide synthase variant (f137l) (at-aos(f137l), cytochrome p450 74a, cyp74a) complexed with 13(s)-hod at 1.60 a resolution PDB_Info PDB_Structure Arabidopsis thaliana Chain B = 1.9e-05 27 30 View alignment SCOP MMDB CATH Chain A = 1.9e-05 27 30 View alignment 3dsi ( Chain: A, B) Crystal structure of arabidopsis thaliana allene oxide synthase (aos, cytochrome p450 74a, cyp74a) complexed with 13(s)-hot at 1.60 a resolution PDB_Info PDB_Structure Arabidopsis thaliana Chain A = 1.9e-05 27 30 View alignment SCOP MMDB CATH Chain B = 1.9e-05 27 30 View alignment 2rcm ( Chain: A, B) Crystal structure of arabidopsis thaliana allene oxide synthase variant (f137l) (at-aos(f137l), cytochrome p450 74a) at 1.73 a resolution PDB_Info PDB_Structure Arabidopsis thaliana Chain A = 1.9e-05 27 30 View alignment SCOP MMDB CATH Chain B = 1.9e-05 27 30 View alignment 2rch ( Chain: A, B) Crystal structure of arabidopsis thaliana allene oxide synthase (aos, cytochrome p450 74a, cyp74a) complexed with 13(s)-hod at 1.85 a resolution PDB_Info PDB_Structure Arabidopsis thaliana Chain A = 1.9e-05 27 30 View alignment SCOP MMDB CATH Chain B = 1.9e-05 27 30 View alignment 3dsk ( Chain: A, B) Crystal structure of arabidopsis thaliana allene oxide synthase variant (f137l) (at-aos(f137l), cytochrome p450 74a, cyp74a) complexed with 12r,13s-vernolic acid at 1.55 a resolution PDB_Info PDB_Structure Arabidopsis thaliana Chain A = 1.9e-05 27 30 View alignment SCOP MMDB CATH Chain B = 1.9e-05 27 30 View alignment 2rcl ( Chain: A, B) Crystal structure of arabidopsis thaliana allene oxide synthase (aos, cytochrome p450 74a, cyp74a) complexed with 12r,13s-vernolic acid at 2.4 a resolution PDB_Info PDB_Structure Arabidopsis thaliana Chain A = 1.9e-05 27 30 View alignment SCOP MMDB CATH Chain B = 1.9e-05 27 30 View alignment 3cli ( Chain: B, A) Crystal structure of arabidopsis thaliana allene oxide synthase (aos, cytochrome p450 74a, cyp74a) at 1.80 a resolution PDB_Info PDB_Structure Arabidopsis thaliana Chain B = 1.9e-05 27 30 View alignment SCOP MMDB CATH Chain A = 1.9e-05 27 30 View alignment 3dbm ( Chain: A) Crystal structure of allene oxide synthase PDB_Info PDB_Structure Parthenium argentatum 3.0e-05 30 26 View alignment SCOP MMDB CATH 3dam ( Chain: A) Crystal structure of allene oxide synthase PDB_Info PDB_Structure Parthenium argentatum 3.0e-05 30 26 View alignment SCOP MMDB CATH 3dan ( Chain: A) Crystal structure of allene oxide synthase PDB_Info PDB_Structure Parthenium argentatum 3.0e-05 30 26 View alignment SCOP MMDB CATH 2iag ( Chain: B, A) Crystal structure of human prostacyclin synthase PDB_Info PDB_Structure Homo sapiens Chain B = 3.6e-05 22 32 View alignment SCOP MMDB CATH Chain A = 3.6e-05 22 32 View alignment 3b6h ( Chain: B, A) Crystal structure of human prostacyclin synthase in complex with inhibitor minoxidil PDB_Info PDB_Structure Homo sapiens Chain B = 3.8e-05 22 32 View alignment SCOP MMDB CATH Chain A = 3.8e-05 22 32 View alignment 3dax ( Chain: A, B) Crystal structure of human cyp7a1 PDB_Info PDB_Structure Homo sapiens Chain A = 0.000279 21 31 View alignment SCOP MMDB CATH Chain B = 0.000279 21 31 View alignment 3b4x ( Chain: A) Crystal structure analysis of sulfolobus tokodaii strain7 cytochrom p450 PDB_Info PDB_Structure Sulfolobus tokodaii 0.002800 29 27 View alignment SCOP MMDB CATH 1ue8 ( Chain: A) Crystal structure of thermophilic cytochrome p450 from sulfolobus tokodaii PDB_Info PDB_Structure Sulfolobus tokodaii 0.002800 29 27 View alignment SCOP MMDB CATH 1n97 ( Chain: A, B) Crystal stucture of cyp175a1 from thermus thermophillus strain hb27 PDB_Info PDB_Structure Thermus thermophilus HB27 Chain A = 0.003599 23 28 View alignment SCOP MMDB CATH Chain B = 0.003599 23 28 View alignment 1wiy ( Chain: B, A) Crystal structure analysis of a 6-coordinated cytochorome p450 from thermus thermophilus hb8 PDB_Info PDB_Structure Thermus thermophilus Chain B = 0.006998 22 29 View alignment SCOP MMDB CATH Chain A = 0.006998 22 29 View alignment

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
ERG5	SGD (2007) Information without a citation in SGD

Alias Name(s)	Reference
CYP61	Kelly SL, et al. (1997) Characterization of Saccharomyces cerevisiae CYP61, sterol delta22-desaturase, and inhibition by azole antifungal agents. J Biol Chem 272(15):9986-8

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YMR015C	SGD Systematic Sequence
855029	NCBI: Gene ID
NP_013728.1	NCBI: RefSeq protein version ID
NP_013728.1	NCBI: RefSeq protein version ID
6323657	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources YeastRC Localization (Seattle) Organelle DB (UMich) YGAC Triples YPL.db at Uni Graz YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]
No community annotation available.

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
64 curated references; 0 references not yet curated
Genetic Interactions Mutants/Phenotypes	Hodg CA, et al. (2010) Integral membrane proteins Brr6 and Apq12 link assembly of the nuclear pore complex to lipid homeostasis in the endoplasmic reticulum. J Cell Sci 123(Pt 1):141-151	|ACC1 |APQ12 |ARE1 |ARE2 |ARV1 |BRR6 |DGA1 |ELO1 |ERG2 |ERG3 |ERG4 |ERG6 |FEN1 |LRO1 |MORE
Regulation of	Zeng T and Li J (2010) Maximization of negative correlations in time-course gene expression data for enhancing understanding of molecular pathways. Nucleic Acids Res 38(1):e1	|ACO2 |ADR1 |CAB2 |CAT8 |CIT1 |ERG2 |ERG26 |ERG27 |ERG4 |ERG6 |GCN4 |GTT1 |HAP1 |HAP3 |MORE
Mutants/Phenotypes Strains/Constructs	Abe F and Hiraki T (2009) Mechanistic role of ergosterol in membrane rigidity and cycloheximide resistance in Saccharomyces cerevisiae. Biochim Biophys Acta 1788(3):743-52	|ERG2 |ERG3 |ERG4 |ERG6 |PDR5 |UPC2
Mutants/Phenotypes Strains/Constructs	Daicho K, et al. (2009) Sorting defects of the tryptophan permease Tat2 in an erg2 yeast mutant. FEMS Microbiol Lett 298(2):218-27	|ERG2 |ERG3 |ERG4 |ERG6 |TAT2 |TRP1
Cell Growth and Metabolism Industrial Applications Transcription	Endo A, et al. (2009) Involvement of ergosterol in tolerance to vanillin, a potential inhibitor of bioethanol fermentation, in Saccharomyces cerevisiae. FEMS Microbiol Lett	|ERG28 |ERG7 |HMG1 |MCR1
Mutants/Phenotypes Strains/Constructs	Jones L, et al. (2009) Cdc42p is activated during vacuole membrane fusion in a sterol-dependent subreaction of priming. J Biol Chem	|CDC42 |ERG2 |ERG3 |ERG4 |ERG6 |RDI1 |SEC17 |SEC18 |STE20
Mutants/Phenotypes Strains/Constructs	Singh J and Tyers M (2009) A Rab escort protein integrates the secretion system with TOR signaling and ribosome biogenesis. Genes Dev 23(16):1944-58	|AKR1 |AVL9 |DPM1 |ERV29 |GAB1 |GPI16 |MRS6 |MSB4 |MSN5 |PKC1 |ROT1 |SEC17 |SEC20 |SEC23 |MORE
Genetic Interactions Mutants/Phenotypes Regulation of Strains/Constructs Transcription	Wei M, et al. (2009) Tor1/Sch9-regulated carbon source substitution is as effective as calorie restriction in life span extension. PLoS Genet 5(5):e1000467	|DAK1 |DAK2 |ERG28 |ERG4 |FMP45 |GCY1 |GIS1 |GPD1 |GPD2 |GRE1 |HOR2 |IME1 |RAS1 |RAS2 |MORE
Mutants/Phenotypes	Yoshikawa K, et al. (2009) Comprehensive phenotypic analysis for identification of genes affecting growth under ethanol stress in Saccharomyces cerevisiae. FEMS Yeast Res 9(1):32-44	|ALD6 |ARO1 |ARO2 |ARO7 |COQ10 |COQ5 |COQ9 |COX11 |COX12 |COX14 |COX16 |COX18 |COX23 |COX7 |MORE
Mutants/Phenotypes Strains/Constructs	de Graaf B, et al. (2009) Cellular pathways for DNA repair and damage tolerance of formaldehyde-induced DNA-protein crosslinks. DNA Repair (Amst) 8(10):1207-14	|ADH1 |ARP5 |BEM4 |CDC26 |CDC50 |CTF4 |DAL81 |ECM30 |ERG3 |ERG6 |LSM1 |MED1 |MGM101 |MMS22 |MORE
Non-Fungal Related Genes/Proteins	Arnqvist L, et al. (2008) Overexpression of CYP710A1 and CYP710A4 in transgenic Arabidopsis plants increases the level of stigmasterol at the expense of sitosterol. Planta 227(2):309-17
Mutants/Phenotypes Strains/Constructs	Grossmann G, et al. (2008) Plasma membrane microdomains regulate turnover of transport proteins in yeast. J Cell Biol 183(6):1075-88	|CAN1 |CAX4 |COG1 |ELP6 |ERG2 |ERG24 |ERG6 |FUR4 |FYV6 |GOS1 |HNT3 |MDG1 |MNN10 |MNN11 |MORE
Fungal Related Genes/Proteins	Iwaki T, et al. (2008) Multiple functions of ergosterol in the fission yeast Schizosaccharomyces pombe. Microbiology 154(Pt 3):830-41	|ERG2 |ERG3 |ERG4 |ERG6
Mutants/Phenotypes Strains/Constructs	Tang F, et al. (2008) A life-span extending form of autophagy employs the vacuole-vacuole fusion machinery. Autophagy 4(7):874-86	|ATG1 |ATG10 |ATG11 |ATG15 |ATG17 |ATG22 |ATG7 |ATG8 |AVT3 |AVT4 |ERG2 |ERG28 |ERG6 |GSG1 |MORE
Genetic Interactions Infection and Antifungals Mutants/Phenotypes Strains/Constructs	Welscher YM, et al. (2008) Natamycin Blocks Fungal Growth by Binding Specifically to Ergosterol without Permeabilizing the Membrane. J Biol Chem 283(10):6393-401	|ERG2 |ERG3 |ERG4 |ERG6
Function/Process Strains/Constructs	Cai PL, et al. (2007) [Effect of over-expression of sterol C-22 desaturase on ergosterol production in yeast strains] Wei Sheng Wu Xue Bao 47(2):274-9
Regulation of Transcription	Hickman MJ and Winston F (2007) Heme Levels Switch the Function of Hap1 of Saccharomyces cerevisiae between Transcriptional Activator and Transcriptional Repressor. Mol Cell Biol 27(21):7414-24	|CYC1 |CYC8 |ERG11 |ERG2 |HAP1 |HSC82 |HSP82 |SSA1 |TUP1
Reviews	Schulz TA and Prinz WA (2007) Sterol transport in yeast and the oxysterol binding protein homologue (OSH) family. Biochim Biophys Acta 1771(6):769-80	|AUS1 |CAT5 |DAN1 |ERG1 |ERG11 |ERG27 |ERG3 |ERG6 |ERG7 |HES1 |KES1 |MGM101 |NCR1 |NPC2 |MORE
Regulation of Transcription	Buck MJ and Lieb JD (2006) A chromatin-mediated mechanism for specification of conditional transcription factor targets. Nat Genet 38(12):1446-51	|ACA1 |ACS1 |ADE3 |ADH1 |AGP1 |AIM38 |ANP1 |AQY1 |ASC1 |AST2 |ATG19 |AZF1 |BDF1 |BSC3 |MORE
Protein Processing/Modification/Regulation Techniques and Reagents	Tagwerker C, et al. (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking. Mol Cell Proteomics 5(4):737-48	|AAC1 |AAC3 |ACB1 |ACC1 |ACS2 |ADE3 |ADE5,7 |ADE6 |ADH4 |ADO1 |AGP1 |AHA1 |AHP1 |ALA1 |MORE
Genetic Interactions Mutants/Phenotypes	Valachovic M, et al. (2006) Cumulative mutations affecting sterol biosynthesis in the yeast Saccharomyces cerevisiae result in synthetic lethality that is suppressed by alterations in sphingolipid profiles. Genetics 173(4):1893-908	|BCK2 |ECM22 |ERG2 |ERG28 |ERG4 |ERG6 |GDA1 |HAP1 |HDA3 |IES1 |RDN25-1 |RDN37-1 |RPN9 |SSN2 |MORE
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Gaigg B, et al. (2005) Synthesis of sphingolipids with very long chain fatty acids but not ergosterol is required for routing of newly synthesized plasma membrane ATPase to the cell surface of yeast. J Biol Chem 280(23):22515-22	|ACB1 |ACC1 |ARE1 |ARE2 |AYR1 |CSG2 |DPL1 |ELO1 |ERG24 |ERG3 |ERG4 |FEN1 |HEM1 |IFA38 |MORE
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Kishimoto T, et al. (2005) Defects in structural integrity of ergosterol and the Cdc50p-Drs2p putative phospholipid translocase cause accumulation of endocytic membranes, onto which actin patches are assembled in yeast. Mol Biol Cell 16(12):5592-609	|ABP1 |ACT1 |BNI1 |CDC42 |CDC50 |DRS2 |ERG2 |ERG3 |ERG4 |ERG6 |GIC1 |LAS17 |SLA2 |SNC1
Protein-protein Interactions Techniques and Reagents	Mo C and Bard M (2005) A systematic study of yeast sterol biosynthetic protein-protein interactions using the split-ubiquitin system. Biochim Biophys Acta 1737(2-3):152-60	|ERG1 |ERG11 |ERG2 |ERG24 |ERG25 |ERG26 |ERG27 |ERG28 |ERG3 |ERG4 |ERG6 |ERG7 |ERG9
Mutants/Phenotypes Strains/Constructs	Sano T, et al. (2005) Regulation of the sphingoid long-chain base kinase Lcb4p by ergosterol and heme: studies in phytosphingosine-resistant mutants. J Biol Chem 280(44):36674-82	|DPL1 |ERG2 |ERG3 |ERG4 |ERG6 |HAP1 |HEM14 |HMG1 |KES1 |LCB3 |LCB4 |PBP1 |PDR5 |TPS1 |MORE
RNA Levels and Processing	Shobayashi M, et al. (2005) Effects of Culture Conditions on Ergosterol Biosynthesis by Saccharomyces cerevisiae. Biosci Biotechnol Biochem 69(12):2381-8	|ERG13 |ERG2 |ERG20 |ERG24 |ERG26 |ERG28 |ERG3 |ERG6 |HMG1
RNA Levels and Processing Techniques and Reagents	Krantz M, et al. (2004) Anaerobicity prepares Saccharomyces cerevisiae cells for faster adaptation to osmotic shock. Eukaryot Cell 3(6):1381-90	|ALD2 |ALD3 |ALD4 |ALD6 |CTT1 |ERG1 |ERG10 |ERG11 |ERG12 |ERG13 |ERG2 |ERG20 |ERG24 |ERG25 |MORE
Function/Process Mutants/Phenotypes Strains/Constructs	Markovich S, et al. (2004) Genomic approach to identification of mutations affecting caspofungin susceptibility in Saccharomyces cerevisiae. Antimicrob Agents Chemother 48(10):3871-6	|BCK1 |CCR4 |CHC1 |CHS3 |CHS7 |CKA2 |CSG2 |ERG3 |ERG6 |FKS1 |ILM1 |MID2 |MNN10 |NPL3 |MORE
Genomic expression study RNA Levels and Processing Regulation of	Parveen M, et al. (2004) Response of Saccharomyces cerevisiae to a monoterpene: evaluation of antifungal potential by DNA microarray analysis. J Antimicrob Chemother 54(1):46-55	|AAD6 |ADH5 |ADH7 |ADY2 |AGA2 |AMS1 |ARG1 |ARN2 |ATF2 |ATX1 |BCK1 |BFR1 |BSC1 |BUD7 |MORE
Regulation of Transcription	Agarwal AK, et al. (2003) Genome-wide expression profiling of the response to polyene, pyrimidine, azole, and echinocandin antifungal agents in Saccharomyces cerevisiae. J Biol Chem 278(37):34998-5015	|AGA1 |AMS1 |ATF2 |AUS1 |BAG7 |BAP2 |BAP3 |CRH1 |CTR1 |CWP1 |CYB5 |DAN1 |DAN4 |ELO1 |MORE
Non-Fungal Related Genes/Proteins	Noda H and Koizumi Y (2003) Sterol biosynthesis by symbiotes: cytochrome P450 sterol C-22 desaturase genes from yeastlike symbiotes of rice planthoppers and anobiid beetles. Insect Biochem Mol Biol 33(6):649-58
Protein Physical Properties Techniques and Reagents	Peng J, et al. (2003) A proteomics approach to understanding protein ubiquitination. Nat Biotechnol 21(8):921-6	|ACS2 |ADE13 |AKL1 |ALD6 |ARO10 |BSD2 |CCT8 |CDC48 |CHD1 |CHS3 |CIT2 |COS4 |CSR2 |CTR9 |MORE
Regulation of Transcription	Zhang W, et al. (2003) Microarray analyses of the metabolic responses of Saccharomyces cerevisiae to organic solvent dimethyl sulfoxide. J Ind Microbiol Biotechnol 30(1):57-69	|AAH1 |ABP140 |ACS2 |ADE1 |ADE12 |ADE17 |ADE4 |ADE8 |ADH2 |ADH4 |ADH5 |ADK1 |ADO1 |ALD3 |MORE
Mutants/Phenotypes Strains/Constructs	Desmoucelles C, et al. (2002) Screening the yeast "disruptome" for mutants affecting resistance to the immunosuppressive drug, mycophenolic acid. J Biol Chem 277(30):27036-44	|ANP1 |BUD30 |CTK1 |CTK3 |DAL81 |DST1 |ERG24 |ERG3 |ERG4 |ERG6 |GCN5 |HOM2 |HPR1 |HTZ1 |MORE
Function/Process	Ruan B, et al. (2002) Alternative pathways of sterol synthesis in yeast. Use of C(27) sterol tracers to study aberrant double-bond migrations and evaluate their relative importance. Steroids 67(13-14):1109-19	|ERG2 |ERG3
Non-Fungal Related Genes/Proteins	Hashizume T, et al. (2001) cDNA cloning and expression of a novel cytochrome p450 (cyp4f12) from human small intestine. Biochem Biophys Res Commun 280(4):1135-41
Non-Fungal Related Genes/Proteins	Imaoka S, et al. (2001) A transgenic mouse expressing human CYP4B1 in the liver. Biochem Biophys Res Commun 284(3):757-62
Function/Process Mutants/Phenotypes Strains/Constructs	Kato M and Wickner W (2001) Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion. EMBO J 20(15):4035-40	|ERG3 |ERG4 |ERG6 |SEC17 |SEC18
Non-Fungal Related Genes/Proteins	Le Bouquin R, et al. (2001) CYP94A5, a new cytochrome P450 from Nicotiana tabacum is able to catalyze the oxidation of fatty acids to the omega-alcohol and to the corresponding diacid. Eur J Biochem 268(10):3083-90
Mutants/Phenotypes Strains/Constructs	Bammert GF and Fostel JM (2000) Genome-wide expression patterns in Saccharomyces cerevisiae: comparison of drug treatments and genetic alterations affecting biosynthesis of ergosterol. Antimicrob Agents Chemother 44(5):1255-65	|ERG2 |ERG25 |ERG6 |RGI1 |TOS6
Mutants/Phenotypes Substrates/Ligands/Cofactors	Jia MH, et al. (2000) Global expression profiling of yeast treated with an inhibitor of amino acid biosynthesis, sulfometuron methyl. Physiol Genomics 3(2):83-92	|ERG3 |GCN4
Genomic expression study Regulation of	Dimster-Denk D, et al. (1999) Comprehensive evaluation of isoprenoid biosynthesis regulation in Saccharomyces cerevisiae utilizing the Genome Reporter Matrix. J Lipid Res 40(5):850-60	|ARE1 |ARE2 |BEM1 |BET2 |BET4 |BTS1 |CAT5 |CDC43 |COQ1 |COQ2 |COQ3 |COQ6 |COX10 |ERG1 |MORE
Fungal Related Genes/Proteins	Lamb DC, et al. (1999) Purification, reconstitution, and inhibition of cytochrome P-450 sterol delta22-desaturase from the pathogenic fungus Candida glabrata. Antimicrob Agents Chemother 43(7):1725-8	|ERG11
Reviews	Daum G, et al. (1998) Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae. Yeast 14(16):1471-510	|ACC1 |ACP1 |AUR1 |CDS1 |CEM1 |CHO1 |CHO2 |CKI1 |CPT1 |CRD1 |CSG2 |DPL1 |DPP1 |EPT1 |MORE
Mutants/Phenotypes Strains/Constructs Techniques and Reagents	Duport C, et al. (1998) Self-sufficient biosynthesis of pregnenolone and progesterone in engineered yeast. Nat Biotechnol 16(2):186-9
Function/Process Genetic Interactions Strains/Constructs	Venkateswarlu K, et al. (1998) NADPH cytochrome P-450 oxidoreductase and susceptibility to ketoconazole. Antimicrob Agents Chemother 42(7):1756-61	|ERG11 |NCP1
Alias Function/Process Strains/Constructs Substrates/Ligands/Cofactors	Venkateswarlu K, et al. (1998) The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity. J Biol Chem 273(8):4492-6	|ERG11 |NCP1
Reviews	van den Brink HM, et al. (1998) Cytochrome P450 enzyme systems in fungi. Fungal Genet Biol 23(1):1-17	|DIT2 |ERG11 |NCP1
Alias Function/Process Protein Physical Properties Substrates/Ligands/Cofactors	Kelly SL, et al. (1997) Characterization of Saccharomyces cerevisiae CYP61, sterol delta22-desaturase, and inhibition by azole antifungal agents. J Biol Chem 272(15):9986-8	|ERG11
Function/Process	Kelly SL, et al. (1997) Sterol 22-desaturase, cytochrome P45061, possesses activity in xenobiotic metabolism. FEBS Lett 412(1):233-5
Mutants/Phenotypes Strains/Constructs	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	|ARE1 |ARE2 |ERG2 |ERG3 |ERG4 |ERG6
DNA/RNA Sequence Features Function/Process Mutants/Phenotypes Protein Physical Properties Protein Sequence Features Strains/Constructs Techniques and Reagents	Skaggs BA, et al. (1996) Cloning and characterization of the Saccharomyces cerevisiae C-22 sterol desaturase gene, encoding a second cytochrome P-450 involved in ergosterol biosynthesis. Gene 169(1):105-9
Function/Process Protein Physical Properties	Kelly SL, et al. (1995) Purification and reconstitution of activity of Saccharomyces cerevisiae P450 61, a sterol delta 22-desaturase. FEBS Lett 377(2):217-20
Reviews	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	|ERG1 |ERG11 |ERG2 |ERG24 |ERG3 |ERG4 |ERG6 |ERG7 |ERG9 |FEN1 |FEN2
Reviews	Parks LW and Casey WM (1995) Physiological implications of sterol biosynthesis in yeast. Annu Rev Microbiol 49:95-116	|ERG1 |ERG10 |ERG11 |ERG12 |ERG13 |ERG2 |ERG20 |ERG24 |ERG25 |ERG3 |ERG4 |ERG6 |ERG7 |ERG8 |MORE
Reviews	Parks LW, et al. (1995) Biochemical and physiological effects of sterol alterations in yeast--a review. Lipids 30(3):227-30	|ERG1 |ERG10 |ERG11 |ERG12 |ERG2 |ERG20 |ERG24 |ERG3 |ERG4 |ERG6 |ERG7 |ERG8 |ERG9 |HMG1 |MORE
Reviews	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	|ACC1 |ACH1 |CDS1 |CHO1 |CHO2 |CKI1 |CTR1 |ERG1 |ERG10 |ERG11 |ERG12 |ERG13 |ERG2 |ERG20 |MORE
Mutants/Phenotypes Regulation of Strains/Constructs Techniques and Reagents	Hata S, et al. (1983) Characterization of a Saccharomyces cerevisiae mutant, N22, defective in ergosterol synthesis and preparation of [28-14C]ergosta-5,7-dien-3 beta-ol with the mutant. J Biochem 94(2):501-10
Fungal Related Genes/Proteins Mutants/Phenotypes Strains/Constructs	Hata S, et al. (1983) Two species of cytochrome P-450 involved in ergosterol biosynthesis of yeast. Biochem Biophys Res Commun 116(1):162-6
Function/Process	Hata S, et al. (1981) Involvement of cytochrome P-450 in delta 22-desaturation in ergosterol biosynthesis of yeast. Biochem Biophys Res Commun 103(1):272-7
Other Features	Nagai J, et al. (1981) Increased proportion of medium chain fatty acids in nystatin-resistant yeast mutants. Lipids 16(6):411-7	|ERG2
Cellular Location	Nishino T, et al. (1981) Subcellular localization of the enzymes involved in the late stage of ergosterol biosynthesis in yeast. J Biochem 89(5):1391-6	|ERG3
Other Features	Pierce AM, et al. (1979) Azasterol inhibitors in yeast. Inhibition of the delta 24-sterol methyltransferase and the 24-methylene sterol delta 24(28)-reductase in sterol mutants of Saccharomyces cerevisiae. Can J Biochem 57(3):201-8	|ERG2 |ERG6
Alias Genetic Interactions Mutants/Phenotypes Strains/Constructs Techniques and Reagents	Bard M, et al. (1977) Sterol mutants of Saccharomyces cerevisiae: chromatographic analyses. Lipids 12(8):645-54	|ERG2 |ERG3 |ERG6

Return to SGD

Send a Message to the SGD Curators