YEAST:ERG6

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	ERG6 (synonyms: ISE1, LIS1, SED6)
Protein Name(s)	Sterol 24-C-methyltransferase Delta(24)-sterol C-methyltransferase
External Links
UniProt	P25087
EMBL	X74249 S72460 Z49810 X53830 BK006946
PIR	S42003
RefSeq	NP_013706.1
ProteinModelPortal	P25087
SMR	P25087
BioGrid	35161
DIP	DIP-3816N
IntAct	P25087
MINT	MINT-537879
STRING	4932.YML008C
SWISS-2DPAGE	P25087
MaxQB	P25087
PaxDb	P25087
PeptideAtlas	P25087
EnsemblFungi	[example_ID YML008C]
GeneID	855003
KEGG	sce:YML008C
SGD	S000004467
eggNOG	COG0500
GeneTree	ENSGT00530000069303
HOGENOM	HOG000171097
InParanoid	P25087
KO	K00559
OMA	FHFCRFS
OrthoDB	EOG7DVDMW
BioCyc	MetaCyc:MONOMER3O-188 YEAST:MONOMER3O-188
SABIO-RK	P25087
UniPathway	UPA00768
NextBio	978157
Proteomes	UP000002311
Genevestigator	P25087
GO	GO:0005783 GO:0005811 GO:0003838 GO:0006696
Gene3D	3.40.50.150
InterPro	IPR013216 IPR030384 IPR029063 IPR013705
Pfam	PF08241 PF08498
SUPFAM	SSF53335
PROSITE	PS51685

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0005741	mitochondrial outer membrane	PMID:16407407^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16823961^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:24769239^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:14576278^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006696	ergosterol biosynthetic process	PMID:2677674^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006696	ergosterol biosynthetic process	PMID:6363386^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005811	lipid droplet	PMID:24868093^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005811	lipid droplet	PMID:10515935^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:11298754^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:9450962^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003838	sterol 24-C-methyltransferase activity	PMID:18563465^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0016126	sterol biosynthetic process	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000189580 PANTHER:PTN002226525 PomBase:SPBC16E9.05 SGD:S000004467 TAIR:locus:2173229	P	Seeded From UniProt	complete
enables	GO:0008757	S-adenosylmethionine-dependent methyltransferase activity	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000189580 PANTHER:PTN000741154 SGD:S000004467 TAIR:locus:2173229 WB:WBGene00019198	F	Seeded From UniProt	complete
involved_in	GO:0006696	ergosterol biosynthetic process	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000189580 PANTHER:PTN000802684 PomBase:SPBC16E9.05 SGD:S000004467	P	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002226525 SGD:S000004467 TAIR:locus:2173229 dictyBase:DDB_G0288907	C	Seeded From UniProt	complete
enables	GO:0003838	sterol 24-C-methyltransferase activity	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000189580 PANTHER:PTN002226525 SGD:S000004467 TAIR:locus:2173229	F	Seeded From UniProt	complete
involved_in	GO:0006694	steroid biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013705	P	Seeded From UniProt	complete
enables	GO:0008168	methyltransferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013216 InterPro:IPR013705 InterPro:IPR030384	F	Seeded From UniProt	complete
enables	GO:0003838	sterol 24-C-methyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.1.1.41	F	Seeded From UniProt	complete
involved_in	GO:0016126	sterol biosynthetic process	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0756 UniPathway:UPA00768	P	Seeded From UniProt	complete
involved_in	GO:0006694	steroid biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0752	P	Seeded From UniProt	complete
enables	GO:0008168	methyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0489	F	Seeded From UniProt	complete
involved_in	GO:0008202	steroid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0753	P	Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	P	Seeded From UniProt	complete
involved_in	GO:0032259	methylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0489	P	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Zahedi, RP et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol. Biol. Cell 17 1436-50 PubMed GONUTS page
↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
↑ Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page
↑ Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
↑ Gaber, RF et al. (1989) The yeast gene ERG6 is required for normal membrane function but is not essential for biosynthesis of the cell-cycle-sparking sterol. Mol. Cell. Biol. 9 3447-56 PubMed GONUTS page
↑ McCammon, MT et al. (1984) Sterol methylation in Saccharomyces cerevisiae. J. Bacteriol. 157 475-83 PubMed GONUTS page
↑ Currie, E et al. (2014) High confidence proteomic analysis of yeast LDs identifies additional droplet proteins and reveals connections to dolichol synthesis and sterol acetylation. J. Lipid Res. 55 1465-1477 PubMed GONUTS page
↑ Athenstaedt, K et al. (1999) Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae. J. Bacteriol. 181 6441-8 PubMed GONUTS page
↑ Pichler, H et al. (2001) A subfraction of the yeast endoplasmic reticulum associates with the plasma membrane and has a high capacity to synthesize lipids. Eur. J. Biochem. 268 2351-61 PubMed GONUTS page
↑ Leber, R et al. (1998) Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles. Mol. Biol. Cell 9 375-86 PubMed GONUTS page
↑ Jayasimha, P & Nes, WD (2008) Photoaffinity labeling and mutational analysis of 24-C-sterol methyltransferase defines the AdoMet binding site. Lipids 43 681-93 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:16407407-1] Zahedi, RP et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol. Biol. Cell 17 1436-50 PubMed GONUTS page

[PMID:16823961-2] Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page

[PMID:24769239-3] Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page

[PMID:14576278-4] Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page

[PMID:2677674-5] Gaber, RF et al. (1989) The yeast gene ERG6 is required for normal membrane function but is not essential for biosynthesis of the cell-cycle-sparking sterol. Mol. Cell. Biol. 9 3447-56 PubMed GONUTS page

[PMID:6363386-6] McCammon, MT et al. (1984) Sterol methylation in Saccharomyces cerevisiae. J. Bacteriol. 157 475-83 PubMed GONUTS page

[PMID:24868093-7] Currie, E et al. (2014) High confidence proteomic analysis of yeast LDs identifies additional droplet proteins and reveals connections to dolichol synthesis and sterol acetylation. J. Lipid Res. 55 1465-1477 PubMed GONUTS page

[PMID:10515935-8] Athenstaedt, K et al. (1999) Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae. J. Bacteriol. 181 6441-8 PubMed GONUTS page

[PMID:11298754-9] Pichler, H et al. (2001) A subfraction of the yeast endoplasmic reticulum associates with the plasma membrane and has a high capacity to synthesize lipids. Eur. J. Biochem. 268 2351-61 PubMed GONUTS page

[PMID:9450962-10] Leber, R et al. (1998) Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles. Mol. Biol. Cell 9 375-86 PubMed GONUTS page

[PMID:18563465-11] Jayasimha, P & Nes, WD (2008) Photoaffinity labeling and mutational analysis of 24-C-sterol methyltransferase defines the AdoMet binding site. Lipids 43 681-93 PubMed GONUTS page

[PMID:21873635-12] 12.0 ^12.1 ^12.2 ^12.3 ^12.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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YEAST:ERG6

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