ERG9/YHR190W Protein Information

Standard Name	Erg9p 1
Systematic Name	Yhr190wp
ORF Classification	Verified
Description	Farnesyl-diphosphate farnesyl transferase (squalene synthase), joins two farnesyl pyrophosphate moieties to form squalene in the sterol biosynthesis pathway (2, 3, 4)
Name Description	ERGosterol biosynthesis 1

Experimental Data
Molecules/cell	10800 5

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	444
Molecular Weight (Da)	51,719
Isoelectric Point (pI)	5.79

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Erg9p (InterPro)
Transmembrane Domains	There are 1 total predicted transmembrane domains (TMHMM)
Physical Interactions	There are 34 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000012A5DA \| P29704 MIPS: YHR190W NCBI: 171481 \| 3686 \| 458934 \| 6321984 \| 729468 \| NP_012060.1 GenBank/EMBL/DDBJ: DAA06882.1 \| M63979 \| U00030 \| X59959
External Classifications	EC: 2.5.1.21 [Squalene synthase]

Amino Acid Sequence (or in FASTA format)
1 MGKLLQLALH PVEMKAALKL KFCRTPLFSI YDQSTSPYLL HCFELLNLTS 51 RSFAAVIREL HPELRNCVTL FYLILRALDT IEDDMSIEHD LKIDLLRHFH 101 EKLLLTKWSF DGNAPDVKDR AVLTDFESIL IEFHKLKPEY QEVIKEITEK 151 MGNGMADYIL DENYNLNGLQ TVHDYDVYCH YVAGLVGDGL TRLIVIAKFA 201 NESLYSNEQL YESMGLFLQK TNIIRDYNED LVDGRSFWPK EIWSQYAPQL 251 KDFMKPENEQ LGLDCINHLV LNALSHVIDV LTYLAGIHEQ STFQFCAIPQ 301 VMAIATLALV FNNREVLHGN VKIRKGTTCY LILKSRTLRG CVEIFDYYLR 351 DIKSKLAVQD PNFLKLNIQI SKIEQFMEEM YQDKLPPNVK PNETPIFLKV 401 KERSRYDDEL VPTQQEEEYK FNMVLSIILS VLLGFYYIYT LHRA*

Amino Acid Sequence (or in FASTA format)

       1  MGKLLQLALH PVEMKAALKL KFCRTPLFSI YDQSTSPYLL HCFELLNLTS
      51  RSFAAVIREL HPELRNCVTL FYLILRALDT IEDDMSIEHD LKIDLLRHFH
     101  EKLLLTKWSF DGNAPDVKDR AVLTDFESIL IEFHKLKPEY QEVIKEITEK
     151  MGNGMADYIL DENYNLNGLQ TVHDYDVYCH YVAGLVGDGL TRLIVIAKFA
     201  NESLYSNEQL YESMGLFLQK TNIIRDYNED LVDGRSFWPK EIWSQYAPQL
     251  KDFMKPENEQ LGLDCINHLV LNALSHVIDV LTYLAGIHEQ STFQFCAIPQ
     301  VMAIATLALV FNNREVLHGN VKIRKGTTCY LILKSRTLRG CVEIFDYYLR
     351  DIKSKLAVQD PNFLKLNIQI SKIEQFMEEM YQDKLPPNVK PNETPIFLKV
     401  KERSRYDDEL VPTQQEEEYK FNMVLSIILS VLLGFYYIYT LHRA*

external links for Erg9p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastGFP
Candida (CGD)	CYC2008 (complexes)	Pfam domains	YeastRC Public Image Repository
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Erg9p

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)	Jennings SM, et al. (1991) Molecular cloning and characterization of the yeast gene for squalene synthetase. Proc Natl Acad Sci U S A 88(14):6038-42
3)	Fegueur M, et al. (1991) Isolation and primary structure of the ERG9 gene of Saccharomyces cerevisiae encoding squalene synthetase. Curr Genet 20(5):365-72
4)	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
5)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41