Basic Information
Name | Squalene synthase (SQS) (SS) (EC 2.5.1.21) (FPP:FPP farnesyltransferase) (Farnesyl-diphosphate farnesyltransferase) |
Uniprot ID | P29704 |
Systematic gene name | YHR190W |
Standard gene name | ERG9 |
Gene names | ERG9 YHR190W |
Description from SGD | YHR190W ERG9 SGDID:S000001233, Chr VIII from 484845-486179, Genome Release 64-3-1, Verified ORF, "Farnesyl-diphosphate farnesyl transferase (squalene synthase); joins two farnesyl pyrophosphate moieties to form squalene in the sterol biosynthesis pathway" |
Protein length | 444 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MGKLLQLALH PVEMKAALKL KFCRTPLFSI YDQSTSPYLL HCFELLNLTS
RSFAAVIREL HPELRNCVTL FYLILRALDT IEDDMSIEHD LKIDLLRHFH
EKLLLTKWSF DGNAPDVKDR AVLTDFESIL IEFHKLKPEY QEVIKEITEK
MGNGMADYIL DENYNLNGLQ TVHDYDVYCH YVAGLVGDGL TRLIVIAKFA
NESLYSNEQL YESMGLFLQK TNIIRDYNED LVDGRSFWPK EIWSQYAPQL
KDFMKPENEQ LGLDCINHLV LNALSHVIDV LTYLAGIHEQ STFQFCAIPQ
VMAIATLALV FNNREVLHGN VKIRKGTTCY LILKSRTLRG CVEIFDYYLR
DIKSKLAVQD PNFLKLNIQI SKIEQFMEEM YQDKLPPNVK PNETPIFLKV
KERSRYDDEL VPTQQEEEYK FNMVLSIILS VLLGFYYIYT LHRA
RSFAAVIREL HPELRNCVTL FYLILRALDT IEDDMSIEHD LKIDLLRHFH
EKLLLTKWSF DGNAPDVKDR AVLTDFESIL IEFHKLKPEY QEVIKEITEK
MGNGMADYIL DENYNLNGLQ TVHDYDVYCH YVAGLVGDGL TRLIVIAKFA
NESLYSNEQL YESMGLFLQK TNIIRDYNED LVDGRSFWPK EIWSQYAPQL
KDFMKPENEQ LGLDCINHLV LNALSHVIDV LTYLAGIHEQ STFQFCAIPQ
VMAIATLALV FNNREVLHGN VKIRKGTTCY LILKSRTLRG CVEIFDYYLR
DIKSKLAVQD PNFLKLNIQI SKIEQFMEEM YQDKLPPNVK PNETPIFLKV
KERSRYDDEL VPTQQEEEYK FNMVLSIILS VLLGFYYIYT LHRA
Legend
- X Phoshorylation
- X K-acetylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[52, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[102, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |
[244, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[390, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |