A squalene monooxygenase that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q14534]
EC 1.14.14.17;
Squalene epoxidase;
SE
Timeframe | Studies on this Protein(%) | All Drugs % |
---|---|---|
pre-1990 | 1 (50.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 1 (50.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
---|---|---|---|---|---|
amiodarone | Homo sapiens (human) | IC50 | 12.0000 | 1 | 1 |
terbinafine | Homo sapiens (human) | IC50 | 6.0000 | 1 | 1 |
terbinafine | Homo sapiens (human) | Ki | 0.0300 | 1 | 1 |
This protein enables 3 target(s):
Target | Category | Definition |
---|---|---|
squalene monooxygenase activity | molecular function | Catalysis of the reaction: H+ + NADPH + O2 + squalene = (S)-2,3-epoxysqualene + H2O + NADP+. [RHEA:25282] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
FAD binding | molecular function | Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. [GOC:mah] |
This protein is located in 3 target(s):
Target | Category | Definition |
---|---|---|
endoplasmic reticulum membrane | cellular component | The lipid bilayer surrounding the endoplasmic reticulum. [GOC:mah] |
membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
intracellular membrane-bounded organelle | cellular component | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators] |
This protein is active in 1 target(s):
Target | Category | Definition |
---|---|---|
endoplasmic reticulum | cellular component | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732] |
This protein is involved in 5 target(s):
Target | Category | Definition |
---|---|---|
response to organic substance | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an organic substance stimulus. [GOC:sm, PMID:23356676] |
sterol biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of sterols, steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule. [GOC:go_curators] |
regulation of cell population proliferation | biological process | Any process that modulates the frequency, rate or extent of cell proliferation. [GOC:jl] |
lipid droplet formation | biological process | A process that results in the assembly, arrangement of constituent parts of a lipid droplet. [PMID:28011631] |
cholesterol metabolic process | biological process | The chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. It is a component of the plasma membrane lipid bilayer and of plasma lipoproteins and can be found in all animal tissues. [ISBN:0198506732] |