SCUBA

CYP2C9 — Cytochrome P450 family 2 subfamily C member 9

CYP2C9 belongs to a gene co-expression module in 1 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

CYP2C9's module in each cell type

Cell typeModuleShares the module with
EnterocytesLong-gene transcript bias
Technical artifact
APC, CNGA1, KLHL24, MAP3K2, PALS1, PLA2G4C, TRHDEView in SCUBA

About the gene

SynonymsCYP2C10, P450IIC9
Chromosome10: 94938658-94990091
Predicted locationIntracellular
Essential geneNo
Protein classEnzymes, Human disease related genes, Metabolic proteins, Predicted intracellular proteins
Molecular functionMonooxygenase, Oxidoreductase
Biological processLipid metabolism, Steroid metabolism, Sterol metabolism

Function

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and steroids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. Exhibits low catalytic activity for the formation of catechol estrogens from 17beta- estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2. Catalyzes bisallylic hydroxylation and hydroxylation with double-bond migration of polyunsaturated fatty acids (PUFA). Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol. Contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S- warfarin, diclofenac, phenytoin, tolbutamide and losartan.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.