CYP1A1 report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of CYP1A1 at tissue level.

III. Associated gene sets

GO_0010041Biological processresponse to iron(III) ion
GO_0006805Biological processxenobiotic metabolic process
GO_0009804Biological processcoumarin metabolic process
GO_0009624Biological processresponse to nematode
GO_0009692Biological processethylene metabolic process
GO_0035902Biological processresponse to immobilization stress
GO_0060137Biological processmaternal process involved in parturition
GO_0019341Biological processdibenzo-p-dioxin catabolic process
GO_0033189Biological processresponse to vitamin A
GO_1904681Biological processresponse to 3-methylcholanthrene
GO_0046685Biological processresponse to arsenic-containing substance
GO_0032496Biological processresponse to lipopolysaccharide
GO_0006631Biological processfatty acid metabolic process
GO_0006694Biological processsteroid biosynthetic process
GO_0006778Biological processporphyrin-containing compound metabolic process
GO_0042904Biological process9-cis-retinoic acid biosynthetic process
GO_0097267Biological processomega-hydroxylase P450 pathway
GO_0042359Biological processvitamin D metabolic process
GO_1900087Biological processpositive regulation of G1/S transition of mitotic cell cycle
GO_0048771Biological processtissue remodeling
GO_0019373Biological processepoxygenase P450 pathway
GO_0009812Biological processflavonoid metabolic process
GO_0055093Biological processresponse to hyperoxia
GO_0071280Biological processcellular response to copper ion
GO_0001666Biological processresponse to hypoxia
GO_0001676Biological processlong-chain fatty acid metabolic process
GO_0050665Biological processhydrogen peroxide biosynthetic process
GO_0009635Biological processresponse to herbicide
GO_0002933Biological processlipid hydroxylation
GO_0042572Biological processretinol metabolic process
GO_0048565Biological processdigestive tract development
GO_0008210Biological processestrogen metabolic process
GO_0042759Biological processlong-chain fatty acid biosynthetic process
GO_0043010Biological processcamera-type eye development
GO_0017143Biological processinsecticide metabolic process
GO_0046209Biological processnitric oxide metabolic process
GO_0032094Biological processresponse to food
GO_0008202Biological processsteroid metabolic process
GO_0070365Biological processhepatocyte differentiation
GO_0071407Biological processcellular response to organic cyclic compound
GO_0009308Biological processamine metabolic process
GO_0005789Cellular componentendoplasmic reticulum membrane
GO_0005743Cellular componentmitochondrial inner membrane
GO_0043231Cellular componentintracellular membrane-bounded organelle
GO_0019899Molecular functionenzyme binding
GO_0016679Molecular functionoxidoreductase activity, acting on diphenols and related substances as donors
GO_0032451Molecular functiondemethylase activity
GO_0070330Molecular functionaromatase activity
GO_0051879Molecular functionHsp90 protein binding
GO_0101020Molecular functionestrogen 16-alpha-hydroxylase activity
GO_0120319Molecular functionlong-chain fatty acid omega-1 hydroxylase activity
GO_0019825Molecular functionoxygen binding
GO_0008391Molecular functionarachidonic acid monooxygenase activity
GO_0016491Molecular functionoxidoreductase activity
GO_0004497Molecular functionmonooxygenase activity
GO_0005506Molecular functioniron ion binding
GO_0020037Molecular functionheme binding
GO_0030544Molecular functionHsp70 protein binding
GO_0102033Molecular functionlong-chain fatty acid omega-hydroxylase activity
GO_0106256Molecular functionhydroperoxy icosatetraenoate dehydratase activity
GO_0016711Molecular functionflavonoid 3'-monooxygenase activity
GO_0005515Molecular functionprotein binding
GO_0070576Molecular functionvitamin D 24-hydroxylase activity
GO_0101021Molecular functionestrogen 2-hydroxylase activity

IV. Literature review

[source]
Gene nameCYP1A1
Protein nameCytochrome P450 1A (EC 1.14.14.1)
Cytochrome P450 1A1 (CYPIA1) (EC 1.14.14.1) (Cytochrome P450 form 6) (Cytochrome P450-C) (Cytochrome P450-P1) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152)
SynonymshCG_40803
DescriptionFUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. .

FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. .

FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. .

FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. .

FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. .

FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins . 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 hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-alpha positions . Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation . Catalyzes the epoxidation of double bonds of certain PUFA . Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system . Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer . May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid . May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) . .

FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. .

FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. .

AccessionsENST00000395048.6 [P04798-1]
ENST00000566503.1
P04798
Q0VHD5
Q5J9B1
A4F3V8
A4F4K3
ENST00000564596.5 [P04798-3]
ENST00000567032.5 [P04798-1]
ENST00000379727.8 [P04798-1]
E7EMT5
A4F4K4
ENST00000562201.5 [P04798-2]
ENST00000617691.4
ENST00000569630.5 [P04798-2]
ENST00000395049.8
A0N0X8