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Cytochrome P450 1A2 (EC 1.14.14.1) (CYPIA2) (Cholesterol 25-hydroxylase) (Cytochrome P(3)450) (Cytochrome P450 4) (Cytochrome P450-P3)

 CP1A2_HUMAN             Reviewed;         516 AA.
P05177; Q16754; Q6NWU3; Q6NWU5; Q9BXX7; Q9UK49;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
12-SEP-2018, sequence version 4.
03-JUL-2019, entry version 202.
RecName: Full=Cytochrome P450 1A2 {ECO:0000303|PubMed:14725854};
EC=1.14.14.- {ECO:0000269|PubMed:21576599, ECO:0000269|PubMed:9435160};
AltName: Full=CYPIA2;
AltName: Full=Cholesterol 25-hydroxylase {ECO:0000305|PubMed:21576599};
AltName: Full=Cytochrome P(3)450;
AltName: Full=Cytochrome P450 4;
AltName: Full=Cytochrome P450-P3;
AltName: Full=Hydroperoxy icosatetraenoate dehydratase {ECO:0000305|PubMed:21068195};
EC=4.2.1.152 {ECO:0000269|PubMed:21068195};
Name=CYP1A2 {ECO:0000303|PubMed:2575218, ECO:0000312|HGNC:HGNC:2596};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3755823; DOI=10.1093/nar/14.16.6773;
Jaiswal A.K., Nebert D.W., Gonzalez F.J.;
"Human P3(450): cDNA and complete amino acid sequence.";
Nucleic Acids Res. 14:6773-6774(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=3462722; DOI=10.1073/pnas.83.18.6731;
Quattrochi L.C., Pendurthi U.R., Okino S.T., Potenza C., Tukey R.H.;
"Human cytochrome P-450 4 mRNA and gene: part of a multigene family
that contains Alu sequences in its mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 83:6731-6735(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2575218; DOI=10.1210/mend-3-9-1399;
Ikeya K., Jaiswal A.K., Owens R.A., Jones J.E., Nebert D.W.,
Kimura S.;
"Human CYP1A2: sequence, gene structure, comparison with the mouse and
rat orthologous gene, and differences in liver 1A2 mRNA expression.";
Mol. Endocrinol. 3:1399-1408(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3681487;
Jaiswal A.K., Nebert D.W., McBride O.W., Gonzalez F.J.;
"Human P(3)450: cDNA and complete protein sequence, repetitive Alu
sequences in the 3' nontranslated region, and localization of gene to
chromosome 15.";
J. Exp. Pathol. 3:1-17(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-314.
TISSUE=Liver;
Zhuge J., Qian Y., Xie H., Yu Y.;
"Sequence of a new human cytochrome P450-1A2 cDNA.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11207026; DOI=10.1097/00008571-200102000-00001;
Corchero J., Pimprale S., Kimura S., Gonzalez F.J.;
"Organization of the CYP1A cluster on human chromosome 15:
implications for gene regulation.";
Pharmacogenetics 11:1-6(2001).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-73; ASN-104;
PHE-111; VAL-205; TRP-281 AND ILE-438.
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-19.
PubMed=3517618;
Wrighton S.A., Campanile C., Thomas P.E., Maines S.L., Watkins P.B.,
Parker G., Mendez-Picon G., Haniu M., Shively J.E., Levin W.,
Guzelian P.S.;
"Identification of a human liver cytochrome P-450 homologous to the
major isosafrole-inducible cytochrome P-450 in the rat.";
Mol. Pharmacol. 29:405-410(1986).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 295-485.
TISSUE=Liver;
PubMed=3000715; DOI=10.1089/dna.1985.4.395;
Quattrochi L.C., Okino S.T., Pendurthi U.R., Tukey R.H.;
"Cloning and isolation of human cytochrome P-450 cDNAs homologous to
dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6.";
DNA 4:395-400(1985).
[11]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=9435160;
Bylund J., Kunz T., Valmsen K., Oliw E.H.;
"Cytochromes P450 with bisallylic hydroxylation activity on
arachidonic and linoleic acids studied with human recombinant enzymes
and with human and rat liver microsomes.";
J. Pharmacol. Exp. Ther. 284:51-60(1998).
[12]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=10681376;
Chen H., Howald W.N., Juchau M.R.;
"Biosynthesis of all-trans-retinoic acid from all-trans-retinol:
catalysis of all-trans-retinol oxidation by human P-450 cytochromes.";
Drug Metab. Dispos. 28:315-322(2000).
[13]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11555828; DOI=10.1053/meta.2001.25592;
Badawi A.F., Cavalieri E.L., Rogan E.G.;
"Role of human cytochrome P450 1A1, 1A2, 1B1, and 3A4 in the 2-, 4-,
and 16alpha-hydroxylation of 17beta-estradiol.";
Metabolism 50:1001-1003(2001).
[14]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=12865317; DOI=10.1210/en.2003-0192;
Lee A.J., Cai M.X., Thomas P.E., Conney A.H., Zhu B.T.;
"Characterization of the oxidative metabolites of 17beta-estradiol and
estrone formed by 15 selectively expressed human cytochrome p450
isoforms.";
Endocrinology 144:3382-3398(2003).
[15]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION OF
VARIANTS ASN-348; PHE-386; TYR-406 AND TRP-431.
PubMed=14725854; DOI=10.1016/j.abb.2003.11.019;
Zhou H., Josephy P.D., Kim D., Guengerich F.P.;
"Functional characterization of four allelic variants of human
cytochrome P450 1A2.";
Arch. Biochem. Biophys. 422:23-30(2004).
[16]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=19965576; DOI=10.1194/jlr.M003061;
Lucas D., Goulitquer S., Marienhagen J., Fer M., Dreano Y.,
Schwaneberg U., Amet Y., Corcos L.;
"Stereoselective epoxidation of the last double bond of
polyunsaturated fatty acids by human cytochromes P450.";
J. Lipid Res. 51:1125-1133(2010).
[17]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=21068195; DOI=10.1124/dmd.110.035121;
Bui P., Imaizumi S., Beedanagari S.R., Reddy S.T., Hankinson O.;
"Human CYP2S1 metabolizes cyclooxygenase- and lipoxygenase-derived
eicosanoids.";
Drug Metab. Dispos. 39:180-190(2011).
[18]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PATHWAY.
PubMed=21576599; DOI=10.1194/jlr.M014084;
Honda A., Miyazaki T., Ikegami T., Iwamoto J., Maeda T., Hirayama T.,
Saito Y., Teramoto T., Matsuzaki Y.;
"Cholesterol 25-hydroxylation activity of CYP3A.";
J. Lipid Res. 52:1509-1516(2011).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 27-515 IN COMPLEX WITH THE
INHIBITOR ALPHA-NAPHTHOFLAVONE AND HEME.
PubMed=17311915; DOI=10.1074/jbc.M611692200;
Sansen S., Yano J.K., Reynald R.L., Schoch G.A., Griffin K.J.,
Stout C.D., Johnson E.F.;
"Adaptations for the oxidation of polycyclic aromatic hydrocarbons
exhibited by the structure of human P450 1A2.";
J. Biol. Chem. 282:14348-14355(2007).
[21]
VARIANT LEU-21.
PubMed=9884316;
Huang J.D., Guo W.C., Lai M.D., Guo Y.L., Lambert G.H.;
"Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in
Chinese.";
Drug Metab. Dispos. 27:98-101(1999).
[22]
VARIANTS ASN-348; PHE-386; TYR-406 AND TRP-431.
PubMed=11295848; DOI=10.1002/humu.49;
Chevalier D., Cauffiez C., Allorge D., Lo-Guidice J.-M., Lhermitte M.,
Lafitte J.-J., Broly F.;
"Five novel natural allelic variants-951A->C, 1042G->A (D348N),
1156A->T (I386F), 1217G->A (C406Y) and 1291C->T (C431Y)-of the human
CYP1A2 gene in a French Caucasian population.";
Hum. Mutat. 17:355-356(2001).
[23]
VARIANTS MET-83; GLN-168; LEU-186; CYS-212; SER-299 AND ILE-438.
PubMed=14563787; DOI=10.1124/jpet.103.055798;
Murayama N., Soyama A., Saito Y., Nakajima Y., Komamura K., Ueno K.,
Kamakura S., Kitakaze M., Kimura H., Goto Y., Saitoh O., Katoh M.,
Ohnuma T., Kawai M., Sugai K., Ohtsuki T., Suzuki C., Minami N.,
Ozawa S., Sawada J.;
"Six novel nonsynonymous CYP1A2 gene polymorphisms: catalytic
activities of the naturally occurring variant enzymes.";
J. Pharmacol. Exp. Ther. 308:300-306(2004).
[24]
VARIANTS CYS-18; ARG-298; VAL-314 AND TRP-431.
PubMed=15469410; DOI=10.1517/14622416.5.7.895;
Solus J.F., Arietta B.J., Harris J.R., Sexton D.P., Steward J.Q.,
McMunn C., Ihrie P., Mehall J.M., Edwards T.L., Dawson E.P.;
"Genetic variation in eleven phase I drug metabolism genes in an
ethnically diverse population.";
Pharmacogenomics 5:895-931(2004).
[25]
VARIANTS ARG-42; GLN-377 AND HIS-456.
PubMed=15770072; DOI=10.2133/dmpk.20.24;
Soyama A., Saito Y., Hanioka N., Maekawa K., Komamura K., Kamakura S.,
Kitakaze M., Tomoike H., Ueno K., Goto Y., Kimura H., Katoh M.,
Sugai K., Saitoh O., Kawai M., Ohnuma T., Ohtsuki T., Suzuki C.,
Minami N., Kamatani N., Ozawa S., Sawada J.;
"Single nucleotide polymorphisms and haplotypes of CYP1A2 in a
Japanese population.";
Drug Metab. Pharmacokinet. 20:24-33(2005).
[26]
VARIANT CYS-18.
PubMed=15643613; DOI=10.1002/humu.20134;
Jiang Z., Dalton T.P., Jin L., Wang B., Tsuneoka Y., Shertzer H.G.,
Deka R., Nebert D.W.;
"Toward the evaluation of function in genetic variability:
characterizing human SNP frequencies and establishing BAC-transgenic
mice carrying the human CYP1A1_CYP1A2 locus.";
Hum. Mutat. 25:196-206(2005).
[27]
EFFECT OF CAFFEINE METABOLISM ON RISKS OF MYOCARDIAL INFARCTION,
POLYMORPHISM, AND FUNCTION.
PubMed=16522833; DOI=10.1001/jama.295.10.1135;
Cornelis M.C., El-Sohemy A., Kabagambe E.K., Campos H.;
"Coffee, CYP1A2 genotype, and risk of myocardial infarction.";
JAMA 295:1135-1141(2006).
-!- FUNCTION: A cytochrome P450 monooxygenase involved in the
metabolism of various endogenous substrates, including fatty
acids, steroid hormones and vitamins (PubMed:9435160,
PubMed:10681376, PubMed:11555828, PubMed:12865317,
PubMed:19965576). 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)
(PubMed:9435160, PubMed:10681376, PubMed:11555828,
PubMed:12865317, PubMed:19965576). Catalyzes the hydroxylation of
carbon-hydrogen bonds (PubMed:11555828, PubMed:12865317). Exhibits
high catalytic activity for the formation of hydroxyestrogens from
estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2
(PubMed:11555828, PubMed:12865317). Metabolizes cholesterol toward
25-hydroxycholesterol, a physiological regulator of cellular
cholesterol homeostasis (PubMed:21576599). May act as a major
enzyme for all-trans retinoic acid biosynthesis in the liver.
Catalyzes two successive oxidative transformation of all-trans
retinol to all-trans retinal and then to the active form all-trans
retinoic acid (PubMed:10681376). Primarily catalyzes
stereoselective epoxidation of the last double bond of
polyunsaturated fatty acids (PUFA), displaying a strong preference
for the (R,S) stereoisomer (PubMed:19965576). Catalyzes bisallylic
hydroxylation and omega-1 hydroxylation of PUFA (PubMed:9435160).
May also participate in eicosanoids metabolism by converting
hydroperoxide species into oxo metabolites (lipoxygenase-like
reaction, NADPH-independent) (PubMed:21068195). Plays a role in
the oxidative metabolism of xenobiotics. Catalyzes the N-
hydroxylation of heterocyclic amines and the O-deethylation of
phenacetin (PubMed:14725854). Metabolizes caffeine via N3-
demethylation (Probable). {ECO:0000269|PubMed:10681376,
ECO:0000269|PubMed:11555828, ECO:0000269|PubMed:12865317,
ECO:0000269|PubMed:14725854, ECO:0000269|PubMed:19965576,
ECO:0000269|PubMed:21068195, ECO:0000269|PubMed:21576599,
ECO:0000269|PubMed:9435160, ECO:0000305|PubMed:16522833}.
-!- CATALYTIC ACTIVITY:
Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein
reductase] = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized
[NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-
COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469,
ChEBI:CHEBI:28744, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:11555828,
ECO:0000269|PubMed:12865317};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213;
Evidence={ECO:0000305|PubMed:11555828,
ECO:0000305|PubMed:12865317};
-!- CATALYTIC ACTIVITY:
Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein
reductase] = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized
[NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-
COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469,
ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62845;
Evidence={ECO:0000269|PubMed:11555828,
ECO:0000269|PubMed:12865317};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281;
Evidence={ECO:0000305|PubMed:11555828,
ECO:0000305|PubMed:12865317};
-!- CATALYTIC ACTIVITY:
Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] =
2-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964,
Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263,
ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:12865317};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209;
Evidence={ECO:0000305|PubMed:12865317};
-!- CATALYTIC ACTIVITY:
Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] =
4-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
reductase]; Xref=Rhea:RHEA:47292, Rhea:RHEA-COMP:11964,
Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618,
ChEBI:CHEBI:58210, ChEBI:CHEBI:87602;
Evidence={ECO:0000269|PubMed:12865317};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293;
Evidence={ECO:0000305|PubMed:12865317};
-!- CATALYTIC ACTIVITY:
Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase]
= 25-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--
hemoprotein reductase]; Xref=Rhea:RHEA:50256, Rhea:RHEA-
COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113,
ChEBI:CHEBI:42977, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:21576599};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50257;
Evidence={ECO:0000305|PubMed:21576599};
-!- CATALYTIC ACTIVITY:
Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein
reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized
[NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-
COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17336,
ChEBI:CHEBI:17898, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:10681376};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093;
Evidence={ECO:0000305|PubMed:10681376};
-!- CATALYTIC ACTIVITY:
Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein
reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized
[NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-
COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17898,
ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:10681376};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089;
Evidence={ECO:0000305|PubMed:10681376};
-!- CATALYTIC ACTIVITY:
Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-
eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
reductase]; Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964,
Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618,
ChEBI:CHEBI:58210, ChEBI:CHEBI:131965;
Evidence={ECO:0000269|PubMed:19965576};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861;
Evidence={ECO:0000305|PubMed:19965576};
-!- CATALYTIC ACTIVITY:
Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-
eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964,
Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618,
ChEBI:CHEBI:58210, ChEBI:CHEBI:131964;
Evidence={ECO:0000269|PubMed:19965576};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857;
Evidence={ECO:0000305|PubMed:19965576};
-!- CATALYTIC ACTIVITY:
Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced
[NADPH--hemoprotein reductase] = (17R,18S)-epoxy-
(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized
[NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-
COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76634;
Evidence={ECO:0000269|PubMed:19965576};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
Evidence={ECO:0000305|PubMed:19965576};
-!- CATALYTIC ACTIVITY:
Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
[NADPH--hemoprotein reductase] = (19R,20S)-epoxy-
(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized
[NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52120, Rhea:RHEA-
COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, ChEBI:CHEBI:136410;
Evidence={ECO:0000269|PubMed:19965576};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121;
Evidence={ECO:0000305|PubMed:19965576};
-!- CATALYTIC ACTIVITY:
Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-
oxo-(6E,8Z,11Z,14Z)-eicosatetraenoate + H2O;
Xref=Rhea:RHEA:48632, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450,
ChEBI:CHEBI:65342; Evidence={ECO:0000269|PubMed:21068195};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633;
Evidence={ECO:0000305|PubMed:21068195};
-!- CATALYTIC ACTIVITY:
Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-
oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O;
Xref=Rhea:RHEA:37947, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444,
ChEBI:CHEBI:75231; EC=4.2.1.152;
Evidence={ECO:0000269|PubMed:21068195};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948;
Evidence={ECO:0000305|PubMed:21068195};
-!- CATALYTIC ACTIVITY:
Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-
oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O;
Xref=Rhea:RHEA:48636, ChEBI:CHEBI:15377, ChEBI:CHEBI:57410,
ChEBI:CHEBI:57446; Evidence={ECO:0000269|PubMed:21068195};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637;
Evidence={ECO:0000305|PubMed:21068195};
-!- CATALYTIC ACTIVITY:
Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-
(9Z,11E)-octadecadienoate + H2O; Xref=Rhea:RHEA:48716,
ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:90781;
Evidence={ECO:0000269|PubMed:21068195};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717;
Evidence={ECO:0000305|PubMed:21068195};
-!- CATALYTIC ACTIVITY:
Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
hemoprotein reductase] = 13-hydroxy-(5Z,8Z,11Z,14Z)-
eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
reductase]; Xref=Rhea:RHEA:52292, Rhea:RHEA-COMP:11964,
Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618,
ChEBI:CHEBI:58210, ChEBI:CHEBI:136524;
Evidence={ECO:0000269|PubMed:9435160};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52293;
Evidence={ECO:0000305|PubMed:9435160};
-!- CATALYTIC ACTIVITY:
Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-
eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964,
Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618,
ChEBI:CHEBI:58210, ChEBI:CHEBI:76627;
Evidence={ECO:0000269|PubMed:9435160};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760;
Evidence={ECO:0000305|PubMed:9435160};
-!- CATALYTIC ACTIVITY:
Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--
hemoprotein reductase] = 11-hydroxy-(9Z,12Z)-octadecadienoate +
H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
Xref=Rhea:RHEA:52284, Rhea:RHEA-COMP:11964, Rhea:RHEA-
COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57618,
ChEBI:CHEBI:58210, ChEBI:CHEBI:136522;
Evidence={ECO:0000269|PubMed:9435160};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52285;
Evidence={ECO:0000305|PubMed:9435160};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=19 uM for 17beta-estradiol (2-hydroxylation)
{ECO:0000269|PubMed:11555828};
KM=9 uM for all-trans retinol {ECO:0000269|PubMed:10681376};
KM=4 uM for 2-amino-6-methyldipyrido[1,2-a:3',2'-d]imidazole
{ECO:0000269|PubMed:14725854};
KM=21 uM for 2-amino-3-methylimidazo[4,5-f]quinoline
{ECO:0000269|PubMed:14725854};
KM=26 uM for 2-amino-2,4-dimethylimidazo[4,5-f]quinoline
{ECO:0000269|PubMed:14725854};
KM=27 uM for 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline
{ECO:0000269|PubMed:14725854};
KM=71 uM for 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine
{ECO:0000269|PubMed:14725854};
KM=25 uM for phenacetin {ECO:0000269|PubMed:14725854};
Vmax=9.2 nmol/min/nmol enzyme toward 17beta-estradiol (2-
hydroxylation) {ECO:0000269|PubMed:11555828};
Vmax=491 pmol/min/nmol enzyme toward all-trans retinol
{ECO:0000269|PubMed:10681376};
-!- PATHWAY: Cofactor metabolism; retinol metabolism.
{ECO:0000269|PubMed:10681376}.
-!- PATHWAY: Steroid metabolism; cholesterol metabolism.
{ECO:0000269|PubMed:21576599}.
-!- PATHWAY: Lipid metabolism; arachidonate metabolism.
{ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:21068195,
ECO:0000269|PubMed:9435160}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane
{ECO:0000269|PubMed:21576599}; Peripheral membrane protein.
-!- TISSUE SPECIFICITY: Liver.
-!- INDUCTION: By nicotine, omeprazole, phenobarbital, primidone and
rifampicin.
-!- POLYMORPHISM: The CYP1A2*1F allele which is quite common (40 to
50%) is due to a substitution of a base in the non-coding region
of the CYP1A2 gene and has the effect of decreasing the enzyme
inducibility. Individuals who are homozygous for the CYP1A2*1F
allele are 'slow' caffeine metabolizers. Thus for these individual
increased intake of caffeine seems to be associated with a
concomitant increase in the risk of non-fatal myocardial
infraction (MI). {ECO:0000305|PubMed:16522833}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Cytochrome P450 Allele Nomenclature Committee;
Note=CYP1A2 alleles;
URL="http://www.cypalleles.ki.se/cyp1a2.htm";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cyp1a2/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Z00036; CAA77335.1; -; mRNA.
EMBL; M55053; AAA52146.1; -; mRNA.
EMBL; M12078; AAA52154.1; -; mRNA.
EMBL; L00389; AAA35738.1; -; Genomic_DNA.
EMBL; L00384; AAA35738.1; JOINED; Genomic_DNA.
EMBL; L00385; AAA35738.1; JOINED; Genomic_DNA.
EMBL; L00386; AAA35738.1; JOINED; Genomic_DNA.
EMBL; L00388; AAA35738.1; JOINED; Genomic_DNA.
EMBL; L00387; AAA35738.1; JOINED; Genomic_DNA.
EMBL; M31667; AAA52163.1; -; Genomic_DNA.
EMBL; M31664; AAA52163.1; JOINED; Genomic_DNA.
EMBL; M31665; AAA52163.1; JOINED; Genomic_DNA.
EMBL; M31666; AAA52163.1; JOINED; Genomic_DNA.
EMBL; AF182274; AAF13599.1; -; mRNA.
EMBL; AF253322; AAK25728.1; -; Genomic_DNA.
EMBL; DQ022432; AAY26399.1; -; Genomic_DNA.
EMBL; BC067424; AAH67424.1; -; mRNA.
EMBL; BC067425; AAH67425.1; -; mRNA.
EMBL; BC067426; AAH67426.1; -; mRNA.
EMBL; BC067427; AAH67427.1; -; mRNA.
EMBL; BC067428; AAH67428.1; -; mRNA.
EMBL; BC067429; AAH67429.1; -; mRNA.
CCDS; CCDS32293.1; -.
PIR; S16718; O4HU4.
RefSeq; NP_000752.2; NM_000761.4.
PDB; 2HI4; X-ray; 1.95 A; A=27-516.
PDBsum; 2HI4; -.
SMR; P05177; -.
BioGrid; 107924; 7.
IntAct; P05177; 2.
STRING; 9606.ENSP00000342007; -.
BindingDB; P05177; -.
ChEMBL; CHEMBL3356; -.
DrugBank; DB07453; 2-PHENYL-4H-BENZO[H]CHROMEN-4-ONE.
DrugBank; DB05812; Abiraterone.
DrugBank; DB01418; Acenocoumarol.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB00787; Aciclovir.
DrugBank; DB06594; Agomelatine.
DrugBank; DB00518; Albendazole.
DrugBank; DB00523; Alitretinoin.
DrugBank; DB00918; Almotriptan.
DrugBank; DB00969; Alosetron.
DrugBank; DB00357; Aminoglutethimide.
DrugBank; DB01424; Aminophenazone.
DrugBank; DB01223; Aminophylline.
DrugBank; DB01118; Amiodarone.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB00381; Amlodipine.
DrugBank; DB00261; Anagrelide.
DrugBank; DB01217; Anastrozole.
DrugBank; DB01435; Antipyrine.
DrugBank; DB06605; Apixaban.
DrugBank; DB00714; Apomorphine.
DrugBank; DB00673; Aprepitant.
DrugBank; DB06413; Armodafinil.
DrugBank; DB06216; Asenapine.
DrugBank; DB01072; Atazanavir.
DrugBank; DB00572; Atropine.
DrugBank; DB06626; Axitinib.
DrugBank; DB00972; Azelastine.
DrugBank; DB00207; Azithromycin.
DrugBank; DB06769; Bendamustine.
DrugBank; DB06770; Benzyl alcohol.
DrugBank; DB06732; beta-Naphthoflavone.
DrugBank; DB00195; Betaxolol.
DrugBank; DB00188; Bortezomib.
DrugBank; DB01558; Bromazepam.
DrugBank; DB01200; Bromocriptine.
DrugBank; DB00297; Bupivacaine.
DrugBank; DB00921; Buprenorphine.
DrugBank; DB01156; Bupropion.
DrugBank; DB00201; Caffeine.
DrugBank; DB06774; Capsaicin.
DrugBank; DB00564; Carbamazepine.
DrugBank; DB00389; Carbimazole.
DrugBank; DB00262; Carmustine.
DrugBank; DB01136; Carvedilol.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB00356; Chlorzoxazone.
DrugBank; DB01166; Cilostazol.
DrugBank; DB00501; Cimetidine.
DrugBank; DB01012; Cinacalcet.
DrugBank; DB00568; Cinnarizine.
DrugBank; DB00537; Ciprofloxacin.
DrugBank; DB00604; Cisapride.
DrugBank; DB00215; Citalopram.
DrugBank; DB01211; Clarithromycin.
DrugBank; DB01407; Clenbuterol.
DrugBank; DB04920; Clevidipine.
DrugBank; DB01013; Clobetasol propionate.
DrugBank; DB00882; Clomifene.
DrugBank; DB01242; Clomipramine.
DrugBank; DB00575; Clonidine.
DrugBank; DB00758; Clopidogrel.
DrugBank; DB00257; Clotrimazole.
DrugBank; DB00363; Clozapine.
DrugBank; DB00286; Conjugated Equine Estrogens.
DrugBank; DB05219; Crisaborole.
DrugBank; DB00924; Cyclobenzaprine.
DrugBank; DB00851; Dacarbazine.
DrugBank; DB04816; Dantron.
DrugBank; DB06292; Dapagliflozin.
DrugBank; DB01254; Dasatinib.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB00705; Delavirdine.
DrugBank; DB01151; Desipramine.
DrugBank; DB00967; Desloratadine.
DrugBank; DB01191; Dexfenfluramine.
DrugBank; DB00633; Dexmedetomidine.
DrugBank; DB00829; Diazepam.
DrugBank; DB00586; Diclofenac.
DrugBank; DB00917; Dinoprostone.
DrugBank; DB01075; Diphenhydramine.
DrugBank; DB00822; Disulfiram.
DrugBank; DB01184; Domperidone.
DrugBank; DB00988; Dopamine.
DrugBank; DB01142; Doxepin.
DrugBank; DB00476; Duloxetine.
DrugBank; DB00974; Edetic Acid.
DrugBank; DB00625; Efavirenz.
DrugBank; DB06210; Eltrombopag.
DrugBank; DB00467; Enoxacin.
DrugBank; DB00494; Entacapone.
DrugBank; DB00668; Epinephrine.
DrugBank; DB00696; Ergotamine.
DrugBank; DB00530; Erlotinib.
DrugBank; DB00199; Erythromycin.
DrugBank; DB00783; Estradiol.
DrugBank; DB00655; Estrone.
DrugBank; DB04574; Estrone sulfate.
DrugBank; DB00898; Ethanol.
DrugBank; DB00773; Etoposide.
DrugBank; DB01628; Etoricoxib.
DrugBank; DB00196; Fluconazole.
DrugBank; DB04841; Flunarizine.
DrugBank; DB01544; Flunitrazepam.
DrugBank; DB00544; Fluorouracil.
DrugBank; DB00472; Fluoxetine.
DrugBank; DB00623; Fluphenazine.
DrugBank; DB00499; Flutamide.
DrugBank; DB01095; Fluvastatin.
DrugBank; DB00176; Fluvoxamine.
DrugBank; DB00998; Frovatriptan.
DrugBank; DB01241; Gemfibrozil.
DrugBank; DB01645; Genistein.
DrugBank; DB08909; Glycerol Phenylbutyrate.
DrugBank; DB00365; Grepafloxacin.
DrugBank; DB00400; Griseofulvin.
DrugBank; DB05708; GTS-21.
DrugBank; DB00629; Guanabenz.
DrugBank; DB00502; Haloperidol.
DrugBank; DB01094; Hesperetin.
DrugBank; DB01355; Hexobarbital.
DrugBank; DB11737; Icotinib.
DrugBank; DB04946; Iloperidone.
DrugBank; DB00619; Imatinib.
DrugBank; DB00458; Imipramine.
DrugBank; DB00724; Imiquimod.
DrugBank; DB01306; Insulin Aspart.
DrugBank; DB09456; Insulin Beef.
DrugBank; DB01307; Insulin Detemir.
DrugBank; DB00047; Insulin Glargine.
DrugBank; DB01309; Insulin Glulisine.
DrugBank; DB00030; Insulin Human.
DrugBank; DB00046; Insulin Lispro.
DrugBank; DB00071; Insulin Pork.
DrugBank; DB00033; Interferon gamma-1b.
DrugBank; DB01029; Irbesartan.
DrugBank; DB00951; Isoniazid.
DrugBank; DB09570; Ixazomib.
DrugBank; DB01026; Ketoconazole.
DrugBank; DB00448; Lansoprazole.
DrugBank; DB01097; Leflunomide.
DrugBank; DB01002; Levobupivacaine.
DrugBank; DB01137; Levofloxacin.
DrugBank; DB00281; Lidocaine.
DrugBank; DB00978; Lomefloxacin.
DrugBank; DB01601; Lopinavir.
DrugBank; DB04871; Lorcaserin.
DrugBank; DB00678; Losartan.
DrugBank; DB01283; Lumiracoxib.
DrugBank; DB00772; Malathion.
DrugBank; DB00934; Maprotiline.
DrugBank; DB00737; Meclizine.
DrugBank; DB01065; Melatonin.
DrugBank; DB00170; Menadione.
DrugBank; DB00532; Mephenytoin.
DrugBank; DB01357; Mestranol.
DrugBank; DB00333; Methadone.
DrugBank; DB00763; Methimazole.
DrugBank; DB01403; Methotrimeprazine.
DrugBank; DB00553; Methoxsalen.
DrugBank; DB01028; Methoxyflurane.
DrugBank; DB00379; Mexiletine.
DrugBank; DB06148; Mianserin.
DrugBank; DB01388; Mibefradil.
DrugBank; DB01110; Miconazole.
DrugBank; DB00834; Mifepristone.
DrugBank; DB00370; Mirtazapine.
DrugBank; DB01171; Moclobemide.
DrugBank; DB00745; Modafinil.
DrugBank; DB00461; Nabumetone.
DrugBank; DB00607; Nafcillin.
DrugBank; DB00788; Naproxen.
DrugBank; DB01149; Nefazodone.
DrugBank; DB00220; Nelfinavir.
DrugBank; DB00238; Nevirapine.
DrugBank; DB06803; Niclosamide.
DrugBank; DB00184; Nicotine.
DrugBank; DB01115; Nifedipine.
DrugBank; DB06712; Nilvadipine.
DrugBank; DB00401; Nisoldipine.
DrugBank; DB00435; Nitric Oxide.
DrugBank; DB00325; Nitroprusside.
DrugBank; DB00368; Norepinephrine.
DrugBank; DB01059; Norfloxacin.
DrugBank; DB00540; Nortriptyline.
DrugBank; DB05990; Obeticholic acid.
DrugBank; DB01165; Ofloxacin.
DrugBank; DB00334; Olanzapine.
DrugBank; DB00338; Omeprazole.
DrugBank; DB00904; Ondansetron.
DrugBank; DB01173; Orphenadrine.
DrugBank; DB09330; Osimertinib.
DrugBank; DB00526; Oxaliplatin.
DrugBank; DB01303; Oxtriphylline.
DrugBank; DB06412; Oxymetholone.
DrugBank; DB00377; Palonosetron.
DrugBank; DB00213; Pantoprazole.
DrugBank; DB00715; Paroxetine.
DrugBank; DB06589; Pazopanib.
DrugBank; DB00487; Pefloxacin.
DrugBank; DB00008; Peginterferon alfa-2a.
DrugBank; DB00022; Peginterferon alfa-2b.
DrugBank; DB00738; Pentamidine.
DrugBank; DB00806; Pentoxifylline.
DrugBank; DB00850; Perphenazine.
DrugBank; DB03783; Phenacetin.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB00191; Phentermine.
DrugBank; DB00388; Phenylephrine.
DrugBank; DB00397; Phenylpropanolamine.
DrugBank; DB01100; Pimozide.
DrugBank; DB01621; Pipotiazine.
DrugBank; DB08910; Pomalidomide.
DrugBank; DB01058; Praziquantel.
DrugBank; DB01087; Primaquine.
DrugBank; DB00794; Primidone.
DrugBank; DB00396; Progesterone.
DrugBank; DB01131; Proguanil.
DrugBank; DB00420; Promazine.
DrugBank; DB01182; Propafenone.
DrugBank; DB00818; Propofol.
DrugBank; DB00571; Propranolol.
DrugBank; DB00339; Pyrazinamide.
DrugBank; DB00908; Quinidine.
DrugBank; DB00468; Quinine.
DrugBank; DB01129; Rabeprazole.
DrugBank; DB00980; Ramelteon.
DrugBank; DB00863; Ranitidine.
DrugBank; DB01367; Rasagiline.
DrugBank; DB02709; Resveratrol.
DrugBank; DB00615; Rifabutin.
DrugBank; DB01045; Rifampicin.
DrugBank; DB08864; Rilpivirine.
DrugBank; DB00740; Riluzole.
DrugBank; DB00503; Ritonavir.
DrugBank; DB00953; Rizatriptan.
DrugBank; DB00533; Rofecoxib.
DrugBank; DB00268; Ropinirole.
DrugBank; DB00296; Ropivacaine.
DrugBank; DB00412; Rosiglitazone.
DrugBank; DB05271; Rotigotine.
DrugBank; DB00778; Roxithromycin.
DrugBank; DB12332; Rucaparib.
DrugBank; DB00418; Secobarbital.
DrugBank; DB01037; Selegiline.
DrugBank; DB01104; Sertraline.
DrugBank; DB06290; Simeprevir.
DrugBank; DB06819; Sodium phenylbutyrate.
DrugBank; DB00398; Sorafenib.
DrugBank; DB00428; Streptozocin.
DrugBank; DB06820; Sulconazole.
DrugBank; DB00605; Sulindac.
DrugBank; DB00382; Tacrine.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB01079; Tegaserod.
DrugBank; DB00976; Telithromycin.
DrugBank; DB01405; Temafloxacin.
DrugBank; DB00300; Tenofovir.
DrugBank; DB00857; Terbinafine.
DrugBank; DB01041; Thalidomide.
DrugBank; DB01412; Theobromine.
DrugBank; DB00277; Theophylline.
DrugBank; DB00730; Thiabendazole.
DrugBank; DB00679; Thioridazine.
DrugBank; DB01623; Thiothixene.
DrugBank; DB00208; Ticlopidine.
DrugBank; DB01007; Tioconazole.
DrugBank; DB00697; Tizanidine.
DrugBank; DB01056; Tocainide.
DrugBank; DB00539; Toremifene.
DrugBank; DB00752; Tranylcypromine.
DrugBank; DB00384; Triamterene.
DrugBank; DB00831; Trifluoperazine.
DrugBank; DB08867; Ulipristal.
DrugBank; DB00577; Valaciclovir.
DrugBank; DB00313; Valproic Acid.
DrugBank; DB08881; Vemurafenib.
DrugBank; DB00661; Verapamil.
DrugBank; DB00682; Warfarin.
DrugBank; DB00549; Zafirlukast.
DrugBank; DB00744; Zileuton.
DrugBank; DB00246; Ziprasidone.
DrugBank; DB00315; Zolmitriptan.
DrugBank; DB00425; Zolpidem.
GuidetoPHARMACOLOGY; 1319; -.
SwissLipids; SLP:000001202; -.
iPTMnet; P05177; -.
PhosphoSitePlus; P05177; -.
BioMuta; CYP1A2; -.
DMDM; 117144; -.
PaxDb; P05177; -.
PeptideAtlas; P05177; -.
PRIDE; P05177; -.
ProteomicsDB; 51818; -.
ProteomicsDB; 51819; -.
Ensembl; ENST00000343932; ENSP00000342007; ENSG00000140505.
GeneID; 1544; -.
KEGG; hsa:1544; -.
UCSC; uc002ayr.2; human.
CTD; 1544; -.
DisGeNET; 1544; -.
GeneCards; CYP1A2; -.
HGNC; HGNC:2596; CYP1A2.
HPA; CAB016531; -.
MalaCards; CYP1A2; -.
MIM; 108330; gene.
MIM; 124060; gene+phenotype.
neXtProt; NX_P05177; -.
OpenTargets; ENSG00000140505; -.
Orphanet; 284121; Toxicity or absent response to clozapine.
PharmGKB; PA27093; -.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00950000183037; -.
HOGENOM; HOG000036991; -.
InParanoid; P05177; -.
KO; K07409; -.
OMA; VIGAMCF; -.
OrthoDB; 920162at2759; -.
PhylomeDB; P05177; -.
TreeFam; TF105095; -.
BioCyc; MetaCyc:HS06728-MONOMER; -.
BRENDA; 1.14.14.1; 2681.
BRENDA; 1.14.99.38; 2681.
Reactome; R-HSA-156581; Methylation.
Reactome; R-HSA-211957; Aromatic amines can be N-hydroxylated or N-dealkylated by CYP1A2.
Reactome; R-HSA-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
Reactome; R-HSA-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
Reactome; R-HSA-9018681; Biosynthesis of protectins.
Reactome; R-HSA-9027307; Biosynthesis of maresin-like SPMs.
SABIO-RK; P05177; -.
UniPathway; UPA00296; -.
UniPathway; UPA00383; -.
UniPathway; UPA00912; -.
EvolutionaryTrace; P05177; -.
GeneWiki; CYP1A2; -.
GenomeRNAi; 1544; -.
PRO; PR:P05177; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140505; Expressed in 164 organ(s), highest expression level in liver.
Genevisible; P05177; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0034875; F:caffeine oxidase activity; IDA:BHF-UCL.
GO; GO:0032451; F:demethylase activity; IDA:UniProtKB.
GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; IDA:UniProtKB.
GO; GO:0101021; F:estrogen 2-hydroxylase activity; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IDA:BHF-UCL.
GO; GO:0016491; F:oxidoreductase activity; IDA:BHF-UCL.
GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IMP:UniProtKB.
GO; GO:0009820; P:alkaloid metabolic process; IDA:BHF-UCL.
GO; GO:0045333; P:cellular respiration; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEA:Ensembl.
GO; GO:0042737; P:drug catabolic process; IMP:BHF-UCL.
GO; GO:0017144; P:drug metabolic process; IDA:BHF-UCL.
GO; GO:0019373; P:epoxygenase P450 pathway; TAS:Reactome.
GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
GO; GO:0042738; P:exogenous drug catabolic process; IDA:BHF-UCL.
GO; GO:0046483; P:heterocycle metabolic process; IDA:BHF-UCL.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; TAS:Reactome.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0032259; P:methylation; TAS:Reactome.
GO; GO:0032787; P:monocarboxylic acid metabolic process; IDA:BHF-UCL.
GO; GO:0016098; P:monoterpenoid metabolic process; IDA:BHF-UCL.
GO; GO:0097267; P:omega-hydroxylase P450 pathway; TAS:Reactome.
GO; GO:0055114; P:oxidation-reduction process; IDA:BHF-UCL.
GO; GO:0071615; P:oxidative deethylation; IDA:BHF-UCL.
GO; GO:0070989; P:oxidative demethylation; IDA:BHF-UCL.
GO; GO:0006778; P:porphyrin-containing compound metabolic process; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0042572; P:retinol metabolic process; IDA:UniProtKB.
GO; GO:0006706; P:steroid catabolic process; IMP:BHF-UCL.
GO; GO:0009403; P:toxin biosynthetic process; IDA:BHF-UCL.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR01683; EP450ICYP1A.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Endoplasmic reticulum; Fatty acid metabolism; Glycoprotein; Heme;
Iron; Lipid metabolism; Lyase; Membrane; Metal-binding; Microsome;
Monooxygenase; Oxidoreductase; Polymorphism; Reference proteome;
Steroid metabolism; Sterol metabolism.
INIT_MET