HUMAN:CP1A2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CYP1A2
Protein Name(s)	Cytochrome P450 1A2 CYPIA2 Cytochrome P(3)450 Cytochrome P450 4 Cytochrome P450-P3
External Links
UniProt	P05177
EMBL	Z00036 L00389 L00384 L00385 L00386 L00388 L00387 M31667 M31664 M31665 M31666 M12078 AF182274 AF253322 DQ022432 BC067424 BC067425 BC067426 BC067427 BC067428 M55053
CCDS	CCDS32293.1
PIR	S16718
RefSeq	NP_000752.2
UniGene	Hs.1361
PDB	2HI4
PDBsum	2HI4
ProteinModelPortal	P05177
SMR	P05177
BioGrid	107924
STRING	9606.ENSP00000342007
BindingDB	P05177
ChEMBL	CHEMBL3356
DrugBank	DB00071 DB01418 DB00316 DB06594 DB00518 DB00523 DB00918 DB00969 DB00357 DB01424 DB01223 DB01118 DB00321 DB00381 DB00261 DB01217 DB01435 DB06605 DB00673 DB06216 DB00572 DB06626 DB00972 DB00207 DB06770 DB00195 DB00188 DB01558 DB01200 DB00297 DB00921 DB01156 DB00201 DB00564 DB00262 DB01136 DB00477 DB00356 DB01166 DB00501 DB01012 DB00568 DB00537 DB00604 DB00215 DB01211 DB01407 DB04920 DB01013 DB00882 DB01242 DB00575 DB00758 DB00257 DB00363 DB00286 DB00924 DB00851 DB06292 DB01254 DB00694 DB00705 DB01151 DB00967 DB01191 DB00633 DB00829 DB00586 DB00917 DB01075 DB01184 DB00988 DB01142 DB00476 DB00974 DB00625 DB06210 DB00467 DB00668 DB00696 DB00530 DB00199 DB00783 DB00655 DB04574 DB00898 DB00773 DB01628 DB04841 DB01544 DB00544 DB00472 DB00623 DB00499 DB01095 DB00176 DB00998 DB01241 DB00400 DB00629 DB00502 DB01094 DB01355 DB04946 DB00619 DB00458 DB00724 DB05278 DB01306 DB01307 DB00047 DB01309 DB00046 DB00030 DB01029 DB00951 DB01026 DB00448 DB01097 DB01002 DB01137 DB00281 DB00978 DB01601 DB04871 DB00678 DB01283 DB00772 DB00934 DB00737 DB01065 DB00170 DB00333 DB00763 DB01403 DB00553 DB01028 DB00379 DB06148 DB01110 DB00370 DB01171 DB00745 DB00461 DB00607 DB00788 DB00220 DB00238 DB06803 DB00184 DB01115 DB06712 DB00401 DB00435 DB00325 DB00368 DB01059 DB00540 DB01165 DB00334 DB00338 DB00904 DB00526 DB01303 DB00377 DB00213 DB06589 DB00487 DB00738 DB00806 DB00850 DB01174 DB00191 DB00388 DB00397 DB01100 DB01621 DB08910 DB01058 DB01087 DB00794 DB00396 DB01131 DB00420 DB01182 DB00818 DB00571 DB00339 DB00908 DB00468 DB01129 DB00980 DB00863 DB01367 DB00615 DB01045 DB08864 DB00740 DB00503 DB00953 DB00268 DB00296 DB00412 DB05271 DB00778 DB00418 DB01037 DB01104 DB06290 DB00398 DB00428 DB00605 DB00675 DB00976 DB00300 DB00857 DB01041 DB01412 DB00277 DB00730 DB00679 DB01623 DB00208 DB01007 DB00697 DB01056 DB00539 DB00752 DB00384 DB00831 DB00313 DB08881 DB00661 DB00682 DB00549 DB00744 DB00246 DB00315 DB00425
PhosphoSite	P05177
DMDM	117144
MaxQB	P05177
PaxDb	P05177
PRIDE	P05177
Ensembl	ENST00000343932
GeneID	1544
KEGG	hsa:1544
UCSC	uc002ayr.1
CTD	1544
GeneCards	GC15P075041
HGNC	HGNC:2596
HPA	CAB016531
MIM	108330 124060
neXtProt	NX_P05177
Orphanet	284121
PharmGKB	PA27093
eggNOG	COG2124
GeneTree	ENSGT00760000118992
HOVERGEN	HBG106944
InParanoid	P05177
KO	K07409
OMA	KCCVFVN
OrthoDB	EOG7RBZ85
PhylomeDB	P05177
TreeFam	TF105095
BioCyc	MetaCyc:HS06728-MONOMER
Reactome	REACT_13721 REACT_150134 REACT_150417 REACT_228214 REACT_6946
SABIO-RK	P05177
EvolutionaryTrace	P05177
GeneWiki	CYP1A2
GenomeRNAi	1544
NextBio	6391
PRO	PR:P05177
Proteomes	UP000005640
Bgee	P05177
CleanEx	HS_CYP1A2
Genevestigator	P05177
GO	GO:0005789 GO:0043231 GO:0070330 GO:0034875 GO:0032451 GO:0009055 GO:0019899 GO:0020037 GO:0005506 GO:0004497 GO:0016491 GO:0016712 GO:0009820 GO:0019369 GO:0045333 GO:0071276 GO:0018894 GO:0042737 GO:0017144 GO:0019373 GO:0042738 GO:0046483 GO:0050665 GO:0030324 GO:0032259 GO:0032787 GO:0016098 GO:0097267 GO:0055114 GO:0071615 GO:0070989 GO:0006778 GO:0009791 GO:0010468 GO:0032355 GO:0035902 GO:0032496 GO:0044281 GO:0006706 GO:0009403 GO:0006805
Gene3D	1.10.630.10
InterPro	IPR001128 IPR017972 IPR002401 IPR008066
Pfam	PF00067
PRINTS	PR00463 PR01683 PR00385
SUPFAM	SSF48264
PROSITE	PS00086

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0070988	demethylation	PMID:2813353^[1]	ECO:0000314			P	Figure 4	complete
involved_in	GO:0071615	oxidative deethylation	PMID:19029318^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0070989	oxidative demethylation	PMID:18619574^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	PMID:16401082^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	PMID:19219744^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0046483	heterocycle metabolic process	PMID:15327587^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042738	exogenous drug catabolic process	PMID:18619574^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042737	drug catabolic process	PMID:18356043^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0034875	caffeine oxidase activity	PMID:18619574^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0032787	monocarboxylic acid metabolic process	PMID:19651758^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:15680923^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00167	F	Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:15680923^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00388	F	Seeded From UniProt	complete
involved_in	GO:0017144	drug metabolic process	PMID:19219744^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0017144	drug metabolic process	PMID:15327587^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	PMID:16401082^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	PMID:19219744^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0016098	monoterpenoid metabolic process	PMID:16401082^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009820	alkaloid metabolic process	PMID:11511187^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009403	toxin biosynthetic process	PMID:11511187^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006706	steroid catabolic process	PMID:18356043^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004497	monooxygenase activity	PMID:15327587^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004497	monooxygenase activity	PMID:19651758^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	PMID:2813353^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0032451	demethylase activity	PMID:2813353^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0020037	heme binding	PMID:17311915^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016712	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	PMID:2813353^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001210461 RGD:2458 RGD:2459 UniProtKB:P05177	C	Seeded From UniProt	complete
enables	GO:0004497	monooxygenase activity	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88588 PANTHER:PTN001210461 RGD:2458 RGD:2459 UniProtKB:P05177	F	Seeded From UniProt	complete
involved_in	GO:0022900	electron transport chain	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0009055	P	Seeded From UniProt	complete
involved_in	GO:0071276	cellular response to cadmium ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
involved_in	GO:0050665	hydrogen peroxide biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
involved_in	GO:0045333	cellular respiration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
involved_in	GO:0030324	lung development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
involved_in	GO:0018894	dibenzo-p-dioxin metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
involved_in	GO:0017144	drug metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
enables	GO:0016712	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	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	F	Seeded From UniProt	complete
involved_in	GO:0010468	regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
involved_in	GO:0009791	post-embryonic development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
involved_in	GO:0009404	toxin metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
involved_in	GO:0006778	porphyrin-containing compound metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
involved_in	GO:0006725	cellular aromatic compound metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00186 ensembl:ENSMUSP00000034860	P	Seeded From UniProt	complete
involved_in	GO:0071280	cellular response to copper ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04799 ensembl:ENSRNOP00000021653	P	Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04799 ensembl:ENSRNOP00000021653	C	Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04799 ensembl:ENSRNOP00000021653	P	Seeded From UniProt	complete
involved_in	GO:0035902	response to immobilization stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04799 ensembl:ENSRNOP00000021653	P	Seeded From UniProt	complete
involved_in	GO:0032496	response to lipopolysaccharide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04799 ensembl:ENSRNOP00000021653	P	Seeded From UniProt	complete
involved_in	GO:0032355	response to estradiol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04799 ensembl:ENSRNOP00000021653	P	Seeded From UniProt	complete
enables	GO:0016712	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	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04799 ensembl:ENSRNOP00000021653	F	Seeded From UniProt	complete
involved_in	GO:0014070	response to organic cyclic compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04799 ensembl:ENSRNOP00000021653	P	Seeded From UniProt	complete
involved_in	GO:0010033	response to organic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04799 ensembl:ENSRNOP00000021653	P	Seeded From UniProt	complete
enables	GO:0004497	monooxygenase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04799 ensembl:ENSRNOP00000021653	F	Seeded From UniProt	complete
enables	GO:0005506	iron ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001128 InterPro:IPR002401 InterPro:IPR008066 InterPro:IPR036396	F	Seeded From UniProt	complete
enables	GO:0016705	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001128 InterPro:IPR002401 InterPro:IPR017972 InterPro:IPR036396	F	Seeded From UniProt	complete
enables	GO:0016712	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	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008066	F	Seeded From UniProt	complete
enables	GO:0020037	heme binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001128 InterPro:IPR002401 InterPro:IPR008066 InterPro:IPR036396	F	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001128 InterPro:IPR002401 InterPro:IPR008066 InterPro:IPR017972 InterPro:IPR036396	P	Seeded From UniProt	complete
enables	GO:0070330	aromatase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.14.14.1	F	Seeded From UniProt	complete
enables	GO:0009055	electron transfer activity	PMID:2813353^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006805	xenobiotic metabolic process	Reactome:R-HSA-211859 Reactome:R-HSA-211981	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	Reactome:R-HSA-9037761 Reactome:R-HSA-9027043 Reactome:R-HSA-76426 Reactome:R-HSA-76386 Reactome:R-HSA-76373 Reactome:R-HSA-5423678 Reactome:R-HSA-5423672 Reactome:R-HSA-2161940 Reactome:R-HSA-2161899 Reactome:R-HSA-2161890 Reactome:R-HSA-2161814 Reactome:R-HSA-2161795 Reactome:R-HSA-156526	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004497	monooxygenase activity	Reactome:R-HSA-76426 Reactome:R-HSA-76386 Reactome:R-HSA-76373 Reactome:R-HSA-5423678	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0097267	omega-hydroxylase P450 pathway	Reactome:R-HSA-2142816	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042759	long-chain fatty acid biosynthetic process	Reactome:R-HSA-9027307 Reactome:R-HSA-9018681	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032259	methylation	Reactome:R-HSA-156581	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019373	epoxygenase P450 pathway	Reactome:R-HSA-2142670	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	P	Seeded From UniProt	complete
enables	GO:0004497	monooxygenase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0503	F	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P	Seeded From UniProt	complete
involved_in	GO:0008202	steroid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0753	P	Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0492	C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256	C	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0097	C	Seeded From UniProt	complete
part_of	GO:0031090	organelle membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0165	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Butler, MA et al. (1989) Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines. Proc. Natl. Acad. Sci. U.S.A. 86 7696-700 PubMed GONUTS page
↑ Jeong, S et al. (2009) Comprehensive in vitro analysis of voriconazole inhibition of eight cytochrome P450 (CYP) enzymes: major effect on CYPs 2B6, 2C9, 2C19, and 3A. Antimicrob. Agents Chemother. 53 541-51 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Kot, M & Daniel, WA (2008) The relative contribution of human cytochrome P450 isoforms to the four caffeine oxidation pathways: an in vitro comparative study with cDNA-expressed P450s including CYP2C isoforms. Biochem. Pharmacol. 76 543-51 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Jiang, Y et al. (2006) Radical intermediates in the catalytic oxidation of hydrocarbons by bacterial and human cytochrome P450 enzymes. Biochemistry 45 533-42 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Laine, JE et al. (2009) Acetaminophen bioactivation by human cytochrome P450 enzymes and animal microsomes. Xenobiotica 39 11-21 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Ward, BA et al. (2004) Characterization of human cytochrome P450 enzymes catalyzing domperidone N-dealkylation and hydroxylation in vitro. Br J Clin Pharmacol 58 277-87 PubMed GONUTS page
↑ ^7.0 ^7.1 Korhonen, T et al. (2008) Identification of the human cytochrome P450 enzymes involved in the in vitro biotransformation of lynestrenol and norethindrone. J. Steroid Biochem. Mol. Biol. 110 56-66 PubMed GONUTS page
↑ ^8.0 ^8.1 Fisher, CD et al. (2009) Hepatic cytochrome P450 enzyme alterations in humans with progressive stages of nonalcoholic fatty liver disease. Drug Metab. Dispos. 37 2087-94 PubMed GONUTS page
↑ ^9.0 ^9.1 Shimada, T et al. (2005) Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b(5) enzymes. Arch. Biochem. Biophys. 435 207-16 PubMed GONUTS page
↑ ^10.0 ^10.1 Stiborová, M et al. (2001) Human enzymes involved in the metabolic activation of carcinogenic aristolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A2. Chem. Res. Toxicol. 14 1128-37 PubMed GONUTS page
↑ Sansen, S et al. (2007) Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. J. Biol. Chem. 282 14348-55 PubMed GONUTS page
↑ ^12.0 ^12.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:2813353-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Butler, MA et al. (1989) Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines. Proc. Natl. Acad. Sci. U.S.A. 86 7696-700 PubMed GONUTS page

[PMID:19029318-2] Jeong, S et al. (2009) Comprehensive in vitro analysis of voriconazole inhibition of eight cytochrome P450 (CYP) enzymes: major effect on CYPs 2B6, 2C9, 2C19, and 3A. Antimicrob. Agents Chemother. 53 541-51 PubMed GONUTS page

[PMID:18619574-3] 3.0 ^3.1 ^3.2 Kot, M & Daniel, WA (2008) The relative contribution of human cytochrome P450 isoforms to the four caffeine oxidation pathways: an in vitro comparative study with cDNA-expressed P450s including CYP2C isoforms. Biochem. Pharmacol. 76 543-51 PubMed GONUTS page

[PMID:16401082-4] 4.0 ^4.1 ^4.2 Jiang, Y et al. (2006) Radical intermediates in the catalytic oxidation of hydrocarbons by bacterial and human cytochrome P450 enzymes. Biochemistry 45 533-42 PubMed GONUTS page

[PMID:19219744-5] 5.0 ^5.1 ^5.2 Laine, JE et al. (2009) Acetaminophen bioactivation by human cytochrome P450 enzymes and animal microsomes. Xenobiotica 39 11-21 PubMed GONUTS page

[PMID:15327587-6] 6.0 ^6.1 ^6.2 Ward, BA et al. (2004) Characterization of human cytochrome P450 enzymes catalyzing domperidone N-dealkylation and hydroxylation in vitro. Br J Clin Pharmacol 58 277-87 PubMed GONUTS page

[PMID:18356043-7] 7.0 ^7.1 Korhonen, T et al. (2008) Identification of the human cytochrome P450 enzymes involved in the in vitro biotransformation of lynestrenol and norethindrone. J. Steroid Biochem. Mol. Biol. 110 56-66 PubMed GONUTS page

[PMID:19651758-8] 8.0 ^8.1 Fisher, CD et al. (2009) Hepatic cytochrome P450 enzyme alterations in humans with progressive stages of nonalcoholic fatty liver disease. Drug Metab. Dispos. 37 2087-94 PubMed GONUTS page

[PMID:15680923-9] 9.0 ^9.1 Shimada, T et al. (2005) Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b(5) enzymes. Arch. Biochem. Biophys. 435 207-16 PubMed GONUTS page

[PMID:11511187-10] 10.0 ^10.1 Stiborová, M et al. (2001) Human enzymes involved in the metabolic activation of carcinogenic aristolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A2. Chem. Res. Toxicol. 14 1128-37 PubMed GONUTS page

[PMID:17311915-11] Sansen, S et al. (2007) Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. J. Biol. Chem. 282 14348-55 PubMed GONUTS page

[PMID:21873635-12] 12.0 ^12.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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HUMAN:CP1A2

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