P33261 (CP2CJ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome P450 2C19
EC=1.14.13.-

Alternative name(s):
(R)-limonene 6-monooxygenase
EC=1.14.13.80
(S)-limonene 6-monooxygenase
EC=1.14.13.48
(S)-limonene 7-monooxygenase
EC=1.14.13.49
CYPIIC17
CYPIIC19
Cytochrome P450-11A
Cytochrome P450-254C
Mephenytoin 4-hydroxylase

Gene names

Name:

CYP2C19

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Responsible for the metabolism of a number of therapeutic agents such as the anticonvulsant drug S-mephenytoin, omeprazole, proguanil, certain barbiturates, diazepam, propranolol, citalopram and imipramine.
Catalytic activity	+-(R)-limonene + NADPH + O2 = (+)-trans-carveol + NADP+ + H2O. --(S)-limonene + NADPH + O2 = (-)-trans-carveol + NADP+ + H2O. --(S)-limonene + NADPH + O2 = (-)-perillyl alcohol + NADP+ + H2O.
Cofactor	Heme group.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Induction	P450 can be induced to high levels in liver and other tissues by various foreign compounds, including drugs, pesticides, and carcinogens.
Polymorphism	Genetic variation in CYP2C19 is responsible for poor drug metabolism [MIM:609535]. Individuals can be characterized as either extensive metabolizers (EM) or poor metabolizers (PM). The PM phenotype is inherited in an autosomal recessive manner, with the EM phenotype comprising both homozygous dominant and heteroyzgote genotypes. There are marked interracial differences in the frequency of this polymorphism. Poor metabolizers represent 2-5% of Caucasians, 13-23% of Asian populations, and as many as 38-79% of individuals of some of the islands of Polynesia and Micronesia. Different alleles of CYP2C19 are known: CYP2C19*1A CYP2C19*1B, CYP2C19*1C, CYP2C19*2A (CYP2C19m1 or CYP2C19m1A), CYP2C19*2B (CYP2C19m1B), CYP2C19*2C (CYP2C19*21), CYP2C19*3A (CYP2C19m2), CYP2C19*3B (CYP2C19*20), CYP2C19*4 (CYP2C19m3), CYP2C19*5A (CYP2C19m4), CYP2C19*5B, CYP2C19*6, CYP2C19*7, CYP2C19*8, CYP2C19*9, CYP2C19*10, CYP2C19*11 CYP2C19*12, CYP2C19*13, CYP2C19*14 CYP2C19*15, CYP2C19*16, CYP2C19*18, CYP2C19*19. Defective CYP2C19*2 and CYP2C19*3 alleles are characterized by a splice mutation and a stop codon, respectively, and account for most of the PM alleles. The sequence shown is that of allele CYP2C19*1B.
Sequence similarities	Belongs to the cytochrome P450 family.
Caution	P450-254C was originally listed as a separate gene (CYP2C17). Resequencing demonstrated that it is not a separate gene, but a chimera. The 5'-portion corresponds to a partial 2C18 clone, and the 3'-portion corresponds to a partial 2C19 clone.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	exogenous drug catabolic process Inferred from direct assay PubMed 19029318. Source: BHF-UCL heterocycle metabolic process Inferred from direct assay PubMed 19651758. Source: BHF-UCL monoterpenoid metabolic process Inferred from direct assay PubMed 16401082. Source: BHF-UCL small molecule metabolic process Traceable author statement. Source: Reactome steroid metabolic process Inferred from mutant phenotype PubMed 18356043. Source: BHF-UCL xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome
Molecular_function	(R)-limonene 6-monooxygenase activity Inferred from electronic annotation. Source: EC (S)-limonene 6-monooxygenase activity Inferred from electronic annotation. Source: EC (S)-limonene 7-monooxygenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxygen binding Traceable author statement PubMed 3442670. Source: ProtInc steroid hydroxylase activity Inferred from mutant phenotype PubMed 18356043. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 490

490

Cytochrome P450 2C19

PRO_0000051708

Sites

Metal binding

435

1

Iron (heme axial ligand)

Natural variations

Natural variant

17

1

L → P in allele CYP2C19*14. Ref.15
Corresponds to variant rs55752064 [ dbSNP | Ensembl ].

VAR_021268

Natural variant

19

1

I → L in allele CYP2C19*15. Ref.3 Ref.15
Corresponds to variant rs17882687 [ dbSNP | Ensembl ].

VAR_021269

Natural variant

51

1

S → G in allele CYP2C19*19. Ref.18

VAR_024083

Natural variant

74

1

M → T. Ref.17
Corresponds to variant rs28399505 [ dbSNP | Ensembl ].

VAR_024718

Natural variant

92

1

E → D. Ref.3 Ref.12
Corresponds to variant rs17878459 [ dbSNP | Ensembl ].

VAR_021270

Natural variant

120

1

W → R in allele CYP2C19*8; loss of activity. Ref.14
Corresponds to variant rs41291556 [ dbSNP | Ensembl ].

VAR_008357

Natural variant

122

1

E → A. Ref.3
Corresponds to variant rs17885179 [ dbSNP | Ensembl ].

VAR_021271

Natural variant

132

1

R → Q in allele CYP2C19*6; loss of activity. Ref.12

VAR_008358

Natural variant

144

1

R → H in allele CYP2C19*9. Ref.3 Ref.15 Ref.17
Corresponds to variant rs17884712 [ dbSNP | Ensembl ].

VAR_021272

Natural variant

150

1

R → H in allele CYP2C19*11. Ref.15
Corresponds to variant rs58973490 [ dbSNP | Ensembl ].

VAR_021273

Natural variant

161

1

A → P. Ref.18

VAR_024084

Natural variant

168

1

F → L. Ref.17
Corresponds to variant rs28399510 [ dbSNP | Ensembl ].

VAR_024719

Natural variant

227

1

P → L in allele CYP2C19*10. Ref.15
Corresponds to variant rs6413438 [ dbSNP | Ensembl ].

VAR_020123

Natural variant

329

1

R → H in allele CYP2C19*18. Ref.18

VAR_024085

Natural variant

331

1

V → I in allele CYP2C19*1A, allele CYP2C19*5A, allele CYP2C19*8 and allele CYP2C19*16. Ref.3 Ref.5 Ref.17 Ref.18
Corresponds to variant rs3758581 [ dbSNP | Ensembl ].

VAR_001255

Natural variant

410

1

R → C in allele CYP2C19*13. Ref.3 Ref.15
Corresponds to variant rs17879685 [ dbSNP | Ensembl ].

VAR_021274

Natural variant

433

1

R → W in allele CYP2C19*5A and allele CYP2C19*5B; loss of activity. Ref.11 Ref.13
Corresponds to variant rs56337013 [ dbSNP | Ensembl ].

VAR_008359

Natural variant

442

1

R → C in allele CYP2C19*16; lowered catalytic activity. Ref.16

VAR_021275

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

490

Helix Strand Turn

Details...

Turn

37 – 39

3

Helix

42 – 44

3

Helix

47 – 49

3

Helix

50 – 61

12

Beta strand

63 – 69

7

Beta strand

72 – 77

6

Helix

80 – 87

8

Turn

88 – 90

3

Helix

91 – 94

4

Helix

103 – 106

4

Turn

107 – 109

3

Helix

117 – 130

14

Beta strand

135 – 139

5

Helix

141 – 158

18

Turn

159 – 161

3

Turn

166 – 168

3

Helix

169 – 182

14

Beta strand

183 – 185

3

Helix

192 – 209

18

Helix

211 – 218

8

Helix

222 – 225

4

Helix

228 – 254

27

Helix

263 – 273

11

Turn

274 – 276

3

Helix

284 – 297

14

Helix

300 – 315

16

Helix

317 – 330

14

Beta strand

333 – 335

3

Helix

339 – 344

6

Helix

346 – 359

14

Beta strand

377 – 379

3

Beta strand

386 – 389

4

Helix

391 – 395

5

Turn

398 – 400

3

Beta strand

401 – 403

3

Helix

409 – 412

4

Beta strand

415 – 417

3

Helix

438 – 455

18

Beta strand

456 – 462

7

Turn

464 – 466

3

Beta strand

475 – 477

3

Beta strand

485 – 489

5

Sequences

	Sequence		Length	Mass (Da)
	P33261 [UniParc]. Last modified March 1, 2005. Version 3. Checksum: 17DB04C50A132C53	FASTA	490	55,931
	10 20 30 40 50 60 MDPFVVLVLC LSCLLLLSIW RQSSGRGKLP PGPTPLPVIG NILQIDIKDV SKSLTNLSKI 70 80 90 100 110 120 YGPVFTLYFG LERMVVLHGY EVVKEALIDL GEEFSGRGHF PLAERANRGF GIVFSNGKRW 130 140 150 160 170 180 KEIRRFSLMT LRNFGMGKRS IEDRVQEEAR CLVEELRKTK ASPCDPTFIL GCAPCNVICS 190 200 210 220 230 240 IIFQKRFDYK DQQFLNLMEK LNENIRIVST PWIQICNNFP TIIDYFPGTH NKLLKNLAFM 250 260 270 280 290 300 ESDILEKVKE HQESMDINNP RDFIDCFLIK MEKEKQNQQS EFTIENLVIT AADLLGAGTE 310 320 330 340 350 360 TTSTTLRYAL LLLLKHPEVT AKVQEEIERV VGRNRSPCMQ DRGHMPYTDA VVHEVQRYID 370 380 390 400 410 420 LIPTSLPHAV TCDVKFRNYL IPKGTTILTS LTSVLHDNKE FPNPEMFDPR HFLDEGGNFK 430 440 450 460 470 480 KSNYFMPFSA GKRICVGEGL ARMELFLFLT FILQNFNLKS LIDPKDLDTT PVVNGFASVP 490 PFYQLCFIPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily." Romkes M., Faletto M.B., Blaisdell J.A., Raucy J.L., Goldstein J.A. Biochemistry 30:3247-3255(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CYP2C19*1A). Tissue: Liver.
[2]	Erratum Romkes M., Faletto M.B., Blaisdell J.A., Raucy J.L., Goldstein J.A. Biochemistry 32:1390-1390(1993) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	NIEHS SNPs program Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-19; ASP-92; ALA-122; HIS-144; ILE-331 AND CYS-410.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Gene structure, upstream region and allelic variants of cyp2c19, the s-mephenytoin hydroxylase." de Morais S.M.F., Blaisdell J.A. Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160 AND 274-490, VARIANT ILE-331.
[6]	"Isolation and characterization of human liver cytochrome P450 2C19: correlation between 2C19 and S-mephenytoin 4'-hydroxylation." Wrighton S.A., Stevens J.C., Becker G.W., VandenBranden M. Arch. Biochem. Biophys. 306:240-245(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-16. Tissue: Liver.
[7]	"Metabolism of (+)- and (-)-limonenes to respective carveols and perillyl alcohols by CYP2C9 and CYP2C19 in human liver microsomes." Miyazawa M., Shindo M., Shimada T. Drug Metab. Dispos. 30:602-607(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Structural characterization of human cytochrome P450 2C19: active site differences between P450s 2C8, 2C9, and 2C19." Reynald R.L., Sansen S., Stout C.D., Johnson E.F. J. Biol. Chem. 287:44581-44591(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 23-489 IN COMPLEX WITH HEME AND SYNTHETIC INHIBITOR, COFACTOR.
[9]	"The major genetic defect responsible for the polymorphism of S-mephenytoin metabolism in humans." de Morais S.M.F., Wilkinson G.R., Blaisdell J., Nakamura K., Meyer U.A., Goldstein J.A. J. Biol. Chem. 269:15419-15422(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN POOR DRUG METABOLISM, IDENTIFICATION OF ALLELE CYP2C19*2A.
[10]	"Identification of a new genetic defect responsible for the polymorphism of (S)-mephenytoin metabolism in Japanese." De Morais S.M.F., Wilkinson G.R., Blaisdell J., Meyer U.A., Nakamura K., Goldstein J.A. Mol. Pharmacol. 46:594-598(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN POOR DRUG METABOLISM, IDENTIFICATION OF ALLELE CYP2C19*3A.
[11]	"Differences in the incidence of the CYP2C19 polymorphism affecting the S-mephenytoin phenotype in Chinese Han and Bai populations and identification of a new rare CYP2C19 mutant allele." Xiao Z.S., Goldstein J.A., Xie H.G., Blaisdell J., Wang W., Jiang C.H., Yan F.X., He N., Huang S.L., Xu Z.H., Zhou H.H. J. Pharmacol. Exp. Ther. 281:604-609(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TRP-433.
[12]	"Identification of new human CYP2C19 alleles (CYP2C19*6 and CYP2C19*2B) in a Caucasian poor metabolizer of mephenytoin." Ibeanu G.C., Goldstein J.A., Meyer U.A., Benhamou S., Bouchardy C., Dayer P., Ghanayem B.I., Blaisdell J. J. Pharmacol. Exp. Ther. 286:1490-1495(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ASP-92 AND GLN-132.
[13]	"An additional defective allele, CYP2C19*5, contributes to the S-mephenytoin poor metabolizer phenotype in Caucasians." Ibeanu G.C., Blaisdell J., Ghanayem B.I., Beyeler C., Benhamou S., Bouchardy C., Wilkinson G.R., Dayer P., Daly A.K., Goldstein J.A. Pharmacogenetics 8:129-135(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TRP-433.
[14]	"A novel transversion in the intron 5 donor splice junction of CYP2C19 and a sequence polymorphism in exon 3 contribute to the poor metabolizer phenotype for the anticonvulsant drug S-mephenytoin." Ibeanu G.C., Blaisdell J., Ferguson R.J., Ghanayem B.I., Brosen K., Benhamou S., Bouchardy C., Wilkinson G.R., Dayer P., Goldstein J.A. J. Pharmacol. Exp. Ther. 290:635-640(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ARG-120.
[15]	"Identification and functional characterization of new potentially defective alleles of human CYP2C19." Blaisdell J., Mohrenweiser H., Jackson J., Ferguson S., Coulter S., Chanas B., Xi T., Ghanayem B., Goldstein J.A. Pharmacogenetics 12:703-711(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PRO-17; LEU-19; HIS-144; HIS-150; LEU-227 AND CYS-410.
[16]	"A novel single nucleotide polymorphism (SNP) of the CYP2C19 gene in a Japanese subject with lowered capacity of mephobarbital 4'-hydroxylation." Morita J., Kobayashi K., Wanibuchi A., Kimura M., Irie S., Ishizaki T., Chiba K. Drug Metab. Pharmacokinet. 19:236-238(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CYS-442.
[17]	"Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population." 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. Pharmacogenomics 5:895-931(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS THR-74; HIS-144; LEU-168 AND ILE-331.
[18]	"Genetic variations and haplotypes of CYP2C19 in a Japanese population." Fukushima-Uesaka H., Saito Y., Maekawa K., Ozawa S., Hasegawa R., Kajio H., Kuzuya N., Yasuda K., Kawamoto M., Kamatani N., Suzuki K., Yanagawa T., Tohkin M., Sawada J. Drug Metab. Pharmacokinet. 20:300-307(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLY-51; PRO-161; HIS-329 AND ILE-331.
+	Additional computationally mapped references.

Web resources

Cytochrome P450 Allele Nomenclature Committee

CYP2C19 alleles

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M61854 mRNA. Translation: AAB59426.1.
M61858 mRNA. Translation: AAA52145.1. Sequence problems.
L07093 mRNA. Translation: AAA36660.1. Sequence problems.
AY796203 Genomic DNA. Translation: AAV41877.1.
AL583836, AL133513 Genomic DNA. Translation: CAH74068.1.
AL133513, AL583836 Genomic DNA. Translation: CAH73444.1.
L39098, L39097 Genomic DNA. Translation: AAL31347.1.
L39102 , L39099, L39100, L39101 Genomic DNA. Translation: AAL31348.1.
L31506 Genomic DNA. No translation available.
L31507 Genomic DNA. No translation available.
L32982 Genomic DNA. No translation available.
L32983 Genomic DNA. No translation available.

IPI

IPI00013323.

PIR

F38462.
G38462.
I52418.

RefSeq

NP_000760.1. NM_000769.1.

UniGene

Hs.282409.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4GQS	X-ray	2.87	A/B/C/D	23-489	[»]

ProteinModelPortal

P33261.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000360372.

PTM databases

PhosphoSite

P33261.

Polymorphism databases

DMDM

60416369.

Proteomic databases

PaxDb

P33261.

PRIDE

P33261.

Protocols and materials databases

DNASU

1557.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371321; ENSP00000360372; ENSG00000165841.

GeneID

1557.

KEGG

hsa:1557.

UCSC

uc010qny.2. human.

Organism-specific databases

CTD

1557.

GeneCards

GC10P096447.

HGNC

HGNC:2621. CYP2C19.

HPA

HPA015066.

MIM

124020. gene.
609535. phenotype.

neXtProt

NX_P33261.

Orphanet

240847. Amitriptyline toxicity.
240865. Clomipramine toxicity.
240883. Imipramine toxicity.
240893. Nortriptyline toxicity.
240931. Resistance to amitriptyline in the treatment of depression.
240933. Resistance to clomipramine in the treatment of depression.
240935. Resistance to clopidogrel in myocardial infarction, cerebrovascular accident, oblitering arteriopathy of the lower limbs.
240939. Resistance to imipramine in the treatment of depression.
240941. Resistance to nortripilline in the treatment of depression.
240949. Resistance to trimipramine in the treatment of depression.
240951. Resistance to venlafaxine in the treatment of depression.
240957. Susceptibility to adverse reaction due to amitriptyline treatment.
240965. Susceptibility to adverse reaction due to clomipramine treatment.
240971. Susceptibility to adverse reaction due to imipramine treatment.
240979. Susceptibility to adverse reaction due to nortriptyline treatment.
240987. Susceptibility to adverse reaction due to trimipramine treatment.
240989. Susceptibility to adverse reaction due to venlafaxine treatment.
241003. Susceptibility to hepatitis due to voriconazole treatment.
240915. Trimipramine toxicity.
240919. Venlafaxine toxicity.
240921. Voriconazole toxicity.

PharmGKB

PA124.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000036992.

HOVERGEN

HBG015789.

InParanoid

P33261.

KO

K07413.

OMA

RIVSTPW.

OrthoDB

EOG48WC22.

PhylomeDB

P33261.

Enzyme and pathway databases

BioCyc

MetaCyc:HS09293-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P33261.

Gene expression databases

Bgee

P33261.

CleanEx

HS_CYP2C19.

Genevestigator

P33261.

GermOnline

ENSG00000165841. Homo sapiens.

Family and domain databases

Gene3D

1.10.630.10. 1 hit.

InterPro

IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00463. EP450I.
PR00385. P450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P33261.

ChEMBL

CHEMBL3622.

DrugBank

DB00546. Adinazolam.
DB01424. Aminophenazone.
DB00321. Amitriptyline.
DB01060. Amoxicillin.
DB01274. Arformoterol.
DB00188. Bortezomib.
DB00395. Carisoprodol.
DB00356. Chlorzoxazone.
DB01166. Cilostazol.
DB00215. Citalopram.
DB01211. Clarithromycin.
DB00349. Clobazam.
DB01151. Desipramine.
DB00967. Desloratadine.
DB00586. Diclofenac.
DB00343. Diltiazem.
DB00625. Efavirenz.
DB00736. Esomeprazole.
DB00927. Famotidine.
DB00949. Felbamate.
DB01216. Finasteride.
DB01544. Flunitrazepam.
DB00176. Fluvoxamine.
DB00983. Formoterol.
DB01320. Fosphenytoin.
DB01018. Guanfacine.
DB00458. Imipramine.
DB00328. Indomethacin.
DB01026. Ketoconazole.
DB00448. Lansoprazole.
DB01259. Lapatinib.
DB00455. Loratadine.
DB01065. Melatonin.
DB00532. Mephenytoin.
DB00333. Methadone.
DB00849. Methylphenobarbital.
DB01171. Moclobemide.
DB00745. Modafinil.
DB00220. Nelfinavir.
DB00622. Nicardipine.
DB00665. Nilutamide.
DB00506. Norgestrel.
DB00338. Omeprazole.
DB00776. Oxcarbazepine.
DB00213. Pantoprazole.
DB00738. Pentamidine.
DB01174. Phenobarbital.
DB00252. Phenytoin.
DB00794. Primidone.
DB00396. Progesterone.
DB01131. Proguanil.
DB00420. Promazine.
DB00908. Quinidine.
DB01129. Rabeprazole.
DB00863. Ranitidine.
DB00503. Ritonavir.
DB01037. Selegiline.
DB01104. Sertraline.
DB00231. Temazepam.
DB00444. Teniposide.
DB00342. Terfenadine.
DB01041. Thalidomide.
DB00679. Thioridazine.
DB00208. Ticlopidine.
DB01124. Tolbutamide.
DB00273. Topiramate.
DB00752. Tranylcypromine.
DB00197. Troglitazone.
DB01361. Troleandomycin.
DB00582. Voriconazole.

GenomeRNAi

1557.

NextBio

6430.

SOURCE

Search...

Entry information

Entry name

CP2CJ_HUMAN

Accession

Primary (citable) accession number: P33261
Secondary accession number(s): P33259 , Q8WZB1, Q8WZB2, Q9UCD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	March 1, 2005
Last modified:	May 1, 2013
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.