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P33261 (CP2CJ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.8

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 componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityPolymorphism
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Traceable author statement. Source: Reactome

drug metabolic process

Inferred from direct assay PubMed 19219744PubMed 19651758. Source: BHF-UCL

epoxygenase P450 pathway

Traceable author statement. Source: Reactome

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

omega-hydroxylase P450 pathway

Traceable author statement. Source: Reactome

oxidation-reduction process

Inferred from direct assay PubMed 16401082PubMed 19219744. 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_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Traceable author statement PubMed 3442670. Source: ProtInc

   Molecular_function(R)-limonene 6-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

(S)-limonene 6-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

(S)-limonene 7-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

enzyme binding

Inferred from physical interaction PubMed 15680923. Source: BHF-UCL

heme binding

Inferred from direct assay Ref.8. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

monooxygenase activity

Inferred from direct assay PubMed 19651758. Source: BHF-UCL

oxidoreductase activity

Inferred from direct assay PubMed 16401082PubMed 19219744. Source: BHF-UCL

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Cytochrome P450 2C19
PRO_0000051708

Sites

Metal binding4351Iron (heme axial ligand)

Natural variations

Natural variant171L → P in allele CYP2C19*14. Ref.15
Corresponds to variant rs55752064 [ dbSNP | Ensembl ].
VAR_021268
Natural variant191I → L in allele CYP2C19*15. Ref.3 Ref.15
Corresponds to variant rs17882687 [ dbSNP | Ensembl ].
VAR_021269
Natural variant511S → G in allele CYP2C19*19. Ref.18
VAR_024083
Natural variant741M → T. Ref.17
Corresponds to variant rs28399505 [ dbSNP | Ensembl ].
VAR_024718
Natural variant921E → D. Ref.3 Ref.12
Corresponds to variant rs17878459 [ dbSNP | Ensembl ].
VAR_021270
Natural variant1201W → R in allele CYP2C19*8; loss of activity. Ref.14
Corresponds to variant rs41291556 [ dbSNP | Ensembl ].
VAR_008357
Natural variant1221E → A. Ref.3
Corresponds to variant rs17885179 [ dbSNP | Ensembl ].
VAR_021271
Natural variant1321R → Q in allele CYP2C19*6; loss of activity. Ref.12
VAR_008358
Natural variant1441R → H in allele CYP2C19*9. Ref.3 Ref.15 Ref.17
Corresponds to variant rs17884712 [ dbSNP | Ensembl ].
VAR_021272
Natural variant1501R → H in allele CYP2C19*11. Ref.15
Corresponds to variant rs58973490 [ dbSNP | Ensembl ].
VAR_021273
Natural variant1611A → P. Ref.18
Corresponds to variant rs181297724 [ dbSNP | Ensembl ].
VAR_024084
Natural variant1681F → L. Ref.17
Corresponds to variant rs28399510 [ dbSNP | Ensembl ].
VAR_024719
Natural variant2271P → L in allele CYP2C19*10. Ref.15
Corresponds to variant rs6413438 [ dbSNP | Ensembl ].
VAR_020123
Natural variant3291R → H in allele CYP2C19*18. Ref.18
VAR_024085
Natural variant3311V → 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 variant4101R → C in allele CYP2C19*13. Ref.3 Ref.15
Corresponds to variant rs17879685 [ dbSNP | Ensembl ].
VAR_021274
Natural variant4331R → 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 variant4421R → C in allele CYP2C19*16; lowered catalytic activity. Ref.16
Corresponds to variant rs192154563 [ dbSNP | Ensembl ].
VAR_021275

Secondary structure

........................................................................... 490
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33261 [UniParc].

Last modified March 1, 2005. Version 3.
Checksum: 17DB04C50A132C53

FASTA49055,931
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.

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 expand/collapse EMBL AC list , 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.
CCDSCCDS7436.1.
PIRF38462.
G38462.
I52418.
RefSeqNP_000760.1. NM_000769.1.
UniGeneHs.282409.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GQSX-ray2.87A/B/C/D23-489[»]
ProteinModelPortalP33261.
SMRP33261. Positions 29-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107935. 1 interaction.
STRING9606.ENSP00000360372.

Chemistry

BindingDBP33261.
ChEMBLCHEMBL3622.
DrugBankDB00546. 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.

PTM databases

PhosphoSiteP33261.

Polymorphism databases

DMDM60416369.

Proteomic databases

PaxDbP33261.
PRIDEP33261.

Protocols and materials databases

DNASU1557.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371321; ENSP00000360372; ENSG00000165841.
GeneID1557.
KEGGhsa:1557.
UCSCuc010qny.2. human.

Organism-specific databases

CTD1557.
GeneCardsGC10P096447.
HGNCHGNC:2621. CYP2C19.
HPAHPA015066.
MIM124020. gene.
609535. phenotype.
neXtProtNX_P33261.
Orphanet240847. 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.
PharmGKBPA124.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000036992.
HOVERGENHBG015789.
InParanoidP33261.
KOK17721.
OMARIVSTPW.
OrthoDBEOG7RBZ85.
PhylomeDBP33261.
TreeFamTF352043.

Enzyme and pathway databases

BioCycMetaCyc:HS09293-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP33261.

Gene expression databases

BgeeP33261.
CleanExHS_CYP2C19.
GenevestigatorP33261.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCYP2C19.
GenomeRNAi1557.
NextBio6430.
PROP33261.
SOURCESearch...

Entry information

Entry nameCP2CJ_HUMAN
AccessionPrimary (citable) accession number: P33261
Secondary accession number(s): P33259 expand/collapse secondary AC list , Q8WZB1, Q8WZB2, Q9UCD4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: March 1, 2005
Last modified: July 9, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM