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Reviewed, UniProtKB/Swiss-Prot P08684 (CP3A4_HUMAN)

Last modified June 16, 2009. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytochrome P450 3A4
Alternative name(s):
    Quinine 3-monooxygenase
    EC=1.14.13.67
    CYPIIIA4
    Nifedipine oxidase
    Cytochrome P450 3A3
    CYPIIIA3
    HLp
    Taurochenodeoxycholate 6-alpha-hydroxylase
    EC=1.14.13.97
    NF-25
    P450-PCN1
    Albendazole monooxygenase
    EC=1.14.13.32
    Albendazole sulfoxidase
Gene names
Name: CYP3A4
Synonyms: CYP3A3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e.g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4-hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. The enzyme also hydroxylates etoposide.

Catalytic activity

Quinine + NADPH + O2 = 3-hydroxyquinine + NADP+ + H2O.

Taurochenodeoxycholate + NADPH + O2 = taurohyocholate + NADP+ + H2O.

Lithocholate + NADPH + O2 = hyodeoxycholate + NADP+ + H2O.

Albendazole + NADPH + O2 = albendazole S-oxide + NADP+ + H2O.

Cofactor

Heme group.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein. Microsome membrane; Single-pass membrane protein.

Tissue specificity

Expressed in prostate and liver.

Induction

By glucocorticoids. Also induced to high levels in liver and other tissues by various foreign compounds, including drugs, pesticides, and carcinogens.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityPolymorphism
   DomainTransmembrane
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processdrug metabolic process

Inferred from direct assay. Source: UniProtKB

oxidation reduction

Inferred from direct assay. Source: UniProtKB

steroid metabolic process

Inferred from mutant phenotype. Source: UniProtKB

vitamin D metabolic process

Inferred by curator. Source: UniProtKB

   Cellular componentcell surface

Inferred from direct assay. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microsome Ref.1

Inferred from direct assay. Source: UniProtKB

   Molecular functionalbendazole 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

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

Inferred from electronic annotation. Source: InterPro

oxygen binding Ref.1

Traceable author statement. Source: ProtInc

quinine 3-monooxygenase activity

Inferred from electronic annotation. Source: EC

steroid binding Ref.15

Inferred from direct assay. Source: UniProtKB

taurochenodeoxycholate 6alpha-hydroxylase activity

Inferred from electronic annotation. Source: EC

testosterone 6-beta-hydroxylase activity

Inferred from mutant phenotype. Source: UniProtKB

vitamin D3 25-hydroxylase activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 503502Cytochrome P450 3A4
PRO_0000051786

Regions

Transmembrane2 – 2221 Potential

Sites

Metal binding4421Iron (heme axial ligand)

Natural variations

Natural variant151L → P in allele CYP3A4*14. dbSNP rs12721634. Ref.19
VAR_011597
Natural variant561G → D in allele CYP3A4*7. Ref.18
VAR_011598
Natural variant961K → E: dbSNP rs3091339.
VAR_037547
Natural variant1181I → V in allele CYP3A4*4. Ref.8
VAR_011599
Natural variant1301R → Q in allele CYP3A4*8. Ref.18
VAR_011600
Natural variant1621R → Q in allele CYP3A4*15. dbSNP rs4986907. Ref.19 Ref.17
VAR_011601
Natural variant1701V → I in allele CYP3A4*9. Ref.18
VAR_011602
Natural variant1741D → H in allele CYP3A4*10. Ref.19 Ref.18 Ref.20
VAR_011603
Natural variant1851T → S in allele CYP3A4*16. dbSNP rs12721627. Ref.19 Ref.20
VAR_011604
Natural variant1891F → S in allele CYP3A4*17; exhibits lower turnover numbers for testosterone and chlorpyrifos. dbSNP rs4987161. Ref.17
VAR_014322
Natural variant2181P → R in allele CYP3A4*5. Ref.8
VAR_011605
Natural variant2221S → P in allele CYP3A4*2; exhibits a lower intrinsic clearance toward nifedipine. Ref.16
VAR_008363
Natural variant2521S → A: dbSNP rs3208363. Ref.1
VAR_037548
Natural variant2931L → P in allele CYP3A4*18; exhibits higher turnover numbers for testosterone and chlorpyrifos. dbSNP rs28371759. Ref.17 Ref.20
VAR_014323
Natural variant3491T → N: dbSNP rs10250778.
VAR_037549
Natural variant3631T → M in allele CYP3A4*11; unstable form. Ref.18
VAR_011606
Natural variant3731L → F in allele CYP3A4*12; has an altered testosterone hydroxylase activity. dbSNP rs12721629. Ref.19 Ref.18
VAR_011607
Natural variant4161P → L in allele CYP3A4*13; lack of expression. dbSNP rs4986909. Ref.18
VAR_011608
Natural variant4311I → T: dbSNP rs1041988. Ref.3 Ref.5
VAR_037550
Natural variant4451M → T in allele CYP3A4*3. dbSNP rs4986910. Ref.17 Ref.16
VAR_008364
Natural variant4671P → S in allele CYP3A4*19. dbSNP rs4986913. Ref.17
VAR_014324

Experimental info

Sequence conflict31L → V in AAA35747. Ref.5
Sequence conflict121W → R in AAF13598. Ref.9
Sequence conflict721W → C in AAA35747. Ref.5
Sequence conflict921T → L in BAA00001. Ref.1
Sequence conflict921T → L in AAA35742. Ref.1
Sequence conflict1061R → E in BAA00001. Ref.1
Sequence conflict1061R → E in AAA35742. Ref.1
Sequence conflict1641A → R in BAA00001. Ref.1
Sequence conflict1641A → R in AAA35742. Ref.1
Sequence conflict1871T → S in BAA00001. Ref.1
Sequence conflict1871T → S in AAA35742. Ref.1
Sequence conflict1931I → V in BAA00001. Ref.1
Sequence conflict1931I → V in AAA35742. Ref.1
Sequence conflict2031F → L in BAA00001. Ref.1
Sequence conflict2031F → L in AAA35742. Ref.1
Sequence conflict224 – 2252TV → I in AAA35747. Ref.5
Sequence conflict2791Q → HK in BAA00001. Ref.1
Sequence conflict2791Q → HK in AAA35742. Ref.1
Sequence conflict3071Y → C in AAF13598. Ref.9
Sequence conflict3921V → W in BAA00001. Ref.1
Sequence conflict3921V → W in AAA35742. Ref.1
Sequence conflict3921V → W in AAA35744. Ref.3
Sequence conflict3921V → W in CAA30944. Ref.4
Sequence conflict3921V → W in AAA35747. Ref.5

Secondary structure

.................................................................................... 503
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08684-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 38ED122BF89F74F7

FASTA50357,343
        10         20         30         40         50         60 
MALIPDLAME TWLLLAVSLV LLYLYGTHSH GLFKKLGIPG PTPLPFLGNI LSYHKGFCMF 

        70         80         90        100        110        120 
DMECHKKYGK VWGFYDGQQP VLAITDPDMI KTVLVKECYS VFTNRRPFGP VGFMKSAISI 

       130        140        150        160        170        180 
AEDEEWKRLR SLLSPTFTSG KLKEMVPIIA QYGDVLVRNL RREAETGKPV TLKDVFGAYS 

       190        200        210        220        230        240 
MDVITSTSFG VNIDSLNNPQ DPFVENTKKL LRFDFLDPFF LSITVFPFLI PILEVLNICV 

       250        260        270        280        290        300 
FPREVTNFLR KSVKRMKESR LEDTQKHRVD FLQLMIDSQN SKETESHKAL SDLELVAQSI 

       310        320        330        340        350        360 
IFIFAGYETT SSVLSFIMYE LATHPDVQQK LQEEIDAVLP NKAPPTYDTV LQMEYLDMVV 

       370        380        390        400        410        420 
NETLRLFPIA MRLERVCKKD VEINGMFIPK GVVVMIPSYA LHRDPKYWTE PEKFLPERFS 

       430        440        450        460        470        480 
KKNKDNIDPY IYTPFGSGPR NCIGMRFALM NMKLALIRVL QNFSFKPCKE TQIPLKLSLG 

       490        500 
GLLQPEKPVV LKVESRDGTV SGA 

« Hide

References

[1]"Complete cDNA sequence of a cytochrome P-450 inducible by glucocorticoids in human liver."
Molowa D.T., Schuetz E.G., Wrighton S.A., Watkins P.B., Kremers P., Mendez-Picon G., Parker G.A., Guzelian P.S.
Proc. Natl. Acad. Sci. U.S.A. 83:5311-5315(1986) [PubMed: 3460094] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-252.
Tissue: Liver.
[2]"Human P450PCN1: sequence, chromosome localization, and direct evidence through cDNA expression that P450PCN1 is nifedipine oxidase."
Gonzalez F.J., Schmid B.J., Umeno M., McBride O.W., Hardwick J.P., Meyer U.A., Gelboin H.V., Idle J.R.
DNA 7:79-86(1988) [PubMed: 3267210] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Isolation and sequence determination of a cDNA clone related to human cytochrome P-450 nifedipine oxidase."
Beaune P.H., Umbenhauer D.R., Bork R.W., Lloyd R.S., Guengerich F.P.
Proc. Natl. Acad. Sci. U.S.A. 83:8064-8068(1986) [PubMed: 3464943] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-431.
[4]"The human cytochrome P450 CYP3 locus: assignment to chromosome 7q22-qter."
Spurr N.K., Gough A.C., Stevenson K., Wolf C.R.
Hum. Genet. 81:171-174(1989) [PubMed: 2563251] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Characterization of mRNA species related to human liver cytochrome P-450 nifedipine oxidase and the regulation of catalytic activity."
Bork R.W., Muto T., Beaune P.H., Srivastava P.K., Lloyd R.S., Guengerich F.P.
J. Biol. Chem. 264:910-919(1989) [PubMed: 2463251] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-431.
Tissue: Liver.
[6]"Establishment of transgenic cell line CHL-3A4 and its metabolic activation."
Chen Q., Wu J., Yu Y.
Zhonghua Yu Fang Yi Xue Za Zhi 32:281-284(1998) [PubMed: 10322772] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[7]"Genomic organization of the human CYP3A locus: identification of a new, inducible CYP3A gene."
Gellner K., Eiselt R., Hustert E., Arnold H., Koch I., Haberl M., Deglmann C.J., Burk O., Buntefuss D., Escher S., Bishop C., Koebe H.-G., Brinkmann U., Klenk H.-P., Kleine K., Meyer U.A., Wojnowski L.
Pharmacogenetics 11:111-121(2001) [PubMed: 11266076] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Novel mutations of CYP3A4 in Chinese."
Hsieh K.-P., Lin Y.-Y., Cheng C.-L., Lai M.-L., Lin M.-S., Siest J.-P., Huang J.-D.
Drug Metab. Dispos. 29:268-273(2001) [PubMed: 11181494] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-118 AND ARG-218.
[9]"Sequence of a new human cytochrome P450-3A4 cDNA."
Zhuge J., Qian Y., Xie H., Yu Y.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[10]"Cytochrome P-450 in human liver microsomes: high-performance liquid chromatographic isolation of three forms and their characterization."
Komori M., Hashizume T., Ohi H., Miura T., Kitada M., Nagashima K., Kamataki T.
J. Biochem. 104:912-916(1988) [PubMed: 3243766] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-25.
[11]"Identification of an inducible form of cytochrome P-450 in human liver."
Watkins P.B., Wrighton S.A., Maurel P., Schuetz E.G., Mendez-Picon G., Parker G.A., Guzelian P.S.
Proc. Natl. Acad. Sci. U.S.A. 82:6310-6314(1985) [PubMed: 3898085] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Tissue: Liver.
[12]"Evidence for involvement of human CYP3A in the 3-hydroxylation of quinine."
Zhang H., Coville P.F., Walker R.J., Miners J.O., Birkett D.J., Wanwimolruk S.
Br. J. Clin. Pharmacol. 43:245-252(1997) [PubMed: 9088578] [Abstract]
Cited for: CHARACTERIZATION.
[13]"Mutual inhibition between quinine and etoposide by human liver microsomes. Evidence for cytochrome P4503A4 involvement in their major metabolic pathways."
Zhao X.J., Kawashiro T., Ishizaki T.
Drug Metab. Dispos. 26:188-191(1998) [PubMed: 9456308] [Abstract]
Cited for: CHARACTERIZATION.
[14]"The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution."
Yano J.K., Wester M.R., Schoch G.A., Griffin K.J., Stout C.D., Johnson E.F.
J. Biol. Chem. 279:38091-38094(2004) [PubMed: 15258162] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 24-503.
[15]"Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone."
Williams P.A., Cosme J., Vinkovic D.M., Ward A., Angove H.C., Day P.J., Vonrhein C., Tickle I.J., Jhoti H.
Science 305:683-686(2004) [PubMed: 15256616] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-503.
[16]"CYP3A4 allelic variants with amino acid substitutions in exons 7 and 12: evidence for an allelic variant with altered catalytic activity."
Sata F., Sapone A., Elizondo G., Stocker P., Miller V.P., Zheng W., Raunio H., Crespi C.L., Gonzalez F.J.
Clin. Pharmacol. Ther. 67:48-56(2000) [PubMed: 10668853] [Abstract]
Cited for: VARIANTS PRO-222 AND THR-445.
[17]"Identification of variants of CYP3A4 and characterization of their abilities to metabolize testosterone and chlorpyrifos."
Dai D., Tang J., Rose R., Hodgson E., Bienstock R.J., Mohrenweiser H.W., Goldstein J.A.
J. Pharmacol. Exp. Ther. 299:825-831(2001) [PubMed: 11714865] [Abstract]
Cited for: VARIANTS GLN-162; SER-189; PRO-293; THR-445 AND SER-467, CHARACTERIZATION OF THE VARIANTS.
[18]"Identification and functional characterization of eight CYP3A4 protein variants."
Eiselt R., Domanski T.L., Zibat A., Mueller R., Presecan-Siedel E., Hustert E., Zanger U.M., Brockmoller J., Klenk H.-P., Meyer U.A., Khan K.K., He Y.-A., Halpert J.R., Wojnowski L.
Pharmacogenetics 11:447-458(2001) [PubMed: 11470997] [Abstract]
Cited for: VARIANTS ASP-56; GLN-130; ILE-170; HIS-174; MET-363; PHE-373 AND LEU-416.
[19]"Common allelic variants of cytochrome P4503A4 and their prevalence in different populations."
Lamba J.K., Lin Y.S., Thummel K., Daly A., Watkins P.B., Strom S., Zhang J., Schuetz E.G.
Pharmacogenetics 12:121-132(2002) [PubMed: 11875366] [Abstract]
Cited for: VARIANTS PRO-15; GLN-162; HIS-174; SER-185 AND PHE-373.
[20]"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: 15469410] [Abstract]
Cited for: VARIANTS HIS-174; SER-185 AND PRO-293.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

D00003 mRNA. Translation: BAA00001.1.
M13785 mRNA. Translation: AAA35742.1.
M18907 mRNA. Translation: AAA35745.1.
M14096 mRNA. Translation: AAA35744.1.
X12387 mRNA. Translation: CAA30944.1.
J04449 mRNA. Translation: AAA35747.1.
AF182273 mRNA. Translation: AAF13598.1.
AF280107 Genomic DNA. Translation: AAG32290.1.
AF209389 Genomic DNA. Translation: AAF21034.1.
IPIIPI00465138.
PIRA29410.
A29815.
RefSeqNP_059488.2.
UniGeneHs.654391

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TQNX-ray2.05A24-503[»]
1W0EX-ray2.80A25-503[»]
1W0FX-ray2.65A25-503[»]
1W0GX-ray2.73A25-503[»]
2J0DX-ray2.75A/B25-502[»]
2V0MX-ray3.80A/B/C/D25-502[»]
ModBaseSearch...

PTM databases

PhosphoSiteP08684.

Proteomic databases

PRIDEP08684.

Genome annotation databases

EnsemblENSG00000160868. Homo sapiens. [Contig view]
GeneID1576.
KEGGhsa:1576.

Organism-specific databases

GeneCardsGC07M099192.
H-InvDBHIX0078878.
HGNCHGNC:2637. CYP3A4.
MIM124010. gene.
PharmGKBPA130.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP08684.
OMAP08684. PDLAMET.

Enzyme and pathway databases

BRENDA1.14.13.67. 247.
1.14.13.97. 247.
ReactomeREACT_13433. Biological oxidations.
REACT_649. Phase 1 functionalization.

Gene expression databases

ArrayExpressP08684.
BgeeP08684.
CleanExHS_CYP3A4.
GermOnlineENSG00000160868. Homo sapiens.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR008072. Cyt_P450_E_CYP3A.
IPR002402. Cyt_P450_E_grp-II.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00464. EP450II.
PR01689. EP450IICYP3A.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00518. Albendazole.
DB00240. Alclometasone.
DB00802. Alfentanil.
DB00346. Alfuzosin.
DB01258. Aliskiren.
DB00918. Almotriptan.
DB00969. Alosetron.
DB00404. Alprazolam.
DB00381. Amlodipine.
DB00701. Amprenavir.
DB00673. Aprepitant.
DB01238. Aripiprazole.
DB00637. Astemizole.
DB01072. Atazanavir.
DB01076. Atorvastatin.
DB00542. Benazepril.
DB01244. Bepridil.
DB00443. Betamethasone.
DB00307. Bexarotene.
DB00188. Bortezomib.
DB00559. Bosentan.
DB01200. Bromocriptine.
DB01222. Budesonide.
DB00297. Bupivacaine.
DB00921. Buprenorphine.
DB00490. Buspirone.
DB01008. Busulfan.
DB00564. Carbamazepine.
DB00185. Cevimeline.
DB01114. Chlorpheniramine.
DB01410. Ciclesonide.
DB01166. Cilostazol.
DB01012. Cinacalcet.
DB00604. Cisapride.
DB01211. Clarithromycin.
DB01190. Clindamycin.
DB00636. Clofibrate.
DB01068. Clonazepam.
DB00758. Clopidogrel.
DB00907. Cocaine.
DB00872. Conivaptan.
DB00286. Conjugated Estrogens.
DB04839. Cyproterone.
DB00496. Darifenacin.
DB01264. Darunavir.
DB01254. Dasatinib.
DB00705. Delavirdine.
DB00304. Desogestrel.
DB01234. Dexamethasone.
DB00829. Diazepam.
DB00320. Dihydroergotamine.
DB00343. Diltiazem.
DB01075. Diphenhydramine.
DB00280. Disopyramide.
DB00204. Dofetilide.
DB00757. Dolasetron.
DB01184. Domperidone.
DB00843. Donepezil.
DB00997. Doxorubicin.
DB01395. Drospirenone.
DB01126. Dutasteride.
DB00625. Efavirenz.
DB00216. Eletriptan.
DB00584. Enalapril.
DB00445. Epirubicin.
DB00700. Eplerenone.
DB00696. Ergotamine.
DB00530. Erlotinib.
DB00199. Erythromycin.
DB01175. Escitalopram.
DB00736. Esomeprazole.
DB01215. Estazolam.
DB00402. Eszopiclone.
DB00977. Ethinyl Estradiol.
DB00593. Ethosuximide.
DB00294. Etonogestrel.
DB00773. Etoposide.
DB01628. Etoricoxib.
DB00990. Exemestane.
DB01023. Felodipine.
DB00813. Fentanyl.
DB00950. Fexofenadine.
DB01216. Finasteride.
DB00196. Fluconazole.
DB00663. Flumethasone Pivalate.
DB00180. Flunisolide.
DB00591. Fluocinolone Acetonide.
DB01047. Fluocinonide.
DB00324. Fluorometholone.
DB00846. Flurandrenolide.
DB00588. Fluticasone Propionate.
DB01319. Fosamprenavir.
DB00947. Fulvestrant.
DB00674. Galantamine.
DB00317. Gefitinib.
DB01241. Gemfibrozil.
DB00889. Granisetron.
DB00365. Grepafloxacin.
DB01218. Halofantrine.
DB00956. Hydrocodone.
DB00769. Hydrocortamate.
DB00741. Hydrocortisone.
DB00327. Hydromorphone.
DB00619. Imatinib.
DB00224. Indinavir.
DB00332. Ipratropium.
DB00762. Irinotecan.
DB00883. Isosorbide Dinitrate.
DB01020. Isosorbide Mononitrate.
DB00270. Isradipine.
DB01167. Itraconazole.
DB01026. Ketoconazole.
DB01259. Lapatinib.
DB00528. Lercanidipine.
DB01006. Letrozole.
DB01002. Levobupivacaine.
DB01227. Levomethadyl Acetate.
DB00451. Levothyroxine.
DB01206. Lomustine.
DB00836. Loperamide.
DB01601. Lopinavir.
DB00455. Loratadine.
DB00678. Losartan.
DB00227. Lovastatin.
DB04835. Maraviroc.
DB00470. Marinol.
DB00643. Mebendazole.
DB00603. Medroxyprogesterone.
DB00333. Methadone.
DB00959. Methylprednisolone.
DB01011. Metyrapone.
DB01388. Mibefradil.
DB00683. Midazolam.
DB00834. Mifepristone.
DB00370. Mirtazapine.
DB00745. Modafinil.
DB00764. Mometasone.
DB00471. Montelukast.
DB00731. Nateglinide.
DB01149. Nefazodone.
DB00220. Nelfinavir.
DB00238. Nevirapine.
DB00622. Nicardipine.
DB01115. Nifedipine.
DB00393. Nimodipine.
DB00401. Nisoldipine.
DB01054. Nitrendipine.
DB00717. Norethindrone.
DB00506. Norgestrel.
DB00646. Nystatin.
DB00904. Ondansetron.
DB01062. Oxybutynin.
DB01229. Paclitaxel.
DB01267. Paliperidone.
DB00377. Palonosetron.
DB00213. Pantoprazole.
DB00910. Paricalcitol.
DB00830. Phenmetrazine.
DB00337. Pimecrolimus.
DB01100. Pimozide.
DB01132. Pioglitazone.
DB01263. Posaconazole.
DB01411. Pranlukast.
DB00860. Prednisolone.
DB00635. Prednisone.
DB00433. Prochlorperazine.
DB01224. Quetiapine.
DB00881. Quinapril.
DB00468. Quinine.
DB01129. Rabeprazole.
DB00243. Ranolazine.
DB00234. Reboxetine.
DB01256. Retapamulin.
DB00615. Rifabutin.
DB01045. Rifampin.
DB06155. Rimonabant.
DB00503. Ritonavir.
DB00533. Rofecoxib.
DB00778. Roxithromycin.
DB00938. Salmeterol.
DB01232. Saquinavir.
DB06144. Sertindole.
DB01105. Sibutramine.
DB00641. Simvastatin.
DB00877. Sirolimus.
DB01261. Sitagliptin.
DB01591. Solifenacin.
DB00398. Sorafenib.
DB01268. Sunitinib.
DB00864. Tacrolimus.
DB00820. Tadalafil.
DB00675. Tamoxifen.
DB00976. Telithromycin.
DB00251. Terconazole.
DB00342. Terfenadine.
DB00624. Testosterone.
DB00906. Tiagabine.
DB00208. Ticlopidine.
DB00911. Tinidazole.
DB01409. Tiotropium.
DB00932. Tipranavir.
DB00539. Toremifene.
DB00897. Triazolam.
DB01157. Trimetrexate.
DB00197. Troglitazone.
DB00580. Valdecoxib.
DB00862. Vardenafil.
DB00570. Vinblastine.
DB00541. Vincristine.
DB00309. Vindesine.
DB00361. Vinorelbine.
DB00582. Voriconazole.
DB00962. Zaleplon.
DB00744. Zileuton.
DB00246. Ziprasidone.
DB00425. Zolpidem.
DB00909. Zonisamide.
NextBio6475.
SOURCESearch...

Entry information

Entry nameCP3A4_HUMAN
AccessionPrimary (citable) accession number: P08684
Secondary accession number(s): P05184, Q16757, Q9UK50
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 114 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents