Reviewed, UniProtKB/Swiss-Prot P08684 (CP3A4_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	drug 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 component	cell 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 function	albendazole 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 503

502

Cytochrome P450 3A4

PRO_0000051786

Regions

Transmembrane

2 – 22

21

Potential

Sites

Metal binding

442

1

Iron (heme axial ligand)

Natural variations

Natural variant

15

1

L → P in allele CYP3A4*14. dbSNP rs12721634. Ref.19

VAR_011597

Natural variant

56

1

G → D in allele CYP3A4*7. Ref.18

VAR_011598

Natural variant

96

1

K → E: dbSNP rs3091339.

VAR_037547

Natural variant

118

1

I → V in allele CYP3A4*4. Ref.8

VAR_011599

Natural variant

130

1

R → Q in allele CYP3A4*8. Ref.18

VAR_011600

Natural variant

162

1

R → Q in allele CYP3A4*15. dbSNP rs4986907. Ref.19 Ref.17

VAR_011601

Natural variant

170

1

V → I in allele CYP3A4*9. Ref.18

VAR_011602

Natural variant

174

1

D → H in allele CYP3A4*10. Ref.19 Ref.18 Ref.20

VAR_011603

Natural variant

185

1

T → S in allele CYP3A4*16. dbSNP rs12721627. Ref.19 Ref.20

VAR_011604

Natural variant

189

1

F → S in allele CYP3A4*17; exhibits lower turnover numbers for testosterone and chlorpyrifos. dbSNP rs4987161. Ref.17

VAR_014322

Natural variant

218

1

P → R in allele CYP3A4*5. Ref.8

VAR_011605

Natural variant

222

1

S → P in allele CYP3A4*2; exhibits a lower intrinsic clearance toward nifedipine. Ref.16

VAR_008363

Natural variant

252

1

S → A: dbSNP rs3208363. Ref.1

VAR_037548

Natural variant

293

1

L → P in allele CYP3A4*18; exhibits higher turnover numbers for testosterone and chlorpyrifos. dbSNP rs28371759. Ref.17 Ref.20

VAR_014323

Natural variant

349

1

T → N: dbSNP rs10250778.

VAR_037549

Natural variant

363

1

T → M in allele CYP3A4*11; unstable form. Ref.18

VAR_011606

Natural variant

373

1

L → F in allele CYP3A4*12; has an altered testosterone hydroxylase activity. dbSNP rs12721629. Ref.19 Ref.18

VAR_011607

Natural variant

416

1

P → L in allele CYP3A4*13; lack of expression. dbSNP rs4986909. Ref.18

VAR_011608

Natural variant

431

1

I → T: dbSNP rs1041988. Ref.3 Ref.5

VAR_037550

Natural variant

445

1

M → T in allele CYP3A4*3. dbSNP rs4986910. Ref.17 Ref.16

VAR_008364

Natural variant

467

1

P → S in allele CYP3A4*19. dbSNP rs4986913. Ref.17

VAR_014324

Experimental info

Sequence conflict

3

1

L → V in AAA35747. Ref.5

Sequence conflict

12

1

W → R in AAF13598. Ref.9

Sequence conflict

72

1

W → C in AAA35747. Ref.5

Sequence conflict

92

1

T → L in BAA00001. Ref.1

Sequence conflict

92

1

T → L in AAA35742. Ref.1

Sequence conflict

106

1

R → E in BAA00001. Ref.1

Sequence conflict

106

1

R → E in AAA35742. Ref.1

Sequence conflict

164

1

A → R in BAA00001. Ref.1

Sequence conflict

164

1

A → R in AAA35742. Ref.1

Sequence conflict

187

1

T → S in BAA00001. Ref.1

Sequence conflict

187

1

T → S in AAA35742. Ref.1

Sequence conflict

193

1

I → V in BAA00001. Ref.1

Sequence conflict

193

1

I → V in AAA35742. Ref.1

Sequence conflict

203

1

F → L in BAA00001. Ref.1

Sequence conflict

203

1

F → L in AAA35742. Ref.1

Sequence conflict

224 – 225

2

TV → I in AAA35747. Ref.5

Sequence conflict

279

1

Q → HK in BAA00001. Ref.1

Sequence conflict

279

1

Q → HK in AAA35742. Ref.1

Sequence conflict

307

1

Y → C in AAF13598. Ref.9

Sequence conflict

392

1

V → W in BAA00001. Ref.1

Sequence conflict

392

1

V → W in AAA35742. Ref.1

Sequence conflict

392

1

V → W in AAA35744. Ref.3

Sequence conflict

392

1

V → W in CAA30944. Ref.4

Sequence conflict

392

1

V → W in AAA35747. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

503

Helix Strand Turn

Details...

Helix

32 – 35

4

Turn

45 – 47

3

Helix

50 – 55

6

Helix

57 – 68

12

Beta strand

70 – 76

7

Beta strand

79 – 84

6

Helix

87 – 94

8

Turn

95 – 101

7

Helix

112 – 116

5

Turn

118 – 120

3

Helix

123 – 132

10

Helix

135 – 137

3

Helix

139 – 143

5

Helix

146 – 166

21

Helix

172 – 186

15

Helix

195 – 197

3

Helix

202 – 207

6

Helix

218 – 225

8

Helix

227 – 229

3

Helix

230 – 235

6

Helix

243 – 257

15

Turn

258 – 263

6

Helix

271 – 279

9

Helix

292 – 323

32

Helix

325 – 338

14

Turn

340 – 342

3

Helix

347 – 352

6

Helix

354 – 366

13

Beta strand

373 – 376

4

Beta strand

381 – 383

3

Beta strand

386 – 388

3

Beta strand

393 – 396

4

Helix

398 – 402

5

Turn

405 – 407

3

Beta strand

408 – 410

3

Helix

416 – 419

4

Turn

421 – 423

3

Helix

424 – 426

3

Turn

429 – 431

3

Helix

445 – 460

16

Beta strand

463 – 466

4

Beta strand

479 – 482

4

Beta strand

485 – 487

3

Beta strand

490 – 495

6

Sequences

	Sequence		Length	Mass (Da)
	P08684-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 38ED122BF89F74F7	FASTA	503	57,343
	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

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

Cytochrome P450 Allele Nomenclature Committee

CYP3A4 alleles

Wikipedia

CYP3A4 entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00465138.

PIR

A29410.
A29815.

RefSeq

NP_059488.2.

UniGene

Hs.654391

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TQN	X-ray	2.05	A	24-503	[»]
1W0E	X-ray	2.80	A	25-503	[»]
1W0F	X-ray	2.65	A	25-503	[»]
1W0G	X-ray	2.73	A	25-503	[»]
2J0D	X-ray	2.75	A/B	25-502	[»]
2V0M	X-ray	3.80	A/B/C/D	25-502	[»]

ModBase

Search...

PTM databases

PhosphoSite

P08684.

Proteomic databases

PRIDE

P08684.

Genome annotation databases

Ensembl

ENSG00000160868. Homo sapiens. [Contig view]

GeneID

1576.

KEGG

hsa:1576.

Organism-specific databases

GeneCards

GC07M099192.

H-InvDB

HIX0078878.

HGNC

HGNC:2637. CYP3A4.

MIM

124010. gene.

PharmGKB

PA130.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P08684.

OMA

P08684. PDLAMET.

Enzyme and pathway databases

BRENDA

1.14.13.67. 247.
1.14.13.97. 247.

Reactome

REACT_13433. Biological oxidations.
REACT_649. Phase 1 functionalization.

Gene expression databases

ArrayExpress

P08684.

Bgee

P08684.

CleanEx

HS_CYP3A4.

GermOnline

ENSG00000160868. Homo sapiens.

Family and domain databases

InterPro

IPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR008072. Cyt_P450_E_CYP3A.
IPR002402. Cyt_P450_E_grp-II.
[Graphical view]

Gene3D

G3DSA:1.10.630.10. Cyt_P450. 1 hit.

PANTHER

PTHR19383. Cyt_P450. 1 hit.

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00464. EP450II.
PR01689. EP450IICYP3A.
PR00385. P450.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00518. 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.

NextBio

6475.

SOURCE

Search...

Entry information

Entry name

CP3A4_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)