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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:40
Primary Accession Number DB01167
Secondary Accession Number
  • APRD00040
Name Itraconazole
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description One of the triazole antifungal agents that inhibits cytochrome P-450-dependent enzymes resulting in impairment of ergosterol synthesis. It has been used against histoplasmosis, blastomycosis, cryptococcal meningitis & aspergillosis. [PubChem]
Synonyms
  1. ITC
  2. ITCZ
  3. ITR
  4. ITZ
  5. Itraconazol [Spanish]
  6. Itraconazolum [Latin]
  7. itraconazole
Brand Names
  1. Hyphanox
  2. Itrizole
  3. Oriconazole
  4. Sporal
  5. Sporanos
  6. Sporanox
  7. Sporonox
  8. Triasporn
Brand Mixtures Not Available
Chemical IUPAC Name 2-butan-2-yl-4-[4-[4-[4-[[(2R,4S)-2-(2,4-dichlorophenyl)-2-(1,2,4-triazol-1-ylmethyl)-1,3-dioxolan-4-yl]methoxy]phenyl]piperazin-1-yl]phenyl]-1,2,4-triazol-3-one
Chemical Formula C35H38Cl2N8O4
Chemical Structure Structure
CAS Registry Number 84625-61-6
InChI Identifier InChI=1/C35H38Cl2N8O4/c1-3-25(2)45-34(46)44(24-40-45)29-7-5-27(6-8-29)41-14-16-42(17-15-41)28-9-11-30(12-10-28)47-19-31-20-48-35(49-31,21-43-23-38-22-39-43)32-13-4-26(36)18-33(32)37/h4-13,18,22-25,31H,3,14-17,19-21H2,1-2H3/t25?,31-,35-/m0/s1
InChI Key VHVPQPYKVGDNFY-ZPGVKDDIBW
KEGG Drug D00350 Link Image
KEGG Compound Not Available
PubChem Compound 55283 Link Image
PubChem Substance 192757 Link Image
ChEBI ID Not Available
PharmGKB ID PA450132 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02231347 Link Image
RxList Link http://www.rxlist.com/cgi/generic/itraconazole.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/spo1411.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Itraconazole Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 705.6330
Monoisotopic Molecular Weight 704.2393
State Solid
Melting Point 166.2 oC
Experimental Water Solubility Insoluble Source: PhysProp
Predicted Water Solubility 9.64e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 6.5 Source: PhysProp
Predicted LogP 5.48 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.86 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 3.70
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1TQN Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CC[C@@H](C)N1N=CN(C1=O)C1=CC=C(C=C1)N1CCN(CC1)C1=CC=C(OC[C@H]2CO[C@@](CN3C=NC=N3)(O2)C2=C(Cl)C=C(Cl)C=C2)C=C1
Canonical SMILES CCC(C)N1N=CN(C1=O)C1=CC=C(C=C1)N1CCN(CC1)C1=CC=C(OCC2COC(CN3C=NC=N3)(O2)C2=C(Cl)C=C(Cl)C=C2)C=C1
Drug Category
  • Antifungal Agents
  • Antifungals
  • Antiprotozoal Agents
  • Antiprotozoals
ATC Codes
AHFS Codes
  • 08:14.08
Indication For the treatment of the following fungal infections in immunocompromised and non-immunocompromised patients: pulmonary and extrapulmonary blastomycosis, histoplasmosis, aspergillosis, and onychomycosis.
Pharmacology Itraconazole is an imidazole/triazole type antifungal agent. Itraconazole is a highly selective inhibitor of fungal cytochrome P-450 sterol C-14 α-demethylation via the inhibition of the enzyme cytochrome P450 14α-demethylase. This enzyme converts lanosterol to ergosterol, and is required in fungal cell wall synthesis. The subsequent loss of normal sterols correlates with the accumulation of 14 α-methyl sterols in fungi and may be partly responsible for the fungistatic activity of fluconazole. Mammalian cell demethylation is much less sensitive to fluconazole inhibition. Itraconazole exhibits in vitro activity against Cryptococcus neoformans and Candida spp. Fungistatic activity has also been demonstrated in normal and immunocompromised animal models for systemic and intracranial fungal infections due to Cryptococcus neoformans and for systemic infections due to Candida albicans.
Mechanism of Action Itraconazole interacts with 14-α demethylase, a cytochrome P-450 enzyme necessary to convert lanosterol to ergosterol. As ergosterol is an essential component of the fungal cell membrane, inhibition of its synthesis results in increased cellular permeability causing leakage of cellular contents. Itraconazole may also inhibit endogenous respiration, interact with membrane phospholipids, inhibit the transformation of yeasts to mycelial forms, inhibit purine uptake, and impair triglyceride and/or phospholipid biosynthesis.
Absorption The absolute oral bioavailability of itraconazole is 55%, and is maximal when taken with a full meal.
Toxicity No significant lethality was observed when itraconazole was administered orally to mice and rats at dosage levels of 320 mg/kg or to dogs at 200 mg/kg.
Protein Binding 99.8%
Biotransformation Itraconazole is extensively metabolized by the liver into a large number of metabolites, including hydroxyitraconazole, the major metabolite. The main metabolic pathways are oxidative scission of the dioxolane ring, aliphatic oxidation at the 1-methylpropyl substituent, N-dealkylation of this 1-methylpropyl substituent, oxidative degradation of the piperazine ring and triazolone scission.
Half Life 21 hours
Dosage Forms
Form Route
Capsule Oral
Liquid Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The imidazole increases the effect of the anticoagulant
Alfentanil The imidazole increases the effect and toxicity of alfentanil
Alfuzosin The antifungal increases the effect of alfuzosin
Almotriptan This potent CYP3A4 inhibitor increases the effect and toxicity of the triptan
Alprazolam The imidazole increases the effect of the benzodiazepine
Aluminium The antacid decreases the effect of the imidazole
Anisindione The imidazole increases the effect of the anticoagulant
Aprepitant This potent CYP3A4 inhibitor increases the effect and toxicity of the triptan
Aripiprazole The imidazole increases the effect of aripiprazole
Astemizole Increased risk of cardiotoxicity and arrhythmias
Atorvastatin Increased risk of myopathy/rhabdomyolysis
Bismuth The antacid decreases the effect of the imidazole
Bosentan The imidazole increases the effect and toxicity of bosentan
Budesonide The imidazole increases levels/effect of budesonide
Buspirone The macrolide increases the effect and toxicity of buspirone
Calcium The antacid decreases the effect of the imidazole
Carbamazepine The imidazole increases the effect of carbamazepine
Celiprolol Itaconazole increases levels/effect of celiprolol
Cerivastatin Increased risk of myopathy/rhabdomyolysis
Chlordiazepoxide The imidazole increases the effect of the benzodiazepine
Ciclesonide Increased effects/toxicity of ciclesonide
Cilostazol The imidazole increases the effect of cilostazol
Cimetidine The anti-H2 decreases the absorption of the imidazole
Cinacalcet The imidazole increases the effect and toxicity of cinacalcet
Cisapride Increased risk of cardiotoxicity and arrhythmias
Clarithromycin The macrolide increases the effect and toxicity of itraconazole
Clonazepam The imidazole increases the effect of the benzodiazepine
Clorazepate The imidazole increases the effect of the benzodiazepine
Cyclosporine The imidazole increases the effect of the immunosuppressant
Darifenacin This potent CYP3A4 inhibitor slows darifenacin/solifenacin metabolism
Diazepam The imidazole increases the effect of the benzodiazepine
Dicumarol The imidazole increases the effect of the anticoagulant
Digoxin Itraconazole increases the effect of digoxin
Dihydroergotamine Possible ergotism and severe ischemia with this combination
Dofetilide This strong CYP3A4 inhibitor increases the effect and toxicity of dofetilide
Eletriptan This potent CYP3A4 inhibitor increases the effect and toxicity of the triptan
Eplerenone The imidazole increases the effect and toxicity of eplerenone
Ergotamine Possible ergotism and severe ischemia with this combination
Erlotinib This potent CYP3A4 inhibitor increases levels/toxicity of erlotinib
Erythromycin The macrolide increases the effect and toxicity of itraconazole
Esomeprazole The proton pump inhibitor decreases the absorption of imidazole
Estazolam The imidazole increases the effect of the benzodiazepine
Ethinyl Estradiol This anti-infectious agent could decreases the effect of the oral contraceptive
Ethotoin Phenytoin decreases the effect of itraconazole
Everolimus The imidazole increases everolimus levels/toxicity
Famotidine The anti-H2 decreases the absorption of the imidazole
Felodipine Increases effect/toxicity of felodipine
Fentanyl The imidazole increases levels/toxicity of fentanyl
Flurazepam The imidazole increases the effect of the benzodiazepine
Fosphenytoin Phenytoin decreases the effect of itraconazole
Gefitinib This potent CYP3A4 inhibitor increases levels/toxicity of gefitinib
Halazepam The imidazole increases the effect of the benzodiazepine
Haloperidol The imidazole increases the effect and toxicity of haloperidol
Imatinib The imidazole increases the levels of imatinib
Josamycin The macrolide increases the effect and toxicity of itraconazole
Lansoprazole The proton pump inhibitor decreases the absorption of imidazole
Levomethadyl Acetate Itraconazole increases the effect/toxicity of levomethadyl
Lovastatin Increased risk of myopathy/rhabdomyolysis
Magnesium The antacid decreases the effect of the imidazole
Magnesium oxide The antacid decreases the effect of the imidazole
Mephenytoin Phenytoin decreases the effect of itraconazole
Mestranol This anti-infectious agent could decrease the effect of the oral contraceptive
Methylprednisolone The imidazole increases the effect and toxicity of the corticosteroid
Midazolam The imidazole increases the effect of the benzodiazepine
Nizatidine The anti-H2 decreases the absorption of the imidazole
Omeprazole The proton pump inhibitor decreases the absorption of imidazole
Pantoprazole The proton pump inhibitor decreases the absorption of imidazole
Phenobarbital The barbiturate decreases the effect of itraconazole
Phenytoin Phenytoin decreases the effect of itraconazole
Pimozide Increased risk of cardiotoxicity and arrhythmias
Prednisolone The imidazole increases the effect and toxicity of the corticosteroid
Prednisone The imidazole increases the effect and toxicity of the corticosteroid
Quazepam The imidazole increases the effect of the benzodiazepine
Quinidine The imidazole increases the effect and toxicity of quinidine
Quinidine barbiturate The imidazole increases the effect and toxicity of quinidine
Rabeprazole The proton pump inhibitor decreases the absorption of imidazole
Ranitidine The anti-H2 decreases the absorption of the imidazole
Ranolazine Increased levels of ranolazine - risk of toxicity
Rifabutin Rifabutin decreases the effect of itraconazole
Rifampin Rifampin decreases the effect of the imidazole
Risperidone Increases the level of risperidone
Ritonavir The imidazole increases the effect and toxicity of ritonavir
Sildenafil The imidazole increases the effect and toxicity of sildenafil
Simvastatin Increased risk of myopathy/rhabdomyolysis
Simvastatin Increased risk of myopathy/rhabdomyolysis
Sirolimus The imidazole increases the effect and toxicity of sirolimus
Solifenacin This potent CYP3A4 inhibitor slows darifenacin/solifenacin metabolism
Sucralfate Sucralfate decreases the absorption of the imidazole
Sunitinib Possible increase in sunitinib levels
Tacrolimus The imidazole increases the effect of immunosuppressant
Terfenadine Increased risk of cardiotoxicity and arrhythmias
Tolterodine The imidazole increases the effect and toxicity of tolterodine
Trazodone This potent CYP3A4 inhibitor increases the effect and toxicity of trazodone
Triazolam The imidazole increases the effect of the benzodiazepine
Vardenafil The imidazole increases the effect and toxicity of vardenafil
Vinblastine The imidazole increases the effect and toxicity of the antineoplasic
Vincristine The imidazole increases the effect and toxicity of the antineoplasic
Warfarin The imidazole increases the effect of the anticoagulant
Food Interactions
  • Avoid milk, calcium containing dairy products, iron, antacids, or aluminum salts 2 hours before or 6 hours after using antacids while on this medication.
  • Avoid taking with grapefruit juice.
  • Take after a full meal.
  • Take with food.
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
  4. PDRhealth Link Image
Organisms Affected
  • Fungi, yeast and protozoans
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A4 (CYP3A4)
  2. Cytochrome P450 2D6 (CYP2D6)
Targets
  1. Cytochrome P450 51
  2. Cytochrome P450 51A1
  3. Multidrug resistance protein 1
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 1 Gene Name CYP3A4
Enzyme 1 SwissProt ID P08684 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67) 
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Cytochrome P450 2D6 (CYP2D6)
Enzyme 2 Gene Name CYP2D6
Enzyme 2 SwissProt ID P10635 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P10635|CP2D6_HUMAN Cytochrome P450 2D6 (EC 1.14.14.1) 
MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQ
LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVF
LARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDK
AVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV
LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVA
DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI
HEVQRFGDIVPLGMTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF
LDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGV
FAFLVSPSPYELCAVPR
Drug Target 1 [top]
Target 1 ID 761
Target 1 Name Cytochrome P450 51
Target 1 Synonyms
  1. CYPLI
  2. EC 1.14.13.70
  3. Lanosterol 14-alpha demethylase
  4. P450-14DM
  5. P450-LIA1
  6. Sterol 14- alpha-demethylase
Target 1 Gene Name ERG11
Target 1 Protein Sequence >Cytochrome P450 51 
MSTENTSLVVELLEYVKLGLSYFQALPLAQRVSIMVALPFVYTITWQLLYSLRKDRPPLV
FYWIPWVGSAIPYGTKPYEFFEDCQKKYGDIFSFMLLGRIMTVYLGPKGHEFIFNAKLAD
VSAEAAYSHLTTPVFGKGVIYDCPNHRLMEQKKFVKGALTKEAFVRYVPLIAEEIYKYFR
NSKNFKINENNSGIVDVMVSQPEMTIFTASRSLLGKEMRDKLDTDFAYLYSDLDKGFTPI
NFVFPNLPLEHYRKRDHAQQAISGTYMSLIKERREKNDIQNRDLIDELMKNSTYKDGTKM
TDQEIANLLIGVLMGGQHTSAATSAWCLLHLAERPDVQEELYQEQMRVLNNDTKELTYDD
LQNMPLLNQMIKETLRLHHPLHSLFRKVMRDVAIPNTSYVVPRDYHVLVSPGYTHLQEEF
FPKPNEFNIHRWDGDAASSSAAGGDEVDYGFGAISKGVSSPYLPFGGGRHRCIGELFAYC
QLGVLMSIFIRTMKWRYPTEGETVPPSDFTSMVTLPTAPAKIYWEKRHPEQKY
Target 1 Number of Residues 541
Target 1 Molecular Weight 61306
Target 1 Theoretical pI 7.07
Target 1 GO Classification
Function
tetrapyrrole binding
heme binding
binding
ion binding
cation binding
transition metal ion binding
iron ion binding
catalytic activity
oxidoreductase activity
monooxygenase activity
Process
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 1 General Function Secondary metabolites biosynthesis, transport and catabolism
Target 1 Specific Function Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
Target 1 Pathways Not Available
Target 1 Reactions
  • obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 3 NADP+ + 4 H2O
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 755693 Link Image
Target 1 UniProtKB/Swiss-Prot ID P50859 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name CP51_CANGA Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >1602 bp 
ATGTCCACTGAAAACACTTCTTTGGTCGTTGAACTATTGGAGTACGTGAAGCTTGGTCTT
TCGTACTTCCAAGCTCTGCCATTGGCGCAGAGAGTGTCTATTATGGTCGCCTTGCCATTT
GTGTACACCATCACATGGCAATTGCTTTACTCCTTGAGAAAGGACAGACCACCACTTGTG
TTCTACTGGATCCCATGGGTCGGCTCTGCTATCCCATACGGTACCAAGCCATACGAGTTC
TTCGAAGACTGCCAAAAGAAATACGGTGATATCTTCTCTTTCATGCTATTGGGTAGAATT
ATGACTGTCTACTTGGGTCCAAAGGGTCACGAATTCATCTTCAACGCCAAGTTGGCCGAT
GTTTCCGCTGAAGCTGCTTACTCCCACTTGACCACCCCAGTGTTCGGTAAAGGTGTTATC
TACGATTGTCCAAACCACAGACTAATGGAACAAAAGAAGTTTGTCAAGGGTGCTTTGACT
AAGGAAGCCTTTGTCAGATACGTTCCATTGATCGCTGAGGAAATCTACAAGTACTTCAGA
AACTCCAAGAACTTCAAGATCAACGAAAACAACTCCGGTATCGTCGACGTTATGGTCTCC
CAACCTGAAATGACTATCTTCACTGCTTCCAGATCCTTGCTAGGTAAGGAAATGAGAGAC
AAGTTGGACACCGACTTCGCTTACTTGTACAGTGACTTGGACAAGGGTTTCACCCCAATT
AACTTCGTCTTCCCTAACTTGCCTCTAGAACACTACAGAAAGAGAGATCATGCCCAACAA
GCTATCTCTGGTACTTACATGTCCTTGATTAAGGAAAGACGTGAGAAGAACGATATCCAA
AACCGTGACTTGATTGATGAATTGATGAAGAACTCCACTTACAAGGATGGTACTAAGATG
ACCGACCAAGAAATTGCCAACCTATTGATTGGTGTCTTGATGGGTGGTCAACATACTTCC
GCTGCTACCTCCGCTTGGTGTCTATTGCATTTGGCTGAAAGACCAGATGTCCAAGAAGAA
TTATACCAAGAACAAATGCGCGTCTTGAACAACGATACCAAGGAATTGACTTACGATGAC
CTACAAAACATGCCTCTATTGAACCAAATGATCAAGGAAACTTTGAGATTGCACCACCCA
TTGCACTCTTTGTTCCGTAAAGTCATGAGAGATGTCGCTATTCCAAACACTTCCTACGTT
GTCCCAAGGGACTACCACGTTCTAGTCTCCCCAGGTTACACTCACTTGCAAGAAGAATTC
TTCCCTAAGCCAAATGAATTCAACATCCACCGTTGGGACGGTGATGCTGCTTCTTCCAGT
GCTGCTGGTGGTGACGAAGTTGATTACGGTTTCGGTGCTATCTCCAAGGGTGTTTCCTCT
CCATACTTGCCATTCGGTGGTGGTAGACACAGATGTATCGGTGAATTGTTCGCTTACTGT
CAATTGGGTGTGTTGATGTCCATTTTCATCAGAACCATGAAATGGCGTTACCCAACTGAA
GGTGAAACTGTCCCACCATCTGACTTCACCTCCATGGTCACCCTACCAACTGCCCCTGCT
AAGATCTACTGGGAAAAGAGACATCCAGAACAAAAGTACTAG
Target 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location Not Available
Target 1 Locus Not Available
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Burgener-Kairuz P, Zuber JP, Jaunin P, Buchman TG, Bille J, Rossier M: Rapid detection and identification of Candida albicans and Torulopsis (Candida) glabrata in clinical specimens by species-specific nested PCR amplification of a cytochrome P-450 lanosterol-alpha-demethylase (L1A1) gene fragment. J Clin Microbiol. 1994 Aug;32(8):1902-7. [PubMed Link Image]
  2. Geber A, Hitchcock CA, Swartz JE, Pullen FS, Marsden KE, Kwon-Chung KJ, Bennett JE: Deletion of the Candida glabrata ERG3 and ERG11 genes: effect on cell viability, cell growth, sterol composition, and antifungal susceptibility. Antimicrob Agents Chemother. 1995 Dec;39(12):2708-17. [PubMed Link Image]
Target 1 Drug References
  1. Henry KW, Nickels JT, Edlind TD: Upregulation of ERG genes in Candida species by azoles and other sterol biosynthesis inhibitors. Antimicrob Agents Chemother. 2000 Oct;44(10):2693-700. [PubMed Link Image]
  2. Morales IJ, Vohra PK, Puri V, Kottom TJ, Limper AH, Thomas CF Jr: Characterization of a lanosterol 14 alpha-demethylase from Pneumocystis carinii. Am J Respir Cell Mol Biol. 2003 Aug;29(2):232-8. Epub 2003 Feb 26. [PubMed Link Image]
  3. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  4. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  5. Gachotte D, Pierson CA, Lees ND, Barbuch R, Koegel C, Bard M: A yeast sterol auxotroph (erg25) is rescued by addition of azole antifungals and reduced levels of heme. Proc Natl Acad Sci U S A. 1997 Oct 14;94(21):11173-8. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 1010
Target 2 Name Cytochrome P450 51A1
Target 2 Synonyms
  1. CYPLI
  2. EC 1.14.13.70
  3. LDM
  4. Lanosterol 14-alpha demethylase
  5. P450-14DM
  6. P45014DM
  7. P450LI
  8. Sterol 14-alpha demethylase
Target 2 Gene Name CYP51A1
Target 2 Protein Sequence >Cytochrome P450 51A1 
MLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQLPAGVKS
PPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNS
KNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETK
EYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWL
LPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDE
VAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDL
NLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLD
FNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFP
TVNYTTMIHTPENPVIRYKRRSK
Target 2 Number of Residues 511
Target 2 Molecular Weight 56807
Target 2 Theoretical pI 8.72
Target 2 GO Classification
Function
tetrapyrrole binding
heme binding
binding
ion binding
cation binding
transition metal ion binding
iron ion binding
catalytic activity
oxidoreductase activity
monooxygenase activity
Process
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 2 General Function Secondary metabolites biosynthesis, transport and catabolism
Target 2 Specific Function Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
Target 2 Pathways Not Available
Target 2 Reactions
  • obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 3 NADP+ + 4 H2O
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 24-44
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 1698396 Link Image
Target 2 UniProtKB/Swiss-Prot ID Q16850 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CP51A_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Microsome (Potential)
Target 2 Gene Sequence >1530 bp 
ATGGCGGCGGCGGCTGGGATGCTGCTGCTGGGCTTGCTGCAGGCGGGTGGGTCGGTGCTG
GGCCAGGCGATGGAGAAGGTGACAGGCGGCAACCTCTTGTCCATGCTGCTGATCGCCTGC
GCCTTCACCCTCAGCCTGGTCTACCTGATCCGTCTGGCCGCCGGCCACCTGGTCCAGCTG
CCCGCAGGGGTGAAAAGTCCTCCATACATTTTCTCCCCAATTCCATTCCTTGGGCATGCC
ATAGCATTTGGGAAAAGTCCAATTGAATTTCTAGAAAATGCATATGAGAAGTATGGACCT
GTATTTAGTTTTACCATGGTAGGCAAGACATTTACTTACCTTCTGGGGAGTGATGCTGCT
GCACTGCTTTTTAATAGTAAAAATGAAGACCTGAATGCAGAAGATGTCTACAGTCGCCTG
ACAACACCTGTGTTTGGGAAGGGAGTTGCATACGATGTGCCTAATCCAGTTTTCTTGGAG
CAGAAGAAAATGTTAAAAAGTGGCCTTAACATAGCCCACTTTAAACAGCATGTTTCTATA
ATTGAAAAAGAAACAAAGGAATACTTTGAGAGTTGGGGAGAAAGTGGAGAAAAAAATGTG
TTTGAAGCTCTTTCTGAGCTCATAATTTTAACAGCTAGCCATTGTTTGCATGGAAAGGAA
ATCAGAAGTCAACTCAATGAAAAGGTAGCACAGCTGTATGCAGATTTGGATGGAGGTTTC
AGCCATGCAGCCTGGCTCTTACCAGGTTGGCTGCCTTTGCCTAGTTTCAGACGCAGGGAC
AGAGCTCATCGGGAAATCAAGGATATTTTCTATAAGGCAATCCAGAAACGCAGACAGTCT
CAAGAAAAAATTGATGACATTCTCCAAACTTTACTAGATGCTACATACAAGGATGGGCGT
CCTTTGACTGATGATGAAGTAGCAGGGATGCTTATTGGATTACTCTTGGCAGGGCAGCAT
ACATCCTCAACTACTAGTGCTTGGATGGGCTTCTTTTTGGCCAGAGACAAAACACTTCAA
AAAAAATGTTATTTAGAACAGAAAACAGTCTGTGGAGAGAATCTGCCTCCTTTAACTTAT
GACCAGCTCAAGGATCTAAATTTACTTGATCGCTGTATAAAAGAAACATTAAGACTTAGA
CCTCCTATAATGATCATGATGAGAATGGCCAGAACTCCTCAGACTGTGGCAGGGTATACC
ATTCCTCCAGGACATCAGGTGTGTGTTTCTCCCACTGTCAATCAAAGACTTAAAGACTCA
TGGGTAGAACGCCTGGACTTTAATCCTGATCGCTACTTACAGGATAACCCAGCATCAGGG
GAAAAGTTTGCCTATGTGCCATTTGGAGCTGGGCGTCATCGTTGTATTGGGGAAAATTTT
GCCTATGTTCAAATTAAGACAATTTGGTCCACTATGCTTCGTTTATATGAATTTGATCTC
ATTGATGGATACTTTCCCACTGTGAATTATACAACTATGATTCACACCCCTGAGAACCCA
GTTATCCGTTACAAACGAAGATCAAAATGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID CYP51A1 Link Image
Target 2 GenAtlas ID CYP51A1 Link Image
Target 2 HGNC ID HGNC:2649 Link Image
Target 2 Chromosome Location 7
Target 2 Locus 7q21.2-q21.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. Stromstedt M, Rozman D, Waterman MR: The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. Arch Biochem Biophys. 1996 May 1;329(1):73-81. [PubMed Link Image]
  3. Rozman D, Stromstedt M, Waterman MR: The three human cytochrome P450 lanosterol 14 alpha-demethylase (CYP51) genes reside on chromosomes 3, 7, and 13: structure of the two retrotransposed pseudogenes, association with a line-1 element, and evolution of the human CYP51 family. Arch Biochem Biophys. 1996 Sep 15;333(2):466-74. [PubMed Link Image]
  4. Rozman D, Stromstedt M, Tsui LC, Scherer SW, Waterman MR: Structure and mapping of the human lanosterol 14alpha-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes. Genomics. 1996 Dec 15;38(3):371-81. [PubMed Link Image]
Target 2 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 1588
Target 3 Name Multidrug resistance protein 1
Target 3 Synonyms
  1. ATP-binding cassette sub-family B member 1
  2. CD243 antigen
  3. EC 3.6.3.44
  4. P-glycoprotein 1
Target 3 Gene Name ABCB1
Target 3 Protein Sequence >Multidrug resistance protein 1 
MDLEGDRNGGAKKKNFFKLNNKSEKDKKEKKPTVSVFSMFRYSNWLDKLYMVVGTLAAII
HGAGLPLMMLVFGEMTDIFANAGNLEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSG
IGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVS
KINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFT
DKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIG
AAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARG
AAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSG
QTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLF
ATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIA
IARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAG
FDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAADESKSEIDALEMSSNDSRS
SLIRKRSTRRSVRGSQAQDRKLSTKEALDESIPPVSFWRIMKLNLTEWPYFVVGVFCAII
NGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKA
GEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNI
ANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEA
IENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFG
AYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDS
YSTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVV
QLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVV
SQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLD
EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL
LAQKGIYFSMVSVQAGTKRQ
Target 3 Number of Residues 1301
Target 3 Molecular Weight 141464
Target 3 Theoretical pI 9.44
Target 3 GO Classification
Function
ATPase activity
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
ATPase activity, coupled to transmembrane movement of substances
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
nucleoside-triphosphatase activity
binding
nucleotide binding
Process
physiological process
cellular physiological process
transport
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 3 General Function Defense mechanisms and drug export
Target 3 Specific Function Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells
Target 3 Pathways Not Available
Target 3 Reactions
  • ATP + H2O + xenobioticin = ADP + phosphate + xenobioticout
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • 52-72
  • 120-140
  • 189-209
  • 216-236
  • 297-317
  • 326-346
  • 711-731
  • 757-777
  • 833-853
  • 854-874
  • 937-957
  • 974-994
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 307180 Link Image
Target 3 UniProtKB/Swiss-Prot ID P08183 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name MDR1_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 3 Gene Sequence >3843 bp 
ATGGATCTTGAAGGGGACCGCAATGGAGGAGCAAAGAAGAAGAACTTTTTTAAACTGAAC
AATAAAAGTGAAAAAGATAAGAAGGAAAAGAAACCAACTGTCAGTGTATTTTCAATGTTT
CGCTATTCAAATTGGCTTGACAAGTTGTATATGGTGGTGGGAACTTTGGCTGCCATCATC
CATGGGGCTGGACTTCCTCTCATGATGCTGGTGTTTGGAGAAATGACAGATATCTTTGCA
AATGCAGGAAATTTAGAAGATCTGATGTCAAACATCACTAATAGAAGTGATATCAATGAT
ACAGGGTTCTTCATGAATCTGGAGGAAGACATGACCAGGTATGCCTATTATTACAGTGGA
ATTGGTGCTGGGGTGCTGGTTGCTGCTTACATTCAGGTTTCATTTTGGTGCCTGGCAGCT
GGAAGACAAATACACAAAATTAGAAAACAGTTTTTTCATGCTATAATGCGACAGGAGATA
GGCTGGTTTGATGTGCACGATGTTGGGGAGCTTAACACCCGACTTACAGATGATGTCTCT
AAGATTAATGAAGTTATTGGTGACAAAATTGGAATGTTCTTTCAGTCAATGGCAACATTT
TTCACTGGGTTTATAGTAGGATTTACACGTGGTTGGAAGCTAACCCTTGTGATTTTGGCC
ATCAGTCCTGTTCTTGGACTGTCAGCTGCTGTCTGGGCAAAGATACTATCTTCATTTACT
GATAAAGAACTCTTAGCGTATGCAAAAGCTGGAGCAGTAGCTGAAGAGGTCTTGGCAGCA
ATTAGAACTGTGATTGCATTTGGAGGACAAAAGAAAGAACTTGAAAGGTACAACAAAAAT
TTAGAAGAAGCTAAAAGAATTGGGATAAAGAAAGCTATTACAGCCAATATTTCTATAGGT
GCTGCTTTCCTGCTGATCTATGCATCTTATGCTCTGGCCTTCTGGTATGGGACCACCTTG
GTCCTCTCAGGGGAATATTCTATTGGACAAGTACTCACTGTATTCTTTTCTGTATTAATT
GGGGCTTTTAGTGTTGGACAGGCATCTCCAAGCATTGAAGCATTTGCAAATGCAAGAGGA
GCAGCTTATGAAATCTTCAAGATAATTGATAATAAGCCAAGTATTGACAGCTATTCGAAG
AGTGGGCACAAACCAGATAATATTAAGGGAAATTTGGAATTCAGAAATGTTCACTTCAGT
TACCCATCTCGAAAAGAAGTTAAGATCTTGAAGGGCCTGAACCTGAAGGTGCAGAGTGGG
CAGACGGTGGCCCTGGTTGGAAACAGTGGCTGTGGGAAGAGCACAACAGTCCAGCTGATG
CAGAGGCTCTATGACCCCACAGAGGGGATGGTCAGTGTTGATGGACAGGATATTAGGACC
ATAAATGTAAGGTTTCTACGGGAAATCATTGGTGTGGTGAGTCAGGAACCTGTATTGTTT
GCCACCACGATAGCTGAAAACATTCGCTATGGCCGTGAAAATGTCACCATGGATGAGATT
GAGAAAGCTGTCAAGGAAGCCAATGCCTATGACTTTATCATGAAACTGCCTCATAAATTT
GACACCCTGGTTGGAGAGAGAGGGGCCCAGTTGAGTGGTGGGCAGAAGCAGAGGATCGCC
ATTGCACGTGCCCTGGTTCGCAACCCCAAGATCCTCCTGCTGGATGAGGCCACGTCAGCC
TTGGACACAGAAAGCGAAGCAGTGGTTCAGGTGGCTCTGGATAAGGCCAGAAAAGGTCGG
ACCACCATTGTGATAGCTCATCGTTTGTCTACAGTTCGTAATGCTGACGTCATCGCTGGT
TTCGATGATGGAGTCATTGTGGAGAAAGGAAATCATGATGAACTCATGAAAGAGAAAGGC
ATTTACTTCAAACTTGTCACAATGCAGACAGCAGGAAATGAAGTTGAATTAGAAAATGCA
GCTGATGAATCCAAAAGTGAAATTGATGCCTTGGAAATGTCTTCAAATGATTCAAGATCC
AGTCTAATAAGAAAAAGATCAACTCGTAGGAGTGTCCGTGGATCACAAGCCCAAGACAGA
AAGCTTAGTACCAAAGAGGCTCTGGATGAAAGTATACCTCCAGTTTCCTTTTGGAGGATT
ATGAAGCTAAATTTAACTGAATGGCCTTATTTTGTTGTTGGTGTATTTTGTGCCATTATA
AATGGAGGCCTGCAACCAGCATTTGCAATAATATTTTCAAAGATTATAGGGGTTTTTACA
AGAATTGATGATCCTGAAACAAAACGACAGAATAGTAACTTGTTTTCACTATTGTTTCTA
GCCCTTGGAATTATTTCTTTTATTACATTTTTCCTTCAGGGTTTCACATTTGGCAAAGCT
GGAGAGATCCTCACCAAGCGGCTCCGATACATGGTTTTCCGATCCATGCTCAGACAGGAT
GTGAGTTGGTTTGATGACCCTAAAAACACCACTGGAGCATTGACTACCAGGCTCGCCAAT
GATGCTGCTCAAGTTAAAGGGGCTATAGGTTCCAGGCTTGCTGTAATTACCCAGAATATA
GCAAATCTTGGGACAGGAATAATTATATCCTTCATCTATGGTTGGCAACTAACACTGTTA
CTCTTAGCAATTGTACCCATCATTGCAATAGCAGGAGTTGTTGAAATGAAAATGTTGTCT
GGACAAGCACTGAAAGATAAGAAAGAACTAGAAGGTGCTGGGAAGATCGCTACTGAAGCA
ATAGAAAACTTCCGAACCGTTGTTTCTTTGACTCAGGAGCAGAAGTTTGAACATATGTAT
GCTCAGAGTTTGCAGGTACCATACAGAAACTCTTTGAGGAAAGCACACATCTTTGGAATT
ACATTTTCCTTCACCCAGGCAATGATGTATTTTTCCTATGCTGGATGTTTCCGGTTTGGA
GCCTACTTGGTGGCACATAAACTCATGAGCTTTGAGGATGTTCTGTTAGTATTTTCAGCT
GTTGTCTTTGGTGCCATGGCCGTGGGGCAAGTCAGTTCATTTGCTCCTGACTATGCCAAA
GCCAAAATATCAGCAGCCCACATCATCATGATCATTGAAAAAACCCCTTTGATTGACAGC
TACAGCACGGAAGGCCTAATGCCGAACACATTGGAAGGAAATGTCACATTTGGTGAAGTT
GTATTCAACTATCCCACCCGACCGGACATCCCAGTGCTTCAGGGACTGAGCCTGGAGGTG
AAGAAGGGCCAGACGCTGGCTCTGGTGGGCAGCAGTGGCTGTGGGAAGAGCACAGTGGTC
CAGCTCCTGGAGCGGTTCTACGACCCCTTGGCAGGGAAAGTGCTGCTTGATGGCAAAGAA
ATAAAGCGACTGAATGTTCAGTGGCTCCGAGCACACCTGGGCATCGTGTCCCAGGAGCCC
ATCCTGTTTGACTGCAGCATTGCTGAGAACATTGCCTATGGAGACAACAGCCGGGTGGTG
TCACAGGAAGAGATCGTGAGGGCAGCAAAGGAGGCCAACATACATGCCTTCATCGAGTCA
CTGCCTAATAAATATAGCACTAAAGTAGGAGACAAAGGAACTCAGCTCTCTGGTGGCCAG
AAACAACGCATTGCCATAGCTCGTGCCCTTGTTAGACAGCCTCATATTTTGCTTTTGGAT
GAAGCCACGTCAGCTCTGGATACAGAAAGTGAAAAGGTTGTCCAAGAAGCCCTGGACAAA
GCCAGAGAAGGCCGCACCTGCATTGTGATTGCTCACCGCCTGTCCACCATCCAGAATGCA
GACTTAATAGTGGTGTTTCAGAATGGCAGAGTCAAGGAGCATGGCACGCATCAGCAGCTG
CTGGCACAGAAAGGCATCTATTTTTCAATGGTCAGTGTCCAGGCTGGAACAAAGCGCCAG
TGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID ABCB1 Link Image
Target 3 GenAtlas ID ABCB1 Link Image
Target 3 HGNC ID HGNC:40 Link Image
Target 3 Chromosome Location 7
Target 3 Locus 7q21.1
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Hoffmeyer S, Burk O, von Richter O, Arnold HP, Brockmoller J, Johne A, Cascorbi I, Gerloff T, Roots I, Eichelbaum M, Brinkmann U: Functional polymorphisms of the human multidrug-resistance gene: multiple sequence variations and correlation of one allele with P-glycoprotein expression and activity in vivo. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3473-8. [PubMed Link Image]
  2. Decleves X, Chevillard S, Charpentier C, Vielh P, Laplanche JL: A new polymorphism (N21D) in the exon 2 of the human MDR1 gene encoding the P-glycoprotein. Hum Mutat. 2000 May;15(5):486. [PubMed Link Image]
  3. Cascorbi I, Gerloff T, Johne A, Meisel C, Hoffmeyer S, Schwab M, Schaeffeler E, Eichelbaum M, Brinkmann U, Roots I: Frequency of single nucleotide polymorphisms in the P-glycoprotein drug transporter MDR1 gene in white subjects. Clin Pharmacol Ther. 2001 Mar;69(3):169-74. [PubMed Link Image]
  4. Kerb R, Hoffmeyer S, Brinkmann U: ABC drug transporters: hereditary polymorphisms and pharmacological impact in MDR1, MRP1 and MRP2. Pharmacogenomics. 2001 Feb;2(1):51-64. [PubMed Link Image]
  5. Saito S, Iida A, Sekine A, Miura Y, Ogawa C, Kawauchi S, Higuchi S, Nakamura Y: Three hundred twenty-six genetic variations in genes encoding nine members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese population. J Hum Genet. 2002;47(1):38-50. [PubMed Link Image]
  6. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  7. Chen CJ, Clark D, Ueda K, Pastan I, Gottesman MM, Roninson IB: Genomic organization of the human multidrug resistance (MDR1) gene and origin of P-glycoproteins. J Biol Chem. 1990 Jan 5;265(1):506-14. [PubMed Link Image]
  8. Gekeler V, Weger S, Probst H: mdr1/P-glycoprotein gene segments analyzed from various human leukemic cell lines exhibiting different multidrug resistance profiles. Biochem Biophys Res Commun. 1990 Jun 15;169(2):796-802. [PubMed Link Image]
  9. Kioka N, Tsubota J, Kakehi Y, Komano T, Gottesman MM, Pastan I, Ueda K: P-glycoprotein gene (MDR1) cDNA from human adrenal: normal P-glycoprotein carries Gly185 with an altered pattern of multidrug resistance. Biochem Biophys Res Commun. 1989 Jul 14;162(1):224-31. [PubMed Link Image]
  10. Chen CJ, Chin JE, Ueda K, Clark DP, Pastan I, Gottesman MM, Roninson IB: Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. Cell. 1986 Nov 7;47(3):381-9. [PubMed Link Image]
  11. 2897240 Choi KH, Chen CJ, Kriegler M, Roninson IB: An altered pattern of cross-resistance in multidrug-resistant human cells results from spontaneous mutations in the mdr1 (P-glycoprotein) gene. Cell. 1988 May 20;53(4):519-29.
  12. 9038218 Chen G, Duran GE, Steger KA, Lacayo NJ, Jaffrezou JP, Dumontet C, Sikic BI: Multidrug-resistant human sarcoma cells with a mutant P-glycoprotein, altered phenotype, and resistance to cyclosporins. J Biol Chem. 1997 Feb 28;272(9):5974-82.
  13. 9473242 Mickley LA, Lee JS, Weng Z, Zhan Z, Alvarez M, Wilson W, Bates SE, Fojo T: Genetic polymorphism in MDR-1: a tool for examining allelic expression in normal cells, unselected and drug-selected cell lines, and human tumors. Blood. 1998 Mar 1;91(5):1749-56.
Target 3 Drug References
  1. Masuda S, Inui K: [Molecular mechanisms on drug transporters in the drug absorption and disposition] Nippon Rinsho. 2002 Jan;60(1):65-73. [PubMed Link Image]
  2. Lilja JJ, Backman JT, Laitila J, Luurila H, Neuvonen PJ: Itraconazole increases but grapefruit juice greatly decreases plasma concentrations of celiprolol. Clin Pharmacol Ther. 2003 Mar;73(3):192-8. [PubMed Link Image]
  3. Sakaeda T, Iwaki K, Kakumoto M, Nishikawa M, Niwa T, Jin JS, Nakamura T, Nishiguchi K, Okamura N, Okumura K: Effect of micafungin on cytochrome P450 3A4 and multidrug resistance protein 1 activities, and its comparison with azole antifungal drugs. J Pharm Pharmacol. 2005 Jun;57(6):759-64. [PubMed Link Image]
  4. Saito M, Hirata-Koizumi M, Miyake S, Hasegawa R: Comparison of information on the pharmacokinetic interactions of Ca antagonists in the package inserts from three countries (Japan, USA and UK). Eur J Clin Pharmacol. 2005 Aug;61(7):531-6. Epub 2005 Jul 23. [PubMed Link Image]
  5. Shon JH, Yoon YR, Hong WS, Nguyen PM, Lee SS, Choi YG, Cha IJ, Shin JG: Effect of itraconazole on the pharmacokinetics and pharmacodynamics of fexofenadine in relation to the MDR1 genetic polymorphism. Clin Pharmacol Ther. 2005 Aug;78(2):191-201. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.