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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:48:13
Primary Accession Number DB01045
Secondary Accession Number
  • APRD00207
  • EXPT02777
Name Rifampin
Drug Type
  • Approved
  • Small Molecule
Description A semisynthetic antibiotic produced from Streptomyces mediterranei. It has a broad antibacterial spectrum, including activity against several forms of Mycobacterium. In susceptible organisms it inhibits DNA-dependent RNA polymerase activity by forming a stable complex with the enzyme. It thus suppresses the initiation of RNA synthesis. Rifampin is bactericidal, and acts on both intracellular and extracellular organisms. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p1160)
Synonyms
  1. RFP
Brand Names
  1. Archidyn
  2. L-5103 Lepetit
  3. R/AMP
  4. RAMP
  5. Rfamipicin
  6. Rifa
  7. Rifadin
  8. Rifadin IV
  9. Rifadine
  10. Rifagen
  11. Rifaldazin
  12. Rifaldazine
  13. Rifaldin
  14. Rifampicin
  15. Rifampicin SV
  16. Rifamycin
  17. Rifamycin Amp
  18. Rifaprodin
  19. Rifoldin
  20. Rifoldine
  21. Riforal
  22. Rimactan
  23. Rimactane
  24. Rimactin
  25. Rimazid
  26. Rofact
  27. Tubocin
Brand Mixtures
  1. Rifamate (Rifampin + Isoniazid)
  2. Rifater (Isoniazid + Pyrazinaamide + Rifampin)
Chemical IUPAC Name (7S,9E,11S,12S,13R,14S,15R,16S,17R,18S,26E)-2,15,17,29-tetrahydroxy-11-methoxy-3,7,12,14,16,18,22-heptamethyl-26-{[(4-methylpiperazin-1-yl)amino]methylidene}-6,23,27-trioxo-8,30-dioxa-24-azatetracyclo[23.3.1.1^{4,7}.0^{5,28}]triaconta-1(28),2,4,9,19,21,25(29)-heptaen-13-yl acetate
Chemical Formula C43H58N4O12
Chemical Structure Structure
CAS Registry Number 13292-46-1
InChI Identifier InChI=1/C43H58N4O12/c1-21-12-11-13-22(2)42(55)45-33-28(20-44-47-17-15-46(9)16-18-47)37(52)30-31(38(33)53)36(51)26(6)40-32(30)41(54)43(8,59-40)57-19-14-29(56-10)23(3)39(58-27(7)48)25(5)35(50)24(4)34(21)49/h11-14,19-21,23-25,29,34-35,39,44,49-51,53H,15-18H2,1-10H3,(H,45,55)/b12-11-,19-14+,22-13+,28-20+/t21-,23-,24-,25-,29-,34+,35+,39-,43-/m0/s1/f/h45H
InChI Key FZYOVNIOYYPUPY-DSWJFXGEDI
KEGG Drug D00211 Link Image
KEGG Compound C06688 Link Image
PubChem Compound 5381226 Link Image
PubChem Substance 168608 Link Image
ChEBI ID 28077 Link Image
PharmGKB ID PA451250 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00393444 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/rifampin.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Rifampin Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 822.9402
Monoisotopic Molecular Weight 822.4051
State Solid
Melting Point 183 oC
Experimental Water Solubility 1.4 mg/mL Source: PhysProp
Predicted Water Solubility 6.71e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.7 Source: PhysProp
Predicted LogP 2.36 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.09 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
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 1SKX Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CO[C@H]1\C=C\O[C@@]2(C)OC3=C(C2=O)C2=C(C(O)=C3C)C(O)=C(NC(=O)\C(C)=C\C=C\[C@H](C)[C@@H](O)[C@H](C)[C@@H](O)[C@H](C)[C@@H](OC(C)=O)[C@H]1C)/C(=C\NN1CCN(C)CC1)C2=O
Canonical SMILES COC1C=COC2(C)OC3=C(C2=O)C2=C(C(O)=C3C)C(O)=C(NC(=O)C(C)=CC=CC(C)C(O)C(C)C(O)C(C)C(OC(C)=O)C1C)C(=CNN1CCN(C)CC1)C2=O
Drug Category
  • Antibiotics
  • Antibiotics, Antitubercular
  • Antituberculosis Agents
  • Enzyme Inhibitors
  • Leprostatic Agents
  • Nucleic Acid Synthesis Inhibitors
ATC Codes
AHFS Codes
  • 08:16.04
Indication For the treatment of Tuberculosis and Tuberculosis-related mycobacterial infections.
Pharmacology Rifampin is an antibiotic that inhibits DNA-dependent RNA polymerase activity in susceptible cells. Specifically, it interacts with bacterial RNA polymerase but does not inhibit the mammalian enzyme. It is bactericidal and has a very broad spectrum of activity against most gram-positive and gram-negative organisms (including Pseudomonas aeruginosa) and specifically Mycobacterium tuberculosis. Because of rapid emergence of resistant bacteria, use is restricted to treatment of mycobacterial infections and a few other indications. Rifampin is well absorbed when taken orally and is distributed widely in body tissues and fluids, including the CSF. It is metabolized in the liver and eliminated in bile and, to a much lesser extent, in urine, but dose adjustments are unnecessary with renal insufficiency.
Mechanism of Action Rifampin acts via the inhibition of DNA-dependent RNA polymerase, leading to a suppression of RNA synthesis and cell death.
Absorption Well absorbed from gastrointestinal tract.
Toxicity LD50=1570 mg/kg (rat), chronic exposure may cause nausea and vomiting and unconsciousness
Protein Binding 89%
Biotransformation Primarily hepatic, rapidly deacetylated.
Half Life 3.35 (+/- 0.66) hours
Dosage Forms
Form Route
Capsule Oral
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Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The rifamycin decreases the anticoagulant effect
Acetohexamide Rifampin decreases the effect of sulfonylurea
Alfentanil Rifampin reduces levels and efficacy of alfentanil
Aminophylline Rifampin decreases the effect of theophylline
Amiodarone Rifampin decreases the effect of amiodarone
Amitriptyline The rifamycin decreases the effect of tricyclics
Amoxapine The rifamycin decreases the effect of tricyclics
Amprenavir In presence of rifampin, anticipate decrease of amprenavir
Anisindione The rifamycin decreases the anticoagulant effect
Aprepitant This CYP3A4 inducer decreases the effect of aprepitant
Atazanavir Rifampin reduces levels and efficacy of atazanavir
Atorvastatin The rifamycin decreases the effect of the statin drug
Atovaquone The agent decreases the effect of atovaquone
Betamethasone The enzyme inducer decreases the effect of the corticosteroid
Bisoprolol Rifampin decreases the effect of the metabolized beta-blocker
Bupropion Rifampin reduces bupropion levels
Buspirone Rifampin decreases the effect of buspirone
Caspofungin Decreased levels/effects of caspofungin
Celecoxib Decreased levels/effect of the NSAID
Cerivastatin The rifamycin decreases the effect of the statin drug
Chloramphenicol Rifampin decreases the effect of chloramphenicol
Chlorpropamide Rifampin decreases the effect of sulfonylurea
Clarithromycin The rifamycin decreases the effect of the macrolide
Clomipramine The rifamycin decreases the effect of tricyclics
Clozapine Rifampin decreases the effect of clozapine
Cortisone acetate The enzyme inducer decreases the effect of the corticosteroid
Cyclosporine The rifamycin decreases the effect of cyclosporine
Dapsone Decreased levels of dapsone
Dasatinib Decreased levels/efficacy of dasatinib
Delavirdine Rifampin decreases the effect of delavirdine
Desipramine The rifamycin decreases the effect of tricyclics
Dexamethasone The enzyme inducer decreases the effect of the corticosteroid
Diazepam Rifampin decreases the effect of benzodiazepine
Diclofenac Decreased levels/effect of the NSAID
Dicumarol The rifamycin decreases the anticoagulant effect
Diltiazem Rifampin decreases levels of diltiazem
Disopyramide Rifampin decreases the effect of disopyramide
Doxepin The rifamycin decreases the effect of tricyclics
Doxycycline The rifamycin decreases the effect of doxycycline
Dyphylline Rifampin decreases the effect of theophylline
Enalapril Rifampin decreases the effect of enalapril
Erlotinib Decreased levels/effect of erlotinib
Erythromycin The rifamycin decreases the effect of the macrolide
Ethinyl Estradiol This product may cause a slight decrease of contraceptive effect
Ethotoin Rifampin decreases the effect of the hydantoin
Etoricoxib Rifampin reduces levels and efficacy of etoricoxib
Fentanyl Rifampin reduces levels and efficacy of alfentanil
Fluconazole Fluconazole decreases the effect of imidazole
Fludrocortisone The enzyme inducer decreases the effect of the corticosteroid
Fluvastatin The rifamycin decreases the effect of the statin drug
Fosamprenavir In presence of rifampin, anticipate decrease of amprenavir
Fosphenytoin Rifampin decreases the effect of the hydantoin
Gefitinib Rifampin reduces levels and efficacy of gefitinib
Glibenclamide Rifampin decreases the effect of sulfonylurea
Gliclazide Rifampin decreases the effect of sulfonylurea
Glimepiride Rifampin decreases the effect of sulfonylurea
Glipizide Rifampin decreases the effect of sulfonylurea
Glisoxepide Rifampin decreases the effect of sulfonylurea
Glycodiazine Rifampin decreases the effect of sulfonylurea
Haloperidol The rifamycin decreases the effect of haloperidol
Hydrocortisone The enzyme inducer decreases the effect of the corticosteroid
Imatinib Rifampin decreases levels of imatinib
Imipramine The rifamycin decreases the effect of tricyclics
Indinavir Rifampin decreases the effect of indinavir
Itraconazole Rifampin decreases the effect of the imidazole
Josamycin The rifamycin decreases the effect of the macrolide
Ketoconazole Rifampin decreases the effect of the imidazole
Lamotrigine Rifampin decreases levels of lamotrigine
Leflunomide Rifampin increases the effect of leflunomide
Losartan Rifampin decreases the effect of losartan
Lovastatin The rifamycin decreases the effect of the statin drug
Mefloquine Rifampin lowers mefloquine levels
Mephenytoin Rifampin decreases the effect of the hydantoin
Mestranol This product may cause a slight decrease of contraceptive effect
Methadone The rifamycin decreases the effect of methadone
Methylprednisolone The enzyme inducer decreases the effect of the corticosteroid
Metoprolol Rifampin decreases the effect of the metabolized beta-blocker
Mexiletine Rifampin decreases the effect of mexiletine
Midazolam Rifampin decreases the effect of benzodiazepine
Morphine Rifampin decreases the effect of morphine/codeine
Mycophenolate mofetil Significant decrease in immunosuppressant levels
Nelfinavir Rifampin decreases the effect of nelfinavir
Nifedipine Rifampin decreases the effect of the calcium channel blocker
Norethindrone This product may cause a slight decrease of contraceptive effect
Nortriptyline The rifamycin decreases the effect of tricyclics
Oxtriphylline Rifampin decreases the effect of theophylline
Paramethasone The enzyme inducer decreases the effect of the corticosteroid
Phenytoin Rifampin decreases the effect of the hydantoin
Praziquantel Significant decrease in praziquantel level
Prednisolone The enzyme inducer decreases the effect of the corticosteroid
Prednisone The enzyme inducer decreases the effect of the corticosteroid
Propafenone Rifampin decreases the effect of propafenone
Propranolol Rifampin decreases the effect of the metabolized beta-blocker
Protriptyline The rifamycin decreases the effect of tricyclics
Quinidine Rifampin decreases the effect of quinidine
Quinidine barbiturate Rifampin decreases the effect of quinidine
Ramelteon Rifampin reduces the levels/effect of ramelteon
Repaglinide Rifampin decreases the effect of repaglinide
Ritonavir Rifampin decreases the effect of ritonavir
Rofecoxib Decreased levels/effect of the NSAID
Rosiglitazone Rifampin reduces levels and efficacy of rosiglitazone
Saquinavir Rifampin decreases the effect of saquinavir
Simvastatin The rifamycin decreases the effect of the statin drug
Sirolimus The rifamycin decreases the effect of sirolimus
Sunitinib Possible decrease in sunitinib levels
Tacrolimus The rifamycin decreases the effect of tacrolimus
Tadalafil Rifampin reduces levels and efficacy of tadalafil
Tamoxifen The rifamycin decreases the effect of anti-estrogen
Telithromycin Rifampin decreases the effect of telithromycin
Terbinafine Rifampin decreases the effect of terbinafine
Theophylline Rifampin decreases the effect of theophylline
Tocainide Rifampin lowers tocainide levels/effects
Tolazamide Rifampin decreases the effect of sulfonylurea
Tolbutamide Rifampin decreases the effect of sulfonylurea
Toremifene The rifamycin decreases the effect of anti-estrogen
Triamcinolone The enzyme inducer decreases the effect of the corticosteroid
Triazolam Rifampin decreases the effect of benzodiazepine
Trimethoprim Rifampin decreases the effect of trimethoprim
Trimipramine The rifamycin decreases the effect of tricyclics
Verapamil Rifampin decreases the effect of the calcium channel blocker
Voriconazole Rifampin decreases the effect of voriconazole
Warfarin The rifamycin decreases the anticoagulant effect
Zaleplon Rifampin decreases the effect of zaleplon
Zidovudine The rifamycin decreases levels of zidovudine
Food Interactions
  • Avoid alcohol.
  • Take on empty stomach: 1 hour before or 2 hours after meals.
  • Take with a full glass of water.
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Mycobacteria
  • Various gram-negative and gram-positive eubacteria
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A4 (CYP3A4)
  2. Cytochrome P450 1A2 (CYP1A2)
  3. Cytochrome P450 2C8 (CYP2C8)
  4. Glucuronosyltransferase
Targets
  1. DNA-directed RNA polymerase beta' chain
  2. DNA-directed RNA polymerase beta chain
  3. Orphan nuclear receptor PXR
  4. 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 1A2 (CYP1A2)
Enzyme 2 Gene Name CYP1A2
Enzyme 2 SwissProt ID P05177 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >P05177|CP1A2_HUMAN Cytochrome P450 1A2 - Homo sapiens (Human). 
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
Phase 1 Metabolizing Enzyme 3 [top]
Enzyme 3 Name Cytochrome P450 2C8 (CYP2C8)
Enzyme 3 Gene Name CYP2C8
Enzyme 3 SwissProt ID P10632 Link Image
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 Protein Sequence >sp|P10632|CP2C8_HUMAN Cytochrome P450 2C8 (EC 1.14.14.1) 
MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKV
YGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRW
KEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICS
VVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALT
RSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTE
TTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSD
LVPTGVPHAVTTDTKFRNYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFK
KSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIVSLP
PSYQICFIPV
Phase 1 Metabolizing Enzyme 4 [top]
Enzyme 4 Name Glucuronosyltransferase
Enzyme 4 Gene Name UGT1A1
Enzyme 4 SwissProt ID P22309 Link Image
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 Protein Sequence >sp|P22309|UD11_HUMAN UDP-glucuronosyltransferase 1-1 precursor 
MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVL
APDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDS
AMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLE
FEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEH
GIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDL
LGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTS
EDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Drug Target 1 [top]
Target 1 ID 208
Target 1 Name DNA-directed RNA polymerase beta' chain
Target 1 Synonyms
  1. EC 2.7.7.6
  2. RNA polymerase beta' subunit
  3. RNAP beta' subunit
  4. Transcriptase beta' chain
Target 1 Gene Name rpoC
Target 1 Protein Sequence >DNA-directed RNA polymerase beta' chain 
MLDVNFFDELRIGLATAEDIRQWSYGEVKKPETINYRTLKPEKDGLFCEKIFGPTRDWEC
YCGKYKRVRFKGIICERCGVEVTRAKVRRERMGHIELAAPVTHIWYFKGVPSRLGYLLDL
APKDLEKIIYFAAYVITSVDEEMRHNELSTLEAEMAVERKAVEDQRDGELEARAQKLEAD
LAELEAEGAKADARRKVRDGGEREMRQIRDRAQRELDRLEDIWSTFTKLAPKQLIVDENL
YRELVDRYGEYFTGAMGAESIQKLIENFDIDAEAESLRDVIRNGKGQKKLRALKRLKVVA
AFQQSGNSPMGMVLDAVPVIPPELRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLIDL
GAPEIIVNNEKRMLQESVDALFDNGRRGRPVTGPGNRPLKSLSDLLKGKQGRFRQNLLGK
RVDYSGRSVIVVGPQLKLHQCGLPKLMALELFKPFVMKRLVDLNHAQNIKSAKRMVERQR
PQVWDVLEEVIAEHPVLLNRAPTLHRLGIQAFEPMLVEGKAIQLHPLVCEAFNADFDGDQ
MAVHLPLSAEAQAEARILMLSSNNILSPASGRPLAMPRLDMVTGLYYLTTEVPGDTGEYQ
PASGDHPETGVYSSPAEAIMAADRGVLSVRAKIKVRLTQLRPPVEIEAELFGHSGWQPGD
AWMAETTLGRVMFNELLPLGYPFVNKQMHKKVQAAIINDLAERYPMIVVAQTVDKLKDAG
FYWATRSGVTVSMADVLVPPRKKEILDHYEERADKVEKQFQRGALNHDERNEALVEIWKE
ATDEVGQALREHYPDDNPIITIVDSGATGNFTQTRTLAGMKGLVTNPKGEFIPRPVKSSF
REGLTVLEYFINTHGARKGLADTALRTADSGYLTRRLVDVSQDVIVREHDCQTERGIVVE
LAERAPDGTLIRDPYIETSAYARTLGTDAVDEAGNVIVERGQDLGDPEIDALLAAGITQV
KVRSVLTCATSTGVCATCYGRSMATGKLVDIGEAVGIVAAQSIGEPGTQLTMRTFHQGGV
GEDITGGLPRVQELFEARVPRGKAPIADVTGRVRLEDGERFYKITIVPDDGGEEVVYDKI
SKRQRLRVFKHEDGSERVLSDGDHVEVGQQLMEGSADPHEVLRVQGPREVQIHLVREVQE
VYRAQGVSIHDKHIEVIVRQMLRRVTIIDSGSTEFLPGSLIDRAEFEAENRRVVAEGGEP
AAGRPVLMGITKASLATDSWLSAASFQETTRVLTDAAINCRSDKLNGLKENVIIGKLIPA
GTGINRYRNIAVQPTEEARAAAYTIPSYEDQYYSPDFGAATGAAVPLDDYGYSDYR
Target 1 Number of Residues 1337
Target 1 Molecular Weight 146771
Target 1 Theoretical pI 6.08
Target 1 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
DNA-directed RNA polymerase activity
binding
nucleic acid binding
DNA binding
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
transcription
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 1 General Function Transcription
Target 1 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Target 1 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Pyrimidine metabolism SMP00046 Link Image map00240 Link Image
RNA polymerase map03020 Link Image
Target 1 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 2143292 Link Image
Target 1 UniProtKB/Swiss-Prot ID P0A674 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name RPOC_MYCTU Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >3951 bp 
GTGCTCGACGTCAACTTCTTCGATGAACTCCGCATCGGTCTTGCTACCGCGGAGGACATC
AGGCAATGGTCCTATGGCGAGGTCAAAAAGCCGGAGACGATCAACTACCGCACGCTTAAG
CCGGAGAAGGACGGCCTGTTCTGCGAGAAGATCTTCGGGCCGACTCGCGACTGGGAATGC
TACTGCGGCAAGTACAAGCGGGTGCGCTTCAAGGGCATCATCTGCGAGCGCTGCGGCGTC
GAGGTGACCCGCGCCAAGGTGCGTCGTGAGCGGATGGGCCACATCGAGCTTGCCGCGCCC
GTCACCCACATCTGGTACTTCAAGGGTGTGCCCTCGCGGCTGGGGTATCTGCTGGACCTG
GCCCCGAAGGACCTGGAGAAGATCATCTACTTCGCTGCCTACGTGATCACCTCGGTCGAC
GAGGAGATGCGCCACAATGAGCTCTCCACGCTCGAGGCCGAAATGGCGGTGGAGCGCAAG
GCCGTCGAAGACCAGCGCGACGGCGAACTAGAGGCCCGGGCGCAAAAGCTGGAGGCCGAC
CTGGCCGAGCTGGAGGCCGAGGGCGCCAAGGCCGATGCGCGGCGCAAGGTTCGCGACGGC
GGCGAGCGCGAGATGCGCCAGATCCGTGACCGCGCGCAGCGTGAGCTGGACCGGTTGGAG
GACATCTGGAGCACTTTCACCAAGCTGGCGCCCAAGCAGCTGATCGTCGACGAAAACCTC
TACCGCGAACTCGTCGACCGCTACGGCGAGTACTTCACCGGTGCCATGGGCGCGGAGTCG
ATCCAGAAGCTGATCGAGAACTTCGACATCGACGCCGAAGCCGAGTCGCTGCGGGATGTC
ATCCGAAACGGCAAGGGGCAGAAGAAGCTTCGCGCCCTCAAGCGGCTGAAGGTGGTTGCG
GCGTTCCAACAGTCGGGCAACTCGCCGATGGGCATGGTGCTCGACGCCGTCCCGGTGATC
CCGCCGGAGCTGCGCCCGATGGTGCAGCTCGACGGCGGCCGGTTCGCCACGTCCGACTTG
AACGACCTGTACCGCAGGGTGATCAACCGCAACAACCGGCTGAAAAGGCTGATCGATCTG
GGTGCGCCGGAAATCATCGTCAACAACGAGAAGCGGATGCTGCAGGAATCCGTGGACGCG
CTGTTCGACAATGGCCGCCGCGGCCGGCCCGTCACCGGGCCGGGCAACCGTCCGCTCAAG
TCGCTTTCCGATCTGCTCAAGGGCAAGCAGGGCCGGTTCCGGCAGAACCTGCTCGGCAAG
CGTGTCGACTACTCGGGCCGGTCGGTCATCGTGGTCGGCCCGCAGCTCAAGCTGCACCAG
TGCGGTCTGCCCAAGCTGATGGCGCTGGAGCTGTTCAAGCCGTTCGTGATGAAGCGGCTG
GTGGACCTCAACCATGCGCAGAACATCAAGAGCGCCAAGCGCATGGTGGAGCGCCAGCGC
CCCCAAGTGTGGGATGTGCTCGAAGAGGTCATCGCCGAGCACCCGGTGTTGCTGAACCGC
GCACCCACCCTGCACCGGTTGGGTATCCAGGCCTTCGAGCCAATGCTGGTGGAAGGCAAG
GCCATTCAGCTGCACCCGTTGGTGTGTGAGGCGTTCAATGCCGACTTCGACGGTGACCAG
ATGGCCGTGCACCTGCCTTTGAGCGCCGAAGCGCAGGCCGAGGCTCGCATTTTGATGTTG
TCCTCCAACAACATCCTGTCGCCGGCATCTGGGCGTCCGTTGGCCATGCCGCGGCTGGAC
ATGGTGACCGGGCTGTACTACCTGACCACCGAGGTCCCCGGGGACACCGGCGAATACCAG
CCGGCCAGCGGGGATCACCCGGAGACTGGTGTCTACTCTTCGCCGGCCGAAGCGATCATG
GCGGCCGACCGCGGTGTCTTGAGCGTGCGGGCCAAGATCAAGGTGCGGCTGACCCAGCTG
CGGCCGCCGGTCGAGATCGAGGCCGAGCTATTCGGCCACAGCGGCTGGCAGCCGGGCGAT
GCGTGGATGGCCGAGACCACGCTGGGCCGGGTGATGTTCAACGAGCTGCTGCCGCTGGGT
TATCCGTTCGTCAACAAGCAGATGCACAAGAAGGTGCAGGCCGCCATCATCAACGACCTG
GCCGAGCGTTACCCGATGATCGTGGTCGCCCAGACCGTCGACAAGCTCAAGGACGCCGGC
TTCTACTGGGCCACCCGCAGCGGCGTGACGGTGTCGATGGCCGACGTGCTGGTGCCGCCG
CGCAAGAAGGAGATCCTCGACCACTACGAGGAGCGCGCGGACAAGGTCGAAAAGCAGTTC
CAGCGTGGCGCTTTGAACCACGACGAGCGCAACGAGGCGCTGGTGGAGATTTGGAAGGAA
GCCACCGACGAGGTCGGTCAGGCGTTGCGGGAGCACTACCCCGACGACAACCCGATCATC
ACCATCGTCGACTCCGGCGCCACCGGCAACTTCACCCAGACTCGAACGCTGGCCGGTATG
AAGGGCCTGGTGACCAACCCGAAGGGTGAGTTCATCCCGCGTCCGGTCAAGTCCTCCTTC
CGTGAGGGCCTGACCGTGCTGGAGTACTTCATCAACACCCACGGCGCTCGAAAGGGCTTG
GCGGACACCGCGTTGCGCACCGCCGACTCCGGCTACCTGACCCGACGTCTGGTGGACGTG
TCCCAGGACGTGATCGTGCGCGAGCACGACTGCCAGACCGAGCGCGGCATCGTCGTCGAG
CTGGCCGAGCGTGCACCCGACGGCACGCTGATCCGCGACCCGTACATCGAAACCTCGGCC
TACGCGCGGACCCTGGGCACCGACGCGGTCGACGAGGCCGGCAACGTCATCGTCGAGCGT
GGTCAAGACCTGGGCGATCCGGAGATTGACGCTCTGTTGGCTGCTGGTATTACCCAGGTC
AAGGTGCGTTCGGTGCTGACGTGTGCCACCAGCACCGGCGTGTGCGCGACCTGCTACGGG
CGTTCCATGGCCACCGGCAAGCTGGTCGACATCGGTGAAGCCGTCGGCATCGTGGCCGCC
CAGTCCATCGGCGAACCCGGCACCCAGCTGACCATGCGCACCTTCCACCAGGGTGGCGTC
GGTGAGGACATCACCGGTGGTCTGCCCCGGGTGCAGGAGCTGTTCGAGGCCCGGGTACCG
CGTGGCAAGGCGCCGATCGCCGACGTCACCGGCCGGGTTCGGCTCGAGGACGGCGAGCGG
TTCTACAAGATCACCATCGTTCCTGACGACGGCGGTGAGGAAGTGGTCTACGACAAGATC
TCCAAGCGGCAGCGGCTGCGGGTGTTCAAGCACGAAGACGGTTCCGAACGGGTGCTCTCC
GATGGCGACCACGTCGAGGTGGGCCAGCAGCTGATGGAAGGCTCGGCCGACCCGCATGAG
GTGCTGCGGGTGCAGGGCCCCCGCGAGGTGCAGATACACCTGGTTCGCGAGGTCCAGGAG
GTCTACCGCGCCCAAGGTGTGTCGATCCACGACAAGCACATCGAGGTGATCGTTCGCCAG
ATGCTGCGCCGGGTGACCATCATCGACTCGGGCTCGACGGAGTTTTTGCCTGGCTCGCTG
ATCGACCGCGCGGAGTTCGAGGCAGAGAACCGCCGAGTGGTGGCCGAGGGCGGTGAGCCC
GCGGCCGGCCGTCCGGTGCTGATGGGCATCACGAAGGCGTCGCTGGCCACCGACTCGTGG
CTGTCGGCGGCGTCGTTCCAGGAGACCACTCGCGTGCTGACCGATGCGGCGATCAACTGC
CGCAGCGATAAGCTCAACGGTCTGAAGGAAAACGTGATCATCGGCAAGCTGATCCCGGCC
GGTACCGGTATCAACCGCTACCGCAACATCGCGGTGCAGCCCACCGAGGAGGCCCGCGCT
GCGGCGTACACCATCCCGTCGTATGAGGATCAGTACTACAGCCCGGACTTCGGTGCGGCC
ACCGGTGCTGCCGTCCCGCTGGACGACTACGGCTACAGCGACTACCGCTAG
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. Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM: Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. J Bacteriol. 2002 Oct;184(19):5479-90. [PubMed Link Image]
  2. Miller LP, Crawford JT, Shinnick TM: The rpoB gene of Mycobacterium tuberculosis. Antimicrob Agents Chemother. 1994 Apr;38(4):805-11. [PubMed Link Image]
  3. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [PubMed Link Image]
Target 1 Drug References
  1. 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]
  2. 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]
  3. Buchstein SR, Hinkle DC: Genetic analysis of two bacterial RNA polymerase mutants that inhibit the growth of bacteriophage T7. Mol Gen Genet. 1982;188(2):211-8. [PubMed Link Image]
  4. Miller LP, Crawford JT, Shinnick TM: The rpoB gene of Mycobacterium tuberculosis. Antimicrob Agents Chemother. 1994 Apr;38(4):805-11. [PubMed Link Image]
  5. Babcock MJ, Buttner MJ, Keler CH, Clarke BR, Morris RA, Lewis CG, Brawner ME: Characterization of the rpoC gene of Streptomyces coelicolor A3(2) and its use to develop a simple and rapid method for the purification of RNA polymerase. Gene. 1997 Sep 1;196(1-2):31-42. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 284
Target 2 Name DNA-directed RNA polymerase beta chain
Target 2 Synonyms
  1. EC 2.7.7.6
  2. RNA polymerase beta subunit
  3. RNAP beta subunit
  4. Transcriptase beta chain
Target 2 Gene Name rpoB
Target 2 Protein Sequence >DNA-directed RNA polymerase beta chain 
MVYSYTEKKRIRKDFGKRPQVLDVPYLLSIQLDSFQKFIEQDPEGQYGLEAAFRSVFPIQ
SYSGNSELQYVSYRLGEPVFDVQECQIRGVTYSAPLRVKLRLVIYEREAPEGTVKDIKEQ
EVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARIIPYR
GSWLDFEFDPKDNLFVRIDRRRKLPATIILRALNYTTEQILDLFFEKVIFEIRDNKLQME
LVPERLRGETASFDIEANGKVYVEKGRRITARHIRQLEKDDVKLIEVPVEYIAGKVVAKD
YIDESTGELICAANMELSLDLLAKLSQSGHKRIETLFTNDLDHGPYISETLRVDPTNDRL
SALVEIYRMMRPGEPPTREAAESLFENLFFSEDRYDLSAVGRMKFNRSLLREEIEGSGIL
SKDDIIDVMKKLIDIRNGKGEVDDIDHLGNRRIRSVGEMAENQFRVGLVRVERAVKERLS
LGDLDTLMPQDMINAKPISAAVKEFFGSSQLSQFMDQNNPLSEITHKRRISALGPGGLTR
ERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLSVYAQTNEYGFLETPYRKVTDGVVT
DEIHYLSAIEEGNYVIAQANSNLDEEGHFVEDLVTCRSKGESSLFSRDQVDYMDVSTQQV
VSVGASLIPFLEHDDANRALMGANMQRQAVPTLRADKPLVGTGMERAVAVDSGVTAVAKR
GGVVQYVDASRIVIKVNEDEMYPGEAGIDIYNLTKYTRSNQNTCINQMPCVSLGEPVERG
DVLADGPSTDLGELALGQNMRVAFMPWNGYNFEDSILVSERVVQEDRFTTIHIQELACVS
RDTKLGPEEITADIPNVGEAALSKLDESGIVYIGAEVTGGDILVGKVTPKGETQLTPEEK
LLRAIFGEKASDVKDSSLRVPNGVSGTVIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDL
SEELQILEAGLFSRIRAVLVAGGVEAEKLDKLPRDRWLELGLTDEEKQNQLEQLAEQYDE
LKHEFEKKLEAKRRKITQGDDLAPGVLKIVKVYLAVKRRIQPGDKMAGRHGNKGVISKIN
PIEDMPYDENGTPVDIVLNPLGVPSRMNIGQILETHLGMAAKGIGDKINAMLKQQQEVAK
LREFIQRAYDLGADVRQKVDLSTFSDEEVMRLAENLRKGMPIATPVFDGAKEAEIKELLK
LGDLPTSGQIRLYDGRTGEQFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLG
GKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGNHQMEPGMP
ESFNVLLKEIRSLGINIELEDE
Target 2 Number of Residues 1364
Target 2 Molecular Weight 150635
Target 2 Theoretical pI 4.89
Target 2 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
DNA-directed RNA polymerase activity
binding
nucleic acid binding
DNA binding
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
transcription
Component
Not Available
Target 2 General Function Transcription
Target 2 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Target 2 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Pyrimidine metabolism SMP00046 Link Image map00240 Link Image
RNA polymerase map03020 Link Image
Target 2 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 42818 Link Image
Target 2 UniProtKB/Swiss-Prot ID P0A8V2 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name RPOB_ECOLI Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Cytoplasmic
Target 2 Gene Sequence >4029 bp 
ATGGTTTACTCCTATACCGAGAAAAAACGTATTCGTAAGGATTTTGGTAAACGTCCACAA
GTTCTGGATGTACCTTATCTCCTTTCTATCCAGCTTGACTCGTTTCAGAAATTTATCGAG
CAAGATCCTGAAGGGCAGTATGGTCTGGAAGCTGCTTTCCGTTCCGTATTCCCGATTCAG
AGCTACAGCGGTAATTCCGAGCTGCAATACGTCAGCTACCGCCTTGGCGAACCGGTGTTT
GACGTCCAGGAATGTCAAATCCGTGGCGTGACCTATTCCGCACCGCTGCGCGTTAAACTG
CGTCTGGTGATCTATGAGCGCGAAGCGCCGGAAGGCACCGTAAAAGACATTAAAGAACAA
GAAGTCTACATGGGCGAAATTCCGCTCATGACAGACAACGGTACCTTTGTTATCAACGGT
ACTGAGCGTGTTATCGTTTCCCAGCTGCACCGTAGTCCGGGCGTCTTCTTTGACTCCGAC
AAAGGTAAAACCCACTCTTCGGGTAAAGTGCTGTATAACGCGCGTATCATCCCTTACCGT
GGTTCCTGGCTGGACTTCGAATTCGATCCGAAGGACAACCTGTTCGTACGTATCGACCGT
CGCCGTAAACTGCCTGCGACCATCATTCTGCGCGCCCTGAACTACACCACAGAGCAGATC
CTCGACCTGTTCTTTGAAAAAGTTATCTTTGAAATCCGTGATAACAAGCTGCAGATGGAA
CTGGTGCCGGAACGCCTGCGTGGTGAAACCGCATCTTTTGACATCGAAGCTAACGGTAAA
GTGTACGTAGAAAAAGGCCGCCGTATCACTGCGCGCCACATTCGCCAGCTGGAAAAAGAC
GACGTCAAACTGATCGAAGTCCCGGTTGAGTACATCGCAGGTAAAGTGGTTGCTAAAGAC
TATATTGATGAGTCTACCGGCGAGCTGATCTGCGCAGCGAACATGGAGCTGAGCCTGGAT
CTGCTGGCTAAGCTGAGCCAGTCTGGTCACAAGCGTATCGAAACGCTGTTCACCAACGAT
CTGGATCACGGCCCATATATCTCTGAAACCTTACGTGTCGACCCAACTAACGACCGTCTG
AGCGCACTGGTAGAAATCTACCGCATGATGCGCCCTGGCGAGCCGCCGACTCGTGAAGCA
GCTGAAAGCCTGTTCGAGAACCTGTTCTTCTCCGAAGACCGTTATGACTTGTCTGCGGTT
GGTCGTATGAAGTTCAACCGTTCTCTGCTGCGCGAAGAAATCGAAGGTTCCGGTATCCTG
AGCAAAGACGACATCATTGATGTTATGAAAAAGCTCATCGATATCCGTAACGGTAAAGGC
GAAGTCGATGATATCGACCACCTCGGCAACCGTCGTATCCGTTCCGTTGGCGAAATGGCG
GAAAACCAGTTCCGCGTTGGCCTGGTACGTGTAGAGCGTGCGGTGAAAGAGCGTCTGTCT
CTGGGCGATCTGGATACCCTGATGCCACAGGATATGATCAACGCCAAGCCGATTTCCGCA
GCAGTGAAAGAGTTCTTCGGTTCCAGCCAGCTGTCTCAGTTTATGGTCCAGAACAACCCG
CTGTCTGAGATTACGCACAAACGTCGTATCTCCGCACTCGGCCCAGGCGGTCTGACCCGT
GAACGTGCAGGCTTCGAAGTTCGAGACGTACACCCGACTCACTACGGTCGCGTATGTCCA
ATCGAAACCCCTGAAGGTCCGAACATCGGTCTGATCAACTCTCTGTCCGTGTACGCACAG
ACTAACGAATACGGCTTCCTTGAGACTCCGTATCGTAAAGTGACCGACGGTGTTGTAACT
GACGAAATTCACTACCTGTCTGCTATCGAAGAAGGCAACTACGTTATCGCCCAGGCGAAC
TCCAACTTGGATGAAGAAGGCCACTTCGTAGAAGACCTGGTAACTTGCCGTAGCAAAGGC
GAATCCAGCTTGTTCAGCCGCGACCAGGTTGACTACATGGACGTATCCACCCAGCAGGTG
GTATCCGTCGGTGCGTCCCTGATCCCGTTCCTGGAACACGATGACGCCAACCGTGCATTG
ATGGGTGCGAACATGCAACGTCAGGCCGTTCCGACTCTGCGCGCTGATAAGCCGCTGGTT
GGTACTGGTATGGAACGTGCTGTTGCCGTTGACTCCGGTGTAACTGCGGTAGCTAAACGT
GGTGGTGTCGTTCAGTACGTGGATGCTTCCCGTATCGTTATCAAAGTTAACGAAGACGAG
ATGTATCCGGGTGAAGCAGGTATCGACATCTACAACCTGACCAAATACACCCGTTCTAAC
CAGAACACCTGTATCAACCAGATGCCGTGTGTGTCTCTGGGTGAACCGGTTGAACGTGGC
GACGTGCTGGCAGACGGTCCGTCCACCGACCTCGGTGAACTGGCGCTTGGTCAGAACATG
CGCGTAGCGTTCATGCCGTGGAATGGTTACAACTTCGAAGACTCCATCCTCGTATCCGAG
CGTGTTGTTCAGGAAGACCGTTTCACCACCATCCACATTCAGGAACTGGCGTGTGTGTCC
CGTGACACCAAGCTGGGTCCGGAAGAGATCACCGCTGACATCCCGAACGTGGGTGAAGCT
GCGCTCTCCAAACTGGATGAATCCGGTATCGTTTACATTGGTGCGGAAGTGACCGGTGGC
GACATTCTGGTTGGTAAGGTAACGCCGAAAGGTGAAACTCAGCTGACCCCAGAAGAAAAA
CTGCTGCGTGCGATCTTCGGTGAGAAAGCCTCTGACGTTAAAGACTCTTCTCTGCGCGTA
CCAAACGGTGTATCCGGTACGGTTATCGACGTTCAGGTCTTTACTCGCGATGGCGTAGAA
AAAGACAAACGTGCGCTGGAAATCGAAGAAATGCAGCTCAAACAGGCGAAGAAAGACCTG
TCTGAAGAACTGCAGATCCTCGAAGCGGGTCTGTTCAGCCGTATCCGTGCTGTGCTGGTA
GCCGGTGGCGTTGAAGCTGAGAAGCTCGACAAACTGCCGCGCGATCGCTGGCTGGAGCTG
GGCCTGACAGACGAAGAGAAACAAAATCAGCTGGAACAGCTGGCTGAGCAGTATGACGAA
CTGAAACACGAGTTCGAGAAGAAACTCGAAGCGAAACGCCGCAAAATCACCCAGGGCGAC
GATCTGGCACCGGGCGTGCTGAAGATTGTTAAGGTATATCTGGCGGTTAAACGCCGTATC
CAGCCTGGTGACAAGATGGCAGGTCGTCACGGTAACAAGGGTGTAATTTCTAAGATCAAC
CCGATCGAAGATATGCCTTACGATGAAAACGGTACGCCGGTAGACATCGTACTGAACCCG
CTGGGCGTACCGTCTCGTATGAACATCGGTCAGATCCTCGAAACCCACCTGGGTATGGCT
GCGAAAGGTATCGGCGACAAGATCAACGCCATGCTGAAACAGCAGCAAGAAGTCGCGAAA
CTGCGCGAATTCATCCAGCGTGCGTACGATCTGGGCGCTGACGTTCGTCAGAAAGTTGAC
CTGAGTACCTTCAGCGATGAAGAAGTTATGCGTCTGGCTGAAAACCTGCGCAAAGGTATG
CCAATCGCAACGCCGGTGTTCGACGGTGCGAAAGAAGCAGAAATTAAAGAGCTGCTGAAA
CTTGGCGACCTGCCGACTTCCGGTCAGATCCGCCTGTACGATGGTCGCACTGGTGAACAG
TTCGAGCGTCCGGTAACCGTTGGTTACATGTACATGCTGAAACTGAACCACCTGGTCGAC
GACAAGATGCACGCGCGTTCCACCGGTTCTTACAGCCTGGTTACTCAGCAGCCGCTGGGT
GGTAAGGCACAGTTCGGTGGTCAGCGTTTCGGGGAGATGGAAGTGTGGGCGCTGGAAGCA
TACGGCGCAGCATACACCCTGCAGGAAATGCTCACCGTTAAGTCTGATGACGTGAACGGT
CGTACCAAGATGTATAAAAACATCGTGGACGGCAACCATCAGATGGAGCCGGGCATGCCA
GAATCCTTCAACGTATTGTTGAAAGAGATTCGTTCGCTGGGTATCAACATCGAACTGGAA
GACGAGTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID Not Available
Target 2 GenAtlas ID Not Available
Target 2 HGNC ID Not Available
Target 2 Chromosome Location Not Available
Target 2 Locus Not Available
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Lee J, Kashlev M, Borukhov S, Goldfarb A: A beta subunit mutation disrupting the catalytic function of Escherichia coli RNA polymerase. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6018-22. [PubMed Link Image]
  2. Post LE, Strycharz GD, Nomura M, Lewis H, Dennis PP: Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1697-701. [PubMed Link Image]
  3. Ovchinnikov YA, Monastyrskaya GS, Gubanov VV, Guryev SO, Chertov OYu, Modyanov NN, Grinkevich VA, Makarova IA, Marchenko TV, Polovnikova IN, Lipkin VM, Sverdlov ED: The primary structure of Escherichia coli RNA polymerase. Nucleotide sequence of the rpoB gene and amino-acid sequence of the beta-subunit. Eur J Biochem. 1981 Jun 1;116(3):621-9. [PubMed Link Image]
  4. Delcuve G, Downing W, Lewis H, Dennis PP: Nucleotide sequence of the proximal portion of the RNA polymerase beta subunit gene of Escherichia coli. Gene. 1980 Nov;11(3-4):367-73. [PubMed Link Image]
  5. Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. [PubMed Link Image]
  6. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
Target 2 Drug References
  1. Nicholson WL, Maughan H: The spectrum of spontaneous rifampin resistance mutations in the rpoB gene of Bacillus subtilis 168 spores differs from that of vegetative cells and resembles that of Mycobacterium tuberculosis. J Bacteriol. 2002 Sep;184(17):4936-40. [PubMed Link Image]
  2. Maughan H, Galeano B, Nicholson WL: Novel rpoB mutations conferring rifampin resistance on Bacillus subtilis: global effects on growth, competence, sporulation, and germination. J Bacteriol. 2004 Apr;186(8):2481-6. [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. He X, Zhuang Y, Li G: [Application of PCR-SSCP technique in detection of rpoB gene mutation in rifampin-resistant Mycobacterium tuberculosis] Zhonghua Jie He He Hu Xi Za Zhi. 1996 Dec;19(6):338-41. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 1284
Target 3 Name Orphan nuclear receptor PXR
Target 3 Synonyms
  1. Orphan nuclear receptor PAR1
  2. Pregnane X receptor
  3. SXR
  4. Steroid and xenobiotic receptor
Target 3 Gene Name NR1I2
Target 3 Protein Sequence >Orphan nuclear receptor PXR 
MEVRPKESWNHADFVHCEDTESVPGKPSVNADEEVGGPQICRVCGDKATGYHFNVMTCEG
CKGFFRRAMKRNARLRCPFRKGACEITRKTRRQCQACRLRKCLESGMKKEMIMSDEAVEE
RRALIKRKKSERTGTQPLGVQGLTEEQRMMIRELMDAQMKTFDTTFSHFKNFRLPGVLSS
GCELPESLQAPSREEAAKWSQVRKDLCSLKVSLQLRGEDGSVWNYKPPADSGGKEIFSLL
PHMADMSTYMFKGIISFAKVISYFRDLPIEDQISLLKGAAFELCQLRFNTVFNAETGTWE
CGRLSYCLEDTAGGFQQLLLEPMLKFHYMLKKLQLHEEEYVLMQAISLFSPDRPGVLQHR
VVDQLQEQFAITLKSYIECNRPQPAHRFLFLKIMAMLTELRSINAQHTQRLLRIQDIHPF
ATPLMQELFGITGS
Target 3 Number of Residues 441
Target 3 Molecular Weight 49762
Target 3 Theoretical pI 8.44
Target 3 GO Classification
Function
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
binding
nucleic acid binding
DNA binding
transcription factor activity
Process
regulation of biological process
regulation of physiological process
regulation of metabolism
regulation of cellular metabolism
regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
regulation of transcription
regulation of transcription, DNA-dependent
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 3 General Function Involved in transcription factor activity
Target 3 Specific Function Orphan receptor; its natural ligand is probably pregnane. Binds to a response element in the CYP3A4 and ABCB1/MDR1 genes promoter. Activates its expression in response to a wide variety of endobiotics and xenobiotics
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 3511138 Link Image
Target 3 UniProtKB/Swiss-Prot ID O75469 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name PXR_HUMAN Link Image
Target 3 PDB ID 1NRL Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Nucleus
Target 3 Gene Sequence >1305 bp 
CTGGAGGTGAGACCCAAAGAAAGCTGGAACCATGCTGACTTTGTACACTGTGAGGACACA
GAGTCTGTTCCTGGAAAGCCCAGTGTCAACGCAGATGAGGAAGTCGGAGGTCCCCAAATC
TGCCGTGTATGTGGGGACAAGGCCACTGGCTATCACTTCAATGTCATGACATGTGAAGGA
TGCAAGGGCTTTTTCAGGAGGGCCATGAAACGCAACGCCCGGCTGAGGTGCCCCTTCCGG
AAGGGCGCCTGCGAGATCACCCGGAAGACCCGGCGACAGTGCCAGGCCTGCCGCCTGCGC
AAGTGCCTGGAGAGCGGCATGAAGAAGGAGATGATCATGTCCGACGAGGCCGTGGAGGAG
AGGCGGGCCTTGATCAAGCGGAAGAAAAGTGAACGGACAGGGACTCAGCCACTGGGAGTG
CAGGGGCTGACAGAGGAGCAGCGGATGATGATCAGGGAGCTGATGGACGCTCAGATGAAA
ACCTTTGACACTACCTTCTCCCATTTCAAGAATTTCCGGCTGCCAGGGGTGCTTAGCAGT
GGCTGCGAGTTGCCAGAGTCTCTGCAGGCCCCATCGAGGGAAGAAGCTGCCAAGTGGAGC
CAGGTCCGGAAAGATCTGTGCTCTTTGAAGGTCTCTCTGCAGCTGCGGGGGGAGGATGGC
AGTGTCTGGAACTACAAACCCCCAGCCGACAGTGGCGGGAAAGAGATCTTCTCCCTGCTG
CCCCACATGGCTGACATGTCAACCTACATGTTCAAAGGCATCATCAGCTTTGCCAAAGTC
ATCTCCTACTTCAGGGACTTGCCCATCGAGGACCAGATCTCCCTGCTGAAGGGGGCCGCT
TTCGAGCTGTGTCAACTGAGATTCAACACAGTGTTCAACGCGGAGACTGGAACCTGGGAG
TGTGGCCGGCTGTCCTACTGCTTGGAAGACACTGCAGGTGGCTTCCAGCAACTTCTACTG
GAGCCCATGCTGAAATTCCACTACATGCTGAAGAAGCTGCAGCTGCATGAGGAGGAGTAT
GTGCTGATGCAGGCCATCTCCCTCTTCTCCCCAGACCGCCCAGGTGTGCTGCAGCACCGC
GTGGTGGACCAGCTGCAGGAGCAATTCGCCATTACTCTGAAGTCCTACATTGAATGCAAT
CGGCCCCAGCCTGCTCATAGGTTCTTGTTCCTGAAGATCATGGCTATGCTCACCGAGCTC
CGCAGCATCAATGCTCAGCACACCCAGCGGCTGCTGCGCATCCAGGACATACACCCCTTT
GCTACGCCCCTCATGCAGGAGTTGTTCGGCATCACAGGTAGCTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID NR1I2 Link Image
Target 3 GenAtlas ID NR1I2 Link Image
Target 3 HGNC ID HGNC:7968 Link Image
Target 3 Chromosome Location 3
Target 3 Locus 3q12-q13.3
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Watkins RE, Wisely GB, Moore LB, Collins JL, Lambert MH, Williams SP, Willson TM, Kliewer SA, Redinbo MR: The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity. Science. 2001 Jun 22;292(5525):2329-33. Epub 2001 Jun 14. [PubMed Link Image]
  2. Zhang J, Kuehl P, Green ED, Touchman JW, Watkins PB, Daly A, Hall SD, Maurel P, Relling M, Brimer C, Yasuda K, Wrighton SA, Hancock M, Kim RB, Strom S, Thummel K, Russell CG, Hudson JR Jr, Schuetz EG, Boguski MS: The human pregnane X receptor: genomic structure and identification and functional characterization of natural allelic variants. Pharmacogenetics. 2001 Oct;11(7):555-72. [PubMed Link Image]
  3. Kawana K, Ikuta T, Kobayashi Y, Gotoh O, Takeda K, Kawajiri K: Molecular mechanism of nuclear translocation of an orphan nuclear receptor, SXR. Mol Pharmacol. 2003 Mar;63(3):524-31. [PubMed Link Image]
  4. Lehmann JM, McKee DD, Watson MA, Willson TM, Moore JT, Kliewer SA: The human orphan nuclear receptor PXR is activated by compounds that regulate CYP3A4 gene expression and cause drug interactions. J Clin Invest. 1998 Sep 1;102(5):1016-23. [PubMed Link Image]
  5. Bertilsson G, Heidrich J, Svensson K, Asman M, Jendeberg L, Sydow-Backman M, Ohlsson R, Postlind H, Blomquist P, Berkenstam A: Identification of a human nuclear receptor defines a new signaling pathway for CYP3A induction. Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12208-13. [PubMed Link Image]
  6. Blumberg B, Sabbagh W Jr, Juguilon H, Bolado J Jr, van Meter CM, Ong ES, Evans RM: SXR, a novel steroid and xenobiotic-sensing nuclear receptor. Genes Dev. 1998 Oct 15;12(20):3195-205. [PubMed Link Image]
Target 3 Drug References Not Available
Drug Target 4 [top]
Target 4 ID 1588
Target 4 Name Multidrug resistance protein 1
Target 4 Synonyms
  1. ATP-binding cassette sub-family B member 1
  2. CD243 antigen
  3. EC 3.6.3.44
  4. P-glycoprotein 1
Target 4 Gene Name ABCB1
Target 4 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 4 Number of Residues 1301
Target 4 Molecular Weight 141464
Target 4 Theoretical pI 9.44
Target 4 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 4 General Function Defense mechanisms and drug export
Target 4 Specific Function Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells
Target 4 Pathways Not Available
Target 4 Reactions
  • ATP + H2O + xenobioticin = ADP + phosphate + xenobioticout
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 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 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 307180 Link Image
Target 4 UniProtKB/Swiss-Prot ID P08183 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name MDR1_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 4 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 4 GenBank Gene ID
Target 4 GeneCard ID ABCB1 Link Image
Target 4 GenAtlas ID ABCB1 Link Image
Target 4 HGNC ID HGNC:40 Link Image
Target 4 Chromosome Location 7
Target 4 Locus 7q21.1
Target 4 SNPs SNPJam Report Link Image
Target 4 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 4 Drug References
  1. Kuypers DR, Verleden G, Naesens M, Vanrenterghem Y: Drug interaction between mycophenolate mofetil and rifampin: possible induction of uridine diphosphate-glucuronosyltransferase. Clin Pharmacol Ther. 2005 Jul;78(1):81-8. [PubMed Link Image]
  2. Gurley BJ, Barone GW, Williams DK, Carrier J, Breen P, Yates CR, Song PF, Hubbard MA, Tong Y, Cheboyina S: Effect of milk thistle (Silybum marianum) and black cohosh (Cimicifuga racemosa) supplementation on digoxin pharmacokinetics in humans. Drug Metab Dispos. 2006 Jan;34(1):69-74. Epub 2005 Oct 12. [PubMed Link Image]
  3. Chen J, Raymond K: Roles of rifampicin in drug-drug interactions: underlying molecular mechanisms involving the nuclear pregnane X receptor. Ann Clin Microbiol Antimicrob. 2006 Feb 15;5:3. [PubMed Link Image]
  4. Lamba J, Strom S, Venkataramanan R, Thummel KE, Lin YS, Liu W, Cheng C, Lamba V, Watkins PB, Schuetz E: MDR1 genotype is associated with hepatic cytochrome P450 3A4 basal and induction phenotype. Clin Pharmacol Ther. 2006 Apr;79(4):325-38. Epub 2006 Feb 20. [PubMed Link Image]
  5. Huang R, Murry DJ, Kolwankar D, Hall SD, Foster DR: Vincristine transcriptional regulation of efflux drug transporters in carcinoma cell lines. Biochem Pharmacol. 2006 Jun 14;71(12):1695-704. Epub 2006 Apr 18. [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.