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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-05-26 19:12:41
Primary Accession Number DB00091
Secondary Accession Number
  • BIOD00003
  • BTD00003
Name Cyclosporine
Drug Type
  • Approved
  • Biotech
  • Investigational
Description A cyclic undecapeptide from an extract of soil fungi. It is a powerful immunosupressant with a specific action on T-lymphocytes. It is used for the prophylaxis of graft rejection in organ and tissue transplantation. (From Martindale, The Extra Pharmacopoeia, 30th ed).
Synonyms
  1. Ciclosporin
  2. Cyclosporin
  3. Cyclosporin A
  4. cyclosporine
Brand Names
  1. Gengraf (Abbott labs)
  2. Neoral (Novartis)
  3. Restasis
  4. Restasis (Allergan Inc)
  5. Sandimmune (Novartis)
  6. Sangcya
Brand Mixtures Not Available
Chemical IUPAC Name 30-ethyl-33-[(E,1R,2R)-1-hydroxy-2-methylhex-4-enyl]-1,4,7,10,12,15,19,25,28-nonamethyl-6,9,18,24-tetrakis(2-methylpropyl)-3,21-di(propan-2-yl)-1,4,7,10,13,16,19,22,25,28,31-undecazacyclotritriacontane-2,5,8,11,14,17,20,23,26,29,32-undecone
Chemical Formula C62H111N11O12
Chemical Structure Structure
Protein Sequence(s) Not Available
CAS Registry Number 59865-13-3
InChI Identifier InChI=1/C62H111N11O12/c1-25-27-28-40(15)52(75)51-56(79)65-43(26-2)58(81)67(18)33-48(74)68(19)44(29-34(3)4)55(78)66-49(38(11)12)61(84)69(20)45(30-35(5)6)54(77)63-41(16)53(76)64-42(17)57(80)70(21)46(31-36(7)8)59(82)71(22)47(32-37(9)10)60(83)72(23)50(39(13)14)62(85)73(51)24/h25,27,34-47,49-52,75H,26,28-33H2,1-24H3,(H,63,77)(H,64,76)(H,65,79)(H,66,78)/b27-25+/t40-,41?,42?,43?,44?,45?,46?,47?,49?,50?,51?,52-/m1/s1/f/h63-66H
InChI Key PMATZTZNYRCHOR-CCMIHKRJDW
KEGG Drug D00184 Link Image
KEGG Compound C05086 Link Image
PubChem Compound 6435893 Link Image
PubChem Substance 199551 Link Image
ChEBI ID 4031 Link Image
PharmGKB ID PA449167 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00593257 Link Image
RxList Link http://www.rxlist.com/cgi/generic/cyclosporine.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Cyclosporine Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Cyclosporine information is found in US patents 4108985; 4210581; 4220641; 4288431; 4396542; 4441644; 4554351; 4814323; 5767069; 5948884; 6444643
Average Molecular Weight 1202.6112
Monoisotopic Molecular Weight 1201.8414
State Liquid
Melting Point 148-151 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 9.53e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.92 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP 4.12 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -5.10 Calculated using ALOGPS
Experimental Caco2 Permeability -6.05 [ADME Research, USCD]
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 Not Available
Isomeric SMILES CC[C@@H]1NC(=O)[C@@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@@H](C(C)C)N(C)C(=O)[C@@H](CC(C)C)N(C)C(=O)[C@@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@@H](C)NC(=O)[C@@H](CC(C)C)N(C)C(=O)[C@@H](NC(=O)[C@@H](CC(C)C)N(C)C(=O)CN(C)C1=O)C(C)C
Canonical SMILES CCC1NC(=O)C(C(O)C(C)CC=CC)N(C)C(=O)C(C(C)C)N(C)C(=O)C(CC(C)C)N(C)C(=O)C(CC(C)C)N(C)C(=O)C(C)NC(=O)C(C)NC(=O)C(CC(C)C)N(C)C(=O)C(NC(=O)C(CC(C)C)N(C)C(=O)CN(C)C1=O)C(C)C
Drug Category
  • Antifungal Agents
  • Antirheumatic Agents
  • Dermatologic Agents
  • Enzyme Inhibitors
  • Immunomodulatory Agents
  • Immunosuppressive Agents
ATC Codes
AHFS Codes
  • 92:00.00
Indication For treatment of transplant rejection, rheumatoid arthritis, severe psoriasis
Pharmacology Used in immunosuppression for prophylactic treatment of organ transplants, cyclosporine exerts specific and reversible inhibition of immunocompetent lymphocytes in the G0-or G1-phase of the cell cycle. T-lymphocytes are preferentially inhibited. The T1-helper cell is the main target, although the T1-suppressor cell may also be suppressed. Sandimmune (cyclosporine) also inhibits lymphokine production and release including interleukin-2.
Mechanism of Action Cyclosporine binds to cyclophillin. The complex then inhibits calcineurin which is normally responsible for activating transcription of interleukin 2. Cyclosporine also inhibits lymphokine production and interleukin release. In ophthalmic applications, the precise mechanism of action is not known. Cyclosporine emulsion is thought to act as a partial immunomodulator in patients whose tear production is presumed to be suppressed due to ocular inflammation associated with keratoconjunctivitis sicca.
Absorption The absorption of cyclosporine from the gastrointestinal tract is incomplete and variable. Compared to an intravenous infusion, the absolute bioavailability of the oral solution is approximately 30% based upon the results in 2 patients.
Toxicity The oral LD50 is 2329 mg/kg in mice, 1480 mg/kg in rats, and > 1000 mg/kg in rabbits. The I.V. LD50 is 148 mg/kg in mice, 104 mg/kg in rats, and 46 mg/kg in rabbits.
Protein Binding Approximately 90% is bound to proteins, primarily lipoproteins.
Biotransformation Hepatic, extensively metabolized.
Half Life Biphasic and variable, approximately 7 hours (range 7 to 19 hours) in children and approximately 19 hours (range 10 to 27 hours) in adults.
Dosage Forms
Form Route
Capsule Oral
Liquid Intravenous
Solution Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acetazolamide Acetazolamide increases the effect and toxicity of cyclosporine
Allopurinol Allopurinol increases the effect and toxicity of cyclosporine
Amiodarone Amiodarone increases the effect and toxicity of cyclosporine
Amobarbital The barbiturate increases the effect of cyclosporine
Amphotericin B Monitor for nephrotoxicity
Amprenavir The protease inhibitor increases the effect of cyclosporine
Aprobarbital The barbiturate increases the effect of cyclosporine
Atazanavir Atazanavir increases the effect and toxicity of immunosuppressant
Atorvastatin Possible myopathy and rhabdomyolysis
Azithromycin The macrolide increases the effect of cyclosporine
Bosentan Increases the effect and toxicity of bosentan
Bupropion Bupropion decreases the effect of cyclosporine
Butabarbital The barbiturate increases the effect of cyclosporine
Butalbital The barbiturate increases the effect of cyclosporine
Butethal The barbiturate increases the effect of cyclosporine
Carbamazepine Carbamazepine decreases the effect of cyclosporine
Carvedilol Carvedilol increases the effect and toxicity of cyclosporine
Caspofungin Cyclosporine increases the effect and toxicity of caspofungin
Cerivastatin Possible myopathy and rhabdomyolysis
Chloramphenicol Chloramphenicol increases the effect of cyclosporine
Chloroquine Chloroquine increases the effect of cyclosporine
Cilastatin Imipenem increases the effect and toxicity of cyclosporine
Ciprofloxacin The quinolone increases the effect and toxicity of cyclosporine
Clarithromycin The macrolide increases the effect of cyclosporine
Clindamycin Clindamycin decreases the effect of cyclosporine
Colchicine Increased toxicity of both drugs
Danazol The androgen increases the effect and toxicity of cyclosporine
Diclofenac Monitor for nephrotoxicity
Digoxin Increases the effect of digoxin
Dihydroquinidine barbiturate The barbiturate increases the effect of cyclosporine
Diltiazem Diltiazem increases the effect and toxicity of cyclosporine
Efavirenz Efavirenz decreases the levels of cyclosporine
Erythromycin The macrolide increases the effect of cyclosporine
Ethinyl Estradiol The contraceptive increases the effect and toxicity of cyclosporine
Ethotoin The hydantoin decreases the effect of cyclosporine
Etodolac Monitor for nephrotoxicity
Etoposide Increases the effect of etoposide
Ezetimibe Increases the effect and toxicity of ezetimibe
Fenoprofen Monitor for nephrotoxicity
Fluconazole Fluconazole increases the effect of the immunosuppressant
Fluoxetine The antidepressant increases the effect and toxicity of cyclosporine
Flurbiprofen Monitor for nephrotoxicity
Fluvastatin Possible myopathy and rhabdomyolysis
Fosamprenavir The protease inhibitor increases the effect of cyclosporine
Foscarnet Monitor for nephrotoxicity
Fosphenytoin The hydantoin decreases the effect of cyclosporine
Glibenclamide The sulfonylurea increases the effect of cyclosporine
Glimepiride The sulfonylurea increases the effect of cyclosporine
Glipizide The sulfonylurea increases the effect of cyclosporine
Griseofulvin Griseofulvin decreases the effect of cyclosporine
Heptabarbital The barbiturate increases the effect of cyclosporine
Hexobarbital The barbiturate increases the effect of cyclosporine
Ibuprofen Monitor for nephrotoxicity
Imatinib Imatinib increases the effect and toxicity of cyclosporine
Imipenem Imipenem increases the effect and toxicity of cyclosporine
Indinavir The protease inhibitor increases the effect of cyclosporine
Indomethacin Monitor for nephrotoxicity
Itraconazole The imidazole increases the effect of immunosuppressant
Josamycin The macrolide increases the effect of cyclosporine
Ketoconazole The imidazole increases the effect of immunosuppressant
Ketoprofen Monitor for nephrotoxicity
Lovastatin Possible myopathy and rhabdomyolysis
Meclofenamic acid Monitor for nephrotoxicity
Mefenamic acid Monitor for nephrotoxicity
Melphalan Melphalan increases toxicity of cyclosporine
Mephenytoin The hydantoin decreases the effect of cyclosporine
Mestranol The contraceptive increases the effect and toxicity of cyclosporine
Methohexital The barbiturate increases the effect of cyclosporine
Methotrexate Increases the effect and toxicity of methotrexate
Methylphenidate Methylphenidate increases the effect and toxicity of cyclosporine
Methylphenobarbital The barbiturate increases the effect of cyclosporine
Metoclopramide Metoclopramide increases serum levels of cyclosporine
Modafinil Modafinil decreases the effect of cyclosporine
Muromonab Muromonab increases the levels of cyclosporine
Nabumetone Monitor for nephrotoxicity
Nafcillin Nafcillin alters serum levels of cyclosporine
Naproxen Monitor for nephrotoxicity
Nefazodone The antidepressant increases the effect and toxicity of cyclosporine
Nelfinavir The protease inhibitor increases the effect of cyclosporine
Nicardipine Nicardipine increases the effect and toxicity of cyclosporine
Nifedipine Increased risk of gingivitis
Norfloxacin The quinolone increases the effect and toxicity of cyclosporine
Octreotide Octreotide decreases the effect of cyclosporine
Omeprazole Omeprazole increases the effect and toxicity of cyclosporine
Orlistat Orlistat decreases the effect of cyclosporine
Oxaprozin Monitor for nephrotoxicity
Oxcarbazepine Oxcarbazepine decreases the effect of cyclosporine
Pentobarbital The barbiturate increases the effect of cyclosporine
Phenobarbital The barbiturate increases the effect of cyclosporine
Phenytoin The hydantoin decreases the effect of cyclosporine
Piroxicam Monitor for nephrotoxicity
Posaconazole Increased level of cyclosporine
Pravastatin Possible myopathy and rhabdomyolysis
Primidone The barbiturate increases the effect of cyclosporine
Probucol Probucol decreases the effect of cyclosporine
Propafenone Propafenone increases the effect and toxicity of cyclosporine
Pyrazinamide Pyrazinamide decreases the effect of cyclosporine
Quinidine barbiturate The barbiturate increases the effect of cyclosporine
Quinupristin Synercid increases the effect of cyclosporine
Repaglinide Increases repaglinide's effect
Rifabutin The rifamycin decreases the effect of cyclosporine
Rifampin The rifamycin decreases the effect of cyclosporine
Ritonavir The protease inhibitor increases the effect of cyclosporine
Rosuvastatin Increases the effect and toxicity of rosuvastatin
Roxithromycin The macrolide increases the effect of cyclosporine
Saquinavir The protease inhibitor increases the effect of cyclosporine
Secobarbital The barbiturate increases the effect of cyclosporine
Sevelamer Sevelamer decreases the effect of cyclosporine
Sibutramine Sibutramine increases the effect and toxicity of cyclosporine
Simvastatin Possible myopathy and rhabdomyolysis
Sirolimus Increases the effect and toxicity of sirolimus
St. John's Wort St. John's Wort decreases the effect of cyclosporine
Sulfadiazine The sulfonamide decreases the effect of cyclosporine
Sulfamethazine The sulfonamide decreases the effect of cyclosporine
Sulfamethoxazole The sulfonamide decreases the effect of cyclosporine
Sulfasalazine The sulfonamide decreases the effect of cyclosporine
Sulfinpyrazone Sulfinpyrazone decreases the effect of cyclosporine
Sulindac Monitor for nephrotoxicity
Tacrolimus Additive toxicities for these agents
Talbutal The sulfonamide decreases the effect of cyclosporine
Telithromycin Telithromycin may possibly increase this agent effect/toxicity
Tenoxicam Monitor for nephrotoxicity
Terbinafine Terbinafine decreases the effect of cyclosporine
Tiaprofenic acid Monitor for nephrotoxicity
Ticlopidine Ticlopidine decreases the effect of cyclosporine
Tolmetin Monitor for nephrotoxicity
Troglitazone Troglitazone decreases the effect of the immunosuppressant
Troleandomycin The macrolide increases the effect of cyclosporine
Ursodeoxycholic acid Ursodiol increases the levels of cyclosporine
Verapamil Verapamil increases the effect of cyclosporine
Voriconazole Voriconazole increases the effect and toxicity of cyclosporine
Food Interactions
  • Avoid salt substitutes containing potassium.
  • Avoid taking with grapefruit or grapefruit juice as grapefruit can significantly increase serum levels of this product.
  • Red wine may reduce cyclosporine levels due to increased metabolism, therefore it appears prudent to avoid red wine (white wine does not appear to affect cyclosporine metabolism).
  • Take without regard to meals.
Pathways Not Available
General References
  1. Lichtiger S, Present DH, Kornbluth A, Gelernt I, Bauer J, Galler G, Michelassi F, Hanauer S: Cyclosporine in severe ulcerative colitis refractory to steroid therapy. N Engl J Med. 1994 Jun 30;330(26):1841-5. [PubMed Link Image]
  2. [PubMed Link Image]
  3. Drugs.com Link Image
  4. [PubMed Link Image]
  5. Wikipedia Link Image
  6. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A5 (CYP3A5)
Targets
  1. Calcium signal-modulating cyclophilin ligand
  2. Peptidyl-prolyl cis-trans isomerase A
  3. Multidrug resistance protein 1
  4. Photoreceptor
  5. Calcineurin subunit B isoform 2
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A5 (CYP3A5)
Enzyme 1 Gene Name CYP3A5
Enzyme 1 SwissProt ID P20815 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P20815|CP3A5_HUMAN Cytochrome P450 3A5 
MDLIPNLAVETWLLLAVSLVLLYLYGTRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKF
DTECYKKYGKMWGTYEGQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISL
AEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIFGAYS
MDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILFPFLTPVFEALNVSL
FPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMIDSQNSKETESHKALSDLELAAQSI
IFIFAGYETTSSVLSFTLYELATHPDVQQKLQKEIDAVLPNKAPPTYDAVVQMEYLDMVV
NETLRLFPVAIRLERTCKKDVEINGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFS
KKKDSIDPYIYTPFGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQG
LLQPEKPIVLKVDSRDGTLSGE
Drug Target 1 [top]
Target 1 ID 421
Target 1 Name Calcium signal-modulating cyclophilin ligand
Target 1 Synonyms
  1. CAML
Target 1 Gene Name CAMLG
Target 1 Protein Sequence >Calcium signal-modulating cyclophilin ligand 
MESMAVATDGGERPGVPAGSGLSASQRRAELRRRKLLMNSEQRINRIMGFHRPGSGAEEE
SQTKSKQQDSDKLNSLSVPSVSKRVVLGDSVSTGTTDQQGGVAEVKGTQLGDKLDSFIKP
PECSSDVNLELRQRNRGDLTADSVQRGSRHGLEQYLSRFEEAMKLRKQLISEKPSQEDGN
TTEEFDSFRIFRLVGCALLALGVRAFVCKYLSIFAPFLTLQLAYMGLYKYFPKSEKKIKT
TVLTAALLLSGIPAEVINRSMDTYSKMGEVFTDLCVYFFTFIFCHELLDYWGSEVP
Target 1 Number of Residues 300
Target 1 Molecular Weight 32953
Target 1 Theoretical pI 8.19
Target 1 GO Classification Not Available
Target 1 General Function Involved in cyclophilin binding
Target 1 Specific Function Likely involved in the mobilization of calcium as a result of the TCR/CD3 complex interaction. Binds to cyclophilin B
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function Not Available
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 190-210
  • 241-257
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 619670 Link Image
Target 1 UniProtKB/Swiss-Prot ID P49069 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name CAMLG_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 1 Gene Sequence >891 bp 
ATGGAGTCGATGGCCGTCGCTACCGACGGCGGGGAGAGGCCGGGGGTCCCAGCGGGCTCA
GGTCTGTCGGCTTCCCAGCGTCGGGCGGAGCTGCGTCGGAGAAAGCTGCTCATGAACTCG
GAACAGCGCATCAACCGGATCATGGGCTTTCACAGGCCCGGGAGCGGCGCGGAAGAAGAA
AGTCAAACAAAATCAAAGCAGCAGGACAGTGATAAACTGAACTCCCTCAGCGTTCCTTCC
GTTTCAAAGCGAGTAGTGCTGGGTGATTCAGTCAGTACAGGAACAACTGACCAGCAGGGT
GGTGTGGCCGAGGTAAAGGGGACCCAACTGGGAGACAAATTGGACTCGTTCATTAAACCA
CCTGAGTGCAGTAGTGATGTCAACCTTGAGCTCCGGCAGCGGAACAGAGGGGACCTGACA
GCGGACTCGGTCCAGAGGGGTTCCCGCCATGGCCTAGAGCAGTACCTTTCCAGATTCGAA
GAAGCAATGAAGCTAAGGAAACAGCTGATTAGTGAAAAACCCAGTCAAGAGGATGGAAAT
ACAACAGAAGAATTTGACTCTTTTCGAATATTTAGATTGGTGGGATGTGCTCTTCTTGCT
CTTGGAGTCAGAGCTTTTGTTTGCAAATACTTGTCCATATTTGCTCCATTTCTTACTTTA
CAACTTGCGTACATGGGATTATACAAATATTTTCCCAAGAGTGAAAAGAAGATAAAGACA
ACAGTACTAACAGCTGCACTTCTATTGTCGGGAATTCCTGCCGAAGTGATAAATCGATCA
ATGGATACCTATAGCAAAATGGGCGAAGTCTTCACAGATCTCTGTGTCTACTTTTTCACT
TTTATCTTTTGTCATGAACTGCTTGATTATTGGGGCTCTGAAGTACCATGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID CAMLG Link Image
Target 1 GenAtlas ID CAMLG Link Image
Target 1 HGNC ID HGNC:1471 Link Image
Target 1 Chromosome Location 5
Target 1 Locus 5q23
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Bram RJ, Crabtree GR: Calcium signalling in T cells stimulated by a cyclophilin B-binding protein. Nature. 1994 Sep 22;371(6495):355-8. [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]
Drug Target 2 [top]
Target 2 ID 1524
Target 2 Name Peptidyl-prolyl cis-trans isomerase A
Target 2 Synonyms
  1. Cyclophilin A
  2. Cyclosporin A-binding protein
  3. EC 5.2.1.8
  4. PPIase A
  5. Rotamase A
Target 2 Gene Name PPIA
Target 2 Protein Sequence >Peptidyl-prolyl cis-trans isomerase A 
MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGF
MCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE
WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE
Target 2 Number of Residues 167
Target 2 Molecular Weight 18013
Target 2 Theoretical pI 7.97
Target 2 GO Classification
Function
Not Available
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
protein folding
Component
Not Available
Target 2 General Function Posttranslational modification, protein turnover, chaperones
Target 2 Specific Function PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
Target 2 Pathways Not Available
Target 2 Reactions
  • peptidylproline (omega=180) = peptidylproline (omega=0)
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 30309 Link Image
Target 2 UniProtKB/Swiss-Prot ID P62937 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name PPIA_HUMAN Link Image
Target 2 PDB ID 1CWM Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasm
Target 2 Gene Sequence >498 bp 
ATGGTCAACCCCACCGTGTTCTTCGACATTGCCGTCGACGGCGAGCCCTTGGGCCGCGTC
TCCTTTGAGCTGTTTGCAGACAAGGTCCCAAAGACAGCAGAAAATTTTCGTGCTCTGAGC
ACTGGAGAGAAAGGATTTGGTTATAAGGGTTCCTGCTTTCACAGAATTATTCCAGGGTTT
ATGTGTCAGGGTGGTGACTTCACACGCCATAATGGCACTGGTGGCAAGTCCATCTATGGG
GAGAAATTTGAAGATGAGAACTTCATCCTAAAGCATACGGGTCCTGGCATCTTGTCCATG
GCAAATGCTGGACCCAACACAAATGGTTCCCAGTTTTTCATCTGCACTGCCAAGACTGAG
TGGTTGGATGGCAAGCATGTGGTGTTTGGCAAAGTGAAAGAAGGCATGAATATTGTGGAG
GCCATGGAGCGCTTTGGGTCCAGGAATGGCAAGACCAGCAAGAAGATCACCATTGCTGAC
TGTGGACAACTCGAATAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID PPIA Link Image
Target 2 GenAtlas ID PPIA Link Image
Target 2 HGNC ID HGNC:9253 Link Image
Target 2 Chromosome Location 7
Target 2 Locus 7p13
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  2. Kallen J, Spitzfaden C, Zurini MG, Wider G, Widmer H, Wuthrich K, Walkinshaw MD: Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature. 1991 Sep 19;353(6341):276-9. [PubMed Link Image]
  3. Ke HM, Zydowsky LD, Liu J, Walsh CT: Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9483-7. [PubMed Link Image]
  4. Liu J, Chen CM, Walsh CT: Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. Biochemistry. 1991 Mar 5;30(9):2306-10. [PubMed Link Image]
  5. Haendler B, Hofer E: Characterization of the human cyclophilin gene and of related processed pseudogenes. Eur J Biochem. 1990 Jul 5;190(3):477-82. [PubMed Link Image]
  6. Haendler B, Hofer-Warbinek R, Hofer E: Complementary DNA for human T-cell cyclophilin. EMBO J. 1987 Apr;6(4):947-50. [PubMed Link Image]
  7. Meier U, Beier-Hellwig K, Klug J, Linder D, Beier HM: Identification of cyclophilin A from human decidual and placental tissue in the first trimester of pregnancy. Hum Reprod. 1995 May;10(5):1305-10. [PubMed Link Image]
  8. Mikol V, Kallen J, Pflugl G, Walkinshaw MD: X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution. J Mol Biol. 1993 Dec 20;234(4):1119-30. [PubMed Link Image]
  9. Theriault Y, Logan TM, Meadows R, Yu L, Olejniczak ET, Holzman TF, Simmer RL, Fesik SW: Solution structure of the cyclosporin A/cyclophilin complex by NMR. Nature. 1993 Jan 7;361(6407):88-91. [PubMed Link Image]
  10. Pflugl G, Kallen J, Schirmer T, Jansonius JN, Zurini MG, Walkinshaw MD: X-ray structure of a decameric cyclophilin-cyclosporin crystal complex. Nature. 1993 Jan 7;361(6407):91-4. [PubMed Link Image]
  11. 8513493 Luban J, Bossolt KL, Franke EK, Kalpana GV, Goff SP: Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell. 1993 Jun 18;73(6):1067-78.
  12. 8652511 Zhao Y, Ke H: Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization. Biochemistry. 1996 Jun 11;35(23):7356-61.
  13. 9299338 Ottiger M, Zerbe O, Guntert P, Wuthrich K: The NMR solution conformation of unligated human cyclophilin A. J Mol Biol. 1997 Sep 12;272(1):64-81.
  14. 9385632 Vajdos FF, Yoo S, Houseweart M, Sundquist WI, Hill CP: Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein. Protein Sci. 1997 Nov;6(11):2297-307.
  15. 9769216 Kallen J, Mikol V, Taylor P, Walkinshaw MD: X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A. J Mol Biol. 1998 Oct 23;283(2):435-49.
Target 2 Drug References
  1. Keckesova Z, Ylinen LM, Towers GJ: Cyclophilin A renders human immunodeficiency virus type 1 sensitive to Old World monkey but not human TRIM5 alpha antiviral activity. J Virol. 2006 May;80(10):4683-90. [PubMed Link Image]
  2. Patwardhan AM, Jeske NA, Price TJ, Gamper N, Akopian AN, Hargreaves KM: The cannabinoid WIN 55,212-2 inhibits transient receptor potential vanilloid 1 (TRPV1) and evokes peripheral antihyperalgesia via calcineurin. Proc Natl Acad Sci U S A. 2006 Jul 25;103(30):11393-8. Epub 2006 Jul 18. [PubMed Link Image]
  3. Redell JB, Zhao J, Dash PK: Acutely increased cyclophilin a expression after brain injury: a role in blood-brain barrier function and tissue preservation. J Neurosci Res. 2007 Jul;85(9):1980-8. [PubMed Link Image]
  4. Schaller T, Ylinen LM, Webb BL, Singh S, Towers GJ: Fusion of cyclophilin A to Fv1 enables cyclosporine-sensitive restriction of human and feline immunodeficiency viruses. J Virol. 2007 Sep;81(18):10055-63. Epub 2007 Jul 3. [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. Grenier J, Fradette C, Morelli G, Merritt GJ, Vranderick M, Ducharme MP: Pomelo juice, but not cranberry juice, affects the pharmacokinetics of cyclosporine in humans. Clin Pharmacol Ther. 2006 Mar;79(3):255-62. Epub 2006 Feb 7. [PubMed Link Image]
  2. Bachmakov I, Werner U, Endress B, Auge D, Fromm MF: Characterization of beta-adrenoceptor antagonists as substrates and inhibitors of the drug transporter P-glycoprotein. Fundam Clin Pharmacol. 2006 Jun;20(3):273-82. [PubMed Link Image]
  3. Kotrych K, Masiuk M, Domanski L, Rozanski J, Drozdzik M: Peripheral blood lymphocytes P-glycoprotein (P-gp, gp-170) expression in allogenic kidney transplant patients. Nephrology (Carlton). 2006 Jun;11(3):257-60. [PubMed Link Image]
  4. Thuerauf N, Fromm MF: The role of the transporter P-glycoprotein for disposition and effects of centrally acting drugs and for the pathogenesis of CNS diseases. Eur Arch Psychiatry Clin Neurosci. 2006 Aug;256(5):281-6. [PubMed Link Image]
  5. Nagira M, Tomita M, Mizuno S, Kumata M, Ayabe T, Hayashi M: Ischemia/reperfusion injury in the monolayers of human intestinal epithelial cell line caco-2 and its recovery by antioxidants. Drug Metab Pharmacokinet. 2006 Jun;21(3):230-7. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 3867
Target 4 Name Photoreceptor
Target 4 Synonyms Not Available
Target 4 Gene Name Not Available
Target 4 Protein Sequence >Photoreceptor 
SSTTSAKSKHSVRVAQTTADAALEAVYEMSGDSGDSFDYSKSVGQSAESVPAGAVTAYLQ
RMQRGGLIQNFGCMVAVEEPNFCVIAYSENASEFLDLIPQAVPSMGEMDVLGIGTDIRTL
FTPSSSAALEKAAATQDISLLNPITVHCRRSGKPLYAIAHRIDIGIVIDFEAVKMIDVPV
SAAAGALQSHKLAARAITRLQALPGGDIELLCDTIVEEVRELTGYDRVMAFKFHEDEHGE
VVAEIRRMDLEPYMGLHYPATDIPQASRFLLMKNRVRLIADCYASPVKLIQDLDIRQPVS
LAGSTLRAPHGCHAQYMGNMGSIASLVMAVIINDNEEYSRGAIQRGRKLWGLVVCQHTSP
RTVPFPLRSVCEFLMQVFGMQLNLHVELGAQLREKHILRTQTLLCDMLLRDAPIGIVSQT
PNIMDLVKCDGAALYYGKRVWLLGTTPTENQIKEIADWLLEHHNDSTGLSTDSLADANYP
GAHLLGDAVCGMAAAKITAKDFLFWFRSHTATEVKWGGAKHDPDEKDDGRKMHPRSSFKA
FLEVVNKRSPPWEDVEMDAIHSLQLILRGSFRDIADSDTKTMIHARLNDLKLQGVEERNA
LANEMSRVLETAAAPILAVDSRGMINAWNAKIAQVTGLPVEEAMHCSLTKDLVLDESVVV
VERLLSLALQGEEEQNVEIKLKTFGTQTTERAVILIVNACCSRDASDTVVGVFFVGQDVT
EQRMFMDRFTRIQGGEKTTVQDPHPLMRPSFDGDEFGRTFKRNSALGGLKDHATGSVERL
DLYLRRAEECMEVMETIPSPKFNNKQCQYLAGKLKAVLQSASLFLRISHHEHHELGASID
MGRHVEIFKLLLALAKEIESFIQGCCKDEWIKAAMTLTNVSEYVSSMGFNLELCKIAFCK
SCAASGSLTLDQIEVICKDEAEVVKRNATIDVDTLFAKVIYDLTEKTLSSDQNDLAIYLL
QRLKRAKPILPSFSSRPSWWNFYDDWSFSEKFFQWIQITGSLGSGSSATVEKAVWLGTPV
AKKTFYGRDNEDFKREVEILAELCHPNITSMFCSPLYRRKCSIIMELMDGDLLALMQRRL
DGNEDHDSPPFSTLEVVDIILQTGEGMNYLHEKGIIHRDLKSMNILVKSVKVTKSEIGYV
HVKVADFGLSKTKDSSTRYSNQTWNRGTNRWMAPEVINLGYESTEGEISFDGKVPKYPLK
SDVYSFGMVCYEVLTGDVPFPEEKNPNNVKRMVLEGVRPDLPAHCPIELKALITDCWNQD
PLKRPSFAVICQKLKYLKYLLMTGFSSYQDSYPSTEELS
Target 4 Number of Residues 1320
Target 4 Molecular Weight 144708
Target 4 Theoretical pI 5.86
Target 4 GO Classification
Function
protein serine/threonine kinase activity
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
receptor activity
transmembrane receptor activity
G-protein coupled receptor activity
rhodopsin-like receptor activity
G-protein coupled photoreceptor activity
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
protein kinase activity
protein histidine kinase activity
two-component sensor molecule activity
signal transducer activity
Process
physiological process
metabolism
macromolecule metabolism
biopolymer metabolism
biopolymer modification
protein modification
protein amino acid phosphorylation
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
two-component signal transduction system (phosphorelay)
cellular process
cell communication
signal transduction
Component
Not Available
Target 4 General Function Not Available
Target 4 Specific Function Not Available
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Essential
Target 4 GenBank ID Protein 1813953 Link Image
Target 4 UniProtKB/Swiss-Prot ID P93098 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name P93098_CERPU Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location Not Available
Target 4 Gene Sequence >3902 bp 
ACTCTTCAACAACCTCAGCAAAGTCGAAGCATAGCGTGCGGGTCGCTCAAACTACGGCAG
ATGCAGCTCTTGAAGCTGTGTACGAAATGTCTGGGGACTCCGGGGACTCTTTTGACTACT
CAAAATCTGTTGGTCAATCTGCAGAGTCGGTTCCTGCAGGGGCAGTAACAGCCTACCTAC
AGCGTATGCAGAGGGGAGGTTTAATCCAAAATTTTGGGTGTATGGTAGCAGTTGAAGAGC
CGAATTTCTGTGTTATAGCGTACAGTGAGAATGCCTCCGAGTTTCTAGATCTGATACCCC
AGGCCGTCCCAAGTATGGGGGAGATGGACGTGCTAGGAATCGGGACGGATATAAGAACTT
TATTCACACCGTCGAGTAGTGCCGCTCTTGAGAAGGCAGCTGCAACTCAGGATATAAGCC
TTCTTAACCCAATCACTGTTCATTGCAGACGCTCAGGGAAACCGTTATATGCCATTGCCC
ATCGCATAGACATTGGTATAGTCATTGACTTTGAGGCGGTGAAAATGATTGATGTTCCAG
TTTCAGCTGCTGCCGGTGCACTGCAATCTCACAAACTTGCGGCCCGGGCTATTACACGAC
TTCAAGCATTACCTGGAGGCGACATAGAGTTGCTTTGTGATACTATTGTTGAGGAGGTGC
GGGAACTTACTGGGTATGACAGGGTGATGGCTTTTAAATTTCATGAAGATGAGCATGGCG
AAGTTGTGGCAGAAATACGTCGCATGGATCTTGAGCCCTATATGGGTCTCCATTATCCGG
CCACTGACATTCCCCAGGCGTCCCGTTTTCTGTTAATGAAGAACAGGGTGCGGTTGATAG
CTGATTGCTATGCGTCTCCAGTGAAACTCATACAAGATCTAGACATTAGGCAGCCAGTCA
GCTTGGCAGGTTCGACTTTACGTGCCCCGCATGGATGTCATGCCCAGTACATGGGTAACA
TGGGCTCCATTGCGTCGCTTGTCATGGCCGTAATCATCAATGATAACGAGGAATATTCAC
GTGGGGCAATTCAAAGAGGTAGAAAGCTGTGGGGACTCGTAGTGTGTCAGCATACATCTC
CACGAACTGTACCGTTTCCACTTCGGTCTGTGTGCGAGTTTTTGATGCAGGTATTTGGTA
TGCAGCTCAACCTCCATGTTGAGCTGGGCGCTCAACTAAGGGAAAAACATATTCTCAGAA
CTCAAACTCTTCTTTGTGACATGCTTCTTCGAGATGCTCCTATTGGAATTGTATCTCAAA
CTCCAAATATTATGGATCTTGTGAAATGTGATGGAGCAGCTCTTTACTATGGGAAGCGAG
TGTGGCTTCTTGGCACGACACCGACTGAGAATCAGATCAAAGAGATTGCAGACTGGTTGC
TAGAGCATCACAACGACTCAACAGGTCTTAGTACGGATAGTTTAGCGGATGCGAATTATC
CAGGTGCACACCTGCTTGGCGACGCTGTTTGTGGTATGGCAGCTGCAAAAATCACTGCGA
AGGATTTCCTTTTCTGGTTCAGGTCTCACACTGCTACAGAGGTCAAATGGGGTGGTGCTA
AACACGATCCAGATGAAAAAGATGATGGCCGAAAAATGCATCCCAGAAGCTCTTTCAAAG
CCTTTTTAGAGGTTGTGAACAAAAGAAGTCCACCCTGGGAAGACGTAGAAATGGATGCTA
TACATTCCCTTCAGCTCATTCTACGTGGCTCCTTTCGAGATATTGCTGACAGCGACACAA
AGACCATGATCCACGCACGTCTGAATGACTTGAAGCTTCAGGGCGTGGAAGAACGAAACG
CCCTCGCTAATGAGATGTCGCGCGTATTAGAAACCGCGGCTGCCCCAATCCTGGCGGTTG
ATTCAAGGGGAATGATTAATGCTTGGAATGCAAAAATAGCACAGGTCACAGGGCTTCCAG
TCGAAGAGGCTATGCATTGTTCGTTGACGAAAGATCTCGTGTTGGATGAGTCAGTGGTGG
TTGTTGAGAGATTACTTTCTCTGGCGTTGCAAGGTGAGGAGGAGCAGAATGTGGAAATCA
AGTTGAAGACCTTTGGCACTCAGACCACTGAAAGAGCAGTTATTCTGATTGTTAACGCCT
GCTGCTCTAGAGATGCGTCGGACACTGTTGTTGGCGTTTTCTTTGTGGGCCAAGATGTAA
CTGAGCAGAGAATGTTCATGGACAGGTTTACTCGTATACAAGGTGGTGAAAAGACCACTG
TCCAGGACCCCCACCCTCTCATGCGTCCAAGTTTTGATGGTGACGAATTTGGACGCACTT
TCAAGAGGAACTCAGCATTGGGGGGTTTGAAAGATCATGCTACCGGATCAGTGGAAAGAC
TTGATTTGTACCTGAGGCGCGCAGAAGAATGTATGGAGGTAATGGAAACGATTCCTTCAC
CAAAATTTAACAACAAGCAGTGCCAATATCTTGCTGGTAAACTCAAAGCAGTTCTTCAGA
GTGCAAGCTTGTTCTTAAGGATATCGCATCATGAACACCATGAACTTGGTGCGTCTATAG
ACATGGGAAGACATGTTGAAATCTTCAAGCTACTGCTTGCATTGGCAAAGGAGATTGAAA
GCTTCATTCAAGGATGCTGCAAAGATGAGTGGATCAAAGCTGCAATGACATTGACAAACG
TGTCGGAGTACGTCTCATCAATGGGATTTAACTTGGAGCTGTGTAAAATTGCCTTCTGCA
AGTCATGTGCAGCAAGTGGAAGCCTCACATTAGATCAAATTGAAGTCATCTGCAAAGATG
AAGCCGAAGTCGTGAAAAGAAATGCTACTATTGATGTAGACACCCTATTTGCGAAGGTAA
TATATGATCTGACTGAGAAGACCTTGAGTAGTGATCAGAATGATCTGGCCATCTACTTAC
TCCAAAGACTTAAAAGAGCCAAGCCTATTCTGCCCTCTTTCTCATCACGACCATCTTGGT
GGAATTTTTATGATGATTGGAGTTTTTCTGAAAAATTCTTTCAGTGGATCCAAATAACAG
GGAGCTTGGGAAGTGGTTCTTCAGCAACTGTAGAAAAGGCAGTGTGGTTGGGAACTCCAG
TTGCCAAGAAGACATTCTATGGACGCGATAACGAAGATTTCAAGAGGGAAGTTGAAATCT
TAGCAGAATTATGTCATCCGAACATCACCTCCATGTTTTGTAGTCCTCTCTACAGGCGCA
AGTGTTCCATTATTATGGAGTTGATGGATGGAGATCTCCTTGCTTTGATGCAAAGAAGAT
TGGACGGAAATGAAGATCATGATTCTCCTCCATTTTCCACTTTGGAAGTTGTTGATATTA
TCCTTCAAACAGGTGAAGGCATGAATTACCTTCATGAAAAAGGAATCATTCACAGGGATC
TGAAGTCAATGAACATTCTTGTGAAAAGTGTGAAGGTAACAAAATCGGAGATTGGATATG
TGCATGTCAAGGTAGCTGACTTTGGTCTTTCAAAGACAAAAGATTCTAGCACAAGATATT
CAAACCAGACTTGGAACAGGGGTACCAATAGATGGATGGCTCCCGAAGTTATAAACCTTG
GTTACGAAAGTACTGAAGGAGAAATCTCATTTGATGGGAAGGTGCCAAAATACCCACTTA
AATCCGATGTTTACAGTTTCGGGATGGTTTGCTATGAGGTATTGACTGGAGATGTTCCTT
TCCCAGAAGAAAAGAATCCCAATAATGTAAAGAGAATGGTCCTGGAGGGTGTCCGCCCAG
ACTTACCTGCTCATTGTCCAATTGAGCTGAAGGCTTTGATTACAGATTGTTGGAACCAAG
ACCCTCTCAAGAGACCGTCCTTTGCTGTCATCTGTCAAAAATTGAAATATTTAAAATATT
TATTGATGACAGGTTTCAGTTCCTATCAAGACTCTTATCCCTCAACTGAAGAACTATCGT
AA
Target 4 GenBank Gene ID
Target 4 GeneCard ID Not Available
Target 4 GenAtlas ID Not Available
Target 4 HGNC ID Not Available
Target 4 Chromosome Location Not Available
Target 4 Locus Not Available
Target 4 SNPs Not Available
Target 4 General References Not Available
Target 4 Drug References
  1. Wang S, Lu B, Wood P, Lund RD: Grafting of ARPE-19 and Schwann cells to the subretinal space in RCS rats. Invest Ophthalmol Vis Sci. 2005 Jul;46(7):2552-60. [PubMed Link Image]
  2. 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]
  3. 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]
Drug Target 5 [top]
Target 5 ID 3868
Target 5 Name Calcineurin subunit B isoform 2
Target 5 Synonyms
  1. CBLP
  2. CNBII
  3. Calcineurin B-like protein
  4. Protein phosphatase 2B regulatory subunit 2
  5. Protein phosphatase 3 regulatory subunit B beta isoform
Target 5 Gene Name PPP3R2
Target 5 Protein Sequence >Calcineurin subunit B isoform 2 
MGNEASYPAEMCSHFDNDEIKRLGRRFKKLDLDKSGSLSVEEFMSLPELRHNPLVRRVID
VFDTDGDGEVDFKEFILGTSQFSVKGDEEQKLRFAFSIYDMDKDGYISNGELFQVLKMMV
GNNLTDWQLQQLVDKTIIILDKDGDGKISFEEFSAVVRDLEIHKKLVLIV
Target 5 Number of Residues 172
Target 5 Molecular Weight 19533
Target 5 Theoretical pI 4.49
Target 5 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 5 General Function Not Available
Target 5 Specific Function Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity
Target 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 33150800 Link Image
Target 5 UniProtKB/Swiss-Prot ID Q96LZ3 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name CANB2_HUMAN Link Image
Target 5 PDB ID Not Available
Target 5 Cellular Location Not Available
Target 5 Gene Sequence >513 bp 
ATGGGAAACGAGGCCAGTTACCCGGCGGAGATGTGCTCCCACTTTGACAATGATGAAATT
AAAAGGCTGGGCAGGAGGTTTAAGAAGTTGGACTTGGACAAATCAGGGTCTCTGAGCGTG
GAGGAGTTCATGTCCCTGCCGGAGCTGCGCCACAACCCGTTGGTGCGGCGAGTGATCGAC
GTCTTCGACACCGACGGTGATGGAGAAGTGGACTTCAAGGAATTCATCCTGGGGACCTCC
CAGTTCAGCGTCAAGGGCGACGAGGAGCAGAAGTTGAGGTTTGCGTTCAGCATTTACGAC
ATGGATAAAGATGGCTACATTTCCAACGGGGAGCTCTTCCAGGTGCTGAAGATGATGGTG
GGCAACAACCTGACGGACTGGCAGCTCCAGCAGCTGGTCGACAAAACCATCATCATCCTG
GACAAGGATGGCGATGGGAAGATATCCTTTGAGGAATTCAGTGCTGTGGTCAGAGACCTG
GAGATCCACAAGAAGCTGGTCCTCATCGTATGA
Target 5 GenBank Gene ID
Target 5 GeneCard ID PPP3R2 Link Image
Target 5 GenAtlas ID PPP3R2 Link Image
Target 5 HGNC ID HGNC:9318 Link Image
Target 5 Chromosome Location 9
Target 5 Locus 9q31.1
Target 5 SNPs SNPJam Report Link Image
Target 5 General References Not Available
Target 5 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]

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.