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Showing drug card for Colchicine (DB01394)

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Version 2.5
Creation Date 2007-07-08 17:02:26
Update Date 2009-02-19 16:04:20
Primary Accession Number DB01394
Secondary Accession Number Not Available
Name Colchicine
Drug Type
  • Approved
  • Small Molecule
Description A major alkaloid from Colchicum autumnale L. and found also in other Colchicum species. Its primary therapeutic use is in the treatment of gout, but it has been used also in the therapy of familial Mediterranean fever (periodic disease). [PubChem]
Synonyms
  1. Colchicin
  2. Colchicina
  3. Colchicinum
Brand Names
  1. Col-probenecid
  2. Colbenemid
  3. Condylon
  4. Proben-C
Brand Mixtures
  1. Arnix Gel (Colchicine + Hahnemann's Causticum + Ivy + Ledum Palustre + Poison Ivy + Propolis + Rhododendron Chrysanthemum + Thuja Occidentalis)
  2. Arnix HP (Apis Mellifica + Bryonia + Colchicine + Hahnemann's Causticum + Ivy + Ledum Palustre + Poison Ivy + Pulsatilla + Rhododendron Chrysanthemum)
  3. Art HP (Apis Mellifica + Bryonia + Colchicine + Hahnemann's Causticum + Ivy + Ledum Palustre + Poison Ivy + Pulsatilla + Rhododendron Chrysanthemum)
  4. DB HP (Colchicine + Eugenia Jambolana + Lactic Acid + Lycopodium Clavatum + Phosphoric Acid + Phosphorus + Uranium Nitrate)
  5. Edemnix HP (Apis Mellifica + Cinchona Officinalis + Colchicine + Ledum Palustre + Lycopodium Clavatum + Poison Ivy + Sambucus Nigra + Strophanthus Hispidus)
  6. Edma HP (Apis Mellifica + Cinchona Officinalis + Colchicine + Ledum Palustre + Lycopodium Clavatum + Poison Ivy + Sambucus Nigra + Strophanthus Hispidus)
  7. Jnt-Nix HP (Bryonia + Colchicine + Kalmia Latifolia + Ledum Palustre + Lycopodium Clavatum + Poison Ivy + Rhododendron Chrysanthemum)
  8. Sciat HP (Aconitinum + Arnica Montana + Colchicine + Esculin + Hypericum Perforatum + Magnesium Phosphate Dibasic + Plumbum Metallicum + Poison Ivy)
  9. Sciatinix HP (Aconitinum + Arnica Montana + Colchicine + Esculin + Hypericum Perforatum + Magnesium Phosphate Dibasic + Plumbum Metallicum + Poison Ivy)
  10. Sucurnix HP (Colchicine + Eugenia Jambolana + Lactic Acid + Lycopodium Clavatum + Phosphoric Acid + Phosphorus + Uranium Nitrate)
Chemical IUPAC Name N-[(7S)-1,2,3,10-tetramethoxy-9-oxo-6,7-dihydro-5H-benzo[d]heptalen-7-yl]acetamide
Chemical Formula C22H25NO6
Chemical Structure Structure
CAS Registry Number 64-86-8
InChI Identifier InChI=1/C22H25NO6/c1-12(24)23-16-8-6-13-10-19(27-3)21(28-4)22(29-5)20(13)14-7-9-18(26-2)17(25)11-15(14)16/h7,9-11,16H,6,8H2,1-5H3,(H,23,24)/t16-/m0/s1/f/h23H
InChI Key IAKHMKGGTNLKSZ-IKNPWOKSDD
KEGG Drug D00570 Link Image
KEGG Compound C07592 Link Image
PubChem Compound 6167 Link Image
PubChem Substance 7847636 Link Image
ChEBI ID Not Available
PharmGKB ID PA449092 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00000396 Link Image
RxList Link http://www.rxlist.com/cgi/generic/colch.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Colchicine Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 399.4370
Monoisotopic Molecular Weight 399.1682
State Solid
Melting Point 156 oC
Experimental Water Solubility 45 mg/mL at 25 oC [SEIDELL,A (1941)] Source: PhysProp
Predicted Water Solubility 2.76e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 1.30 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP 1.59 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.16 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 1.85
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 COC1=CC=C2C(=CC1=O)[C@H](CCC1=CC(OC)=C(OC)C(OC)=C21)NC(C)=O
Canonical SMILES COC1=CC=C2C(=CC1=O)C(CCC1=CC(OC)=C(OC)C(OC)=C21)NC(C)=O
Drug Category
  • Gout Suppressants
  • Tubulin Modulators
ATC Codes
AHFS Codes
  • 92:00.00
  • 92:02.00*
Indication For treatment and relief of pain in attacks of acute gouty arthritis.
Pharmacology Colchicine is a highly poisonous alkaloid, originally extracted from plants of the genus Colchicum (Autumn crocus, also known as the "Meadow saffron"). Originally used to treat rheumatic complaints and especially gout, it was also prescribed for its cathartic and emetic effects. Its present medicinal use is mainly in the treatment of gout; as well, it is being investigated for its potential use as an anti-cancer drug. It can also be used as initial treatment for pericarditis and preventing recurrences of the condition.
Mechanism of Action The precise mechanism of action has not been completely established. In patients with gout, colchicine apparently interrupts the cycle of monosodium urate crystal deposition in joint tissues and the resultant inflammatory response that initiates and sustains an acute attack. Colchicine decreases leukocyte chemotaxis and phagocytosis and inhibits the formation and release of a chemotactic glycoprotein that is produced during phagocytosis of urate crystals. Colchicine also inhibits urate crystal deposition, which is enhanced by a low pH in the tissues, probably by inhibiting oxidation of glucose and subsequent lactic acid production in leukocytes. Colchicine has no analgesic or antihyperuricemic activity. Colchicine inhibits microtubule assembly in various cells, including leukocytes, probably by binding to and interfering with polymerization of the microtubule subunit tubulin. Although some studies have found that this action probably does not contribute significantly to colchicine's antigout action, a recent in vitro study has shown that it may be at least partially involved.
Absorption Colchicine is rapidly absorbed after oral administration, probably from the jejunum and ileum. However, the rate and extent of absorption are variable, depending on the tablet dissolution rate; variability in gastric emptying, intestinal motility, and pH at the absorption site; and the extent to which colchicine is bound to microtubules in gastrointestinal mucosal cells.
Toxicity The onset of toxic effects is usually delayed for several hours or more after the ingestion of an acute overdose. Nausea, vomiting, abdominal pain, and diarrhea occur first. The diarrhea may be bloody due to hemorrhagic gastroenteritis. Burning sensations of the throat, stomach, and skin may be prominent symptoms. Extensive vascular damage may result in shock. Kidney damage, evidenced by hematuria and oliguria, may occur. Muscular weakness may be marked, and ascending paralysis of the central nervous system may develop; the patient usually remains conscious. Delirium and convulsions may occur. Death due to respiratory arrest may result. Although death from the ingestion of as little as 7 mg has been reported, much larger doses have been survived .
Protein Binding Low to moderate (30 to 50%).
Biotransformation Probably hepatic. Although colchicine metabolites have not been identified in humans, metabolism by mammalian hepatic microsomes has been demonstrated in vitro.
Half Life Elimination half-life is approximately 1 hour in healthy subjects, although a study with an extended sampling time reported mean terminal elimination half-life values of approximately 9 to 10.5 hours. Other studies have reported half-life values of approximately 2 hours in patients with alcoholic cirrhosis and approximately 2.5 hours in patients with familial Mediterranean fever.
Dosage Forms
Form Route
Solution / drops Oral
Solution / drops Oral
Tablet Oral
Tablet Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Atorvastatin Increased risk of rhabdomyolysis with this combination
Cerivastatin Increased risk of rhabdomyolysis with this combination
Clarithromycin Severe colchicine toxicity can occur
Cyclosporine Increased toxicity of both drugs
Erythromycin Severe colchicine toxicity can occur
Fluvastatin Increased risk of rhabdomyolysis with this combination
Lovastatin Increased risk of rhabdomyolysis with this combination
Pravastatin Increased risk of rhabdomyolysis with this combination
Rosuvastatin Increased risk of rhabdomyolysis with this combination
Simvastatin Increased risk of rhabdomyolysis with this combination
Telithromycin Severe colchicine toxicity can occur
Troleandomycin Severe colchicine toxicity can occur
Verapamil Verapamil increases colchicine's effect and toxicity
Food Interactions
  • Avoid alcohol since it increases uric acid levels.
  • Drink liberally.
  • Take without regard to meals.
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Tubulin beta-1 chain
  2. Tubulin beta chain
  3. Pyrin
  4. Multidrug resistance protein 1
Drug Target 1 [top]
Target 1 ID 29
Target 1 Name Tubulin beta-1 chain
Target 1 Synonyms Not Available
Target 1 Gene Name TUBB1
Target 1 Protein Sequence >Tubulin beta-1 chain 
MREIVHIQIGQCGNQIGAKFWEMIGEEHGIDLAGSDRGASALQLERISVYYNEAYGRKYV
PRAVLVDLEPGTMDSIRSSKLGALFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVLEVV
RHESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRIMNSFSVMPSPKVSDTVV
EPYNAVLSIHQLIENADACFCIDNEALYDICFRTLKLTTPTYGDLNHLVSLTMSGITTSL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNTM
AACDLRRGRYLTVACIFRGKMSTKEVDQQLLSVQTRNSSCFVEWIPNNVKVAVCDIPPRG
LSMAATFIGNNTAIQEIFNRVSEHFSAMFKRKAFVHWYTSEGMDINEFGEAENNIHDLVS
EYQQFQDAKAVLEEDEEVTEEAEMEPEDKGH
Target 1 Number of Residues 458
Target 1 Molecular Weight 50328
Target 1 Theoretical pI 4.82
Target 1 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
guanyl nucleotide binding
GTP 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
GTPase activity
structural molecule activity
Process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
protein polymerization
physiological process
cellular physiological process
cell organization and biogenesis
organelle organization and biogenesis
cytoskeleton organization and biogenesis
microtubule-based process
microtubule-based movement
Component
protein complex
organelle
non-membrane-bound organelle
intracellular non-membrane-bound organelle
cytoskeleton
microtubule cytoskeleton
microtubule
Target 1 General Function Cell cycle control, cell division, chromosome partitioning
Target 1 Specific Function Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 11230445 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q9H4B7 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name TBB1_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >1356 bp 
ATGCGTGAAATTGTCCATATTCAGATTGGCCAGTGTGGCAACCAGATCGGAGCCAAGTTC
TGGGAGATGATTGGTGAGGAACACGGGATCGACTTGGCTGGGAGCGACCGCGGGGCCTCG
GCCTTGCAGCTGGAGAGAATCAGCGTGTACTACAACGAAGCCTACGGTAGGAAATATGTG
CCCCGAGCAGTCTTGGTGGACCTAGAACCTGGGACGATGGACAGCATTCGATCTAGCAAA
TTAGGAGCTCTCTTTCAACCCGACAGTTTTGTCCATGGTAACTCTGGGGCTGGCAACAAC
TGGGCCAAAGGCCACTACACGGAGGGAGCCGAGCTGATCGAGAATGTCCTAGAGGTGGTG
AGGCACGAGAGTGAGAGCTGTGACTGCCTGCAGGGCTTCCAGATCGTCCACTCCCTGGGC
GGGGGCACAGGCTCCGGGATGGGCACTCTGCTCATGAACAAGATTAGAGAGGAGTACCCG
GACCGGATCATGAATTCCTTCAGCGTCATGCCTTCTCCCAAGGTGTCGGACACGGTGGTG
GAGCCCTACAACGCGGTTCTGTCTATCCACCAGCTGATTGAGAATGCAGATGCCTGTTTC
TGCATTGACAATGAGGCCCTCTATGACATCTGCTTCCGTACCCTGAAGCTGACGACACCC
ACCTATGGGGATCTCAACCACCTAGTGTCCTTGACCATGAGCGGCATAACCACCTCCCTC
CGGTTCCCGGGTCAGCTCAACGCAGACCTGCGCAAGCTGGCGGTGAACATGGTCCCCTTC
CCCCGCCTGCACTTCTTTATGCCCGGCTTTGCCCCACTCACGGCCCAGGGCAGCCAGCAG
TACCGAGCCCTCTCCGTGGCCGAGCTCACCCAGCAGATGTTCGATGCCCGCAATACCATG
GCTGCCTGTGACCTCCGCCGTGGCCGCTACCTCACAGTGGCCTGCATTTTCCGGGGCAAG
ATGTCCACCAAGGAAGTGGACCAGCAACTGCTCTCCGTGCAGACCAGGAACAGCAGCTGC
TTTGTGGAGTGGATTCCCAACAACGTCAAGGTGGCTGTCTGCGACATCCCGCCCCGGGGG
CTGAGCATGGCCGCCACCTTCATTGGCAACAACACGGCCATCCAAGAGATCTTTAATAGG
GTCTCTGAGCATTTCTCAGCCATGTTCAAAAGGAAAGCTTTTGTGCACTGGTACACCAGC
GAAGGGATGGACATAAACGAATTTGGGGAAGCTGAAAATAACATCCATGATTTGGTATCC
GAGTACCAACAATTTCAAGATGCCAAAGCAGTTCTAGAGGAAGATGAAGAGGTCACGGAG
GAGGCAGAAATGGAGCCAGAAGATAAGGGACATTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID TUBB1 Link Image
Target 1 GenAtlas ID TUBB1 Link Image
Target 1 HGNC ID HGNC:16257 Link Image
Target 1 Chromosome Location 20
Target 1 Locus 20q13.32
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  2. 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]
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 161
Target 2 Name Tubulin beta chain
Target 2 Synonyms
  1. Tubulin beta-5 chain
Target 2 Gene Name TUBB2A
Target 2 Protein Sequence >Tubulin beta-2 chain 
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEEDFGEEAEEEA
Target 2 Number of Residues 451
Target 2 Molecular Weight 49671
Target 2 Theoretical pI 4.52
Target 2 GO Classification
Function
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
GTPase activity
binding
nucleotide binding
purine nucleotide binding
guanyl nucleotide binding
GTP binding
structural molecule activity
Process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
protein polymerization
physiological process
cellular physiological process
cell organization and biogenesis
organelle organization and biogenesis
cytoskeleton organization and biogenesis
microtubule-based process
microtubule-based movement
Component
protein complex
cell
intracellular
cytoplasm
organelle
non-membrane-bound organelle
intracellular non-membrane-bound organelle
cytoskeleton
microtubule cytoskeleton
microtubule
Target 2 General Function Cell cycle control, cell division, chromosome partitioning
Target 2 Specific Function Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 338695 Link Image
Target 2 UniProtKB/Swiss-Prot ID P07437 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name TBB2_HUMAN Link Image
Target 2 PDB ID 1SA1 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasmic
Target 2 Gene Sequence >1335 bp 
ATGAGGGAAATCGTGCACATCCAGGCTGGTCAATGTGGCAACCAGATCGGTGCCAAGTTC
TGGGAGGTGATCAGTGATGAACATGGCATCGACCCCACCGGCACCTACCACGGGGACAGC
GACCTGCAGCTGGACCGCATCTCTGTGTACTACAATGAAGCCACAGGTGGCAAATATGTT
CCTCGTGCCATCCTGGTGGATCTAGAACCTGGGACCATGGACTCTGTTCGCTCAGGTCCT
TTTGGCCAGATCTTTAGACCAGACAACTTTGTATTTGGTCAGTCTGGGGCAGGTAACAAC
TGGGCCAAAGGCCACTACACAGAGGGCGCCGAGCTGGTTGATTCTGTCCTGGATGTGGTA
CGGAAGGAGGCAGAGAGCTGTGACTGCCTGCAGGGCTTCCAGCTGACCCACTCACTGGGC
GGGGGCACAGGCTCTGGAATGGGCACTCTCCTTATCAGCAAGATCCGAGAAGAATACCCT
GATCGCATCATGAATACCTTCAGTGTGGTGCCTTCACCCAAAGTGTCTGACACCGTGGTC
GAGCCCTACAATGCCACCCTCTCCGTCCATCAGTTGGTAGAGAATACTGATGAGACCTAT
TGCATTGACAACGAGGCCCTCTATGATATCTGCTTCCGCACTCTGAGGCTGACCACACCA
ACCTACGGGGATCTGAACCACCTTGTCTCAGGCACCATGGAGTGTGTCACCACCTGCCTC
CGTTTCCCTGGCCAGCTCAATGCTGACCTCCGCAAGTTGGCAGTCAACATGGTCCCCTTC
CCACGTCTCCATTTCTTTATGCCTGGCTTTGCCCCTCTCACCAGCCGTGGAAGCCAGCAG
TATCGAGCTCTCACAGTGCCGGACCTCACCCAGCAGGTCTTCGATGCCAAGAACATGATG
GCTGCCTGTGACCCCCGCCACGGCCGATACCTCACCGTGGCTGCTGTCTTCCGTGGTCGG
ATGTCCATGAAGGAGGTCGATGAGCAGATGCTTAACGTGCAGAACAAGAACAGCAGCTAC
TTTGTGGAATGGATCCCCAACAATGTCAAGACAGCCGTCTGTGACATCCCACCTCGTGGC
CTCAAGATGGCAGTCACCTTCATTGGCAATAGCACAGCCATCCAGGAGCTCTTCAAGCGC
ATCTCGGAGCAGTTCACTGCCATGTTCCGCCGGAAGGCCTTCCTCCACTGGTACACAGGC
GAGGGCATGGACGAGATGGAGTTCACCGAGGCTGAGAGCAACATGAACGACCTCGTCTCT
GAGTATCAGCAGTACCAGGATGCCACCGCAGAAGAGGAGGAGGATTTCGGTGAGGAGGCC
GAAGAGGAGGCCTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID TUBB Link Image
Target 2 GenAtlas ID TUBB Link Image
Target 2 HGNC ID HGNC:20778 Link Image
Target 2 Chromosome Location 6
Target 2 Locus 6p25
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Crabtree DV, Ojima I, Geng X, Adler AJ: Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site. Bioorg Med Chem. 2001 Aug;9(8):1967-76. [PubMed Link Image]
  2. Lee MG, Lewis SA, Wilde CD, Cowan NJ: Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes. Cell. 1983 Jun;33(2):477-87. [PubMed Link Image]
  3. Hall JL, Dudley L, Dobner PR, Lewis SA, Cowan NJ: Identification of two human beta-tubulin isotypes. Mol Cell Biol. 1983 May;3(5):854-62. [PubMed Link Image]
Target 2 Drug References
  1. Yee KW, Hagey A, Verstovsek S, Cortes J, Garcia-Manero G, O'Brien SM, Faderl S, Thomas D, Wierda W, Kornblau S, Ferrajoli A, Albitar M, McKeegan E, Grimm DR, Mueller T, Holley-Shanks RR, Sahelijo L, Gordon GB, Kantarjian HM, Giles FJ: Phase 1 study of ABT-751, a novel microtubule inhibitor, in patients with refractory hematologic malignancies. Clin Cancer Res. 2005 Sep 15;11(18):6615-24. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 962
Target 3 Name Pyrin
Target 3 Synonyms
  1. Marenostrin
Target 3 Gene Name MEFV
Target 3 Protein Sequence >Pyrin 
MAKTPSDHLLSTLEELVPYDFEKFKFKLQNTSVQKEHSRIPRSQIQRARPVKMATLLVTY
YGEEYAVQLTLQVLRAINQRLLAEELHRAAIQEYSTQENGTDDSAASSSLGENKPRSLKT
PDHPEGNEGNGPRPYGGGAASLRCSQPEAGRGLSRKPLSKRREKASEGLDAQGKPRTRSP
ALPGGRSPGPCRALEGGQAEVRLRRNASSAGRLQGLAGGAPGQKECRPFEVYLPSGKMRP
RSLEVTISTGEKAPANPEILLTLEEKTAANLDSATEPRARPTPDGGASADLKEGPGNPEH
SVTGRPPDTAASPRCHAQEGDPVDGTCVRDSCSFPEAVSGHPQASGSRSPGCPRCQDSHE
RKSPGSLSPQPLPQCKRHLKQVQLLFCEDHDEPICLICSLSQEHQGHRVRPIEEVALEHK
KKIQKQLEHLKKLRKSGEEQRSYGEEKAVSFLKQTEALKQRVQRKLEQVYYFLEQQEHFF
VASLEDVGQMVGQIRKAYDTRVSQDIALLDALIGELEAKECQSEWELLQDIGDILHRAKT
VPVPEKWTTPQEIKQKIQLLHQKSEFVEKSTKYFSETLRSEMEMFNVPELIGAQAHAVNV
ILDAETAYPNLIFSDDLKSVRLGNKWERLPDGPQRFDSCIIVLGSPSFLSGRRYWEVEVG
DKTAWILGACKTSISRKGNMTLSPENGYWVVIMMKENEYQASSVPPTRLLIKEPPKRVGI
FVDYRVGSISFYNVTARSHIYTFASCSFSGPLQPIFSPGTRDGGKNTAPLTICPVGGQGP
D
Target 3 Number of Residues 794
Target 3 Molecular Weight 86445
Target 3 Theoretical pI 8.11
Target 3 GO Classification
Function
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
Process
Not Available
Component
cell
intracellular
Target 3 General Function Involved in actin binding
Target 3 Specific Function Probably controls the inflammatory response in myelomonocytic cells at the level of the cytoskeleton organization
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 2407316 Link Image
Target 3 UniProtKB/Swiss-Prot ID O15553 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name MEFV_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Isoform 1:Cytoplasm. Isoform 2:Nucleus. Note=Associated with microtubules and with the filamentous a
Target 3 Gene Sequence >2346 bp 
ATGGCTAAGACCCCTAGTGACCATCTGCTGTCCACCCTGGAGGAGCTGGTGCCCTATGAC
TTCGAGAAGTTCAAGTTCAAGCTGCAGAACACCAGTGTGCAGAAGGAGCACTCCAGGATC
CCCCGGAGCCAGATCCAGAGAGCCAGGCCGGTGAAGATGGCCACTCTGCTGGTCACCTAC
TATGGGGAAGAGTACGCCGTGCAGCTCACCCTGCAGGTCCTGCGGGCCATCAACCAGCGC
CTGCTGGCCGAGGAGCTCCACAGGGCAGCCATTCAGGAATATTCCACACAAGAAAACGGC
ACAGATGATTCCGCAGCGTCCAGCTCCCTGGGGGAGAACAAGCCCAGGAGCCTGAAGACT
CCAGACCACCCCGAGGGGAACGAGGGGAACGGCCCTCGGCCGTACGGGGGCGGAGCTGCC
AGCCTGCGGTGCAGCCAGCCCGAGGCCGGGAGGGGGCTGTCGAGGAAGCCCCTGAGCAAA
CGCAGAGAGAAGGCCTCGGAGGGCCTGGACGCGCAGGGCAAGCCTCGGACCCGGAGCCCG
GCCCTGCCGGGCGGGAGAAGCCCCGGCCCCTGCAGGGCGCTAGAGGGGGGCCAGGCCGAG
GTCCGGCTGCGCAGAAACGCCAGCTCCGCGGGGAGGCTGCAGGGGCTGGCGGGGGGCGCC
CCGGGGCAGAAGGAGTGCAGGCCCTTCGAAGTGTACCTGCCCTCGGGAAAGATGCGACCT
AGAAGCCTTGAGGTCACCATTTCTACAGGGGAGAAGGCGCCCGCAAATCCAGAAATTCTC
CTGACTCTAGAGGAAAAGACAGCTGCGAATCTGGACTCGGCAACAGAACCCCGGGCAAGG
CCCACTCCGGATGGAGGGGCATCTGCGGACCTGAAGGAAGGCCCTGGAAATCCAGAACAT
TCGGTCACCGGAAGGCCACCAGACACGGCTGCGAGTCCCCGCTGCCACGCCCAGGAAGGA
GACCCAGTTGACGGTACCTGTGTGCGTGATTCCTGCAGCTTCCCCGAGGCAGTTTCTGGG
CACCCCCAGGCCTCAGGCAGCCGCTCACCTGGCTGCCCCCGGTGCCAGGACTCCCATGAA
AGGAAGAGCCCGGGAAGCCTAAGCCCCCAGCCCCTGCCACAGTGTAAGCGCCACCTGAAG
CAGGTCCAGCTGCTCTTCTGTGAGGATCACGATGAGCCCATCTGCCTCATCTGCAGTCTG
AGTCAGGAGCACCAAGGCCACCGGGTGCGCCCCATTGAGGAGGTCGCCCTGGAACACAAG
AAGAAAATTCAGAAGCAGCTGGAGCATCTGAAGAAGCTGAGAAAATCAGGGGAGGAGCAG
CGATCCTATGGGGAGGAGAAGGCAGTGAGCTTTCTGAAACAAACTGAAGCGCTGAAGCAG
CGGGTGCAGAGGAAGCTGGAGCAGGTGTACTACTTCCTGGAACAGCAGGAGCATTTCTTT
GTGGCCTCACTGGAGGACGTGGGCCAGATGGTTGGGCAGATCAGGAAGGCATATGACACC
CGCGTATCCCAGGACATCGCCCTGCTCGATGCGCTGATTGGGGAACTGGAGGCCAAGGAG
TGCCAGTCAGAATGGGAACTTCTGCAGGACATTGGAGACATCTTGCACAGGGCTAAGACA
GTGCCTGTCCCTGAAAAGTGGACCACTCCTCAAGAGATAAAACAAAAGATCCAACTCCTC
CACCAGAAGTCAGAGTTTGTGGAGAAGAGCACAAAGTACTTCTCAGAAACCCTGCGTTCA
GAAATGGAAATGTTCAATGTTCCAGAGCTGATTGGCGCTCAGGCACATGCTGTTAATGTG
ATTCTGGATGCAGAAACCGCTTACCCCAACCTCATCTTCTCTGATGATCTGAAGAGTGTT
AGACTTGGAAACAAGTGGGAGAGGCTGCCTGATGGCCCGCAAAGATTTGACAGCTGTATC
ATTGTTCTGGGCTCTCCGAGTTTCCTCTCTGGCCGCCGTTACTGGGAGGTGGAGGTTGGA
GACAAGACAGCATGGATCCTGGGAGCCTGCAAGACATCCATAAGCAGGAAAGGGAACATG
ACTCTGTCGCCAGAGAATGGCTACTGGGTGGTGATAATGATGAAGGAAAATGAGTACCAG
GCGTCCAGCGTTCCCCCGACCCGCCTGCTAATAAAGGAGCCTCCCAAGCGTGTGGGCATC
TTCGTGGACTACAGAGTTGGAAGCATCTCCTTTTACAATGTGACAGCCAGATCCCACATC
TATACATTCGCCAGCTGCTCTTTCTCTGGGCCCCTTCAACCTATCTTCAGCCCTGGGACA
CGTGATGGAGGGAAGAACACAGCTCCTCTGACTATCTGTCCAGTGGGTGGTCAGGGGCCT
GACTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID MEFV Link Image
Target 3 GenAtlas ID MEFV Link Image
Target 3 HGNC ID HGNC:6998 Link Image
Target 3 Chromosome Location 16
Target 3 Locus 16p13.3
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Booth DR, Gillmore JD, Booth SE, Pepys MB, Hawkins PN: Pyrin/marenostrin mutations in familial Mediterranean fever. QJM. 1998 Sep;91(9):603-6. [PubMed Link Image]
  2. Aksentijevich I, Torosyan Y, Samuels J, Centola M, Pras E, Chae JJ, Oddoux C, Wood G, Azzaro MP, Palumbo G, Giustolisi R, Pras M, Ostrer H, Kastner DL: Mutation and haplotype studies of familial Mediterranean fever reveal new ancestral relationships and evidence for a high carrier frequency with reduced penetrance in the Ashkenazi Jewish population. Am J Hum Genet. 1999 Apr;64(4):949-62. [PubMed Link Image]
  3. Shohat M, Magal N, Shohat T, Chen X, Dagan T, Mimouni A, Danon Y, Lotan R, Ogur G, Sirin A, Schlezinger M, Halpern GJ, Schwabe A, Kastner D, Rotter JI, Fischel-Ghodsian N: Phenotype-genotype correlation in familial Mediterranean fever: evidence for an association between Met694Val and amyloidosis. Eur J Hum Genet. 1999 Apr;7(3):287-92. [PubMed Link Image]
  4. Cazeneuve C, Sarkisian T, Pecheux C, Dervichian M, Nedelec B, Reinert P, Ayvazyan A, Kouyoumdjian JC, Ajrapetyan H, Delpech M, Goossens M, Dode C, Grateau G, Amselem S: MEFV-Gene analysis in armenian patients with Familial Mediterranean fever: diagnostic value and unfavorable renal prognosis of the M694V homozygous genotype-genetic and therapeutic implications. Am J Hum Genet. 1999 Jul;65(1):88-97. [PubMed Link Image]
  5. Akar N, Misiroglu M, Yalcinkaya F, Akar E, Cakar N, Tumer N, Akcakus M, Tastan H, Matzner Y: MEFV mutations in Turkish patients suffering from Familial Mediterranean Fever. Hum Mutat. 2000 Jan;15(1):118-9. [PubMed Link Image]
  6. Tidow N, Chen X, Muller C, Kawano S, Gombart AF, Fischel-Ghodsian N, Koeffler HP: Hematopoietic-specific expression of MEFV, the gene mutated in familial Mediterranean fever, and subcellular localization of its corresponding protein, pyrin. Blood. 2000 Feb 15;95(4):1451-5. [PubMed Link Image]
  7. Ben-Chetrit E, Lerer I, Malamud E, Domingo C, Abeliovich D: The E148Q mutation in the MEFV gene: is it a disease-causing mutation or a sequence variant? Hum Mutat. 2000 Apr;15(4):385-6. [PubMed Link Image]
  8. Centola M, Wood G, Frucht DM, Galon J, Aringer M, Farrell C, Kingma DW, Horwitz ME, Mansfield E, Holland SM, O'Shea JJ, Rosenberg HF, Malech HL, Kastner DL: The gene for familial Mediterranean fever, MEFV, is expressed in early leukocyte development and is regulated in response to inflammatory mediators. Blood. 2000 May 15;95(10):3223-31. [PubMed Link Image]
  9. Dode C, Pecheux C, Cazeneuve C, Cattan D, Dervichian M, Goossens M, Delpech M, Amselem S, Grateau G: Mutations in the MEFV gene in a large series of patients with a clinical diagnosis of familial Mediterranean fever. Am J Med Genet. 2000 Jun 5;92(4):241-6. [PubMed Link Image]
  10. Domingo C, Touitou I, Bayou A, Ozen S, Notarnicola C, Dewalle M, Demaille J, Buades R, Sayadat C, Levy M, Ben-Chetrit E: Familial Mediterranean fever in the 'Chuetas' of Mallorca: a question of Jewish origin or genetic heterogeneity. Eur J Hum Genet. 2000 Apr;8(4):242-6. [PubMed Link Image]
  11. 11115844 Papin S, Duquesnoy P, Cazeneuve C, Pantel J, Coppey-Moisan M, Dargemont C, Amselem S: Alternative splicing at the MEFV locus involved in familial Mediterranean fever regulates translocation of the marenostrin/pyrin protein to the nucleus. Hum Mol Genet. 2000 Dec 12;9(20):3001-9.
  12. 11139244 Akar E, Yalcinkaya F, Akar N: Is the Ala138Gly alteration of MEFV gene important for amyloidosis? Hum Mutat. 2001;17(1):71.
  13. 11464238 Touitou I: The spectrum of Familial Mediterranean Fever (FMF) mutations. Eur J Hum Genet. 2001 Jul;9(7):473-83.
  14. 11468188 Mansfield E, Chae JJ, Komarow HD, Brotz TM, Frucht DM, Aksentijevich I, Kastner DL: The familial Mediterranean fever protein, pyrin, associates with microtubules and colocalizes with actin filaments. Blood. 2001 Aug 1;98(3):851-9.
  15. 11470495 Timmann C, Muntau B, Kuhne K, Gelhaus A, Horstmann RD: Two novel mutations R653H and E230K in the Mediterranean fever gene associated with disease. Mutat Res. 2001 Aug 8;479(1-2):235-9.
  16. 12124996 Aldea A, Casademont J, Arostegui JI, Rius J, Maso M, Vives J, Yague J: I591T MEFV mutation in a Spanish kindred: is it a mild mutation, a benign polymorphism, or a variant influenced by another modifier? Hum Mutat. 2002 Aug;20(2):148-50.
  17. 12384939 Notarnicola C, Didelot MN, Kone-Paut I, Seguret F, Demaille J, Touitou I: Reduced MEFV messenger RNA expression in patients with familial Mediterranean fever. Arthritis Rheum. 2002 Oct;46(10):2785-93.
  18. 9288094 A candidate gene for familial Mediterranean fever. The French FMF Consortium. Nat Genet. 1997 Sep;17(1):25-31.
  19. 9288758 Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever. The International FMF Consortium. Cell. 1997 Aug 22;90(4):797-807.
  20. 9668175 Bernot A, da Silva C, Petit JL, Cruaud C, Caloustian C, Castet V, Ahmed-Arab M, Dross C, Dupont M, Cattan D, Smaoui N, Dode C, Pecheux C, Nedelec B, Medaxian J, Rozenbaum M, Rosner I, Delpech M, Grateau G, Demaille J, Weissenbach J, Touitou I: Non-founder mutations in the MEFV gene establish this gene as the cause of familial Mediterranean fever (FMF). Hum Mol Genet. 1998 Aug;7(8):1317-25.
Target 3 Drug References
  1. Abedat S, Urieli-Shoval S, Shapira E, Calko S, Ben-Chetrit E, Matzner Y: Effect of colchicine and cytokines on MEFV expression and C5a inhibitor activity in human primary fibroblast cultures. Isr Med Assoc J. 2002 Jan;4(1):7-12. [PubMed Link Image]
  2. Leibovitch I, Alster Y, Lazar M, Langevitz P, Livneh A, Loewenstein A: Corneal wound healing in a patient treated with colchicine for familial Mediterranean Fever (FMF). Rheumatology (Oxford). 2003 Aug;42(8):1021-2. [PubMed Link Image]
  3. Koukoui L, Blau A, Kopolovic J, Pras M, Livneh A: A possible favorable effect of colchicine in IgA nephropathy in a carrier of a MEFV mutation. Clin Nephrol. 2004 Sep;62(3):226-8. [PubMed Link Image]
  4. Cerquaglia C, Diaco M, Nucera G, La Regina M, Montalto M, Manna R: Pharmacological and clinical basis of treatment of Familial Mediterranean Fever (FMF) with colchicine or analogues: an update. Curr Drug Targets Inflamm Allergy. 2005 Feb;4(1):117-24. [PubMed Link Image]
  5. Onat AM, Ozturk MA, Ozcakar L, Ureten K, Kaymak SU, Kiraz S, Ertenli I, Calguneri M: Selective serotonin reuptake inhibitors reduce the attack frequency in familial mediterranean Fever. Tohoku J Exp Med. 2007 Jan;211(1):9-14. [PubMed Link Image]
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. Cisternino S, Rousselle C, Dagenais C, Scherrmann JM: Screening of multidrug-resistance sensitive drugs by in situ brain perfusion in P-glycoprotein-deficient mice. Pharm Res. 2001 Feb;18(2):183-90. [PubMed Link Image]
  2. Tahir SK, Han EK, Credo B, Jae HS, Pietenpol JA, Scatena CD, Wu-Wong JR, Frost D, Sham H, Rosenberg SH, Ng SC: A-204197, a new tubulin-binding agent with antimitotic activity in tumor cell lines resistant to known microtubule inhibitors. Cancer Res. 2001 Jul 15;61(14):5480-5. [PubMed Link Image]
  3. Asawakarn T, Cladera J, O'Shea P: Effects of the membrane dipole potential on the interaction of saquinavir with phospholipid membranes and plasma membrane receptors of Caco-2 cells. J Biol Chem. 2001 Oct 19;276(42):38457-63. Epub 2001 Aug 10. [PubMed Link Image]
  4. Kane SE, Matsumoto L, Metz MZ, Donohue CA, Lingeman RG, Lin SW, Doroshow JH: MDR1 bicistronic vectors: analysis of selection stringency, amplified gene expression, and vector stability in cell lines. Biochem Pharmacol. 2001 Sep 15;62(6):693-704. [PubMed Link Image]
  5. Ando H, Nishio Y, Ito K, Nakao A, Wang L, Zhao YL, Kitaichi K, Takagi K, Hasegawa T: Effect of endotoxin on P-glycoprotein-mediated biliary and renal excretion of rhodamine-123 in rats. Antimicrob Agents Chemother. 2001 Dec;45(12):3462-7. [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.