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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:48:13
Primary Accession Number DB01023
Secondary Accession Number
  • APRD00374
Name Felodipine
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description A dihydropyridine calcium antagonist with positive inotropic effects. It lowers blood pressure by reducing peripheral vascular resistance through a highly selective action on smooth muscle in arteriolar resistance vessels. [PubChem]
Synonyms
  1. Dl-Felodipine
  2. Felodipina [INN-Spanish]
  3. Felodipine [Usan:Ban:Inn]
  4. Felodipinum [INN-Latin]
  5. felodipine
Brand Names
  1. AGON SR
  2. Agon
  3. Feloday
  4. Felodur ER
  5. Felogard
  6. Flodil
  7. Hydac
  8. Lexxel
  9. Modip
  10. Munobal
  11. Munobal Retard
  12. Penedil
  13. Perfudal
  14. Plandil
  15. Plendil
  16. Plendil Depottab
  17. Plendil ER
  18. Plendil Retard
  19. Preslow
  20. Prevex
  21. Renedil
  22. Splendil
Brand Mixtures Not Available
Chemical IUPAC Name O3-ethyl O5-methyl 4-(2,3-dichlorophenyl)-2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylate
Chemical Formula C18H19Cl2NO4
Chemical Structure Structure
CAS Registry Number 72509-76-3
InChI Identifier InChI=1/C18H19Cl2NO4/c1-5-25-18(23)14-10(3)21-9(2)13(17(22)24-4)15(14)11-7-6-8-12(19)16(11)20/h6-8,15,21H,5H2,1-4H3
InChI Key RZTAMFZIAATZDJ-UHFFFAOYAS
KEGG Drug D00319 Link Image
KEGG Compound Not Available
PubChem Compound 3333 Link Image
PubChem Substance 189780 Link Image
ChEBI ID Not Available
PharmGKB ID Not Available
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02222000 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/felo.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Felodipine Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference P. B. Berntsson et al., U.S. Pat. 4,264,611 (1980)
Average Molecular Weight 384.2540
Monoisotopic Molecular Weight 383.0691
State Solid
Melting Point 145oC
Experimental Water Solubility 19.7 mg/L Source: PhysProp
Predicted Water Solubility 7.15e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 3.8 Source: PhysProp
Predicted LogP 4.36 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.73 Calculated using ALOGPS
Experimental Caco2 Permeability -4.64 [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 CCOC(=O)C1=C(C)NC(C)=C([C@H]1C1=C(Cl)C(Cl)=CC=C1)C(=O)OC
Canonical SMILES CCOC(=O)C1=C(C)NC(C)=C(C1C1=C(Cl)C(Cl)=CC=C1)C(=O)OC
Drug Category
  • Anti-Arrhythmia Agents
  • Antiarrhythmic Agents
  • Antihypertensive Agents
  • Calcium Channel Blockers
  • Dihydropyridines
  • Vasodilator Agents
ATC Codes
AHFS Codes
  • 24:28.08
Indication For the treatment of hypertension and angina.
Pharmacology Felodipine, a dihydropyridine calcium-channel blocker, is used alone or with an angiotensin-converting enzyme inhibitor, to treat hypertension, chronic stable angina pectoris, and Prinzmetal's variant angina. Felodipine is similar to other peripheral vasodilators. Felodipine inhibits the influx of extra cellular calcium across the myocardial and vascular smooth muscle cell membranes blocking the calcium channels. The decrease in intracellular calcium inhibits the contractile processes of the myocardial smooth muscle cells, causing dilation of the coronary and systemic arteries, increased oxygen delivery to the myocardial tissue, decreased total peripheral resistance, decreased systemic blood pressure, and decreased afterload.
Mechanism of Action Felodipine is a calcium channel blocker. It reversibly competes with nitrendipine and/or other calcium channel blockers for dihydropyridine binding sites, blocks voltage-dependent calcium currents in vascular smooth muscle and cultured rabbit atrial cells, and blocks potassium-induced contracture of the rat portal vein. By blocking the calcium channels, felodipine inhibits the influx of extracellular calcium across the myocardial and vascular smooth muscle cell membranes and results in a decrease of peripheral vascular resistance.
Absorption 15%
Toxicity Symptoms of overdose include excessive peripheral vasodilation with marked hypotension and possibly bradycardia. Oral rat LD50 is 1050 mg/kg.
Protein Binding 99%
Biotransformation Hepatic
Half Life 14.1 hours
Dosage Forms
Form Route
Tablet, extended release Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Amobarbital The barbiturate decreases the effect of felodipine
Aprobarbital The barbiturate decreases the effect of felodipine
Butabarbital The barbiturate decreases the effect of felodipine
Butalbital The barbiturate decreases the effect of felodipine
Butethal The barbiturate decreases the effect of felodipine
Carbamazepine Carbamazepine decreases the effect of felodipine
Dihydroquinidine barbiturate The barbiturate decreases the effect of felodipine
Erythromycin Erythromycin increases the effect of felodipine
Ethotoin The hydantoin decreases the effect of felodipine
Fosphenytoin The hydantoin decreases the effect of felodipine
Heptabarbital The barbiturate decreases the effect of felodipine
Hexobarbital The barbiturate decreases the effect of felodipine
Itraconazole Itraconazole increases effect/toxicity of felodipine
Josamycin Erythromycin increases the effect of felodipine
Mephenytoin The hydantoin decreases the effect of felodipine
Methohexital The barbiturate decreases the effect of felodipine
Methylphenobarbital The barbiturate decreases the effect of felodipine
Nelfinavir Nelfinavir increases the effect and toxicity of felodipine
Oxcarbazepine Oxcarbazepine decreases the levels of felodipine
Pentobarbital The barbiturate decreases the effect of felodipine
Phenobarbital The barbiturate decreases the effect of felodipine
Phenytoin The hydantoin decreases the effect of felodipine
Primidone The barbiturate decreases the effect of felodipine
Quinidine barbiturate The barbiturate decreases the effect of felodipine
Quinupristin This combination presents an increased risk of toxicity
Secobarbital The barbiturate decreases the effect of felodipine
Tacrolimus Felodipine increases tacrolimus levels
Talbutal The barbiturate decreases the effect of felodipine
Food Interactions
  • Grapefruit and grapefruit juice should be avoided throughout treatment as grapefruit can significantly increase serum levels of this product.
  • Take without regard to meals.
Pathways
Name SMPDB Link KEGG Link
Felodipine Pathway SMP00377 Link Image
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A4 (CYP3A4)
Targets
  1. Calmodulin
  2. Voltage-dependent calcium channel subunit alpha-2/delta-1
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 1 Gene Name CYP3A4
Enzyme 1 SwissProt ID P08684 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67) 
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Drug Target 1 [top]
Target 1 ID 465
Target 1 Name Calmodulin
Target 1 Synonyms
  1. CaM
Target 1 Gene Name CALM1
Target 1 Protein Sequence >Calmodulin 
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK
Target 1 Number of Residues 150
Target 1 Molecular Weight 16707
Target 1 Theoretical pI 3.84
Target 1 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 1 General Function Involved in calcium ion binding
Target 1 Specific Function Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases
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 179888 Link Image
Target 1 UniProtKB/Swiss-Prot ID P62158 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name CALM_HUMAN Link Image
Target 1 PDB ID 1IQ5 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >450 bp 
ATGGCTGACCAGCTGACTGAGGAGCAGATTGCAGAGTTCAAGGAGGCCTTCTCCCTCTTT
GACAAGGATGGAGATGGCACTATCACCACCAAGGAGTTGGGGACAGTGATGAGATCCCTG
GGACAGAACCCCACTGAAGCAGAGCTGCAGGATATGATCAATGAGGTGGATGCAGATGGG
AACGGGACCATTGACTTCCCGGAGTTCCTGACCATGATGGCCAGAAAGATGAAGGACACA
GACAGTGAGGAGGAGATCCGAGAGGCGTTCCGTGTCTTTGACAAGGATGGGAATGGCTAC
ATCAGCGCCGCAGAGCTGCGTCACGTAATGACGAACCTGGGGGAGAAGCTGACCGATGAG
GAGGTGGATGAGATGATCAGGGAGGCTGACATCGATGGAGATGGCCAGGTCAATTATGAA
GAGTTTGTACAGATGATGACTGCAAAGTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID CALM1 Link Image
Target 1 GenAtlas ID CALM1 Link Image
Target 1 HGNC ID HGNC:1442 Link Image
Target 1 Chromosome Location 14
Target 1 Locus 14q24-q31
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Drum CL, Yan SZ, Bard J, Shen YQ, Lu D, Soelaiman S, Grabarek Z, Bohm A, Tang WJ: Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature. 2002 Jan 24;415(6870):396-402. [PubMed Link Image]
  2. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  3. Koller M, Schnyder B, Strehler EE: Structural organization of the human CaMIII calmodulin gene. Biochim Biophys Acta. 1990 Oct 23;1087(2):180-9. [PubMed Link Image]
  4. SenGupta B, Friedberg F, Detera-Wadleigh SD: Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species. J Biol Chem. 1987 Dec 5;262(34):16663-70. [PubMed Link Image]
  5. Fischer R, Koller M, Flura M, Mathews S, Strehler-Page MA, Krebs J, Penniston JT, Carafoli E, Strehler EE: Multiple divergent mRNAs code for a single human calmodulin. J Biol Chem. 1988 Nov 15;263(32):17055-62. [PubMed Link Image]
  6. Wawrzynczak EJ, Perham RN: Isolation and nucleotide sequence of a cDNA encoding human calmodulin. Biochem Int. 1984 Aug;9(2):177-85. [PubMed Link Image]
  7. Sasagawa T, Ericsson LH, Walsh KA, Schreiber WE, Fischer EH, Titani K: Complete amino acid sequence of human brain calmodulin. Biochemistry. 1982 May 11;21(10):2565-9. [PubMed Link Image]
  8. Rhyner JA, Ottiger M, Wicki R, Greenwood TM, Strehler EE: Structure of the human CALM1 calmodulin gene and identification of two CALM1-related pseudogenes CALM1P1 and CALM1P2. Eur J Biochem. 1994 Oct 1;225(1):71-82. [PubMed Link Image]
  9. Toutenhoofd SL, Foletti D, Wicki R, Rhyner JA, Garcia F, Tolon R, Strehler EE: Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3. Cell Calcium. 1998 May;23(5):323-38. [PubMed Link Image]
Target 1 Drug References
  1. Johnson JD, Andrews CT, Khabbaza EJ, Mills JS: The interaction of felodipine with calcium-binding proteins. J Cardiovasc Pharmacol. 1987;10 Suppl 1:S53-9. [PubMed Link Image]
  2. Walsh MP, Sutherland C, Scott-Woo GC: Effects of felodipine (a dihydropyridine calcium channel blocker) and analogues on calmodulin-dependent enzymes. Biochem Pharmacol. 1988 Apr 15;37(8):1569-80. [PubMed Link Image]
  3. Lamers JM, Cysouw KJ, Verdouw PD: Slow calcium channel blockers and calmodulin. Effect of felodipine, nifedipine, prenylamine and bepridil on cardiac sarcolemmal calcium pumping ATPase. Biochem Pharmacol. 1985 Nov 1;34(21):3837-43. [PubMed Link Image]
  4. Lamers JM, Verdouw PD, Mas-Oliva J: The effects of felodipine and bepridil on calcium-stimulated calmodulin binding and calcium pumping ATPase of cardiac sarcolemma before and after removal of endogenous calmodulin. Mol Cell Biochem. 1987 Dec;78(2):169-76. [PubMed Link Image]
  5. Ronca-Testoni S, Hrelia S, Hakim G, Rossi CA: Interaction of smooth muscle relaxant drugs with calmodulin and cyclic nucleotide phosphodiesterase. Experientia. 1985 Jan 15;41(1):75-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 762
Target 2 Name Voltage-dependent calcium channel subunit alpha-2/delta-1
Target 2 Synonyms
  1. Dihydropyridine-sensitive L-type calcium channel subunits alpha- 2/delta precursor
Target 2 Gene Name CACNA2D1
Target 2 Protein Sequence >Voltage-dependent calcium channel subunit alpha-2/delta-1 
MAAGCLLALTLTLFQSLLIGPSSEEPFPSAVTIKSWVDKMQEDLVTLAKTASGVNQLVDI
YEKYQDLYTVEPNNARQLVEIAARDIEKLLSNRSKALVSLALEAEKVQAAHQWREDFASN
EVVYYNAKDDLDPEKNDSEPGSQRIKPVFIEDANFGRQISYQHAAVHIPTDIYEGSTIVL
NELNWTSALDEVFKKNREEDPSLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRR
RPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQD
VSCFQHLVQANVRNKKVLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIML
FTDGGEERAQEIFNKYNKDKKVRVFRFSVGQHNYERGPIQWMACENKGYYYEIPSIGAIR
INTQEYLDVLGRPMVLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNITGQFENKTNLK
NQLILGVMGVDVSLEDIKRLTPRFTLCPNGYYFAIDPNGYVLLHPNLQPKNPKSQEPVTL
DFLDAELENDIKVEIRNKMIDGESGEKTFRTLVKSQDERYIDKGNRTYTWTPVNGTDYSL
ALVLPTYSFYYIKAKLEETITQARSKKGKMKDSETLKPDNFEESGYTFIAPRDYCNDLKI
SDNNTEFLLNFNEFIDRKTPNNPSCNADLINRVLLDAGFTNELVQNYWSKQKNIKGVKAR
FVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYESGI
MVSKAVEIYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVI
LDDGGFLLMANHDDYTNQIGRFFGEIDPSLMRHLVNISVYAFNKSYDYQSVCEPGAAPKQ
GAGHRSAYVPSVADILQIGWWATAAAWSILQQFLLSLTFPRLLEAVEMEDDDFTASLSKQ
SCITEQTQYFFDNDSKSFSGVLDCGNCSRIFHGEKLMNTNLIFIMVESKGTCPCDTRLLI
QAEQTSDGPNPCDMVKQPRYRKGPDVCFDNNVLEDYTDCGGVSGLNPSLWYIIGIQFLLL
WLVSGSTHRLL
Target 2 Number of Residues 1109
Target 2 Molecular Weight 123184
Target 2 Theoretical pI 4.86
Target 2 GO Classification
Function
Not Available
Process
Not Available
Component
cell
membrane
Target 2 General Function Cell motility
Target 2 Specific Function Calcium channel protein which plays an important role in excitation-contraction coupling
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-24
Target 2 Transmembrane Regions
  • 446-469906-9301067-1086
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 179762 Link Image
Target 2 UniProtKB/Swiss-Prot ID P54289 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CAC2D_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 2 Gene Sequence >3276 bp 
ATGGCTGCTGGCTGCCTGCTGGCCTTGACTCTGACACTTTTCCAATCTTTGCTCATCGGC
CCCTCGTCGGAGGAGCCGTTCCCTTCGGCCGTCACTATCAAATCATGGGTGGATAAGATG
CAAGAAGACCTTGTCACACTGGCAAAAACAGCAAGTGGAGTCAATCAGCTTGTTGATATT
TATGAGAAATATCAAGATTTGTATACTGTGGAACCAAATAATGCACGCCAGCTGGTAGAA
ATTGCAGCCAGGGATATTGAGAAACTTCTGAGCAACAGATCTAAAGCCCTGGTGAGCCTG
GCATTGGAAGCGGAGAAAGTTCAAGCAGCTCACCAGTGGAGAGAAGATTTTGCAAGCAAT
GAAGTTGTCTACTACAATGCAAAGGATGATCTCGATCCTGAGAAAAATGACAGTGAGCCA
GGCAGCCAGAGGATAAAACCTGTTTTCATTGAAGATGCTAATTTTGGACGACAAATATCT
TATCAGCACGCAGCAGTCCATATTCCTACTGACATCTATGAGGGCTCAACAATTGTGTTA
AATGAACTCAACTGGACAAGTGCCTTAGATGAAGTTTTCAAAAAGAATCGCGAGGAAGAC
CCTTCATTATTGTGGCAGGTTTTTGGCAGTGCCACTGGCCTAGCTCGATATTATCCAGCT
TCACCATGGGTTGATAATAGTAGAACTCCAAATAAGATTGACCTTTATGATGTACGCAGA
AGACCATGGTACATCCAAGGAGCTGCATCTCCTAAAGACATGCTTATTCTGGTGGATGTG
AGTGGAAGTGTTAGTGGATTGACACTTAAACTGATCCGAACATCTGTCTCCGAAATGTTA
GAAACCCTCTCAGATGATGATTTCGTGAATGTAGCTTCATTTAACAGCAATGCTCAGGAT
GTAAGCTGTTTTCAGCACCTTGTCCAAGCAAATGTAAGAAATAAAAAAGTGTTGAAAGAC
GCGGTGAATAATATCACAGCCAAAGGAATTACAGATTATAAGAAGGGCTTTAGTTTTGCT
TTTGAACAGCTGCTTAATTATAATGTTTCCAGAGCAAACTGCAATAAGATTATTATGCTA
TTCACGGATGGAGGAGAAGAGAGAGCCCAGGAGATATTTAACAAATACAATAAAGATAAA
AAAGTACGTGTATTCAGGTTTTCAGTTGGTCAACACAATTATGAGAGAGGACCTATTCAG
TGGATGGCCTGTGAAAACAAAGGTTATTATTATGAAATTCCTTCCATTGGTGCAATAAGA
ATCAATACTCAGGAATATTTGGATGTTTTGGGAAGACCAATGGTTTTAGCAGGAGACAAA
GCTAAGCAAGTCCAATGGACAAATGTGTACCTGGATGCATTGGAACTGGGACTTGTCATT
ACTGGAACTCTTCCGGTCTTCAACATAACCGGCCAATTTGAAAATAAGACAAACTTAAAG
AACCAGCTGATTCTTGGTGTGATGGGAGTAGATGTGTCTTTGGAAGATATTAAAAGACTG
ACACCACGTTTTACACTGTGCCCCAATGGGTATTACTTTGCAATCGATCCTAATGGTTAT
GTTTTATTACATCCAAATCTTCAGCCAAAGAACCCCAAATCTCAGGAGCCAGTAACATTG
GATTTCCTTGATGCAGAGTTAGAGAATGATATTAAAGTGGAGATTCGAAATAAGATGATT
GATGGGGAAAGTGGAGAAAAAACATTCAGAACTCTGGTTAAATCTCAAGATGAGAGATAT
ATTGACAAAGGAAACAGGACATACACATGGACACCTGTCAATGGCACAGATTACAGTTTG
GCCTTGGTATTACCAACCTACAGTTTTTACTATATAAAAGCCAAACTAGAAGAGACAATA
ACTCAGGCCAGATCAAAAAAGGGCAAAATGAAGGATTCGGAAACCCTGAAGCCAGATAAT
TTTGAAGAATCTGGCTATACATTCATAGCACCAAGAGATTACTGCAATGACCTGAAAATA
TCGGATAATAACACTGAATTTCTTTTAAATTTCAACGAGTTTATTGATAGAAAAACTCCA
AACAACCCATCATGTAACGCGGATTTGATTAATAGAGTCTTGCTTGATGCAGGCTTTACA
AATGAACTTGTCCAAAATTACTGGAGTAAGCAGAAAAATATCAAGGGAGTGAAAGCACGA
TTTGTTGTGACTGATGGTGGGATTACCAGAGTTTATCCCAAAGAGGCTGGAGAAAATTGG
CAAGAAAACCCAGAGACATATGAGGACAGCTTCTATAAAAGGAGCCTAGATAATGATAAC
TATGTTTTCACTGCTCCCTACTTTAACAAAAGTGGACCTGGTGCCTATGAATCGGGCATT
ATGGTAAGCAAAGCTGTAGAAATATATATTCAAGGGAAACTTCTTAAACCTGCAGTTGTT
GGAATTAAAATTGATGTAAATTCCTGGATAGAGAATTTCACCAAAACCTCAATCAGAGAT
CCGTGTGCTGGTCCAGTTTGTGACTGCAAAAGAAACAGTGACGTAATGGATTGTGTGATT
CTGGATGATGGTGGGTTTCTTCTGATGGCAAATCATGATGATTATACTAATCAGATTGGA
AGATTTTTTGGAGAGATTGATCCCAGCTTGATGAGACACCTGGTTAATATATCAGTTTAT
GCTTTTAACAAATCTTATGATTATCAGTCAGTATGTGAGCCCGGTGCTGCACCAAAACAA
GGAGCAGGACATCGCTCAGCATATGTGCCATCAGTAGCAGACATATTACAAATTGGCTGG
TGGGCCACTGCTGCTGCCTGGTCTATTCTACAGCAGTTTCTCTTGAGTTTGACCTTTCCA
CGACTCCTTGAGGCAGTTGAGATGGAGGATGATGACTTCACGGCCTCCCTGTCCAAGCAG
AGCTGCATTACTGAACAAACCCAGTATTTCTTCGATAACGACAGTAAATCATTCAGTGGT
GTATTAGACTGTGGAAACTGTTCCAGAATCTTTCATGGAGAAAAGCTTATGAACACCAAC
TTAATATTCATAATGGTTGAGAGCAAAGGGACATGTCCATGTGACACACGACTGCTCATA
CAAGCGGAGCAGACTTCTGACGGTCCAAATCCTTGTGACATGGTTAAGCAACCTAGATAC
CGAAAAGGGCCTGATGTCTGCTTTGATAACAATGTCTTGGAGGATTATACTGACTGTGGT
GGTGTTTCTGGATTAAATCCCTCCCTGTGGTATATCATTGGAATCCAGTTTCTACTACTT
TGGCTGGTATCTGGCAGCACACACCGGCTGTTATGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID CACNA2D1 Link Image
Target 2 GenAtlas ID CACNA2D1 Link Image
Target 2 HGNC ID HGNC:1399 Link Image
Target 2 Chromosome Location 7
Target 2 Locus 7q21-q22
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Williams ME, Feldman DH, McCue AF, Brenner R, Velicelebi G, Ellis SB, Harpold MM: Structure and functional expression of alpha 1, alpha 2, and beta subunits of a novel human neuronal calcium channel subtype. Neuron. 1992 Jan;8(1):71-84. [PubMed Link Image]
  2. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
Target 2 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.