Drugbank Logo

Showing drug card for Pimozide (DB01100)

Legend: drug field target field enzyme field

for drugs
Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:05:53
Primary Accession Number DB01100
Secondary Accession Number
  • APRD00218
Name Pimozide
Drug Type
  • Approved
  • Small Molecule
Description A diphenylbutylpiperidine that is effective as an antipsychotic agent and as an alternative to haloperidol for the suppression of vocal and motor tics in patients with Tourette syndrome. Although the precise mechanism of action is unknown, blockade of postsynaptic dopamine receptors has been postulated. (From AMA Drug Evaluations Annual, 1994, p403)
Synonyms
  1. Pimozida [INN-Spanish]
  2. Pimozidum [INN-Latin]
Brand Names
  1. Halomonth
  2. Neoperidole
  3. Opiran
  4. Orap
Brand Mixtures Not Available
Chemical IUPAC Name 3-[1-[4,4-bis(4-fluorophenyl)butyl]piperidin-4-yl]-1H-benzimidazol-2-one
Chemical Formula C28H29F2N3O
Chemical Structure Structure
CAS Registry Number 2062-78-4
InChI Identifier InChI=1/C28H29F2N3O/c29-22-11-7-20(8-12-22)25(21-9-13-23(30)14-10-21)4-3-17-32-18-15-24(16-19-32)33-27-6-2-1-5-26(27)31-28(33)34/h1-2,5-14,24-25H,3-4,15-19H2,(H,31,34)/f/h31H
InChI Key YVUQSNJEYSNKRX-VJSLDGLSCK
KEGG Drug D00560 Link Image
KEGG Compound C07566 Link Image
PubChem Compound 16362 Link Image
PubChem Substance 9769 Link Image
ChEBI ID Not Available
PharmGKB ID PA450965 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00573817 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/orap.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Pimozide Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 461.5462
Monoisotopic Molecular Weight 461.2279
State Solid
Melting Point 214-218 oC
Experimental Water Solubility 10 mg/L Source: PhysProp
Predicted Water Solubility 1.73e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 5.6 Source: PhysProp
Predicted LogP 6.36 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -5.43 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 8.63
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 FC1=CC=C(C=C1)C(CCCN1CCC(CC1)N1C(=O)NC2=CC=CC=C12)C1=CC=C(F)C=C1
Canonical SMILES FC1=CC=C(C=C1)C(CCCN1CCC(CC1)N1C(=O)NC2=CC=CC=C12)C1=CC=C(F)C=C1
Drug Category
  • Anti-Dyskinesia Agents
  • Antipsychotic Agents
  • Dopamine Antagonists
ATC Codes
AHFS Codes
  • 28:16.08.92
Indication Used for the suppression of motor and phonic tics in patients with Tourette's Disorder who have failed to respond satisfactorily to standard treatment.
Pharmacology Pimozide is an orally active antipsychotic drug product which shares with other antipsychotics the ability to blockade dopaminergic receptors on neurons in the central nervous system. However, receptor blockade is often accompanied by a series of secondary alterations in central dopamine metabolism and function which may contribute to both pimozide's therapeutic and untoward effects. In addition, pimozide, in common with other antipsychotic drugs, has various effects on other central nervous system receptor systems which are not fully characterized. Pimozide also has less potential for inducing sedation and hypotension as it has more specific dopamine receptor blocking activity than other neuroleptic agents (and is therefore a suitable alternative to haloperidol).
Mechanism of Action The ability of pimozide to suppress motor and phonic tics in Tourette's Disorder is thought to be primarily a function of its dopaminergic blocking activity. Pimozide binds to the dopamine D2 receptor in the CNS. It also appears to block voltage-operated calcium channels and acts as an antagonist at opiate receptors (OP2).
Absorption Greater than 50% absorption after oral administration. Serum peak appears 6-8 hours post ingestion.
Toxicity LD50 = 1100 mg/kg (rat, oral), 228 mg/kg (mouse, oral)
Protein Binding Not Available
Biotransformation Notable first-pass metabolism in the liver, primarily by N-dealkylation via the cytochrome P450 isoenzymes CYP3A and CYP1A2 (and possibly CYP2D6). The activity of the two major metabolites has not been determined.
Half Life 29 ± 10 hours (single-dose study of healthy volunteers).
Dosage Forms
Form Route
Tablet Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Amprenavir Amprenavir increases the effect and toxicity of pimozide
Aprepitant Increased risk of cardiotoxicity and arrhythmias
Atazanavir The protease inhibitor increases the effect and toxicity of pimozide
Citalopram The SSRI increases the effect and toxicity of pimozide
Clarithromycin Increased risk of cardiotoxicity and arrhythmias
Donepezil Possible antagonism of action
Erythromycin Increased risk of cardiotoxicity and arrhythmias
Escitalopram The SSRI increases the effect and toxicity of pimozide
Fluconazole Increased risk of cardiotoxicity and arrhythmias
Fosamprenavir Amprenavir increases the effect and toxicity of pimozide
Galantamine Possible antagonism of action
Imatinib Imatinib increases the effect and toxicity of pimozide
Indinavir The protease inhibitor increases the effect and toxicity of pimozide
Itraconazole Increased risk of cardiotoxicity and arrhythmias
Josamycin Increased risk of cardiotoxicity and arrhythmias
Ketoconazole Increased risk of cardiotoxicity and arrhythmias
Mesoridazine Increased risk of cardiotoxicity and arrhythmias
Nefazodone increases the effect and toxicity of pimozide
Nelfinavir Nelfinavir increases the effect and toxicity of pimozide
Paroxetine Increased risk of cardiotoxicity/arrhythmias
Posaconazole Contraindicated co-administration
Ritonavir The protease inhibitor increases the effect and toxicity of pimozide
Rivastigmine Possible antagonism of action
Saquinavir The protease inhibitor increases the effect and toxicity of pimozide
Sertraline The SSRI increases the effect and toxicity of pimozide
Telithromycin Increased risk of cardiotoxicity and arrhythmias
Thioridazine Increased risk of cardiotoxicity and arrhythmias
Troleandomycin Increased risk of cardiotoxicity and arrhythmias
Voriconazole Increased risk of cardiotoxicity and arrhythmias
Zileuton Increased risk of cardiotoxicity and arrhythmias
Ziprasidone Increased risk of cardiotoxicity and arrhythmias
Food Interactions
  • Grapefruit and grapefruit juice should be avoided throughout treatment. Grapefruit can increase serum levels of this product.
  • Take without regard to meals.
Pathways Not Available
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)
  2. Cytochrome P450 1A2 (CYP1A2)
  3. Aromatic-L-amino-acid decarboxylase (AADC)
Targets
  1. Potassium voltage-gated channel subfamily H member 2
  2. Calmodulin
  3. Delta-type opioid receptor
  4. Voltage-dependent T-type calcium channel subunit alpha-1G
  5. D(2) dopamine receptor
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 1 Gene Name CYP3A4
Enzyme 1 SwissProt ID P08684 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67) 
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Cytochrome P450 1A2 (CYP1A2)
Enzyme 2 Gene Name CYP1A2
Enzyme 2 SwissProt ID P05177 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >P05177|CP1A2_HUMAN Cytochrome P450 1A2 - Homo sapiens (Human). 
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
Phase 1 Metabolizing Enzyme 3 [top]
Enzyme 3 Name Aromatic-L-amino-acid decarboxylase (AADC)
Enzyme 3 Gene Name DDC
Enzyme 3 SwissProt ID P20711 Link Image
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 Protein Sequence >sp|P20711|DDC_HUMAN Aromatic-L-amino-acid decarboxylase 
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
Drug Target 1 [top]
Target 1 ID 101
Target 1 Name Potassium voltage-gated channel subfamily H member 2
Target 1 Synonyms
  1. Eag-related protein 1
  2. Erg1
  3. Ether-a-go-go-related gene potassium channel 1
  4. Ether-a-go-go-related protein 1
  5. H-ERG
  6. Voltage-gated potassium channel subunit Kv11.1
  7. eag homolog
Target 1 Gene Name KCNH2
Target 1 Protein Sequence >Potassium voltage-gated channel subfamily H member 2 
MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVM
QRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG
AVIMFILNFEVVMEKDMVGSPAHDTNHRGPPTSWLAPGRAKTFRLKLPALLALTARESSV
RSGGAGGAGAPGAVVVDVDLTPAAPSSESLALDEVTAMDNHVAGLGPAEERRALVGPGSP
PRSAPGQLPSPRAHSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGVLPPPP
RHASTGAMHPLRSGLLNSTSDSDLVRYRTISKIPQITLNFVDLKGDPFLASPTSDREIIA
PKIKERTHNVTEKVTQVLSLGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIY
TAVFTPYSAAFLLKETEEGPPATECGYACQPLAVVDLIVDIMFIVDILINFRTTYVNANE
EVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLD
RYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSRIGWLHNLGDQIGKPYNSS
GLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVS
AIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGF
PECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALY
FISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLE
VLDMYPEFSDHFWSSLEITFNLRDTNMIPGSPGSTELEGGFSRQRKRKLSFRRRTDKDTE
QPGEVSALGPGRAGAGPSSRGRPGGPWGESPSSGPSSPESSEDEGPGRSSSPLRLVPFSS
PRPPGEPPGGEPLMEDCEKSSDTCNPLSGAFSGVSNIFSFWGDSRGRQYQELPRCPAPTP
SLLNIPLSSPGRRPRGDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSA
VTTPGPGPTSTSPLLPVSPLPTLTLDSLSQVSQFMACEELPPGAPELPQEGPTRRLSLPG
QLGALTSQPLHRHGSDPGS
Target 1 Number of Residues 1178
Target 1 Molecular Weight 126656
Target 1 Theoretical pI 7.97
Target 1 GO Classification
Function
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
transporter activity
ion transporter activity
ion channel activity
voltage-gated ion channel activity
voltage-gated potassium channel activity
Process
two-component signal transduction system (phosphorelay)
cellular process
cell communication
signal transduction
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
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
potassium ion transport
Component
cell
membrane
Target 1 General Function Voltage-gated signal transduction
Target 1 Specific Function Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr). Isoform 3 has no channel activity by itself, but modulates channel characteristics when associated with isoform 1
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 404-424
  • 451-471
  • 496-516
  • 521-541
  • 548-568
  • 639-659
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 487738 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q12809 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name KCNH2_HUMAN Link Image
Target 1 PDB ID 1BYW Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 1 Gene Sequence >3480 bp 
ATGCCGGTGCGGAGGGGCCACGTCGCGCCGCAGAACACCTTCCTGGACACCATCATCCGC
AAGTTTGAGGGCCAGAGCCGTAAGTTCATCATCGCCAACGCTCGGGTGGAGAACTGCGCC
GTCATCTACTGCAACGACGGCTTCTGCGAGCTGTGCGGCTACTCGCGGGCCGAGGTGATG
CAGCGACCCTGCACCTGCGACTTCCTGCACGGGCCGCGCACGCAGCGCCGCGCTGCCGCG
CAGATCGCGCAGGCACTGCTGGGCGCCGAGGAGCGCAAAGTGGAAATCGCCTTCTACCGG
AAAGATGGGAGCTGCTTCCTATGTCTGGTGGATGTGGTGCCCGTGAAGAACGAGGATGGG
GCTGTCATCATGTTCATCCTCAATTTCGAGGTGGTGATGGAGAAGGACATGGTGGGGTCC
CCGGCTCATGACACCAACCACCGGGGCCCCCCCACCAGCTGGCTGGCCCCAGGCCGCGCC
AAGACCTTCCGCCTGAAGCTGCCCGCGCTGCTGGCGCTGACGGCCCGGGAGTCGTCGGTG
CGGTCGGGCGGCGCGGGCGGCGCGGGCGCCCCGGGGGCCGTGGTGGTGGACGTGGACCTG
ACGCCCGCGGCACCCAGCAGCGAGTCGCTGGCCCTGGACGAAGTGACAGCCATGGACAAC
CACGTGGCAGGGCTCGGGCCCGCGGAGGAGCGGCGTGCGCTGGTGGGTCCCGGCTCTCCG
CCCCGCAGCGCGCCCGGCCAGCTCCCATCGCCCCGGGCGCACAGCCTCAACCCCGACGCC
TCGGGCTCCAGCTGCAGCCTGGCCCGGACGCGCTCCCGAGAAAGCTGCGCCAGCGTGCGC
CGCGCCTCGTCGGCCGACGACATCGAGGCCATGCGCGCCGGGGTGCTGCCCCCGCCACCG
CGCCACGCCAGCACCGGGGCCATGCACCCACTGCGCAGCGGCTTGCTCAACTCCACCTCG
GACTCCGACCTCGTGCGCTACCGCACCATTAGCAAGATTCCCCAAATCACCCTCAACTTT
GTGGACCTCAAGGGCGACCCCTTCTTGGCTTCGCCCACCAGTGACCGTGAGATCATAGCA
CCTAAGATAAAGGAGCGAACCCACAATGTCACTGAGAAGGTCACCCAGGTCCTGTCCCTG
GGCGCCGACGTGCTGCCTGAGTACAAGCTGCAGGCACCGCGCATCCACCGCTGGACCATC
CTGCATTACAGCCCCTTCAAGGCCGTGTGGGACTGGCTCATCCTGCTGCTGGTCATCTAC
ACGGCTGTCTTCACACCCTACTCGGCTGCCTTCCTGCTGAAGGAGACGGAAGAAGGCCCG
CCTGCTACCGAGTGTGGCTACGCCTGCCAGCCGCTGGCTGTGGTGGACCTCATCGTGGAC
ATCATGTTCATTGTGGACATCCTCATCAACTTCCGCACCACCTACGTCAATGCCAACGAG
GAGGTGGTCAGCCACCCCGGCCGCATCGCCGTCCACTACTTCAAGGGCTGGTTCCTCATC
GACATGGTGGCCGCCATCCCCTTCGACCTGCTCATCTTCGGCTCTGGCTCTGAGGAGCTG
ATCGGGCTGCTGAAGACTGCGCGGCTGCTGCGGCTGGTGCGCGTGGCGCGGAAGCTGGAT
CGCTACTCAGAGTACGGCGCGGCCGTGCTGTTCTTGCTCATGTGCACCTTTGCGCTCATC
GCGCACTGGCTAGCCTGCATCTGGTACGCCATCGGCAACATGGAGCAGCCACACATGGAC
TCACGCATCGGCTGGCTGCACAACCTGGGCGACCAGATAGGCAAACCCTACAACAGCAGC
GGCCTGGGCGGCCCCTCCATCAAGGACAAGTATGTGACGGCGCTCTACTTCACCTTCAGC
AGCCTCACCAGTGTGGGCTTCGGCAACGTCTCTCCCAACACCAACTCAGAGAAGATCTTC
TCCATCTGCGTCATGCTCATTGGCTCCCTCATGTATGCTAGCATCTTCGGCAACGTGTCG
GCCATCATCCAGCGGCTGTACTCGGGCACAGCCCGCTACCACACACAGATGCTGCGGGTG
CGGGAGTTCATCCGCTTCCACCAGATCCCCAATCCCCTGCGCCAGCGCCTCGAGGAGTAC
TTCCAGCACGCCTGGTCCTACACCAACGGCATCGACATGAACGCGGTGCTGAAGGGCTTC
CCTGAGTGCCTGCAGGCTGACATCTGCCTGCACCTGAACCGCTCACTGCTGCAGCACTGC
AAACCCTTCCGAGGGGCCACCAAGGGCTGCCTTCGGGCCCTGGCCATGAAGTTCAAGACC
ACACATGCACCGCCAGGGGACACACTGGTGCATGCTGGGGACCTGCTCACCGCCCTGTAC
TTCATCTCCCGGGGCTCCATCGAGATCCTGCGGGGCGACGTCGTCGTGGCCATCCTGGGG
AAGAATGACATCTTTGGGGAGCCTCTGAACCTGTATGCAAGGCCTGGCAAGTCGAACGGG
GATGTGCGGGCCCTCACCTACTGTGACCTACACAAGATCCATCGGGACGACCTGCTGGAG
GTGCTGGACATGTACCCTGAGTTCTCCGACCACTTCTGGTCCAGCCTGGAGATCACCTTC
AACCTGCGAGATACCAACATGATCCCGGGCTCCCCCGGCAGTACGGAGTTAGAGGGTGGC
TTCAGTCGGCAACGCAAGCGCAAGTTGTCCTTCCGCAGGCGCACGGACAAGGACACGGAG
CAGCCAGGGGAGGTGTCGGCCTTGGGGCCGGGCCGGGCGGGGGCAGGGCCGAGTAGCCGG
GGCCGGCCGGGGGGGCCGTGGGGGGAGAGCCCGTCCAGTGGCCCCTCCAGCCCTGAGAGC
AGTGAGGATGAGGGCCCAGGCCGCAGCTCCAGCCCCCTCCGCCTGGTGCCCTTCTCCAGC
CCCAGGCCCCCCGGAGAGCCGCCGGGTGGGGAGCCCCTGATGGAGGACTGCGAGAAGAGC
AGCGACACTTGCAACCCCCTGTCAGGCGCCTTCTCAGGAGTGTCCAACATTTTCAGCTTC
TGGGGGGACAGTCGGGGCCGCCAGTACCAGGAGCTCCCTCGATGCCCCGCCCCCACCCCC
AGCCTCCTCAACATCCCCCTCTCCAGCCCGGGTCGGCGGCCCCGGGGCGACGTGGAGAGC
AGGCTGGATGCCCTCCAGCGCCAGCTCAACAGGCTGGAGACCCGGCTGAGTGCAGACATG
GCCACTGTCCTGCAGCTGCTACAGAGGCAGATGACGCTGGTCCCGCCCGCCTACAGTGCT
GTGACCACCCCGGGGCCTGGCCCCACTTCCACATCCCCGCTGTTGCCCGTCAGCCCCCTC
CCCACCCTCACCTTGGACTCGCTTTCTCAGGTTTCCCAGTTCATGGCGTGTGAGGAGCTG
CCCCCGGGGGCCCCAGAGCTTCCCCAAGAAGGCCCCACACGACGCCTCTCCCTACCGGGC
CAGCTGGGGGCCCTCACCTCCCAGCCCCTGCACAGACACGGCTCGGACCCGGGCAGTTAG
Target 1 GenBank Gene ID
Target 1 GeneCard ID KCNH2 Link Image
Target 1 GenAtlas ID KCNH2 Link Image
Target 1 HGNC ID HGNC:6251 Link Image
Target 1 Chromosome Location 7
Target 1 Locus 7q35-q36
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Berthet M, Denjoy I, Donger C, Demay L, Hammoude H, Klug D, Schulze-Bahr E, Richard P, Funke H, Schwartz K, Coumel P, Hainque B, Guicheney P: C-terminal HERG mutations: the role of hypokalemia and a KCNQ1-associated mutation in cardiac event occurrence. Circulation. 1999 Mar 23;99(11):1464-70. [PubMed Link Image]
  2. Chen J, Zou A, Splawski I, Keating MT, Sanguinetti MC: Long QT syndrome-associated mutations in the Per-Arnt-Sim (PAS) domain of HERG potassium channels accelerate channel deactivation. J Biol Chem. 1999 Apr 9;274(15):10113-8. [PubMed Link Image]
  3. Abbott GW, Sesti F, Splawski I, Buck ME, Lehmann MH, Timothy KW, Keating MT, Goldstein SA: MiRP1 forms IKr potassium channels with HERG and is associated with cardiac arrhythmia. Cell. 1999 Apr 16;97(2):175-87. [PubMed Link Image]
  4. Jongbloed RJ, Wilde AA, Geelen JL, Doevendans P, Schaap C, Van Langen I, van Tintelen JP, Cobben JM, Beaufort-Krol GC, Geraedts JP, Smeets HJ: Novel KCNQ1 and HERG missense mutations in Dutch long-QT families. Hum Mutat. 1999;13(4):301-10. [PubMed Link Image]
  5. Yoshida H, Horie M, Otani H, Takano M, Tsuji K, Kubota T, Fukunami M, Sasayama S: Characterization of a novel missense mutation in the pore of HERG in a patient with long QT syndrome. J Cardiovasc Electrophysiol. 1999 Sep;10(9):1262-70. [PubMed Link Image]
  6. Larsen LA, Svendsen IH, Jensen AM, Kanters JK, Andersen PS, Moller M, Sorensen SA, Sandoe E, Jacobsen JR, Vuust J, Christiansen M: Long QT syndrome with a high mortality rate caused by a novel G572R missense mutation in KCNH2. Clin Genet. 2000 Feb;57(2):125-30. [PubMed Link Image]
  7. Paulussen A, Yang P, Pangalos M, Verhasselt P, Marrannes R, Verfaille C, Vandenberk I, Crabbe R, Konings F, Luyten W, Armstrong M: Analysis of the human KCNH2(HERG) gene: identification and characterization of a novel mutation Y667X associated with long QT syndrome and a non-pathological 9 bp insertion. Hum Mutat. 2000 May;15(5):483. [PubMed Link Image]
  8. Cui J, Melman Y, Palma E, Fishman GI, McDonald TV: Cyclic AMP regulates the HERG K(+) channel by dual pathways. Curr Biol. 2000 Jun 1;10(11):671-4. [PubMed Link Image]
  9. Laitinen P, Fodstad H, Piippo K, Swan H, Toivonen L, Viitasalo M, Kaprio J, Kontula K: Survey of the coding region of the HERG gene in long QT syndrome reveals six novel mutations and an amino acid polymorphism with possible phenotypic effects. Hum Mutat. 2000 Jun;15(6):580-1. [PubMed Link Image]
  10. Splawski I, Shen J, Timothy KW, Lehmann MH, Priori S, Robinson JL, Moss AJ, Schwartz PJ, Towbin JA, Vincent GM, Keating MT: Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, KCNE1, and KCNE2. Circulation. 2000 Sep 5;102(10):1178-85. [PubMed Link Image]
  11. 11374908 Soejima H, Kawamoto S, Akai J, Miyoshi O, Arai Y, Morohka T, Matsuo S, Niikawa N, Kimura A, Okubo K, Mukai T: Isolation of novel heart-specific genes using the BodyMap database. Genomics. 2001 May 15;74(1):115-20.
  12. 12062363 Hayashi K, Shimizu M, Ino H, Yamaguchi M, Mabuchi H, Hoshi N, Higashida H: Characterization of a novel missense mutation E637K in the pore-S6 loop of HERG in a patient with long QT syndrome. Cardiovasc Res. 2002 Apr;54(1):67-76.
  13. 12063277 Gong Q, Anderson CL, January CT, Zhou Z: Role of glycosylation in cell surface expression and stability of HERG potassium channels. Am J Physiol Heart Circ Physiol. 2002 Jul;283(1):H77-84.
  14. 7889573 Curran ME, Splawski I, Timothy KW, Vincent GM, Green ED, Keating MT: A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome. Cell. 1995 Mar 10;80(5):795-803.
  15. 8159766 Warmke JW, Ganetzky B: A family of potassium channel genes related to eag in Drosophila and mammals. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3438-42.
  16. 8635257 Benson DW, MacRae CA, Vesely MR, Walsh EP, Seidman JG, Seidman CE, Satler CA: Missense mutation in the pore region of HERG causes familial long QT syndrome. Circulation. 1996 May 15;93(10):1791-5.
  17. 8877771 Dausse E, Berthet M, Denjoy I, Andre-Fouet X, Cruaud C, Bennaceur M, Faure S, Coumel P, Schwartz K, Guicheney P: A mutation in HERG associated with notched T waves in long QT syndrome. J Mol Cell Cardiol. 1996 Aug;28(8):1609-15.
  18. 8914737 Satler CA, Walsh EP, Vesely MR, Plummer MH, Ginsburg GS, Jacob HJ: Novel missense mutation in the cyclic nucleotide-binding domain of HERG causes long QT syndrome. Am J Med Genet. 1996 Oct 2;65(1):27-35.
  19. 9024139 Tanaka T, Nagai R, Tomoike H, Takata S, Yano K, Yabuta K, Haneda N, Nakano O, Shibata A, Sawayama T, Kasai H, Yazaki Y, Nakamura Y: Four novel KVLQT1 and four novel HERG mutations in familial long-QT syndrome. Circulation. 1997 Feb 4;95(3):565-7.
  20. 9230439 McDonald TV, Yu Z, Ming Z, Palma E, Meyers MB, Wang KW, Goldstein SA, Fishman GI: A minK-HERG complex regulates the cardiac potassium current I(Kr). Nature. 1997 Jul 17;388(6639):289-92.
  21. 9351446 Lees-Miller JP, Kondo C, Wang L, Duff HJ: Electrophysiological characterization of an alternatively processed ERG K+ channel in mouse and human hearts. Circ Res. 1997 Nov;81(5):719-26.
  22. 9351462 London B, Trudeau MC, Newton KP, Beyer AK, Copeland NG, Gilbert DJ, Jenkins NA, Satler CA, Robertson GA: Two isoforms of the mouse ether-a-go-go-related gene coassemble to form channels with properties similar to the rapidly activating component of the cardiac delayed rectifier K+ current. Circ Res. 1997 Nov;81(5):870-8.
  23. 9452080 Akimoto K, Furutani M, Imamura S, Furutani Y, Kasanuki H, Takao A, Momma K, Matsuoka R: Novel missense mutation (G601S) of HERG in a Japanese long QT syndrome family. Hum Mutat. 1998;Suppl 1:S184-6.
  24. 9544837 Satler CA, Vesely MR, Duggal P, Ginsburg GS, Beggs AH: Multiple different missense mutations in the pore region of HERG in patients with long QT syndrome. Hum Genet. 1998 Mar;102(3):265-72.
  25. 9600240 Itoh T, Tanaka T, Nagai R, Kamiya T, Sawayama T, Nakayama T, Tomoike H, Sakurada H, Yazaki Y, Nakamura Y: Genomic organization and mutational analysis of HERG, a gene responsible for familial long QT syndrome. Hum Genet. 1998 Apr;102(4):435-9.
  26. 9693036 Splawski I, Shen J, Timothy KW, Vincent GM, Lehmann MH, Keating MT: Genomic structure of three long QT syndrome genes: KVLQT1, HERG, and KCNE1. Genomics. 1998 Jul 1;51(1):86-97.
  27. 9765245 Kupershmidt S, Snyders DJ, Raes A, Roden DM: A K+ channel splice variant common in human heart lacks a C-terminal domain required for expression of rapidly activating delayed rectifier current. J Biol Chem. 1998 Oct 16;273(42):27231-5.
  28. 9845367 Morais Cabral JH, Lee A, Cohen SL, Chait BT, Li M, Mackinnon R: Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain. Cell. 1998 Nov 25;95(5):649-55.
Target 1 Drug References
  1. Kang J, Wang L, Cai F, Rampe D: High affinity blockade of the HERG cardiac K(+) channel by the neuroleptic pimozide. Eur J Pharmacol. 2000 Mar 31;392(3):137-40. [PubMed Link Image]
  2. Osypenko VM, Degtiar VIe, Naid'onov VG, Shuba IaM: [Blockade of HERG K+ channels expressed in Xenopus oocytes by antipsychotic agents] Fiziol Zh. 2001;47(1):17-25. [PubMed Link Image]
  3. Shuba YM, Degtiar VE, Osipenko VN, Naidenov VG, Woosley RL: Testosterone-mediated modulation of HERG blockade by proarrhythmic agents. Biochem Pharmacol. 2001 Jul 1;62(1):41-9. [PubMed Link Image]
  4. Kang J, Chen XL, Rampe D: The antipsychotic drugs sertindole and pimozide block erg3, a human brain K(+) channel. Biochem Biophys Res Commun. 2001 Aug 24;286(3):499-504. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 465
Target 2 Name Calmodulin
Target 2 Synonyms
  1. CaM
Target 2 Gene Name CALM1
Target 2 Protein Sequence >Calmodulin 
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK
Target 2 Number of Residues 150
Target 2 Molecular Weight 16707
Target 2 Theoretical pI 3.84
Target 2 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 2 General Function Involved in calcium ion binding
Target 2 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 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 179888 Link Image
Target 2 UniProtKB/Swiss-Prot ID P62158 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CALM_HUMAN Link Image
Target 2 PDB ID 1IQ5 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >450 bp 
ATGGCTGACCAGCTGACTGAGGAGCAGATTGCAGAGTTCAAGGAGGCCTTCTCCCTCTTT
GACAAGGATGGAGATGGCACTATCACCACCAAGGAGTTGGGGACAGTGATGAGATCCCTG
GGACAGAACCCCACTGAAGCAGAGCTGCAGGATATGATCAATGAGGTGGATGCAGATGGG
AACGGGACCATTGACTTCCCGGAGTTCCTGACCATGATGGCCAGAAAGATGAAGGACACA
GACAGTGAGGAGGAGATCCGAGAGGCGTTCCGTGTCTTTGACAAGGATGGGAATGGCTAC
ATCAGCGCCGCAGAGCTGCGTCACGTAATGACGAACCTGGGGGAGAAGCTGACCGATGAG
GAGGTGGATGAGATGATCAGGGAGGCTGACATCGATGGAGATGGCCAGGTCAATTATGAA
GAGTTTGTACAGATGATGACTGCAAAGTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID CALM1 Link Image
Target 2 GenAtlas ID CALM1 Link Image
Target 2 HGNC ID HGNC:1442 Link Image
Target 2 Chromosome Location 14
Target 2 Locus 14q24-q31
Target 2 SNPs SNPJam Report Link Image
Target 2 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 2 Drug References
  1. Papadopoulos V, Brown AS, Hall PF: Calcium-calmodulin-dependent phosphorylation of cytoskeletal proteins from adrenal cells. Mol Cell Endocrinol. 1990 Dec 3;74(2):109-23. [PubMed Link Image]
  2. Wang XB, Sato N, Greer MA, Greer SE, McAdams S: Role of extracellular calcium and calmodulin in prolactin secretion induced by hyposmolarity, thyrotropin-releasing hormone, and high K+ in GH4C1 cells. Acta Endocrinol (Copenh). 1990 Aug;123(2):218-24. [PubMed Link Image]
  3. Strobl JS, Kirkwood KL, Lantz TK, Lewine MA, Peterson VA, Worley JF 3rd: Inhibition of human breast cancer cell proliferation in tissue culture by the neuroleptic agents pimozide and thioridazine. Cancer Res. 1990 Sep 1;50(17):5399-405. [PubMed Link Image]
  4. Cimino M, Weiss B: Characteristics of the binding of phenoxybenzamine to calmodulin. Biochem Pharmacol. 1988 Jul 15;37(14):2739-45. [PubMed Link Image]
  5. Mody I, Baimbridge KG, Miller JJ: Blockade of tetanic- and calcium-induced long-term potentiation in the hippocampal slice preparation by neuroleptics. Neuropharmacology. 1984 Jun;23(6):625-31. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 467
Target 3 Name Delta-type opioid receptor
Target 3 Synonyms
  1. DOR-1
Target 3 Gene Name OPRD1
Target 3 Protein Sequence >Delta-type opioid receptor 
MEPAPSAGAELQPPLFANASDAYPSAFPSAGANASGPPGARSASSLALAIAITALYSAVC
AVGLLGNVLVMFGIVRYTKMKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELL
CKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVG
VPIMVMAVTRPRDGAVVCMLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRL
RSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDIDRRDPLVVAAL
HLCIALGYANSSLNPVLYAFLDENFKRCFRQLCRKPCGRPDPSSFSRAREATARERVTAC
TPSDGPGGGAAA
Target 3 Number of Residues 378
Target 3 Molecular Weight 40413
Target 3 Theoretical pI 9.17
Target 3 GO Classification
Function
signal transducer activity
receptor activity
transmembrane receptor activity
G-protein coupled receptor activity
rhodopsin-like receptor activity
peptide receptor activity, G-protein coupled
opioid receptor activity
delta-opioid receptor activity
Process
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 3 General Function Involved in delta-opioid receptor activity
Target 3 Specific Function Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Highly stereoselective. receptor for enkephalins
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • 46-75
  • 85-102
  • 125-144
  • 175-190
  • 216-238
  • 262-284
  • 294-310
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 27545517 Link Image
Target 3 UniProtKB/Swiss-Prot ID P41143 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name OPRD_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 3 Gene Sequence >1119 bp 
ATGGAACCGGCCCCCTCCGCCGGCGCCGAGCTGCAGCCCCCGCTCTTCGCCAACGCCTCG
GACGCCTACCCTAGCGCCTTCCCCAGCGCTGGCGCCAATGCGTCGGGGCCGCCAGGCGCG
CGGAGCGCCTCGTCCCTCGCCCTGGCAATCGCCATCACCGCGCTCTACTCGGCCGTGTGC
GCCGTGGGGCTGCTGGGCAACGTGCTTGTCATGTTCGGCATCGTCCGGTACACTAAGATG
AAGACGGCCACCAACATCTACATCTTCAACCTGGCCTTAGCCGATGCGCTGGCCACCAGC
ACGCTGCCTTTCCAGAGTGCCAAGTACCTGATGGAGACGTGGCCCTTCGGCGAGCTGCTC
TGCAAGGCTGTGCTCTCCATCGACTACTACAATATGTTCACCAGCATCTTCACGCTCACC
ATGATGAGTGTTGACCGCTACATCGCTGTCTGCCACCCTGTCAAGGCCCTGGACTTCCGC
ACGCCTGCCAAGGCCAAGCTGATCAACATCTGTATCTGGGTCCTGGCCTCAGGCGTTGGC
GTGCCCATCATGGTCATGGCTGTGACCCGTCCCCGGGACGGGGCAGTGGTGTGCATGCTC
CAGTTCCCCAGCCCCAGCTGGTACTGGGACACGGTGACCAAGATCTGCGTGTTCCTCTTC
GCCTTCGTGGTGCCCATCCTCATCATCACCGTGTGCTATGGCCTCATGCTGCTGCGCCTG
CGCAGTGTGCGCCTGCTGTCGGGCTCCAAGGAGAAGGACCGCAGCCTGCGGCGCATCACG
CGCATGGTGCTGGTGGTTGTGGGCGCCTTCGTGGTGTGTTGGGCGCCCATCCACATCTTC
GTCATCGTCTGGACGCTGGTGGACATCGACCGGCGCGACCCGCTGGTGGTGGCTGCGCTG
CACCTGTGCATCGCGCTGGGCTACGCCAATAGCAGCCTCAACCCCGTGCTCTACGCTTTC
CTCGACGAGAACTTCAAGCGCTGCTTCCGCCAGCTCTGCCGCAAGCCCTGCGGCCGCCCA
GACCCCAGCAGCTTCAGCCGCGCCCGCGAAGCCACGGCCCGCGAGCGTGTCACCGCCTGC
ACCCCGTCCGATGGTCCCGGCGGTGGCGCTGCCGCCTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID OPRD1 Link Image
Target 3 GenAtlas ID OPRD1 Link Image
Target 3 HGNC ID HGNC:8153 Link Image
Target 3 Chromosome Location 1
Target 3 Locus 1p36.1-p34.3
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Gelernter J, Kranzler HR: Variant detection at the delta opioid receptor (OPRD1) locus and population genetics of a novel variant affecting protein sequence. Hum Genet. 2000 Jul;107(1):86-8. [PubMed Link Image]
  2. Simonin F, Befort K, Gaveriaux-Ruff C, Matthes H, Nappey V, Lannes B, Micheletti G, Kieffer B: The human delta-opioid receptor: genomic organization, cDNA cloning, functional expression, and distribution in human brain. Mol Pharmacol. 1994 Dec;46(6):1015-21. [PubMed Link Image]
  3. Knapp RJ, Malatynska E, Fang L, Li X, Babin E, Nguyen M, Santoro G, Varga EV, Hruby VJ, Roeske WR, et al.: Identification of a human delta opioid receptor: cloning and expression. Life Sci. 1994;54(25):PL463-9. [PubMed Link Image]
Target 3 Drug References
  1. Murphy LL, Adrian BA, Kohli M: Inhibition of luteinizing hormone secretion by delta9-tetrahydrocannabinol in the ovariectomized rat: effect of pretreatment with neurotransmitter or neuropeptide receptor antagonists. Steroids. 1999 Sep;64(9):664-71. [PubMed Link Image]
  2. Sokolowska-Mikolajczyk M, Socha M, Mikolajczyk T, Chyb J, Epler P: The effects of naltrexone, an opioid receptor antagonist, on plasma LH levels in common carp (Cyprinus carpio L.). Comp Biochem Physiol C Toxicol Pharmacol. 2002 Apr;131(4):417-24. [PubMed Link Image]
  3. Shukla R, MacKenzie-Taylor D, Rech RH: Evidence for 5-HT2 receptor mediation in quipazine anorexia. Psychopharmacology (Berl). 1990;100(1):115-8. [PubMed Link Image]
  4. Su TP: Evidence for sigma opioid receptor: binding of [3H]SKF-10047 to etorphine-inaccessible sites in guinea-pig brain. J Pharmacol Exp Ther. 1982 Nov;223(2):284-90. [PubMed Link Image]
  5. Rauhala P, Idanpaan-Heikkila JJ, Lang A, Tuominen RK, Mannisto PT: Cold exposure attenuates effects of secretagogues on serum prolactin and growth hormone levels in male rats. Am J Physiol. 1995 Apr;268(4 Pt 1):E758-65. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 535
Target 4 Name Voltage-dependent T-type calcium channel subunit alpha-1G
Target 4 Synonyms
  1. Cav3.1c
  2. NBR13
  3. Voltage- gated calcium channel subunit alpha Cav3.1
Target 4 Gene Name CACNA1G
Target 4 Protein Sequence >Voltage-dependent T-type calcium channel subunit alpha-1G 
MDEEEDGAGAEESGQPRSFMRLNDLSGAGGRPGPGSAEKDPGSADSEAEGLPYPALAPVV
FFYLSQDSRPRSWCLRTVCNPWFERISMLVILLNCVTLGMFRPCEDIACDSQRCRILQAF
DDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVR
TVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNR
CFLPENFSLPLSVDLERYYQTENEDESPFICSQPRENGMRSCRSVPTLRGDGGGGPPCGL
DYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIM
YFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNA
STLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAAGVRVGLLSSPAPLGGQETQPSS
SCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRAPRASPEIQDRDANGSRRLMLPPPSTP
ALSGAPPGGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPE
TLKEKALVEVAASSGPPTLTSLNIPPGPYSSMHKLLETQSTGACQSSCKISSPCLKADSG
ACGPDSCPYCARAGAGEVELADREMPDSDSEAVYEFTQDAQHSDLRDPHSRRQRSLGPDA
EPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNI
VFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMR
VLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTL
PDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLV
AILVEGFQAEEISKREDASGQLSCIQLPVDSQGGDANKSESEPDFFSPSLDGDGDRKKCL
ALVSLGEHPELRKSLLPPLIIHTAATPMSLPKSTSTGLGEALGPASRRTSSSGSAEPGAA
HEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQ
DEEESSEEERASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRGSASEHQDCN
GKSASGRLARALRPDDPPLDGDDADDEGNLSKGERVRAWIRARLPACCLERDSWSAYIFP
PQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAV
FLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVL
RLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFV
CQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVG
VDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRL
RRLEKKRRNLMLDDVIASGSSASAASEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGV
IGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDL
AIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQAL
PQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVST
GDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKE
AKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGPDSPDSPKPGALHPAAHARSASH
FSLEHPTDRQLFDTISLLIQGSLEWELKLMDELAGPGGQPSAFPSAPSLGGSDPQIPLAE
MEALSLTSEIVSEPSCSLALTDDSLPDDMHTLLLSALESNMQPHPTELPGPDLLTVRKSG
VSRTHSLPNDSYMCRHGSTAEGPLGHRGWGLPKAQSGSVLSVHSQPADTSYILQLPKDAP
HLLQPHSAPTWGTIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLAEVSGPS
PPLARAYSFWGQSSTQAQQHSRSHSKISKHMTPPAPCPGPEPNWGKGPPETRSSLELDTE
LSWISGDLLPPGGQEEPPSPRDLKKCYSVEAQSCQRRPTSWLDEQRRHSIAVSCLDSGSQ
PHLGTDPSNLGGQPLGGPGSRPKKKLSPPSITIDPPESQGPRTPPSPGICLRRRAPSSDS
KDPLASGPPDSMAASPSPKKDVLSLSGLSSDPADLDP
Target 4 Number of Residues 2416
Target 4 Molecular Weight 262474
Target 4 Theoretical pI 6.57
Target 4 GO Classification
Function
transporter activity
ion transporter activity
ion channel activity
voltage-gated ion channel activity
voltage-gated calcium channel activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
di-, tri-valent inorganic cation transport
calcium ion transport
Component
intrinsic to membrane
integral to membrane
cell
membrane
protein complex
voltage-gated calcium channel complex
Target 4 General Function Involved in voltage-gated calcium channel activity
Target 4 Specific Function Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1G gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group and are strongly blocked by mibefradil. A particularity of this type of channels is an opening at quite negative potentials and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • 81-101
  • 120-141
  • 151-170
  • 176-193
  • 214-234
  • 371-395
  • 744-764
  • 778-799
  • 806-824
  • 833-856
  • 868-888
  • 940-964
  • 1273-1295
  • 1314-1334
  • 1345-1364
  • 1379-1400
  • 1411-1434
  • 1512-1537
  • 1611-1631
  • 1646-1667
  • 1675-1693
  • 1708-1731
  • 1746-1766
  • 1827-1854
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 6625659 Link Image
Target 4 UniProtKB/Swiss-Prot ID O43497 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name CAC1G_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 4 Gene Sequence >7134 bp 
ATGGACGAGGAGGAGGATGGAGCGGGCGCCGAGGAGTCGGGACAGCCCCGGAGCTTCATG
CGGCTCAACGACCTGTCGGGGGCCGGGGGCCGGCCGGGGCCGGGGTCAGCAGAAAAGGAC
CCGGGCAGCGCGGACTCCGAGGCGGAGGGGCTGCCGTACCCGGCGCTGGCCCCGGTGGTT
TTCTTCTACTTGAGCCAGGACAGCCGCCCGCGGAGCTGGTGTCTCCGCACGGTCTGTAAC
CCCTGGTTTGAGCGCATCAGCATGTTGGTCATCCTTCTCAACTGCGTGACCCTGGGCATG
TTCCGGCCATGCGAGGACATCGCCTGTGACTCCCAGCGCTGCCGGATCCTGCAGGCCTTT
GATGACTTCATCTTTGCCTTCTTTGCCGTGGAGATGGTGGTGAAGATGGTGGCCTTGGGC
ATCTTTGGGAAAAAGTGTTACCTGGGAGACACTTGGAACCGGCTTGACTTTTTCATCGTC
ATCGCAGGGATGCTGGAGTACTCGCTGGACCTGCAGAACGTCAGCTTCTCAGCTGTCAGG
ACAGTCCGTGTGCTGCGACCGCTCAGGGCCATTAACCGGGTGCCCAGCATGCGCATCCTT
GTCACGTTGCTGCTGGATACGCTGCCCATGCTGGGCAACGTCCTGCTGCTCTGCTTCTTC
GTCTTCTTCATCTTCGGCATCGTCGGCGTCCAGCTGTGGGCAGGGCTGCTTCGGAACCGA
TGCTTCCTACCTGAGAATTTCAGCCTCCCCCTGAGCGTGGACCTGGAGCGCTATTACCAG
ACAGAGAACGAGGATGAGAGCCCCTTCATCTGCTCCCAGCCACGCGAGAACGGCATGCGG
TCCTGCAGAAGCGTGCCCACGCTGCGCGGGGACGGGGGCGGTGGCCCACCTTGCGGTCTG
GACTATGAGGCCTACAACAGCTCCAGCAACACCACCTGTGTCAACTGGAACCAGTACTAC
ACCAACTGCTCAGCGGGGGAGCACAACCCCTTCAAGGGCGCCATCAACTTTGACAACATT
GGCTATGCCTGGATCGCCATCTTCCAGGTCATCACGCTGGAGGGCTGGGTCGACATCATG
TACTTTGTGATGGATGCTCATTCCTTCTACAATTTCATCTACTTCATCCTCCTCATCATC
GTGGGCTCCTTCTTCATGATCAACCTGTGCCTGGTGGTGATTGCCACGCAGTTCTCAGAG
ACCAAGCAGCGGGAAAGCCAGCTGATGCGGGAGCAGCGTGTGCGGTTCCTGTCCAACGCC
AGCACCCTGGCTAGCTTCTCTGAGCCCGGCAGCTGCTATGAGGAGCTGCTCAAGTACCTG
GTGTACATCCTTCGTAAGGCAGCCCGCAGGCTGGCTCAGGTCTCTCGGGCAGCAGGTGTG
CGGGTTGGGCTGCTCAGCAGCCCAGCACCCCTCGGGGGCCAGGAGACCCAGCCCAGCAGC
AGCTGCTCTCGCTCCCACCGCCGCCTATCCGTCCACCACCTGGTGCACCACCACCACCAC
CATCACCACCACTACCACCTGGGCAATGGGACGCTCAGGGCCCCCCGGGCCAGCCCGGAG
ATCCAGGACAGGGATGCCAATGGGTCCCGCAGGCTCATGCTGCCACCACCCTCGACGCCT
GCCCTCTCCGGGGCCCCCCCTGGTGGCGCAGAGTCTGTGCACAGCTTCTACCATGCCGAC
TGCCACTTAGAGCCAGTCCGCTGCCAGGCGCCCCCTCCCAGGTCCCCATCTGAGGCATCC
GGCAGGACTGTGGGCAGCGGGAAGGTGTATCCCACCGTGCACACCAGCCCTCCACCGGAG
ACGCTGAAGGAGAAGGCACTAGTAGAGGTGGCTGCCAGCTCTGGGCCCCCAACCCTCACC
AGCCTCAACATCCCACCCGGGCCCTACAGCTCCATGCACAAGCTGCTGGAGACACAGAGT
ACAGGTGCCTGCCAAAGCTCTTGCAAGATCTCCAGCCCTTGCTTGAAAGCAGACAGTGGA
GCCTGTGGTCCAGACAGCTGCCCCTACTGTGCCCGGGCCGGGGCAGGGGAGGTGGAGCTC
GCCGACCGTGAAATGCCTGACTCAGACAGCGAGGCAGTTTATGAGTTCACACAGGATGCC
CAGCACAGCGACCTCCGGGACCCCCACAGCCGGCGGCAACGGAGCCTGGGCCCAGATGCA
GAGCCCAGCTCTGTGCTGGCCTTCTGGAGGCTAATCTGTGACACCTTCCGAAAGATTGTG
GACAGCAAGTACTTTGGCCGGGGAATCATGATCGCCATCCTGGTCAACACACTCAGCATG
GGCATCGAATACCACGAGCAGCCCGAGGAGCTTACCAACGCCCTAGAAATCAGCAACATC
GTCTTCACCAGCCTCTTTGCCCTGGAGATGCTGCTGAAGCTGCTTGTGTATGGTCCCTTT
GGCTACATCAAGAATCCCTACAACATCTTCGATGGTGTCATTGTGGTCATCAGCGTGTGG
GAGATCGTGGGCCAGCAGGGGGGCGGCCTGTCGGTGCTGCGGACCTTCCGCCTGATGCGT
GTGCTGAAGCTGGTGCGCTTCCTGCCGGCGCTGCAGCGGCAGCTGGTGGTGCTCATGAAG
ACCATGGACAACGTGGCCACCTTCTGCATGCTGCTTATGCTCTTCATCTTCATCTTCAGC
ATCCTGGGCATGCATCTCTTCGGCTGCAAGTTTGCCTCTGAGCGGGATGGGGACACCCTG
CCAGACCGGAAGAATTTTGACTCCTTGCTCTGGGCCATCGTCACTGTCTTTCAGATCCTG
ACCCAGGAGGACTGGAACAAAGTCCTCTACAATGGTATGGCCTCCACGTCGTCCTGGGCG
GCCCTTTATTTCATTGCCCTCATGACCTTCGGCAACTACGTGCTCTTCAATTTGCTGGTC
GCCATTCTGGTGGAGGGCTTCCAGGCGGAGGAAATCAGCAAACGGGAAGATGCGAGTGGA
CAGTTAAGCTGTATTCAGCTGCCTGTCGACTCCCAGGGGGGAGATGCCAACAAGTCCGAA
TCAGAGCCCGATTTCTTCTCACCCAGCCTGGATGGTGATGGGGACAGGAAGAAGTGCTTG
GCCTTGGTGTCCCTGGGAGAGCACCCGGAGCTGCGGAAGAGCCTGCTGCCGCCTCTCATC
ATCCACACGGCCGCCACACCCATGTCGCTGCCCAAGAGCACCAGCACGGGCCTGGGCGAG
GCGCTGGGCCCTGCGTCGCGCCGCACCAGCAGCAGCGGGTCGGCAGAGCCTGGGGCGGCC
CACGAGATGAAGTCACCGCCCAGCGCCCGCAGCTCTCCGCACAGCCCCTGGAGCGCTGCA
AGCAGCTGGACCAGCAGGCGCTCCAGCCGGAACAGCCTCGGCCGTGCACCCAGCCTGAAG
CGGAGAAGCCCAAGTGGAGAGCGGCGGTCCCTGTTGTCGGGAGAAGGCCAGGAGAGCCAG
GATGAAGAGGAGAGCTCAGAAGAGGAGCGGGCCAGCCCTGCGGGCAGTGACCATCGCCAC
AGGGGGTCCCTGGAGCGGGAGGCCAAGAGTTCCTTTGACCTGCCAGACACACTGCAGGTG
CCAGGGCTGCATCGCACTGCCAGTGGCCGAGGGTCTGCTTCTGAGCACCAGGACTGCAAT
GGCAAGTCGGCTTCAGGGCGCCTGGCCCGGGCCCTGCGGCCTGATGACCCCCCACTGGAT
GGGGATGACGCCGATGACGAGGGCAACCTGAGCAAAGGGGAACGGGTCCGCGCGTGGATC
CGAGCCCGACTCCCTGCCTGCTGCCTCGAGCGAGACTCCTGGTCAGCCTACATCTTCCCT
CCTCAGTCCAGGTTCCGCCTCCTGTGTCACCGGATCATCACCCACAAGATGTTCGACCAC
GTGGTCCTTGTCATCATCTTCCTTAACTGCATCACCATCGCCATGGAGCGCCCCAAAATT
GACCCCCACAGCGCTGAACGCATCTTCCTGACCCTCTCCAATTACATCTTCACCGCAGTC
TTTCTGGCTGAAATGACAGTGAAGGTGGTGGCACTGGGCTGGTGCTTCGGGGAGCAGGCG
TACCTGCGGAGCAGTTGGAACGTGCTGGACGGGCTGTTGGTGCTCATCTCCGTCATCGAC
ATTCTGGTGTCCATGGTCTCTGACAGCGGCACCAAGATCCTGGGCATGCTGAGGGTGCTG
CGGCTGCTGCGGACCCTGCGCCCGCTCAGGGTGATCAGCCGGGCGCAGGGGCTGAAGCTG
GTGGTGGAGACGCTGATGTCCTCACTGAAACCCATCGGCAACATTGTAGTCATCTGCTGT
GCCTTCTTCATCATTTTCGGCATCTTGGGGGTGCAGCTCTTCAAAGGGAAGTTTTTCGTG
TGCCAGGGCGAGGATACCAGGAACATCACCAATAAATCGGACTGTGCCGAGGCCAGTTAC
CGGTGGGTCCGGCACAAGTACAACTTTGACAACCTTGGCCAGGCCCTGATGTCCCTGTTC
GTTTTGGCCTCCAAGGATGGTTGGGTGGACATCATGTACGATGGGCTGGATGCTGTGGGC
GTGGACCAGCAGCCCATCATGAACCACAACCCCTGGATGCTGCTGTACTTCATCTCGTTC
CTGCTCATTGTGGCCTTCTTTGTCCTGAACATGTTTGTGGGTGTGGTGGTGGAGAACTTC
CACAAGTGTCGGCAGCACCAGGAGGAAGAGGAGGCCCGGCGGCGGGAGGAGAAGCGCCTA
CGAAGACTGGAGAAAAAGAGAAGGAATCTAATGCTGGACGATGTAATTGCTTCCGGCAGC
TCAGCCAGCGCTGCGTCAGAAGCCCAGTGCAAACCTTACTACTCCGACTACTCCCGCTTC
CGGCTCCTCGTCCACCACTTGTGCACCAGCCACTACCTGGACCTCTTCATCACAGGTGTC
ATCGGGCTGAACGTGGTCACCATGGCCATGGAGCACTACCAGCAGCCCCAGATTCTGGAT
GAGGCTCTGAAGATCTGCAACTACATCTTCACTGTCATCTTTGTCTTGGAGTCAGTTTTC
AAACTTGTGGCCTTTGGTTTCCGTCGGTTCTTCCAGGACAGGTGGAACCAGCTGGACCTG
GCCATTGTGCTGCTGTCCATCATGGGCATCACGCTGGAGGAAATCGAGGTCAACGCCTCG
CTGCCCATCAACCCCACCATCATCCGCATCATGAGGGTGCTGCGCATTGCCCGAGTGCTG
AAGCTGCTGAAGATGGCTGTGGGCATGCGGGCGCTGCTGGACACGGTGATGCAGGCCCTG
CCCCAGGTGGGGAACCTGGGACTTCTCTTCATGTTGTTGTTTTTCATCTTTGCAGCTCTG
GGCGTGGAGCTCTTTGGAGACCTGGAGTGTGACGAGACACACCCCTGTGAGGGCCTGGGC
CGTCATGCCACCTTTCGGAACTTTGGCATGGCCTTCCTAACCCTCTTCCGAGTCTCCACA
GGTGACAATTGGAATGGCATTATGAAGGACACCCTCCGGGACTGTGACCAGGAGTCCACC
TGCTACAACACGGTCATCTCGCCTATCTACTTTGTGTCCTTCGTGCTGACGGCCCAGTTC
GTGCTAGTCAACGTGGTGATCGCCGTGCTGATGAAGCACCTGGAGGAGAGCAACAAGGAG
GCCAAGGAGGAGGCCGAGCTAGAGGCTGAGCTGGAGCTGGAGATGAAGACCCTCAGCCCC
CAGCCCCACTCGCCACTGGGCAGCCCCTTCCTCTGGCCTGGGGTCGAGGGCCCCGACAGC
CCCGACAGCCCCAAGCCTGGGGCTCTGCACCCAGCGGCCCACGCGAGATCAGCCTCCCAC
TTTTCCCTGGAGCACCCCACGGACAGGCAGCTGTTTGACACCATATCCCTGCTGATCCAG
GGCTCCCTGGAGTGGGAGCTGAAGCTGATGGACGAGCTGGCAGGCCCAGGGGGCCAGCCC
TCTGCCTTCCCTTCTGCCCCCAGCCTGGGAGGCTCCGACCCACAGATCCCTCTAGCTGAG
ATGGAGGCTCTGTCTCTGACGTCAGAGATTGTGTCTGAACCGTCCTGCTCTCTAGCTCTG
ACGGATGACTCTTTGCCTGATGACATGCACACACTCTTACTTAGTGCCCTGGAGAGCAAT
ATGCAGCCCCACCCCACGGAGCTGCCAGGACCAGACTTACTGACTGTGCGGAAGTCTGGG
GTCAGCCGAACGCACTCTCTGCCCAATGACAGCTACATGTGTCGGCATGGGAGCACTGCC
GAGGGGCCCCTGGGACACAGGGGCTGGGGGCTCCCCAAAGCTCAGTCAGGCTCCGTCTTG
TCCGTTCACTCCCAGCCAGCAGATACCAGCTACATCCTGCAGCTTCCCAAAGATGCACCT
CATCTGCTCCAGCCCCACAGCGCCCCAACCTGGGGCACCATCCCCAAACTGCCCCCACCA
GGACGCTCCCCTTTGGCTCAGAGGCCACTCAGGCGCCAGGCAGCAATAAGGACTGACTCC
TTGGACGTTCAGGGTCTGGGCAGCCGGGAAGACCTGCTGGCAGAGGTGAGTGGGCCCTCC
CCGCCCCTGGCCCGGGCCTACTCTTTCTGGGGCCAGTCAAGTACCCAGGCACAGCAGCAC
TCCCGCAGCCACAGCAAGATCTCCAAGCACATGACCCCGCCAGCCCCTTGCCCAGGCCCA
GAACCCAACTGGGGCAAGGGCCCTCCAGAGACCAGAAGCAGCTTAGAGTTGGACACGGAG
CTGAGCTGGATTTCAGGAGACCTCCTGCCCCCTGGCGGCCAGGAGGAGCCCCCATCCCCA
CGGGACCTGAAGAAGTGCTACAGCGTGGAGGCCCAGAGCTGCCAGCGCCGGCCTACGTCC
TGGCTGGATGAGCAGAGGAGACACTCTATCGCCGTCAGCTGCCTGGACAGCGGCTCCCAA
CCCCACCTGGGCACAGACCCCTCTAACCTTGGGGGCCAGCCTCTTGGGGGGCCTGGGAGC
CGGCCCAAGAAAAAACTCAGCCCGCCTAGTATCACCATAGACCCCCCCGAGAGCCAAGGT
CCTCGGACCCCGCCCAGCCCTGGTATCTGCCTCCGGAGGAGGGCTCCGTCCAGCGACTCC
AAGGATCCCTTGGCCTCTGGCCCCCCTGACAGCATGGCTGCCTCGCCCTCCCCAAAGAAA
GATGTGCTGAGTCTCTCCGGTTTATCCTCTGACCCAGCAGACCTGGACCCCTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID CACNA1G Link Image
Target 4 GenAtlas ID CACNA1G Link Image
Target 4 HGNC ID HGNC:1394 Link Image
Target 4 Chromosome Location 17
Target 4 Locus 17q22
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Toyota M, Ho C, Ohe-Toyota M, Baylin SB, Issa JP: Inactivation of CACNA1G, a T-type calcium channel gene, by aberrant methylation of its 5' CpG island in human tumors. Cancer Res. 1999 Sep 15;59(18):4535-41. [PubMed Link Image]
  2. Mittman S, Guo J, Agnew WS: Structure and alternative splicing of the gene encoding alpha1G, a human brain T calcium channel alpha1 subunit. Neurosci Lett. 1999 Oct 29;274(3):143-6. [PubMed Link Image]
  3. Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [PubMed Link Image]
  4. Cribbs LL, Gomora JC, Daud AN, Lee JH, Perez-Reyes E: Molecular cloning and functional expression of Ca(v)3.1c, a T-type calcium channel from human brain. FEBS Lett. 2000 Jan 21;466(1):54-8. [PubMed Link Image]
  5. Monteil A, Chemin J, Bourinet E, Mennessier G, Lory P, Nargeot J: Molecular and functional properties of the human alpha(1G) subunit that forms T-type calcium channels. J Biol Chem. 2000 Mar 3;275(9):6090-100. [PubMed Link Image]
  6. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  7. Perez-Reyes E, Cribbs LL, Daud A, Lacerda AE, Barclay J, Williamson MP, Fox M, Rees M, Lee JH: Molecular characterization of a neuronal low-voltage-activated T-type calcium channel. Nature. 1998 Feb 26;391(6670):896-900. [PubMed Link Image]
Target 4 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 5 [top]
Target 5 ID 831
Target 5 Name D(2) dopamine receptor
Target 5 Synonyms
  1. Dopamine D2 receptor
Target 5 Gene Name DRD2
Target 5 Protein Sequence >D(2) dopamine receptor 
MDPLNLSWYDDDLERQNWSRPFNGSDGKADRPHYNYYATLLTLLIAVIVFGNVLVCMAVS
REKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTA
SILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISIVWVLSFTISCPLLFGLNNADQN
ECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRRRRKRVNTKRSSRAFRAHLRAPL
KGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARRAQELEMEMLSSTSPPERTRYSPIPP
SHHQLTLPDPSHHGLHSTPDSPAKPEKNGHAKDHPKIAKIFEIQTMPNGKTRTSLKTMSR
RKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSA
VNPIIYTTFNIEFRKAFLKILHC
Target 5 Number of Residues 450
Target 5 Molecular Weight 50620
Target 5 Theoretical pI 9.85
Target 5 GO Classification
Function
signal transducer activity
receptor activity
transmembrane receptor activity
G-protein coupled receptor activity
rhodopsin-like receptor activity
amine receptor activity
dopamine receptor activity
Process
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 5 General Function Involved in dopamine receptor activity
Target 5 Specific Function This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase
Target 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • 38-60
  • 72-97
  • 109-130
  • 152-174
  • 187-210
  • 374-397
  • 406-429
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 181432 Link Image
Target 5 UniProtKB/Swiss-Prot ID P14416 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name DRD2_HUMAN Link Image
Target 5 PDB ID Not Available
Target 5 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 5 Gene Sequence >1332 bp 
ATGGATCCACTGAATCTGTCCTGGTATGATGATGATCTGGAGAGGCAGAACTGGAGCCGG
CCCTTCAACGGGTCAGACGGGAAGGCGGACAGACCCCACTACAACTACTATGCCACACTG
CTCACCCTGCTCATCGCTGTCATCGTCTTCGGCAACGTGCTGGTGTGCATGGCTGTGTCC
CGCGAGAAGGCGCTGCAGACCACCACCAACTACCTGATCGTCAGCCTCGCAGTGGCCGAC
CTCCTCGTCGCCACACTGGTCATGCCATGGGTTGTCTACCTGGAGGTGGTAGGTGAGTGG
AAATTCAGCAGGATTCACTGTGACATCTTCGTCACTCTGGACGTCATGATGTGCACGGCG
AGCATCCTGAACTTGTGTGCCATCAGCATCGACAGGTACACAGCTGTGGCCATGCCCATG
CTGTACAATACGCGCTACAGCTCCAAGCGCCGGGTCACCGTCATGATCTCCATCGTCTGG
GTCCTGTCCTTCACCATCTCCTGCCCACTCCTCTTCGGACTCAATAACGCAGACCAGAAC
GAGTGCATCATTGCCAACCCGGCCTTCGTGGTCTACTCCTCCATCGTCTCCTTCTACGTG
CCCTTCATTGTCACCCTGCTGGTCTACATCAAGATCTACATTGTCCTCCGCAGACGCCGC
AAGCGAGTCAACACCAAACGCAGCAGCCGAGCTTTCAGGGCCCACCTGAGGGCTCCACTA
AAGGGCAACTGTACTCACCCCGAGGACATGAAACTCTGCACCGTTATCATGAAGTCTAAT
GGGAGTTTCCCAGTGAACAGGCGGAGAGTGGAGGCTGCCCGGCGAGCCCAGGAGCTGGAG
ATGGAGATGCTCTCCAGCACCAGCCCACCCGAGAGGACCCGGTACAGCCCCATCCCACCC
AGCCACCACCAGCTGACTCTCCCCGACCCGTCCCACCACGGTCTCCACAGCACTCCTGAC
AGCCCCGCCAAACCAGAGAAGAATGGGCATGCCAAAGACCACCCCAAGATTGCCAAGATC
TTTGAGATCCAGACCATGCCCAATGGCAAAACCCGGACCTCCCTCAAGACCATGAGCCGT
AGAAAGCTCTCCCAGCAGAAGGAGAAGAAAGCCACTCAGATGCTCGCCATTGTTCTCGGC
GTGTTCATCATCTGCTGGCTGCCCTTCTTCATCACACACATCCTGAACATACACTGTGAC
TGCAACATCCCGCCTGTCCTGTACAGCGCCTTCACGTGGCTGGGCTATGTCAACAGCGCC
GTGAACCCCATCATCTACACCACCTTCAACATTGAGTTCCGCAAGGCCTTCCTGAAGATC
CTTCACTGCTGA
Target 5 GenBank Gene ID
Target 5 GeneCard ID DRD2 Link Image
Target 5 GenAtlas ID DRD2 Link Image
Target 5 HGNC ID HGNC:3023 Link Image
Target 5 Chromosome Location 11
Target 5 Locus 11q23
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Klein C, Brin MF, Kramer P, Sena-Esteves M, de Leon D, Doheny D, Bressman S, Fahn S, Breakefield XO, Ozelius LJ: Association of a missense change in the D2 dopamine receptor with myoclonus dystonia. Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):5173-6. [PubMed Link Image]
  2. Seeman P, Nam D, Ulpian C, Liu IS, Tallerico T: New dopamine receptor, D2(Longer), with unique TG splice site, in human brain. Brain Res Mol Brain Res. 2000 Mar 10;76(1):132-41. [PubMed Link Image]
  3. Araki K, Kuwano R, Morii K, Hayashi S, Minoshima S, Shimizu N, Katagiri T, Usui H, Kumanishi T, Takahashi Y: Structure and expression of human and rat D2 dopamine receptor genes. Neurochem Int. 1992 Jul;21(1):91-8. [PubMed Link Image]
  4. Dearry A, Falardeau P, Shores C, Caron MG: D2 dopamine receptors in the human retina: cloning of cDNA and localization of mRNA. Cell Mol Neurobiol. 1991 Oct;11(5):437-53. [PubMed Link Image]
  5. Stormann TM, Gdula DC, Weiner DM, Brann MR: Molecular cloning and expression of a dopamine D2 receptor from human retina. Mol Pharmacol. 1990 Jan;37(1):1-6. [PubMed Link Image]
  6. Robakis NK, Mohamadi M, Fu DY, Sambamurti K, Refolo LM: Human retina D2 receptor cDNAs have multiple polyadenylation sites and differ from a pituitary clone at the 5' non-coding region. Nucleic Acids Res. 1990 Mar 11;18(5):1299. [PubMed Link Image]
  7. Selbie LA, Hayes G, Shine J: DNA homology screening: isolation and characterization of the human D2A dopamine receptor subtype. Adv Second Messenger Phosphoprotein Res. 1990;24:9-14. [PubMed Link Image]
  8. Dal Toso R, Sommer B, Ewert M, Herb A, Pritchett DB, Bach A, Shivers BD, Seeburg PH: The dopamine D2 receptor: two molecular forms generated by alternative splicing. EMBO J. 1989 Dec 20;8(13):4025-34. [PubMed Link Image]
  9. Grandy DK, Marchionni MA, Makam H, Stofko RE, Alfano M, Frothingham L, Fischer JB, Burke-Howie KJ, Bunzow JR, Server AC, et al.: Cloning of the cDNA and gene for a human D2 dopamine receptor. Proc Natl Acad Sci U S A. 1989 Dec;86(24):9762-6. [PubMed Link Image]
  10. Selbie LA, Hayes G, Shine J: The major dopamine D2 receptor: molecular analysis of the human D2A subtype. DNA. 1989 Nov;8(9):683-9. [PubMed Link Image]
  11. 7902708 Itokawa M, Arinami T, Futamura N, Hamaguchi H, Toru M: A structural polymorphism of human dopamine D2 receptor, D2(Ser311-->Cys). Biochem Biophys Res Commun. 1993 Nov 15;196(3):1369-75.
  12. 8471125 Seeman P, Ohara K, Ulpian C, Seeman MV, Jellinger K, Van Tol HH, Niznik HB: Schizophrenia: normal sequence in the dopamine D2 receptor region that couples to G-proteins. DNA polymorphisms in D2. Neuropsychopharmacology. 1993 Feb;8(2):137-42.
Target 5 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed Link Image]
  2. Seeman P: Atypical antipsychotics: mechanism of action. Can J Psychiatry. 2002 Feb;47(1):27-38. [PubMed Link Image]
  3. Silva MR, Bernardi MM, Cruz-Casallas PE, Felicio LF: Pimozide injections into the Nucleus accumbens disrupt maternal behaviour in lactating rats. Pharmacol Toxicol. 2003 Jul;93(1):42-7. [PubMed Link Image]
  4. Muscat R, Sampson D, Willner P: Dopaminergic mechanism of imipramine action in an animal model of depression. Biol Psychiatry. 1990 Aug 1;28(3):223-30. [PubMed Link Image]
  5. Zarrindast MR, Heidari MR: On the mechanisms by which theophylline changes core body temperature in mice. Eur J Pharmacol. 1994 May 12;257(1-2):13-20. [PubMed Link Image]
  6. Freedman SB, Patel S, Marwood R, Emms F, Seabrook GR, Knowles MR, McAllister G: Expression and pharmacological characterization of the human D3 dopamine receptor. J Pharmacol Exp Ther. 1994 Jan;268(1):417-26. [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.