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Showing drug card for Bepridil (DB01244)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:01
Primary Accession Number DB01244
Secondary Accession Number
  • APRD00727
Name Bepridil
Drug Type
  • Approved
  • Small Molecule
Description A long-acting calcium-blocking agent with significant anti-anginal activity. The drug produces significant coronary vasodilation and modest peripheral effects. It has antihypertensive and selective anti-arrhythmia activities and acts as a calmodulin antagonist. [PubChem]
Synonyms
  1. Bepadin
Brand Names
  1. Vascor
Brand Mixtures Not Available
Chemical IUPAC Name N-[3-(2-methylpropoxy)-2-pyrrolidin-1-ylpropyl]-N-(phenylmethyl)aniline
Chemical Formula C24H34N2O
Chemical Structure Structure
CAS Registry Number 64706-54-3
InChI Identifier InChI=1/C24H34N2O/c1-21(2)19-27-20-24(25-15-9-10-16-25)18-26(23-13-7-4-8-14-23)17-22-11-5-3-6-12-22/h3-8,11-14,21,24H,9-10,15-20H2,1-2H3
InChI Key UIEATEWHFDRYRU-UHFFFAOYAT
KEGG Drug Not Available
KEGG Compound C06847 Link Image
PubChem Compound 2351 Link Image
PubChem Substance 186733 Link Image
ChEBI ID Not Available
PharmGKB ID PA448597 Link Image
HET ID BEP Link Image
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link http://www.rxlist.com/cgi/generic2/bepridil.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Bepridil Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 366.5396
Monoisotopic Molecular Weight 366.2671
State Solid
Melting Point Not Available
Experimental Water Solubility Slightly soluble Source: PhysProp
Predicted Water Solubility 6.55e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 5.2 Source: PhysProp
Predicted LogP 5.33 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.75 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES CC(C)COC[C@@H](CN(CC1=CC=CC=C1)C1=CC=CC=C1)N1CCCC1
Canonical SMILES CC(C)COCC(CN(CC1=CC=CC=C1)C1=CC=CC=C1)N1CCCC1
Drug Category
  • Anti-Arrhythmia Agents
  • Antiarrhythmic Agents
  • Antihypertensive Agents
  • Calcium Channel Blockers
  • Vasodilator Agents
ATC Codes
AHFS Codes Not Available
Indication For the treatment of chronic stable angina (classic effort-associated angina).
Pharmacology Bepridil is a calcium channel blocker that has well characterized anti-anginal properties and known but poorly characterized type 1 anti-arrhythmic and anti-hypertensive properties. It is not related chemically to other calcium channel blockers such as diltiazem hydrochloride, nifedipine and verapamil hydrochloride.
Mechanism of Action Bepridil has inhibitory effects on both the slow calcium (L-type) and fast sodium inward currents in myocardial and vascular smooth muscle, interferes with calcium binding to calmodulin, and blocks both voltage and receptor operated calcium channels. Bepridil inhibits the transmembrane influx of calcium ions into cardiac and vascular smooth muscle. This has been demonstrated in isolated myocardial and vascular smooth muscle preparations in which both the slope of the calcium dose response curve and the maximum calcium-induced inotropic response were significantly reduced by bepridil. In cardiac myocytes in vitro, bepridil was shown to be tightly bound to actin. Bepridil regularly reduces heart rate and arterial pressure at rest and at a given level of exercise by dilating peripheral arterioles and reducing total peripheral resistance (afterload) against which the heart works.
Absorption Rapidly and completely absorbed after oral administration.
Toxicity There has been one experience with overdosage in which a patient inadvertently took a single dose of 1600 mg of bepridil. The patient was observed for 72 hours in intensive care, but no significant adverse experiences were noted.
Protein Binding 99%
Biotransformation Hepatic.
Half Life 24-50 hours
Dosage Forms
Form Route
Tablet, film coated 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 bepridil
Astemizole Increased risk of cardiotoxicity and arrhythmias
Atazanavir Atazanavir increases the effect and toxicity of bepridil
Cisapride Increased risk of cardiotoxicity and arrhythmias
Fosamprenavir Amprenavir increases the effect and toxicity of bepridil
Gatifloxacin Increased risk of cardiotoxicity and arrhythmias
Grepafloxacin Increased risk of cardiotoxicity and arrhythmias
Levofloxacin Increased risk of cardiotoxicity and arrhythmias
Moxifloxacin Increased risk of cardiotoxicity and arrhythmias
Ritonavir Ritonavir increases the effect and toxicity of bepridil
Sparfloxacin Increased risk of cardiotoxicity and arrhythmias
Terfenadine Increased risk of cardiotoxicity and arrhythmias
Food Interactions
  • Take with food to reduce nausea.
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)
Targets
  1. Sodium channel protein type 5 subunit alpha
  2. Voltage-dependent P/Q-type calcium channel subunit alpha-1A
  3. Calmodulin
  4. Potassium voltage-gated channel subfamily KQT member 1
  5. Sodium/potassium-transporting ATPase alpha-1 chain
  6. Troponin C, slow skeletal and cardiac muscles
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 220
Target 1 Name Sodium channel protein type 5 subunit alpha
Target 1 Synonyms
  1. HH1
  2. Sodium channel protein type V subunit alpha
  3. Sodium channel protein, cardiac muscle alpha-subunit
  4. Voltage-gated sodium channel subunit alpha Nav1.5
Target 1 Gene Name SCN5A
Target 1 Protein Sequence >Sodium channel protein type 5 subunit alpha 
MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQA
SKKLPDLYGNPPQELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPV
RRAAVKILVHSLFNMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARA
FCLHAFTFLRDPWNWLDFSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIV
GALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLV
WESLDLYLSDPENYLLKNGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAW
AFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQN
QATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRK
RMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSE
ADFADDENSTARESESHHTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGV
VSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQ
RALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTD
LTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQG
WNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALG
NLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWI
ETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQ
LALARIQRGLRFVKRTTWDFCCGLLRHRPQKPAALAAQGQLPSCIATPYSPPPPETEKVP
PTRKETQFEEGEQPGQGTPGDPEPVCVPIAVAESDTDDQEEDEENSLGTEEESSKQQESQ
PVSGWPRGPPDSRTWSQVSATASSEAEASASQADWRQQWKAEPQAPGCGETPEDSCSEGS
TADMTNTAELLEQIPDLGQDVKDPEDCFTEGCVRRCPCCAVDTTQAPGKVWWRLRKTCYH
IVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVA
YGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGM
RVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNN
KSQCESLNLTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQW
EYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKK
LGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKINIL
AKINLLFVAIFTGECIVKLAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPT
LFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFA
YVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPTLPNSNGSRG
DCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEK
FDPEATQFIEYSVLSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKR
VLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSAMVIQRAFRRHLLQRS
LKHASFLFRQQAGSGLSEEDAPEREGLIAYVMSENFSRPLGPPSSSSISSTSFPPSYDSV
TRATSDNLQVRGSDYSHSEDLADFPPSPDRDRESIV
Target 1 Number of Residues 2049
Target 1 Molecular Weight 227165
Target 1 Theoretical pI 5.23
Target 1 GO Classification
Function
voltage-gated ion channel activity
voltage-gated sodium channel activity
transporter activity
ion transporter activity
ion channel activity
Process
cation transport
monovalent inorganic cation transport
sodium ion transport
physiological process
cellular physiological process
transport
ion transport
Component
protein complex
voltage-gated sodium channel complex
cell
membrane
Target 1 General Function Involved in ion channel activity
Target 1 Specific Function This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant Na(+) channel isoform. This channel is responsible for the initial upstroke of the action potential in the electrocardiogram
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 127-150
  • 159-178
  • 192-210
  • 217-236
  • 253-276
  • 390-415
  • 712-736
  • 748-771
  • 780-799
  • 806-825
  • 842-862
  • 914-939
  • 1201-1224
  • 1238-1263
  • 1270-1291
  • 1296-1317
  • 1337-1359
  • 1444-1470
  • 1524-1547
  • 1559-1582
  • 1589-1612
  • 1623-1644
  • 1660-1682
  • 1748-1772
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 184039 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q14524 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name SCN5A_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 1 Gene Sequence >6051 bp 
ATGGCAAACTTCCTATTACCTCGGGGCACCAGCAGCTTCCGCAGGTTCACACGGGAGTCC
CTGGCAGCCATCGAGAAGCGCATGGCGGAGAAGCAAGCCCGCGGCTCAACCACCTTGCAG
GAGAGCCGAGAGGGGCTGCCCGAGGAGGAGGCTCCCCGGCCCCAGCTGGACCTGCAGGCC
TCCAAAAAGCTGCCAGATCTCTATGGCAATCCACCCCAAGAGCTCATCGGAGAGCCCCTG
GAGGACCTGGACCCCTTCTATAGCACCCAAAAGACTTTCATCGTACTGAATAAAGGCAAG
ACCATCTTCCGGTTCAGTGCCACCAACGCCTTGTATGTCCTCAGTCCCTTCCACCCAGTT
CGGAGAGCGGCTGTGAAGATTCTGGTTCACTCGCTCTTCAACATGCTCATCATGTGCACC
ATCCTCACCAACTGCGTGTTCATGGCCCAGCACGACCCTCCACCCTGGACCAAGTATGTC
GAGTACACCTTCACCGCCATTTACACCTTTGAGTCTCTGGTCAAGATTCTGGCTCGAGCT
TTCTGCCTGCACGCGTTCACTTTCCTTCGGGACCCATGGAACTGGCTGGACTTTAGTGTG
ATTATCATGGCATACACAACTGAATTTGTGGACCTGGGCAATGTCTCAGCCTTACGCACC
TTCCGAGTCCTCCGGGCCCTGAAAACTATATCAGTCATTTCAGGGCTGAAGACCATCGTG
GGGGCCCTGATCCAGTCTGTGAAGAAGCTGGCTGATGTGATGGTCCTCACAGTCTTCTGC
CTCAGCGTCTTTGCCCTCATCGGCCTGCAGCTCTTCATGGGCAACCTAAGGCACAAGTGT
GTGCGCAACTTCACAGCGCTCAACGGCACCAACGGCTCCGTGGAGGCCGACGGCTTGGTC
TGGGAATCCCTGGACCTTTACCTCAGTGATCCAGAAAATTACCTGCTCAAGAACGGCACC
TCTGATGTGTTACTGTGTGGGAACAGCTCTGACGCTGGGACATGTCCGGAGGGCTACCGG
TGCCTAAAGGCAGGCGAGAACCCCGACCACGGCTACACCAGCTTCGATTCCTTTGCCTGG
GCCTTTCTTGCACTCTTCCGCCTGATGACGCAGGACTGCTGGGAGCGCCTCTATCAGCAG
ACCCTCAGGTCCGCAGGGAAGATCTACATGATCTTCTTCATGCTTGTCATCTTCCTGGGG
TCCTTCTACCTGGTGAACCTGATCCTGGCCGTGGTCGCAATGGCCTATGAGGAGCAAAAC
CAAGCCACCATCGCTGAGACCGAGGAGAAGGAAAAGCGCTTCCAGGAGGCCATGGAAATG
CTCAAGAAAGAACACGAGGCCCTCACCATCAGGGGTGTGGATACCGTGTCCCGTAGCTCC
TTGGAGATGTCCCCTTTGGCCCCAGTAAACAGCCATGAGAGAAGAAGCAAGAGGAGAAAA
CGGATGTCTTCAGGAACTGAGGAGTGTGGGGAGGACAGGCTCCCCAAGTCTGACTCAGAA
GATGGTCCCAGAGCAATGAATCATCTCAGCCTCACCCGTGGCCTCAGCAGGACTTCTATG
AAGCCACGTTCCAGCCGCGGGAGCATTTTCACCTTTCGCAGGCGAGACCTGGGTTCTGAA
GCAGATTTTGCAGATGATGAAAACAGCACAGCGCGGGAGAGCGAGAGCCACCACACATCA
CTGCTGGTGCCCTGGCCCCTGCGCCGGACCAGTGCCCAGGGACAGCCCAGTCCCGGAACC
TCGGCTCCTGGCCACGCCCTCCATGGCAAAAAGAACAGCACTGTGGACTGCAATGGGGTG
GTCTCATTACTGGGGGCAGGCGACCCAGAGGCCACATCCCCAGGAAGCCACCTCCTCCGC
CCTGTGATGCTAGAGCACCCGCCAGACACGACCACGCCATCGGAGGAGCCAGGCGGCCCC
CAGATGCTGACCTCCCAGGCTCCGTGTGTAGATGGCTTCGAGGAGCCAGGAGCACGGCAG
CGGGCCCTCAGCGCAGTCAGCGTCCTCACAAGCGCACTGGAAGAGTTAGAGGAGTCTCGC
CACAAGTGTCCACCATGCTGGAACCGTCTCGCCCAGCGCTACCTGATCTGGGAGTGCTGC
CCGCTGTGGATGTCCATCAAGCAGGGAGTGAAGTTGGTGGTCATGGACCCGTTTACTGAC
CTCACCATCACTATGTGCATCGTACTCAACACACTCTTCATGGCGCTGGAGCACTACAAC
ATGACAAGTGAATTCGAGGAGATGCTGCAGGTCGGAAACCTGGTCTTCACAGGGATTTTC
ACAGCAGAGATGACCTTCAAGATCATTGCCCTCGACCCCTACTACTACTTCCAACAGGGC
TGGAACATCTTCGACAGCATCATCGTCATCCTTAGCCTCATGGAGCTGGGCCTGTCCCGC
ATGAGCAACTTGTCGGTGCTGCGCTCCTTCCGCCTGCTGCGGGTCTTCAAGCTGGCCAAA
TCATGGCCCACCCTGAACACACTCATCAAGATCATCGGGAACTCAGTGGGGGCACTGGGG
AACCTGACACTGGTGCTAGCCATCATCGTGTTCATCTTTGCTGTGGTGGGCATGCAGCTC
TTTGGCAAGAACTACTCGGAGCTGAGGGACAGCGACTCAGGCCTGCTGCCTCGCTGGCAC
ATGATGGACTTCTTTCATGCCTTCCTAATCATCTTCCGCATCCTCTGTGGAGAGTGGATC
GAGACCATGTGGGACTGCATGGAGGTGTCGGGGCAGTCATTATGCCTGCTGGTCTTCTTG
CTTGTTATGGTCATTGGCAACCTTGTGGTCCTGAATCTCTTCCTGGCCTTGCTGCTCAGC
TCCTTCAGTGCAGACAACCTCACAGCCCCTGATGAGGACAGAGAGATGAACAACCTCCAG
CTGGCCCTGGCCCGCATCCAGAGGGGCCTGCGCTTTGTCAAGCGGACCACCTGGGATTTC
TGCTGTGGTCTCCTGCGGCACCGGCCTCAGAAGCCCGCAGCCCTTGCCGCCCAGGGCCAG
CTGCCCAGCTGCATTGCCACCCCCTACTCCCCGCCACCCCCAGAGACGGAGAAGGTGCCT
CCCACCCGCAAGGAAACACAGTTTGAGGAAGGCGAGCAACCAGGCCAGGGCACCCCCGGG
GATCCAGAGCCCGTGTGTGTGCCCATCGCTGTGGCCGAGTCAGACACAGATGACCAAGAA
GAGGATGAGGAGAACAGCCTGGGCACGGAGGAGGAGTCCAGCAAGCAGCAGGAATCCCAG
CCTGTGTCCGGCTGGCCCAGAGGCCCTCCGGATTCCAGGACCTGGAGCCAGGTGTCAGCG
ACTGCCTCCTCTGAGGCCGAGGCCAGTGCATCTCAGGCCGACTGGCGGCAGCAGTGGAAA
GCGGAACCCCAGGCCCCAGGGTGCGGTGAGACCCCAGAGGACAGTTGCTCCGAGGGCAGC
ACAGCAGACATGACCAACACCGCTGAGCTCCTGGAGCAGATCCCTGACCTCGGCCAGGAT
GTCAAGGACCCAGAGGACTGCTTCACTGAAGGCTGTGTCCGGCGCTGTCCCTGCTGTGCG
GTGGACACCACACAGGCCCCAGGGAAGGTCTGGTGGCGGTTGCGCAAGACCTGCTACCAC
ATCGTGGAGCACAGCTGGTTCGAGACATTCATCATCTTCATGATCCTACTCAGCAGTGGA
GCGCTGGCCTTCGAGGACATCTACCTAGAGGAGCGGAAGACCATCAAGGTTCTGCTTGAG
TATGCCGACAAGATGTTCACATATGTCTTCGTGCTGGAGATGCTGCTCAAGTGGGTGGCC
TACGGCTTCAAGAAGTACTTCACCAATGCCTGGTGCTGGCTCGACTTCCTCATCGTAGAC
GTCTCTCTGGTCAGCCTGGTGGCCAACACCCTGGGCTTTGCCGAGATGGGCCCCATCAAG
TCACTGCGGACGCTGCGTGCACTCCGTCCTCTGAGAGCTCTGTCACGATTTGAGGGCATG
AGGGTGGTGGTCAATGCCCTGGTGGGCGCCATCCCGTCCATCATGAACGTCCTCCTCGTC
TGCCTCATCTTCTGGCTCATCTTCAGCATCATGGGCGTGAACCTCTTTGCGGGGAAGTTT
GGGAGGTGCATCAACCAGACAGAGGGAGACTTGCCTTTGAACTACACCATCGTGAACAAC
AAGAGCCAGTGTGAGTCCTTGAACTTGACCGGAGAATTGTACTGGACCAAGGTGAAAGTC
AACTTTGACAACGTGGGGGCCGGGTACCTGGCCCTTCTGCAGGTGGCAACATTTAAAGGC
TGGATGGACATTATGTATGCAGCTGTGGACTCCAGGGGGTATGAAGAGCAGCCTCAGTGG
GAATACAACCTCTACATGTACATCTATTTTGTCATTTTCATCATCTTTGGGTCTTTCTTC
ACCCTGAACCTCTTTATTGGTGTCATCATTGACAACTTCAACCAACAGAAGAAAAAGTTA
GGGGGCCAGGACATCTTCATGACAGAGGAGCAGAAGAAGTACTACAATGCCATGAAGAAG
CTGGGCTCCAAGAAGCCCCAGAAGCCCATCCCACGGCCCCTGAACAAGTACCAGGGCTTC
ATATTCGACATTGTGACCAAGCAGGCCTTTGACGTCACCATCATGTTTCTGATCTGCTTG
AATATGGTGACCATGATGGTGGAGACAGATGACCAAAGTCCTGAGAAAATCAACATCTTG
GCCAAGATCAACCTGCTCTTTGTGGCCATCTTCACAGGCGAGTGTATTGTCAAGCTGGCT
GCCCTGCGCCACTACTACTTCACCAACAGCTGGAATATCTTCGACTTCGTGGTTGTCATC
CTCTCCATCGTGGGCACTGTGCTCTCGGACATCATCCAGAAGTACTTCTTCTCCCCGACG
CTCTTCCGAGTCATCCGCCTGGCCCGAATAGGCCGCATCCTCAGACTGATCCGAGGGGCC
AAGGGGATCCGCACGCTGCTCTTTGCCCTCATGATGTCCCTGCCTGCCCTCTTCAACATC
GGGCTGCTGCTCTTCCTCGTCATGTTCATCTACTCCATCTTTGGCATGGCCAACTTCGCT
TATGTCAAGTGGGAGGCTGGCATCGACGACATGTTCAACTTCCAGACCTTCGCCAACAGC
ATGCTGTGCCTCTTCCAGATCACCACGTCGGCCGGCTGGGATGGCCTCCTCAGCCCCATC
CTCAACACTGGGCCGCCCTACTGCGACCCCACTCTGCCCAACAGCAATGGCTCTCGGGGG
GACTGCGGGAGCCCAGCCGTGGGCATCCTCTTCTTCACCACCTACATCATCATCTCCTTC
CTCATCGTGGTCAACATGTACATTGCCATCATCCTGGAGAACTTCAGCGTGGCCACGGAG
GAGAGCACCGAGCCCCTGAGTGAGGACGACTTCGATATGTTCTATGAGATCTGGGAGAAA
TTTGACCCAGAGGCCACTCAGTTTATTGAGTATTCGGTCCTGTCTGACTTTGCCGACGCC
CTGTCTGAGCCACTCCGTATCGCCAAGCCCAACCAGATAAGCCTCATCAACATGGACCTG
CCCATGGTGAGTGGGGACCGCATCCATTGCATGGACATTCTCTTTGCCTTCACCAAAAGG
GTCCTGGGGGAGTCTGGGGAGATGGACGCCCTGAAGATCCAGATGGAGGAGAAGTTCATG
GCAGCCAACCCATCCAAGATCTCCTACGAGCCCATCACCACCACACTCCGGCGCAAGCAC
GAAGAGGTGTCGGCCATGGTTATCCAGAGAGCCTTCCGCAGGCACCTGCTGCAACGCTCT
TTGAAGCATGCCTCCTTCCTCTTCCGTCAGCAGGCGGGCAGCGGCCTCTCCGAAGAGGAT
GCCCCTGAGCGAGAGGGCCTCATCGCCTACGTGATGAGTGAGAACTTCTCCCGACCCCTT
GGCCCACCCTCCAGCTCCTCCATCTCCTCCACTTCCTTCCCACCCTCCTATGACAGTGTC
ACTAGAGCCACCAGCGATAACCTCCAGGTGCGGGGGTCTGACTACAGCCACAGTGAAGAT
CTCGCCGACTTCCCCCCTTCTCCGGACAGGGACCGTGAGTCCATCGTGTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID SCN5A Link Image
Target 1 GenAtlas ID SCN5A Link Image
Target 1 HGNC ID HGNC:10593 Link Image
Target 1 Chromosome Location 3
Target 1 Locus 3p21
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Wei J, Wang DW, Alings M, Fish F, Wathen M, Roden DM, George AL Jr: Congenital long-QT syndrome caused by a novel mutation in a conserved acidic domain of the cardiac Na+ channel. Circulation. 1999 Jun 22;99(24):3165-71. [PubMed Link Image]
  2. Wattanasirichaigoon D, Vesely MR, Duggal P, Levine JC, Blume ED, Wolff GS, Edwards SB, Beggs AH: Sodium channel abnormalities are infrequent in patients with long QT syndrome: identification of two novel SCN5A mutations. Am J Med Genet. 1999 Oct 29;86(5):470-6. [PubMed Link Image]
  3. 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]
  4. Wehrens XH, Rossenbacker T, Jongbloed RJ, Gewillig M, Heidbuchel H, Doevendans PA, Vos MA, Wellens HJ, Kass RS: A novel mutation L619F in the cardiac Na+ channel SCN5A associated with long-QT syndrome (LQT3): a role for the I-II linker in inactivation gating. Hum Mutat. 2003 May;21(5):552. [PubMed Link Image]
  5. Gellens ME, George AL Jr, Chen LQ, Chahine M, Horn R, Barchi RL, Kallen RG: Primary structure and functional expression of the human cardiac tetrodotoxin-insensitive voltage-dependent sodium channel. Proc Natl Acad Sci U S A. 1992 Jan 15;89(2):554-8. [PubMed Link Image]
  6. Bennett PB, Yazawa K, Makita N, George AL Jr: Molecular mechanism for an inherited cardiac arrhythmia. Nature. 1995 Aug 24;376(6542):683-5. [PubMed Link Image]
  7. Wang Q, Shen J, Splawski I, Atkinson D, Li Z, Robinson JL, Moss AJ, Towbin JA, Keating MT: SCN5A mutations associated with an inherited cardiac arrhythmia, long QT syndrome. Cell. 1995 Mar 10;80(5):805-11. [PubMed Link Image]
  8. Wang Q, Shen J, Li Z, Timothy K, Vincent GM, Priori SG, Schwartz PJ, Keating MT: Cardiac sodium channel mutations in patients with long QT syndrome, an inherited cardiac arrhythmia. Hum Mol Genet. 1995 Sep;4(9):1603-7. [PubMed Link Image]
  9. Makita N, Shirai N, Nagashima M, Matsuoka R, Yamada Y, Tohse N, Kitabatake A: A de novo missense mutation of human cardiac Na+ channel exhibiting novel molecular mechanisms of long QT syndrome. FEBS Lett. 1998 Feb 13;423(1):5-9. [PubMed Link Image]
  10. An RH, Wang XL, Kerem B, Benhorin J, Medina A, Goldmit M, Kass RS: Novel LQT-3 mutation affects Na+ channel activity through interactions between alpha- and beta1-subunits. Circ Res. 1998 Jul 27;83(2):141-6. [PubMed Link Image]
Target 1 Drug References
  1. Sugao M, Fujiki A, Nishida K, Sakabe M, Tsuneda T, Iwamoto J, Mizumaki K, Inoue H: Repolarization dynamics in patients with idiopathic ventricular fibrillation: pharmacological therapy with bepridil and disopyramide. J Cardiovasc Pharmacol. 2005 Jun;45(6):545-9. [PubMed Link Image]
  2. Ohgo T, Okamura H, Noda T, Satomi K, Suyama K, Kurita T, Aihara N, Kamakura S, Ohe T, Shimizu W: Acute and chronic management in patients with Brugada syndrome associated with electrical storm of ventricular fibrillation. Heart Rhythm. 2007 Jun;4(6):695-700. Epub 2007 Feb 20. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 392
Target 2 Name Voltage-dependent P/Q-type calcium channel subunit alpha-1A
Target 2 Synonyms
  1. BI
  2. Brain calcium channel I
  3. Calcium channel, L type, alpha-1 polypeptide isoform 4
  4. Voltage- gated calcium channel subunit alpha Cav2.1
Target 2 Gene Name CACNA1A
Target 2 Protein Sequence >Voltage-dependent P/Q-type calcium channel subunit alpha-1A 
MARFGDEMPARYGGGGSGAAAGVVVGSGGGRGAGGSRQGGQPGAQRMYKQSMAQRARTMA
LYNPIPVRQNCLTVNRSLFLFSEDNVVRKYAKKITEWPPFEYMILATIIANCIVLALEQH
LPDDDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFAFHKGSYLRNGWNVMDFVVVLTG
ILATVGTEFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMIPLLQIGLLLFFAILIF
AIIGLEFYMGKFHTTCFEEGTDDIQGESPAPCGTEEPARTCPNGTKCQPYWEGPNNGITQ
FDNILFAVLTVFQCITMEGWTDLLYNSNDASGNTWNWLYFIPLIIIGSFFMLNLVLGVLS
GEFAKERERVENRRAFLKLRRQQQIERELNGYMEWISKAEEVILAEDETDGEQRHPFDGA
LRRTTIKKSKTDLLNPEEAEDQLADIASVGSPFARASIKSAKLENSTFFHKKERRMRFYI
RRMVKTQAFYWTVLSLVALNTLCVAIVHYNQPEWLSDFLYYAEFIFLGLFMSEMFIKMYG
LGTRPYFHSSFNCFDCGVIIGSIFEVIWAVIKPGTSFGISVLRALRLLRIFKVTKYWASL
RNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFDEGTPPTNFDTFPAAIMT
VFQILTGEDWNEVMYDGIKSQGGVQGGMVFSIYFIVLTLFGNYTLLNVFLAIAVDNLANA
QELTKDEQEEEEAANQKLALQKAKEVAEVSPLSAANMSIAVKEQQKNQKPAKSVWEQRTS
EMRKQNLLASREALYNEMDPDERWKAAYTRHLRPDMKTHLDRPLVVDPQENRNNNTNKSR
AAEPTVDQRLGQQRAEDFLRKQARYHDRARDPSGSAGLDARRPWAGSQEAELSREGPYGR
ESDHHAREGSLEQPGFWEGEAERGKAGDPHRRHVHRQGGSRESRSGSPRTGADGEHRRHR
AHRRPGEEGPEDKAERRARHREGSRPARGGEGEGEGPDGGERRRRHRHGAPATYEGDARR
EDKERRHRRRKENQGSGVPVSGPNLSTTRPIQQDLGRQDPPLAEDIDNMKNNKLATAESA
APHGSLGHAGLPQSPAKMGNSTDPGPMLAIPAMATNPQNAASRRTPNNPGNPSNPGPPKT
PENSLIVTNPSGTQTNSAKTARKPDHTTVDIPPACPPPLNHTVVQVNKNANPDPLPKKEE
EKKEEEEDDRGEDGPKPMPPYSSMFILSTTNPLRRLCHYILNLRYFEMCILMVIAMSSIA
LAAEDPVQPNAPRNNVLRYFDYVFTGVFTFEMVIKMIDLGLVLHQGAYFRDLWNILDFIV
VSGALVAFAFTGNSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVFNI
LIVYMLFMFIFAVVAVQLFKGKFFHCTDESKEFEKDCRGKYLLYEKNEVKARDREWKKYE
FHYDNVLWALLTLFTVSTGEGWPQVLKHSVDATFENQGPSPGYRMEMSIFYVVYFVVFPF
FFVNIFVALIIITFQEQGDKMMEEYSLEKNERACIDFAISAKPLTRHMPQNKQSFQYRMW
QFVVSPPFEYTIMAMIALNTIVLMMKFYGASVAYENALRVFNIVFTSLFSLECVLKVMAF
GILNYFRDAWNIFDFVTVLGSITDILVTEFGNNFINLSFLRLFRAARLIKLLRQGYTIRI
LLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIGIDVEDEDSDEDEFQITEHNNFR
TFFQALMLLFRSATGEAWHNIMLSCLSGKPCDKNSGILTRECGNEFAYFYFVSFIFLCSF
LMLNLFVAVIMDNFEYLTRDSSILGPHHLDEYVRVWAEYDPAAWGRMPYLDMYQMLRHMS
PPLGLGKKCPARVAYKRLLRMDLPVADDNTVHFNSTLMALIRTALDIKIAKGGADKQQMD
AELRKEMMAIWPNLSQKTLDLLVTPHKSTDLTVGKIYAAMMIMEYYRQSKAKKLQAMREE
QDRTPLMFQRMEPPSPTQEGGPGQNALPSTQLDPGGALMAHESGLKESPSWVTQRAQEMF
QKTGTWSPEQGPPTDMPNSQPNSQSVEMREMGRDGYSDSEHYLPMEGQGRAASMPRLPAE
NQRRRGRPRGNNLSTISDTSPMKRSASVLGPKARRLDDYSLERVPPEENQRHHQRRRDRS
HRASERSLGRYTDVDTGLGTDLSMTTQSGDLPSKERDQERGRPKDRKHRQHHHHHHHHHH
PPPPDKDRYAQERPDHGRARARDQRWSRSPSEGREHMAHRQGSSSVSGSPAPSTSGTSTP
RRGRRQLPQTPSTPRPHVSYSPVIRKAGGSGPPQQQQQQQQQQQAVARPGRAATSGPRRY
PGPTAEPLAGDRPPTGGHSSGRSPRMERRVPGPARSESPRACRHGGARWPASGPHVSEGP
PGPRHHGYYRGSDYDEADGPGSGGGEEAMAGAYDAPPPVRHASSGATGRSPRTPRASGPA
CASPSRHGRRLPNGYYPAHGLARPRGPGSRKGLHEPYSESDDDWC
Target 2 Number of Residues 2546
Target 2 Molecular Weight 282368
Target 2 Theoretical pI 9.10
Target 2 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 2 General Function Involved in voltage-gated calcium channel activity
Target 2 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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the "high-voltage activated" (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin- IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA)
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 99-117
  • 136-155
  • 168-185
  • 191-209
  • 229-248
  • 336-360
  • 488-506
  • 522-541
  • 550-568
  • 579-597
  • 617-636
  • 690-714
  • 1243-1261
  • 1278-1297
  • 1310-1328
  • 1340-1358
  • 1378-1397
  • 1485-1509
  • 1565-1593
  • 1599-1618
  • 1627-1645
  • 1653-1671
  • 1691-1710
  • 1783-1807
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 2213913 Link Image
Target 2 UniProtKB/Swiss-Prot ID O00555 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CAC1A_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 2 Gene Sequence >7533 bp 
ATGGCCCGCTTCGGAGACGAGATGCCGGCCCGCTACGGGGGAGGAGGCTCCGGGGCAGCC
GCCGGGGTGGTCGTGGGCAGCGGAGGCGGGCGAGGAGCCGGGGGCAGCCGGCAGGGCGGG
CAGCCCGGGGCGCAAAGGATGTACAAGCAGTCAATGGCGCAGAGAGCGCGGACCATGGCA
CTCTACAACCCCATCCCCGTCCGACAGAACTGCCTCACGGTTAACCGGTCTCTCTTCCTC
TTCAGCGAAGACAACGTGGTGAGAAAATACGCCAAAAAGATCACCGAATGGCCTCCCTTT
GAATATATGATTTTAGCCACCATCATAGCGAATTGCATCGTCCTCGCACTGGAGCAGCAT
CTGCCTGATGATGACAAGACCCCGATGTCTGAACGGCTGGATGACACAGAACCATACTTC
ATTGGAATTTTTTGTTTCGAGGCTGGAATTAAAATCATTGCCCTTGGGTTTGCCTTCCAC
AAAGGCTCCTACTTGAGGAATGGCTGGAATGTCATGGACTTTGTGGTGGTGCTAACGGGC
ATCTTGGCGACAGTTGGGACGGAGTTTGACCTACGGACGCTGAGGGCAGTTCGAGTGCTG
CGGCCGCTCAAGCTGGTGTCTGGAATCCCAAGTTTACAAGTCGTCCTGAAGTCGATCATG
AAGGCGATGATCCCTTTGCTGCAGATCGGCCTCCTCCTATTTTTTGCAATCCTTATTTTT
GCAATCATAGGGTTAGAATTTTATATGGGAAAATTTCATACCACCTGCTTTGAAGAGGGG
ACAGATGACATTCAGGGTGAGTCTCCGGCTCCATGTGGGACAGAAGAGCCCGCCCGCACC
TGCCCCAATGGGACCAAATGTCAGCCCTACTGGGAAGGGCCCAACAACGGGATCACTCAG
TTCGACAACATCCTGTTTGCAGTGCTGACTGTTTTCCAGTGCATAACCATGGAAGGGTGG
ACTGATCTCCTCTACAATAGCAACGATGCCTCAGGGAACACTTGGAACTGGTTGTACTTC
ATCCCCCTCATCATCATCGGCTCCTTTTTTATGCTGAACCTTGTGCTGGGTGTGCTGTCA
GGGGAGTTTGCCAAAGAAAGGGAACGGGTGGAGAACCGGCGGGCTTTTCTGAAGCTGAGG
CGGCAACAACAGATTGAACGTGAGCTCAATGGGTACATGGAATGGATCTCAAAAGCAGAA
GAGGTGATCCTCGCCGAGGATGAAACTGACGGGGAGCAGAGGCATCCCTTTGATGGAGCT
CTGCGGAGAACCACCATAAAGAAAAGCAAGACAGATTTGCTCAACCCCGAAGAGGCTGAG
GATCAGCTGGCTGATATAGCCTCTGTGGGTTCTCCCTTCGCCCGAGCCAGCATTAAAAGT
GCCAAGCTGGAGAACTCGACCTTTTTTCACAAAAAGGAGAGGAGGATGCGTTTCTACATC
CGCCGCATGGTCAAAACTCAGGCCTTCTACTGGACTGTACTCAGTTTGGTAGCTCTCAAC
ACGCTGTGTGTTGCTATTGTTCACTACAACCAGCCCGAGTGGCTCTCCGACTTCCTTTAC
TATGCAGAATTCATTTTCTTAGGACTCTTTATGTCCGAAATGTTTATAAAAATGTACGGG
CTTGGGACGCGGCCTTACTTCCACTCTTCCTTCAACTGCTTTGACTGTGGGGTTATCATT
GGGAGCATCTTCGAGGTCATCTGGGCTGTCATAAAACCTGGCACATCCTTTGGAATCAGC
GTGTTACGAGCCCTCAGGTTATTGCGTATTTTCAAAGTCACAAAGTACTGGGCATCTCTC
AGAAACCTGGTCGTCTCTCTCCTCAACTCCATGAAGTCCATCATCAGCCTGTTGTTTCTC
CTTTTCCTGTTCATTGTCGTCTTCGCCCTTTTGGGAATGCAACTCTTCGGCGGCCAGTTT
AATTTCGATGAAGGGACTCCTCCCACCAACTTCGATACTTTTCCAGCAGCAATAATGACG
GTGTTTCAGATCCTGACGGGCGAAGACTGGAACGAGGTCATGTACGACGGGATCAAGTCT
CAGGGGGGCGTGCAGGGCGGCATGGTGTTCTCCATCTATTTCATTGTACTGACGCTCTTT
GGGAACTACACCCTCCTGAATGTGTTCTTGGCCATCGCTGTGGACAATCTGGCCAACGCC
CAGGAGCTCACCAAGGTGGAGGCGGACGAGCAAGAGGAAGAAGAAGCAGCGAACCAGAAA
CTTGCCCTACAGAAAGCCAAGGAGGTGGCAGAAGTGAGTCCTCTGTCCGCGGCCAACATG
TCTATAGCTGTGAAAGAGCAACAGAAGAATCAAAAGCCAGCCAAGTCCGTGTGGGAGCAG
CGGACCAGTGAGATGCGAAAGCAGAACTTGCTGGCCAGCCGGGAGGCCCTGTATAACGAA
ATGGACCCGGACGAGCGCTGGAAGGCTGCCTACACGCGGCACCTGCGGCCAGACATGAAG
ACGCACTTGGACCGGCCGCTGGTGGTGGACCCGCAGGAGAACCGCAACAACAACACCAAC
AAGAGCCGGGCGGCCGAGCCCACCGTGGACCAGCGCCTCGGCCAGCAGCGCGCCGAGGAC
TTCCTCAGGAAACAGGCCCGCTACCACGATCGGGCCCGGGACCCCAGCGGCTCGGCGGGC
CTGGACGCACGGAGGCCCTGGGCGGGAAGCCAGGAGGCCGAGCTGAGCCGGGAGGGACCC
TACGGCCGCGAGTCGGACCACCACGCCCGGGAGGGCAGCCTGGAGCAACCCGGGTTCTGG
GAGGGCGAGGCCGAGCGAGGCAAGGCCGGGGACCCCCACCGGAGGCACGTGCACCGGCAG
GGGGGCAGCAGGGAGAGCCGCAGCGGGTCCCCGCGCACGGGCGCGGACGGGGAGCATCGA
CGTCATCGCGCGCACCGCAGGCCCGGGGAGGAGGGTCCGGAGGACAAGGCGGAGCGGAGG
GCGCGGCACCGCGAGGGCAGCCGGCCGGCCCGGGGCGGCGAGGGCGAGGGCGAGGGCCCC
GACGGGGGCGAGCGCAGGAGAAGGCACCGGCATGGCGCTCCAGCCACGTACGAGGGGGAC
GCGCGGAGGGAGGACAAGGAGCGGAGGCATCGGAGGAGGAAAGAGAACCAGGGCTCCGGG
GTCCCTGTGTCGGGCCCCAACCTGTCAACCACCCGGCCAATCCAGCAGGACCTGGGCCGC
CAAGACCCACCCCTGGCAGAGGATATTGACAACATGAAGAACAACAAGCTGGCCACCGCG
GAGTCGGCCGCTCCCCACGGCAGCCTTGGCCACGCCGGCCTGCCCCAGAGCCCAGCCAAG
ATGGGAAACAGCACCGACCCCGGCCCCATGCTGGCCATCCCTGCCATGGCCACCAACCCC
CAGAACGCCGCCAGCCGCCGGACGCCCAACAACCCGGGGAACCCATCCAATCCCGGCCCC
CCCAAGACCCCCGAGAATAGCCTTATCGTCACCAACCCCAGCGGCACCCAGACCAATTCA
GCTAAGACTGCCAGGAAACCCGACCACACCACAGTGGACATCCCCCCAGCCTGCCCACCC
CCCCTCAACCACACCGTCGTACAAGTGAACAAAAACGCCAACCCAGACCCACTGCCAAAA
AAAGAGGAAGAGAAGAAGGAGGAGGAGGAAGACGACCGTGGGGAAGACGGCCCTAAGCCA
ATGCCTCCCTATAGCTCCATGTTCATCCTGTCCACGACCAACCCCCTTCGCCGCCTGTGC
CATTACATCCTGAACCTGCGCTACTTTGAGATGTGCATCCTCATGGTCATTGCCATGAGC
AGCATCGCCCTGGCCGCCGAGGACCCTGTGCAGCCCAACGCACCTCGGAACAACGTGCTG
CGATACTTTGACTACGTTTTTACAGGCGTCTTCACCTTTGAGATGGTGATCAAGATGATT
GACCTGGGGCTCGTCCTGCATCAGGGTGCCTACTTCCGTGACCTCTGGAATATTCTCGAC
TTCATAGTGGTCAGTGGGGCCCTGGTAGCCTTTGCCTTCACTGGCAATAGCAAAGGAAAA
GACATCAACACGATTAAATCCCTCCGAGTCCTCCGGGTGCTACGACCTCTTAAAACCATC
AAGCGGCTGCCAAAGCTCAAGGCTGTGTTTGACTGTGTGGTGAACTCACTTAAAAACGTC
TTCAACATCCTCATCGTCTACATGCTATTCATGTTCATCTTCGCCGTGGTGGCTGTGCAG
CTCTTCAAGGGGAAATTCTTCCACTGCACTGACGAGTCCAAAGAGTTTGAGAAAGATTGT
CGAGGCAAATACCTCCTCTACGAGAAGAATGAGGTGAAGGCGCGAGACCGGGAGTGGAAG
AAGTATGAATTCCATTACGACAATGTGCTGTGGGCTCTGCTGACCCTCTTCACCGTGTCC
ACGGGAGAAGGCTGGCCACAGGTCCTCAAGCATTCGGTGGACGCCACCTTTGAGAACCAG
GGCCCCAGCCCCGGGTACCGCATGGAGATGTCCATTTTCTACGTCGTCTACTTTGTGGTG
TTCCCCTTCTTCTTTGTCAATATCTTTGTGGCCTTGATCATCATCACCTTCCAGGAGCAA
GGGGACAAGATGATGGAGGAATACAGCCTGGAGAAAAATGAGAGGGCCTGCATTGATTTC
GCCATCAGCGCCAAGCCGCTGACCCGACACATGCCGCAGAACAAGCAGAGCTTCCAGTAC
CGCATGTGGCAGTTCGTGGTGTCTCCGCCTTTCGAGTACACGATCATGGCCATGATCGCC
CTCAACACCATCGTGCTTATGATGAAGTTCTATGGGGCTTCTGTTGCTTATGAAAATGCC
CTGCGGGTGTTCAACATCGTCTTCACCTCCCTCTTCTCTCTGGAATGTGTGCTGAAAGTC
ATGGCTTTTGGGATTCTGAATTATTTCCGCGATGCCTGGAACATCTTCGACTTTGTGACT
GTTCTGGGCAGCATCACCGATATCCTCGTGACTGAGTTTGGGAATCCGAATAACTTCATC
AACCTGAGCTTTCTCCGCCTCTTCCGAGCTGCCCGGCTCATCAAACTTCTCCGTCAGGGT
TACACCATCCGCATTCTTCTCTGGACCTTTGTGCAGTCCTTCAAGGCCCTGCCTTATGTC
TGTCTGCTGATCGCCATGCTCTTCTTCATCTATGCCATCATTGGGATGCAGGTGTTTGGT
AACATTGGCATCGACGTGGAGGACGAGGACAGTGATGAAGATGAGTTCCAAATCACTGAG
CACAATAACTTCCGGACCTTCTTCCAGGCCCTCATGCTTCTCTTCCGGAGTGCCACCGGG
GAAGCTTGGCACAACATCATGCTTTCCTGCCTCAGCGGGAAACCGTGTGATAAGAACTCT
GGCATCCTGACTCGAGAGTGTGGCAATGAATTTGCTTATTTTTACTTTGTTTCCTTCATC
TTCCTCTGCTCGTTTCTGATGCTGAATCTCTTTGTCGCCGTCATCATGGACAACTTTGAG
TACCTCACCCGAGACTCCTCCATCCTGGGCCCCCACCACCTGGATGAGTACGTGCGTGTC
TGGGCCGAGTATGACCCCGCAGCTTGGGGCCGCATGCCTTACCTGGACATGTATCAGATG
CTGAGACACATGTCTCCGCCCCTGGGTCTGGGGAAGAAGTGTCCGGCCAGAGTGGCTTAC
AAGCGGCTTCTGCGGATGGACCTGCCCGTCGCAGATGACAACACCGTCCACTTCAATTCC
ACCCTCATGGCTCTGATCCGCACAGCCCTGGACATCAAGATTGCCAAGGGAGGAGCCGAC
AAACAGCAGATGGACGCTGAGCTGCGGAAGGAGATGATGGCGATTTGGCCCAATCTGTCC
CAGAAGACGCTAGACCTGCTGGTCACACCTCACAAGTCCACGGACCTCACCGTGGGGAAG
ATCTACGCAGCCATGATGATCATGGAGTACTACCGGCAGAGCAAGGCCAAGAAGCTGCAG
GCCATGCGCGAGGAGCAGGACCGGACACCCCTCATGTTCCAGCGCATGGAGCCCCCGTCC
CCAACGCAGGAAGGGGGACCTGGCCAGAACGCCCTCCCCTCCACCCAGCTGGACCCAGGA
GGAGCCCTGATGGCTCACGAAAGCGGCCTCAAGGAGAGCCCGTCCTGGGTGACCCAGCGT
GCCCAGGAGATGTTCCAGAAGACGGGCACATGGAGTCCGGAACAAGGCCCCCCTACCGAC
ATGCCCAACAGCCAGCCTAACTCTCAGTCCGTGGAGATGCGAGAGATGGGCAGAGATGGC
TACTCCGACAGCGAGCACTACCTCCCCATGGAAGGCCAGGGCCGGGCTGCCTCCATGCCC
CGCCTCCCTGCAGAGAACCAGAGGAGAAGGGGCCGGCCACGTGGGAATAACCTCAGTACC
ATCTCAGACACCAGCCCCATGAAGCGTTCAGCCTCCGTGCTGGGCCCCAAGGCCCGACGC
CTGGACGATTACTCGCTGGAGCGGGTCCCGCCCGAGGAGAACCAGCGGCACCACCAGCGG
CGCCGCGACCGCAGCCACCGCGCCTCTGAGCGCTCCCTGGGCCGCTACACCGATGTGGAC
ACAGGCTTGGGGACAGACCTGAGCATGACCACCCAATCCGGGGACCTGCCGTCGAAGGAG
CGGGACCAGGAGCGGGGCCGGCCCAAGGATCGGAAGCATCGACAGCACCACCACCACCAC
CACCACCACCACCATCCCCCGCCCCCCGACAAGGACCGCTATGCCCAGGAACGGCCGGAC
CACGGCCGGGCACGGGCTCGGGACCAGCGCTGGTCCCGCTCGCCCAGCGAGGGCCGAGAG
CACATGGCGCACCGGCAGGGCAGTAGTTCCGTAAGTGGAAGCCCAGCCCCCTCAACATCT
GGTACCAGCACTCCGCGGCGGGGCCGCCGCCAGCTCCCCCAGACCCCCTCCACCCCCCGG
CCACACGTGTCCTATTCCCCTGTGATCCGTAAGGCCGGCGGCTCGGGGCCCCCGCAGCAG
CAGCAGCAGCAGCAGCAGCAGCAGCAGGCGGTGGCCAGGCCGGGCCGGGCGGCCACCAGC
GGCCCTCGGAGGTACCCAGGCCCCACGGCCGAGCCTCTGGCCGGAGATCGGCCGCCCACG
GGGGGCCACAGCAGCGGCCGCTCGCCCAGGATGGAGAGGCGGGTCCCAGGCCCGGCCCGG
AGCGAGTCCCCCAGGGCCTGTCGACACGGCGGGGCCCGGTGGCCGGCATCTGGCCCGCAC
GTGTCCGAGGGGCCCCCGGGTCCCCGGCACCATGGCTACTACCGGGGCTCCGACTACGAC
GAGGCCGATGGCCCGGGCAGCGGGGGCGGCGAGGAGGCCATGGCCGGGGCCTACGACGCG
CCACCCCCCGTACGACACGCGTCCTCGGGCGCCACCGGGCGCTCGCCCAGGACTCCCCGG
GCCTCGGGCCCGGCCTGCGCCTCGCCTTCTCGGCACGGCCGGCGACTCCCCAACGGCTAC
TACCCGGCGCACGGACTGGCCAGGCCCCGCGGGCCGGGCTCCAGGAAGGGCCTGCACGAA
CCCTACAGCGAGAGTGACGATGATTGGTGCTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID CACNA1A Link Image
Target 2 GenAtlas ID CACNA1A Link Image
Target 2 HGNC ID HGNC:1388 Link Image
Target 2 Chromosome Location 19
Target 2 Locus 19p13.2-p13.1
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Hans M, Urrutia A, Deal C, Brust PF, Stauderman K, Ellis SB, Harpold MM, Johnson EC, Williams ME: Structural elements in domain IV that influence biophysical and pharmacological properties of human alpha1A-containing high-voltage-activated calcium channels. Biophys J. 1999 Mar;76(3):1384-400. [PubMed Link Image]
  2. Barry EL, Viglione MP, Kim YI, Froehner SC: Expression and antibody inhibition of P-type calcium channels in human small-cell lung carcinoma cells. J Neurosci. 1995 Jan;15(1 Pt 1):274-83. [PubMed Link Image]
  3. Margolis RL, Breschel TS, Li SH, Kidwai AS, Antonarakis SE, McInnis MG, Ross CA: Characterization of cDNA clones containing CCA trinucleotide repeats derived from human brain. Somat Cell Mol Genet. 1995 Jul;21(4):279-84. [PubMed Link Image]
  4. Ophoff RA, Terwindt GM, Vergouwe MN, van Eijk R, Oefner PJ, Hoffman SM, Lamerdin JE, Mohrenweiser HW, Bulman DE, Ferrari M, Haan J, Lindhout D, van Ommen GJ, Hofker MH, Ferrari MD, Frants RR: Familial hemiplegic migraine and episodic ataxia type-2 are caused by mutations in the Ca2+ channel gene CACNL1A4. Cell. 1996 Nov 1;87(3):543-52. [PubMed Link Image]
  5. Zhuchenko O, Bailey J, Bonnen P, Ashizawa T, Stockton DW, Amos C, Dobyns WB, Subramony SH, Zoghbi HY, Lee CC: Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the alpha 1A-voltage-dependent calcium channel. Nat Genet. 1997 Jan;15(1):62-9. [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]
Drug Target 3 [top]
Target 3 ID 465
Target 3 Name Calmodulin
Target 3 Synonyms
  1. CaM
Target 3 Gene Name CALM1
Target 3 Protein Sequence >Calmodulin 
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK
Target 3 Number of Residues 150
Target 3 Molecular Weight 16707
Target 3 Theoretical pI 3.84
Target 3 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 3 General Function Involved in calcium ion binding
Target 3 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 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 179888 Link Image
Target 3 UniProtKB/Swiss-Prot ID P62158 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name CALM_HUMAN Link Image
Target 3 PDB ID 1IQ5 Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >450 bp 
ATGGCTGACCAGCTGACTGAGGAGCAGATTGCAGAGTTCAAGGAGGCCTTCTCCCTCTTT
GACAAGGATGGAGATGGCACTATCACCACCAAGGAGTTGGGGACAGTGATGAGATCCCTG
GGACAGAACCCCACTGAAGCAGAGCTGCAGGATATGATCAATGAGGTGGATGCAGATGGG
AACGGGACCATTGACTTCCCGGAGTTCCTGACCATGATGGCCAGAAAGATGAAGGACACA
GACAGTGAGGAGGAGATCCGAGAGGCGTTCCGTGTCTTTGACAAGGATGGGAATGGCTAC
ATCAGCGCCGCAGAGCTGCGTCACGTAATGACGAACCTGGGGGAGAAGCTGACCGATGAG
GAGGTGGATGAGATGATCAGGGAGGCTGACATCGATGGAGATGGCCAGGTCAATTATGAA
GAGTTTGTACAGATGATGACTGCAAAGTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID CALM1 Link Image
Target 3 GenAtlas ID CALM1 Link Image
Target 3 HGNC ID HGNC:1442 Link Image
Target 3 Chromosome Location 14
Target 3 Locus 14q24-q31
Target 3 SNPs SNPJam Report Link Image
Target 3 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 3 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 4 [top]
Target 4 ID 741
Target 4 Name Potassium voltage-gated channel subfamily KQT member 1
Target 4 Synonyms
  1. IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1
  2. KQT-like 1
  3. Voltage-gated potassium channel subunit Kv7.1
Target 4 Gene Name KCNQ1
Target 4 Protein Sequence >Potassium voltage-gated channel subfamily KQT member 1 
MAAASSPPRAERKRWGWGRLPGARRGSAGLAKKCPFSLELAEGGPAGGALYAPIAPGAPG
PAPPASPAAPAAPPVASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGW
KCFVYHFAVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGC
RSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLH
VDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYA
DALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQR
QKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKK
KKFKLDKDNGVTPGEKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFM
RTNSFAEDLDLEGETLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRD
VIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVT
QLDQRLALITDMLHQLLSLHGGSTPGSGGPPREGGAHITQPCGSGGSVDPELFLPSNTLP
TYEQLTVPRRGPDEGS
Target 4 Number of Residues 687
Target 4 Molecular Weight 74699
Target 4 Theoretical pI 10.39
Target 4 GO Classification
Function
voltage-gated ion channel activity
voltage-gated potassium channel activity
transporter activity
ion transporter activity
ion channel activity
Process
cation transport
monovalent inorganic cation transport
potassium ion transport
physiological process
cellular physiological process
transport
ion transport
Component
protein complex
voltage-gated potassium channel complex
cell
membrane
Target 4 General Function Inorganic ion transport and metabolism
Target 4 Specific Function Probably important in cardiac repolarization. Associates with KCNE1 (MinK) to form the I(Ks) cardiac potassium current. Elicits a rapidly activating, potassium-selective outward current. Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current in CHO cells in which cloned KCNQ1/KCNE1 channels were coexpressed with M1 muscarinic receptors. May associate also with KCNE3 (MiRP2) to form the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions, which is reduced in cystic fibrosis and pathologically stimulated in cholera and other forms of secretory diarrhea
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • 122-142
  • 148-168
  • 197-217
  • 226-248
  • 262-282
  • 328-348
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 2465531 Link Image
Target 4 UniProtKB/Swiss-Prot ID P51787 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name KCNQ1_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 4 Gene Sequence >2031 bp 
ATGGCCGCGGCCTCCTCCCCGCCCAGGGCCGAGAGGAAGCGCTGGGGTTGGGGCCGCCTG
CCAGGCGCCCGGCGGGGCAGCGCGGGCCTGGCCAAGAAGTGCCCCTTCTCGCTGGAGCTG
GCGGAGGGCGGCCCGGCGGGCGGCGCGCTCTACGCGCCCATCGCGCCCGGCGCCCCAGGT
CCCGCGCCCCCTGCGTCCCCGGCCGCGCCCGCCGCGCCCCCAGTTGCCTCCGACCTTGGC
CCGCGGCCGCCGGTGAGCCTAGACCCGCGCGTCTCCATTTACAGCACGCGCCGCCCGGTG
TTGGCGCGCACCCACGTCCAGGGCCGCGTCTACAACTTCCTCGAGCGTCCCACCGGCTGG
AAATGCTTCGTTTACCACTTCGCCGTCTTCCTCATCGTCCTGGTCTGCCTCATCTTCAGC
GTGCTGTCCACCATCGAGCAGTATGCCGCCCTGGCCACGGGGACTCTCTTCTGGATGGAG
ATCGTGCTGGTGGTGTTCTTCGGGACGGAGTACGTGGTCCGCCTCTGGTCCGCCGGCTGC
CGCAGCAAGTACGTGGGCCTCTGGGGGCGGCTGCGCTTTGCCCGGAAGCCCATTTCCATC
ATCGACCTCATCGTGGTCGTGGCCTCCATGGTGGTCCTCTGCGTGGGCTCCAAGGGGCAG
GTGTTTGCCACGTCGGCCATCAGGGGCATCCGCTTCCTGCAGATCCTGAGGATGCTACAC
GTCGACCGCCAGGGAGGCACCTGGAGGCTCCTGGGCTCCGTGGTCTTCATCCACCGCCAG
GAGCTGATAACCACCCTGTACATCGGCTTCCTGGGCCTCATCTTCTCCTCGTACTTTGTG
TACCTGGCTGAGAAGGACGCGGTGAACGAGTCAGGCCGCGTGGAGTTCGGCAGCTACGCA
GATGCGCTGTGGTGGGGGGTGGTCACAGTCACCACCATCGGCTATGGGGACAAGGTGCCC
CAGACGTGGGTCGGGAAGACCATCGCCTCCTGCTTCTCTGTCTTTGCCATCTCCTTCTTT
GCGCTCCCAGCGGGGATTCTTGGCTCGGGGTTTGCCCTGAAGGTGCAGCAGAAGCAGAGG
CAGAAGCACTTCAACCGGCAGATCCCGGCGGCAGCCTCACTCATTCAGACCGCATGGAGG
TGCTATGCTGCCGAGAACCCCGACTCCTCCACCTGGAAGATCTACATCCGGAAGGCCCCC
CGGAGCCACACTCTGCTGTCACCCAGCCCCAAACCCAAGAAGTCTGTGGTGGTAAAGAAA
AAAAAGTTCAAGCTGGACAAAGACAATGGGGTGACTCCTGGAGAGAAGATGCTCACAGTC
CCCCATATCACGTGCGACCCCCCAGAAGAGCGGCGGCTGGACCACTTCTCTGTCGACGGC
TATGACAGTTCTGTAAGGAAGAGCCCAACACTGCTGGAAGTGAGCATGCCCCATTTCATG
AGAACCAACAGCTTCGCCGAGGACCTGGACCTGGAAGGGGAGACTCTGCTGACACCCATC
ACCCACATCTCACAGCTGCGGGAACACCATCGGGCCACCATTAAGGTCATTCGACGCATG
CAGTACTTTGTGGCCAAGAAGAAATTCCAGCAAGCGCGGAAGCCTTACGATGTGCGGGAC
GTCATTGAGCAGTACTCGCAGGGCCACCTCAACCTCATGGTGCGCATCAAGGAGCTGCAG
AGGAGGCTGGACCAGTCCATTGGGAAGCCCTCACTGTTCATCTCCGTCTCAGAAAAGAGC
AAGGATCGCGGCAGCAACACGATCGGCGCCCGCCTGAACCGAGTAGAAGACAAGGTGACG
CAGCTGGACCAGAGGCTGGCACTCATCACCGACATGCTTCACCAGCTGCTCTCCTTGCAC
GGTGGCAGCACCCCCGGCAGCGGCGGCCCCCCCAGAGAGGGCGGGGCCCACATCACCCAG
CCCTGCGGCAGTGGCGGCTCCGTCGACCCTGAGCTCTTCCTGCCCAGCAACACCCTGCCC
ACCTACGAGCAGCTGACCGTGCCCAGGAGGGGCCCCGATGAGGGGTCCTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID KCNQ1 Link Image
Target 4 GenAtlas ID KCNQ1 Link Image
Target 4 HGNC ID HGNC:6294 Link Image
Target 4 Chromosome Location 11
Target 4 Locus 11p15.5
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Neyroud N, Richard P, Vignier N, Donger C, Denjoy I, Demay L, Shkolnikova M, Pesce R, Chevalier P, Hainque B, Coumel P, Schwartz K, Guicheney P: Genomic organization of the KCNQ1 K+ channel gene and identification of C-terminal mutations in the long-QT syndrome. Circ Res. 1999 Feb 19;84(3):290-7. [PubMed Link Image]
  2. Mohammad-Panah R, Demolombe S, Neyroud N, Guicheney P, Kyndt F, van den Hoff M, Baro I, Escande D: Mutations in a dominant-negative isoform correlate with phenotype in inherited cardiac arrhythmias. Am J Hum Genet. 1999 Apr;64(4):1015-23. [PubMed Link Image]
  3. 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]
  4. Larsen LA, Christiansen M, Vuust J, Andersen PS: High-throughput single-strand conformation polymorphism analysis by automated capillary electrophoresis: robust multiplex analysis and pattern-based identification of allelic variants. Hum Mutat. 1999;13(4):318-27. [PubMed Link Image]
  5. Denjoy I, Lupoglazoff JM, Donger C, Berthet M, Richard P, Neyroud N, Villain E, Lucet V, Coumel P, Guicheney P: [Congenital long QT syndrome. The value of genetics in prognostic evaluation] Arch Mal Coeur Vaiss. 1999 May;92(5):557-63. [PubMed Link Image]
  6. Franqueza L, Lin M, Shen J, Splawski I, Keating MT, Sanguinetti MC: Long QT syndrome-associated mutations in the S4-S5 linker of KvLQT1 potassium channels modify gating and interaction with minK subunits. J Biol Chem. 1999 Jul 23;274(30):21063-70. [PubMed Link Image]
  7. Larsen LA, Fosdal I, Andersen PS, Kanters JK, Vuust J, Wettrell G, Christiansen M: Recessive Romano-Ward syndrome associated with compound heterozygosity for two mutations in the KVLQT1 gene. Eur J Hum Genet. 1999 Sep;7(6):724-8. [PubMed Link Image]
  8. Schroeder BC, Waldegger S, Fehr S, Bleich M, Warth R, Greger R, Jentsch TJ: A constitutively open potassium channel formed by KCNQ1 and KCNE3. Nature. 2000 Jan 13;403(6766):196-9. [PubMed Link Image]
  9. Schmitt N, Schwarz M, Peretz A, Abitbol I, Attali B, Pongs O: A recessive C-terminal Jervell and Lange-Nielsen mutation of the KCNQ1 channel impairs subunit assembly. EMBO J. 2000 Feb 1;19(3):332-40. [PubMed Link Image]
  10. Tranebjaerg L, Bathen J, Tyson J, Bitner-Glindzicz M: Jervell and Lange-Nielsen syndrome: a Norwegian perspective. Am J Med Genet. 1999 Sep 24;89(3):137-46. [PubMed Link Image]
  11. 10713961 Selyanko AA, Hadley JK, Wood IC, Abogadie FC, Jentsch TJ, Brown DA: Inhibition of KCNQ1-4 potassium channels expressed in mammalian cells via M1 muscarinic acetylcholine receptors. J Physiol. 2000 Feb 1;522 Pt 3:349-55.
  12. 10728423 Chouabe C, Neyroud N, Richard P, Denjoy I, Hainque B, Romey G, Drici MD, Guicheney P, Barhanin J: Novel mutations in KvLQT1 that affect Iks activation through interactions with Isk. Cardiovasc Res. 2000 Mar;45(4):971-80.
  13. 10973849 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.
  14. 12522251 Chen YH, Xu SJ, Bendahhou S, Wang XL, Wang Y, Xu WY, Jin HW, Sun H, Su XY, Zhuang QN, Yang YQ, Li YB, Liu Y, Xu HJ, Li XF, Ma N, Mou CP, Chen Z, Barhanin J, Huang W: KCNQ1 gain-of-function mutation in familial atrial fibrillation. Science. 2003 Jan 10;299(5604):251-4.
  15. 8528244 Wang Q, Curran ME, Splawski I, Burn TC, Millholland JM, VanRaay TJ, Shen J, Timothy KW, Vincent GM, de Jager T, Schwartz PJ, Toubin JA, Moss AJ, Atkinson DL, Landes GM, Connors TD, Keating MT: Positional cloning of a novel potassium channel gene: KVLQT1 mutations cause cardiac arrhythmias. Nat Genet. 1996 Jan;12(1):17-23.
  16. 8818942 de Jager T, Corbett CH, Badenhorst JC, Brink PA, Corfield VA: Evidence of a long QT founder gene with varying phenotypic expression in South African families. J Med Genet. 1996 Jul;33(7):567-73.
  17. 8872472 Russell MW, Dick M 2nd, Collins FS, Brody LC: KVLQT1 mutations in three families with familial or sporadic long QT syndrome. Hum Mol Genet. 1996 Sep;5(9):1319-24.
  18. 8900283 Sanguinetti MC, Curran ME, Zou A, Shen J, Spector PS, Atkinson DL, Keating MT: Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel. Nature. 1996 Nov 7;384(6604):80-3.
  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. 9108097 Yang WP, Levesque PC, Little WA, Conder ML, Shalaby FY, Blanar MA: KvLQT1, a voltage-gated potassium channel responsible for human cardiac arrhythmias. Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):4017-21.
  21. 9272155 van den Berg MH, Wilde AA, Robles de Medina EO, Meyer H, Geelen JL, Jongbloed RJ, Wellens HJ, Geraedts JP: The long QT syndrome: a novel missense mutation in the S6 region of the KVLQT1 gene. Hum Genet. 1997 Sep;100(3-4):356-61.
  22. 9302275 Wollnik B, Schroeder BC, Kubisch C, Esperer HD, Wieacker P, Jentsch TJ: Pathophysiological mechanisms of dominant and recessive KVLQT1 K+ channel mutations found in inherited cardiac arrhythmias. Hum Mol Genet. 1997 Oct;6(11):1943-9.
  23. 9305853 Jiang M, Tseng-Crank J, Tseng GN: Suppression of slow delayed rectifier current by a truncated isoform of KvLQT1 cloned from normal human heart. J Biol Chem. 1997 Sep 26;272(39):24109-12.
  24. 9312006 Chouabe C, Neyroud N, Guicheney P, Lazdunski M, Romey G, Barhanin J: Properties of KvLQT1 K+ channel mutations in Romano-Ward and Jervell and Lange-Nielsen inherited cardiac arrhythmias. EMBO J. 1997 Sep 1;16(17):5472-9.
  25. 9323054 Shalaby FY, Levesque PC, Yang WP, Little WA, Conder ML, Jenkins-West T, Blanar MA: Dominant-negative KvLQT1 mutations underlie the LQT1 form of long QT syndrome. Circulation. 1997 Sep 16;96(6):1733-6.
  26. 9386136 Donger C, Denjoy I, Berthet M, Neyroud N, Cruaud C, Bennaceur M, Chivoret G, Schwartz K, Coumel P, Guicheney P: KVLQT1 C-terminal missense mutation causes a forme fruste long-QT syndrome. Circulation. 1997 Nov 4;96(9):2778-81.
  27. 9482580 Saarinen K, Swan H, Kainulainen K, Toivonen L, Viitasalo M, Kontula K: Molecular genetics of the long QT syndrome: two novel mutations of the KVLQT1 gene and phenotypic expression of the mutant gene in a large kindred. Hum Mutat. 1998;11(2):158-65.
  28. 9570196 Li H, Chen Q, Moss AJ, Robinson J, Goytia V, Perry JC, Vincent GM, Priori SG, Lehmann MH, Denfield SW, Duff D, Kaine S, Shimizu W, Schwartz PJ, Wang Q, Towbin JA: New mutations in the KVLQT1 potassium channel that cause long-QT syndrome. Circulation. 1998 Apr 7;97(13):1264-9.
  29. 9641694 Priori SG, Schwartz PJ, Napolitano C, Bianchi L, Dennis A, De Fusco M, Brown AM, Casari G: A recessive variant of the Romano-Ward long-QT syndrome? Circulation. 1998 Jun 23;97(24):2420-5.
  30. 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.
  31. 9702906 Ackerman MJ, Schroeder JJ, Berry R, Schaid DJ, Porter CJ, Michels VV, Thibodeau SN: A novel mutation in KVLQT1 is the molecular basis of inherited long QT syndrome in a near-drowning patient's family. Pediatr Res. 1998 Aug;44(2):148-53.
  32. 9781056 Neyroud N, Denjoy I, Donger C, Gary F, Villain E, Leenhardt A, Benali K, Schwartz K, Coumel P, Guicheney P: Heterozygous mutation in the pore of potassium channel gene KvLQT1 causes an apparently normal phenotype in long QT syndrome. Eur J Hum Genet. 1998 Mar-Apr;6(2):129-33.
  33. 9799083 Itoh T, Tanaka T, Nagai R, Kikuchi K, Ogawa S, Okada S, Yamagata S, Yano K, Yazaki Y, Nakamura Y: Genomic organization and mutational analysis of KVLQT1, a gene responsible for familial long QT syndrome. Hum Genet. 1998 Sep;103(3):290-4.
  34. 9927399 Priori SG, Napolitano C, Schwartz PJ: Low penetrance in the long-QT syndrome: clinical impact. Circulation. 1999 Feb 2;99(4):529-33.
Target 4 Drug References
  1. Chouabe C, Drici MD, Romey G, Barhanin J: Effects of calcium channel blockers on cloned cardiac K+ channels IKr and IKs. Therapie. 2000 Jan-Feb;55(1):195-202. [PubMed Link Image]
  2. Yumoto Y, Horie M, Kubota T, Ninomiya T, Kobori A, Takenaka K, Takano M, Niwano S, Izumi T: Bepridil block of recombinant human cardiac IKs current shows a time-dependent unblock. J Cardiovasc Pharmacol. 2004 Feb;43(2):178-82. [PubMed Link Image]
  3. Chouabe C, Drici MD, Romey G, Barhanin J, Lazdunski M: HERG and KvLQT1/IsK, the cardiac K+ channels involved in long QT syndromes, are targets for calcium channel blockers. Mol Pharmacol. 1998 Oct;54(4):695-703. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 806
Target 5 Name Sodium/potassium-transporting ATPase alpha-1 chain
Target 5 Synonyms
  1. EC 3.6.3.9
  2. Na(+)/K(+) ATPase alpha-1 subunit
  3. Sodium pump subunit alpha 1
  4. Sodium/potassium-transporting ATPase alpha-1 chain precursor
Target 5 Gene Name ATP1A1
Target 5 Protein Sequence >Sodium/potassium-transporting ATPase alpha-1 chain precursor 
MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLS
RGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAA
TEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSI
NAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETR
NIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAV
FLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKN
LEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLA
LSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEI
PFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQN
AYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVP
DAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDA
KACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVN
DSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTL
TSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPK
TDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVED
SYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFE
ETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKE
TYY
Target 5 Number of Residues 1040
Target 5 Molecular Weight 112897
Target 5 Theoretical pI 5.15
Target 5 GO Classification
Function
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
catalytic activity
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
monovalent inorganic cation transporter activity
transporter activity
ion transporter activity
cation transporter activity
ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
Process
metabolism
monovalent inorganic cation transport
physiological process
cellular physiological process
transport
ion transport
cation transport
Component
intrinsic to membrane
integral to membrane
cell
membrane
Target 5 General Function Inorganic ion transport and metabolism
Target 5 Specific Function This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients
Target 5 Pathways Not Available
Target 5 Reactions
  • ATP + H2O + Na+in + K+out = ADP + phosphate + Na+out + K+in
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • 88-108
  • 132-152
  • 289-308
  • 321-338
  • 773-792
  • 803-823
  • 844-866
  • 919-938
  • 952-970
  • 986-1006
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 219942 Link Image
Target 5 UniProtKB/Swiss-Prot ID P05023 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name AT1A1_HUMAN Link Image
Target 5 PDB ID 1MO8 Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 5 Gene Sequence >3072 bp 
ATGGGGAAGGGGGTTGGACGTGATAAGTATGAGCCTGCAGCTGTTTCAGAACAAGGTGAT
AAAAAGGGCAAAAAGGGCAAAAAAGACAGGGACATGGATGAACTGAAGAAAGAAGTTTCT
ATGGATGATCATAAACTTAGCCTTGATGAACTTCATCGTAAATATGGAACAGACTTGAGC
CGGGGATTAACATCTGCTCGTGCAGCTGAGATCCTGGCGCGAGATGGTCCCAACGCCCTC
ACTCCCCCTCCCACTACTCCTGAATGGATCAAGTTTTGTCGGCAGCTCTTTGGGGGGTTC
TCAATGTTACTGTGGATTGGAGCGATTCTTTGTTTCTTGGCTTATAGCATCCAAGCTGCT
ACAGAAGAGGAACCTCAAAACGATAATCTGTACCTGGGTGTGGTGCTATCAGCCGTTGTA
ATCATAACTGGTTGCTTCTCCTACTATCAAGAAGCTAAAAGTTCAAAGATCATGGAATCC
TTCAAAAACATGGTCCCTCAGCAAGCCCTTGTGATTCGAAATGGTGAGAAAATGAGCATA
AATGCGGAGGAAGTTGTGGTTGGGGATCTGGTGGAAGTAAAAGGAGGAGACCGAATTCCT
GCTGACCTCAGAATCATATCTGCAAATGGCTGCAAGGTGGATAACTCCTCGCTCACTGGT
GAATCAGAACCCCAGACTAGGTCTCCAGATTTCACAAATGAAAACCCCCTGGAGACGAGG
AACATTGCCTTCTTTTCAACAAATTGTGTTGAAGGCACCGCACGTGGTATTGTTGTCTAC
ACTGGGGATCGCACTGTGATGGGAAGAATTGCCACACTTGCTTCTGGGCTGGAAGGAGGC
CAGACCCCCATTGCTGCAGAAATTGAACATTTTATCCACATCATCACGGGTGTGGCTGTG
TTCCTGGGTGTGTCTTTCTTCATCCTTTCTCTCATCCTTGAGTACACCTGGCTTGAGGCT
GTCATCTTCCTCATCGGTATCATCGTAGCCAATGTGCCGGAAGGTTTGCTGGCCACTGTC
ACGGTCTGTCTGACACTTACTGCCAAACGCATGGCAAGGAAAAACTGCTTAGTGAAGAAC
TTAGAAGCTGTGGAGACCTTGGGGTCCACGTCCACCATCTGCTCTGATAAAACTGGAACT
CTGACTCAGAACCGGATGACAGTGGCCCACATGTGGTTTGACAATCAAATCCATGAAGCT
GATACGACAGAGAATCAGAGTGGTGTCTCTTTTGACAAGACTTCAGCTACCTGGCTTGCT
CTGTCCAGAATTGCAGGTCTTTGTAACAGGGCAGTGTTTCAGGCTAACCAGGAAAACCTA
CCTATTCTTAAGCGGGCAGTTGCAGGAGATGCCTCTGAGTCAGCACTCTTAAAGTGCATA
GAGCTGTGCTGTGGTTCCGTGAAGGAGATGAGAGAAAGATACGCCAAAATCGTCGAGATA
CCCTTCAACTCCACCAACAAGTACCAGTTGTCTATTCATAAGAACCCCAACACATCGGAG
CCCCAACACCTGTTGGTGATGAAGGGCGCCCCAGAAAGGATCCTAGACCGTTGCAGCTCT
ATCCTCCTCCACGGCAAGGAGCAGCCCCTGGATGAGGAGCTGAAAGACGCCTTTCAGAAC
GCCTATTTGGAGCTGGGGGGCCTCGGAGAACGAGTCCTAGGTTTCTGCCACCTCTTTCTG
CCAGATGAACAGTTTCCTGAAGGGTTCCAGTTTGACACTGACGATGTGAATTTCCCTATC
GATAATCTGTGCTTTGTTGGGCTCATCTCCATGATTGACCCTCCACGGGCGGCCGTTCCT
GATGCCGTGGGCAAATGTCGAAGTGCTGGAATTAAGGTCATCATGGTCACAGGAGACCAT
CCAATCACAGCTAAAGCTATTGCCAAAGGTGTGGGCATCATCTCAGAAGGCAATGAGACC
GTGGAAGACATTGCTGCCCGCCTCAACATCCCAGTCAGCCAGGTGAACCCCAGGGATGCC
AAGGCCTGCGTAGTACACGGCAGTGATCTAAAGGACATGACCTCCGAGCAGCTGGATGAC
ATTTTGAAGTACCACACTGAGATAGTGTTTGCCAGGACCTCCCCTCAGCAGAAGCTCATC
ATTGTGGAAGGCTGCCAAAGACAGGGTGCTATCGTGGCTGTGACTGGTGACGGTGTGAAT
GACTCTCCAGCTTTGAAGAAAGCAGACATTGGGGTTGCTATGGGGATTGCTGGCTCAGAT
GTGTCCAAGCAAGCTGCTGACATGATTCTTCTGGATGACAACTTTGCCTCAATTGTGACT
GGAGTAGAGGAAGGTCGTCTGATCTTTGATAACTTGAAGAAATCCATTGCTTATACCTTA
ACCAGTAACATTCCCGAGATCACCCCGTTCCTGATATTTATTATTGCAAACATTCCACTA
CCACTGGGGACTGTCACCATCCTCTGCATTGACTTGGGCACTGACATGGTTCCTGCCATC
TCCCTGGCTTATGAGCAGGCTGAGAGTGACATCATGAAGAGACAGCCCAGAAATCCCAAA
ACAGACAAACTTGTGAATGAGCGGCTGATCAGCATGGCCTATGGGCAGATTGGAATGATC
CAGGCCCTGGGAGGCTTCTTTACTTACTTTGTGATTCTGGCTGAGAACGGCTTCCTCCCA
ATTCACCTGTTGGGCCTCCGAGTGGACTGGGATGACCGCTGGATCAACGATGTGGAAGAC
AGCTACGGGCAGCAGTGGACCTATGAGCAGAGGAAAATCGTGGAGTTCACCTGCCACACA
GCCTTCTTCGTCAGTATCGTGGTGGTGCAGTGGGCCGACTTGGTCATCTGTAAGACCAGG
AGGAATTCGGTCTTCCAGCAGGGGATGAAGAACAAGATCTTGATATTTGGCCTCTTTGAA
GAGACAGCCCTGGCTGCTTTCCTTTCCTACTGCCCTGGAATGGGTGTTGCTCTTAGGATG
TATCCCCTCAAACCTACCTGGTGGTTCTGTGCCTTCCCCTACTCTCTTCTCATCTTCGTA
TATGACGAAGTCAGAAAACTCATCATCAGGCGACGCCCTGGCGGCTGGGTGGAGAAGGAA
ACCTACTATTAG
Target 5 GenBank Gene ID
Target 5 GeneCard ID ATP1A1 Link Image
Target 5 GenAtlas ID ATP1A1 Link Image
Target 5 HGNC ID HGNC:799 Link Image
Target 5 Chromosome Location 1
Target 5 Locus 1p21
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Shull MM, Pugh DG, Lingrel JB: The human Na, K-ATPase alpha 1 gene: characterization of the 5'-flanking region and identification of a restriction fragment length polymorphism. Genomics. 1990 Mar;6(3):451-60. [PubMed Link Image]
  2. Kawakami K, Ohta T, Nojima H, Nagano K: Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence. J Biochem (Tokyo). 1986 Aug;100(2):389-97. [PubMed Link Image]
  3. Chehab FF, Kan YW, Law ML, Hartz J, Kao FT, Blostein R: Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue expression, DNA polymorphism, and chromosomal localization. Proc Natl Acad Sci U S A. 1987 Nov;84(22):7901-5. [PubMed Link Image]
  4. Shull MM, Lingrel JB: Multiple genes encode the human Na+,K+-ATPase catalytic subunit. Proc Natl Acad Sci U S A. 1987 Jun;84(12):4039-43. [PubMed Link Image]
  5. Sverdlov ED, Monastyrskaya GS, Broude NE, Ushkaryov YuA, Allikmets RL, Melkov AM, Smirnov YuV, Malyshev IV, Dulobova IE, Petrukhin KE, et al.: The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit. FEBS Lett. 1987 Jun 15;217(2):275-8. [PubMed Link Image]
  6. Ruiz A, Bhat SP, Bok D: Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium. Gene. 1995 Apr 3;155(2):179-84. [PubMed Link Image]
Target 5 Drug References
  1. Kovacic H, Gallice P, Crevat A: Inhibition of sodium pump by bepridil. An in vitro and microcalorimetric study. Biochem Pharmacol. 1992 Oct 20;44(8):1529-34. [PubMed Link Image]
  2. Raess BU, Record DM: Inhibition of erythrocyte Ca2(+)-pump by Ca2+ antagonists. Biochem Pharmacol. 1990 Dec 1;40(11):2549-55. [PubMed Link Image]
  3. Smith SJ, England PJ: The effects of reported Ca2+ sensitisers on the rates of Ca2+ release from cardiac troponin C and the troponin-tropomyosin complex. Br J Pharmacol. 1990 Aug;100(4):779-85. [PubMed Link Image]
  4. 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]
  5. Fuchs J, Mainka L, Reifart N, Zimmer G: Effects of bepridil on heart mitochondrial membrane and the isolated rat heart preparation. Arzneimittelforschung. 1986 Feb;36(2):209-12. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 1561
Target 6 Name Troponin C, slow skeletal and cardiac muscles
Target 6 Synonyms
  1. TN-C
Target 6 Gene Name TNNC1
Target 6 Protein Sequence >Troponin C, slow skeletal and cardiac muscles 
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEM
IDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIM
LQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Target 6 Number of Residues 163
Target 6 Molecular Weight 18403
Target 6 Theoretical pI 3.78
Target 6 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 6 General Function Involved in calcium ion binding
Target 6 Specific Function Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components:Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments
Target 6 Pathways Not Available
Target 6 Reactions Not Available
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 37208 Link Image
Target 6 UniProtKB/Swiss-Prot ID P63316 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name TNNC1_HUMAN Link Image
Target 6 PDB ID 1LA0 Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location Not Available
Target 6 Gene Sequence >486 bp 
ATGGATGACATCTACAAGGCTGCGGTAGAGCAGCTGACAGAAGAGCAGAAAAATGAGTTC
AAGGCAGCCTTCGACATCTTCGTGCTGGGCGCTGAGGATGGCTGCATCAGCACCAAGGAG
CTGGGCAAGGTGATGAGGATGCTGGGCCAGAACCCCACCCCTGAGGAGCTGCAGGAGATG
ATCGATGAGGTGGACGAGGACGGCAGCGGCACGGTGGACTTTGATGAGTTCCTGGTCATG
ATGGTTCGGTGCATGAAGGACGACAGCAAAGGGAAATCTGAGGAGGAGCTGTCTGACCTC
TTCCGCATGTTTGACAAAAATGCTGATGGCTACATCGACCTGGATGAGCTGAAGATAATG
CTGCAGGCTACAGGCGAGACCATCACGGAGGACGACATCGAGGAGCTCATGAAGGACGGA
GACAAGAACAACGACGGCCGCATCGACTATGATGAGTTCCTGGAGTTCATGAAGGGTGTG
GAGTAG
Target 6 GenBank Gene ID
Target 6 GeneCard ID TNNC1 Link Image
Target 6 GenAtlas ID TNNC1 Link Image
Target 6 HGNC ID HGNC:11943 Link Image
Target 6 Chromosome Location 3
Target 6 Locus 3p21.3-p14.3
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Schreier T, Kedes L, Gahlmann R: Cloning, structural analysis, and expression of the human slow twitch skeletal muscle/cardiac troponin C gene. J Biol Chem. 1990 Dec 5;265(34):21247-53. [PubMed Link Image]
  2. Gahlmann R, Wade R, Gunning P, Kedes L: Differential expression of slow and fast skeletal muscle troponin C. Slow skeletal muscle troponin C is expressed in human fibroblasts. J Mol Biol. 1988 May 20;201(2):379-91. [PubMed Link Image]
  3. Roher A, Lieska N, Spitz W: The amino acid sequence of human cardiac troponin-C. Muscle Nerve. 1986 Jan;9(1):73-7. [PubMed Link Image]
  4. Spyracopoulos L, Li MX, Sia SK, Gagne SM, Chandra M, Solaro RJ, Sykes BD: Calcium-induced structural transition in the regulatory domain of human cardiac troponin C. Biochemistry. 1997 Oct 7;36(40):12138-46. [PubMed Link Image]
Target 6 Drug References
  1. Abusamhadneh E, Abbott MB, Dvoretsky A, Finley N, Sasi S, Rosevear PR: Interaction of bepridil with the cardiac troponin C/troponin I complex. FEBS Lett. 2001 Sep 28;506(1):51-4. [PubMed Link Image]
  2. Wang X, Li MX, Sykes BD: Structure of the regulatory N-domain of human cardiac troponin C in complex with human cardiac troponin I147-163 and bepridil. J Biol Chem. 2002 Aug 23;277(34):31124-33. Epub 2002 Jun 11. [PubMed Link Image]
  3. MacLachlan LK, Reid DG, Mitchell RC, Salter CJ, Smith SJ: Binding of a calcium sensitizer, bepridil, to cardiac troponin C. A fluorescence stopped-flow kinetic, circular dichroism, and proton nuclear magnetic resonance study. J Biol Chem. 1990 Jun 15;265(17):9764-70. [PubMed Link Image]
  4. Kleerekoper Q, Liu W, Choi D, Putkey JA: Identification of binding sites for bepridil and trifluoperazine on cardiac troponin C. J Biol Chem. 1998 Apr 3;273(14):8153-60. [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.