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Showing drug card for Procainamide (DB01035)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:48:13
Primary Accession Number DB01035
Secondary Accession Number
  • APRD00509
Name Procainamide
Drug Type
  • Approved
  • Small Molecule
Description A derivative of procaine with less CNS action. [PubChem]
Synonyms Not Available
Brand Names
  1. Biocoryl
  2. Novocainamid
  3. Novocainamide
  4. Novocaine Amide
  5. Novocamid
  6. Procainamide Hcl
  7. Procaine Amide
  8. Procamide
  9. Procan
  10. Procan Sr
  11. Procanbid
  12. Procapan
  13. Promine
  14. Pronestyl
  15. Pronestyl-Sr
Brand Mixtures Not Available
Chemical IUPAC Name 4-amino-N-(2-diethylaminoethyl)benzamide
Chemical Formula C13H21N3O
Chemical Structure Structure
CAS Registry Number 51-06-9
InChI Identifier InChI=1/C13H21N3O/c1-3-16(4-2)10-9-15-13(17)11-5-7-12(14)8-6-11/h5-8H,3-4,9-10,14H2,1-2H3,(H,15,17)/f/h15H
InChI Key REQCZEXYDRLIBE-YAQRNVERCK
KEGG Drug Not Available
KEGG Compound C07401 Link Image
PubChem Compound 4913 Link Image
PubChem Substance 9605 Link Image
ChEBI ID Not Available
PharmGKB ID PA451108 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00713341 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/procain.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Procainamide Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Shannon SK et al., J Comb Chem. 2003 Nov-Dec;5(6):860-8 Xu CZ. Yao Xue Xue Bao. 1979 Nov;14(11):681-4
Average Molecular Weight 235.3253
Monoisotopic Molecular Weight 235.1685
State Solid
Melting Point 165-169 oC
Experimental Water Solubility 5050 mg/L Source: PhysProp
Predicted Water Solubility 3.02e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 1.3 Source: PhysProp
Predicted LogP 1.42 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -1.89 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 9.32
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 CCN(CC)CCNC(=O)C1=CC=C(N)C=C1
Canonical SMILES CCN(CC)CCNC(=O)C1=CC=C(N)C=C1
Drug Category
  • Anti-Arrhythmia Agents
  • Antiarrhythmic Agents
ATC Codes
AHFS Codes
  • 24:04.04.04
Indication For the treatment of life-threatening ventricular arrhythmias.
Pharmacology Procainamide is an agent indicated for production of local or regional anesthesia and in the treatment of ventricular tachycardia occurring during cardiac manipulation, such as surgery or catheterization, or which may occur during acute myocardial infarction, digitalis toxicity, or other cardiac diseases. The mode of action of the antiarrhythmic effect of Procainamide appears to be similar to that of procaine and quinidine. Ventricular excitability is depressed and the stimulation threshold of the ventricle is increased during diastole. The sinoatrial node is, however, unaffected.
Mechanism of Action Procainamide is sodium channel blocker. It stabilizes the neuronal membrane by inhibiting the ionic fluxes required for the initiation and conduction of impulses thereby effecting local anesthetic action.
Absorption 75 to 95%
Toxicity LD50=95 mg/kg (rat, IV); LD50=312 mg/kg (mouse, oral); LD50=103 mg/kg (mouse, IV); LD50=250 mg/kg (rabbit, IV)
Protein Binding 15 to 20%
Biotransformation Hepatic
Half Life ~2.5-4.5 hours
Dosage Forms
Form Route
Capsule Oral
Solution Intramuscular
Tablet, extended release Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Amiodarone Amiodarone increases serum levels and toxicity of procainamide
Cimetidine The histamine H2-receptor antagonist increases the effect of procainamide
Ciprofloxacin The quinolone increases the effect of procainamide
Cisapride Increased risk of cardiotoxicity and arrhythmias
Dihydroquinidine barbiturate Quinidine increases the effect of procainamide
Donepezil Possible antagonism of action
Galantamine Possible antagonism of action
Levofloxacin The quinolone increases the effect of procainamide
Mesoridazine Increased risk of cardiotoxicity and arrhythmias
Ofloxacin The quinolone increases the effect of procainamide
Quinidine Quinidine increases the effect of procainamide
Quinidine barbiturate Quinidine increases the effect of procainamide
Ranitidine The histamine H2-receptor antagonist increases the effect of procainamide
Ranolazine Possible additive effect on QT prolongation
Rivastigmine Possible antagonism of action
Terfenadine Increased risk of cardiotoxicity and arrhythmias
Thioridazine Increased risk of cardiotoxicity and arrhythmias
Trimethoprim Trimethoprim increases serum levels of procainamide
Vardenafil Increased risk of cardiotoxicity and arrhythmias
Ziprasidone Increased risk of cardiotoxicity and arrhythmias
Food Interactions
  • Avoid alcohol.
  • Take with food to reduce irritation.
Pathways
Name SMPDB Link KEGG Link
Procainamide (Antiarrhythmic) Pathway SMP00324 Link Image
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 2D6 (CYP2D6)
  2. Cholinesterase
Targets
  1. Sodium channel protein type 5 subunit alpha
  2. DNA (cytosine-5)-methyltransferase 1
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 2D6 (CYP2D6)
Enzyme 1 Gene Name CYP2D6
Enzyme 1 SwissProt ID P10635 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P10635|CP2D6_HUMAN Cytochrome P450 2D6 (EC 1.14.14.1) 
MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQ
LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVF
LARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDK
AVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV
LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVA
DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI
HEVQRFGDIVPLGMTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF
LDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGV
FAFLVSPSPYELCAVPR
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Cholinesterase
Enzyme 2 Gene Name BCHE
Enzyme 2 SwissProt ID P06276 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >Cholinesterase 
MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP
YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC
LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG
FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG
SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI
LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY
GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV
VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER
RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT
KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV
GL
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. Brugada J, Brugada R, Brugada P: [Brugada syndrome] Arch Mal Coeur Vaiss. 1999 Jul;92(7):847-50. [PubMed Link Image]
  2. Brugada R, Brugada J, Antzelevitch C, Kirsch GE, Potenza D, Towbin JA, Brugada P: Sodium channel blockers identify risk for sudden death in patients with ST-segment elevation and right bundle branch block but structurally normal hearts. Circulation. 2000 Feb 8;101(5):510-5. [PubMed Link Image]
  3. Chen SM, Kuo CT, Lin KH, Chiang FT: Brugada syndrome without mutation of the cardiac sodium channel gene in a Taiwanese patient. J Formos Med Assoc. 2000 Nov;99(11):860-2. [PubMed Link Image]
  4. Brugada J, Brugada P, Brugada R: The syndrome of right bundle branch block ST segment elevation in V1 to V3 and sudden death--the Brugada syndrome. Europace. 1999 Jul;1(3):156-66. [PubMed Link Image]
  5. Weiss R, Barmada MM, Nguyen T, Seibel JS, Cavlovich D, Kornblit CA, Angelilli A, Villanueva F, McNamara DM, London B: Clinical and molecular heterogeneity in the Brugada syndrome: a novel gene locus on chromosome 3. Circulation. 2002 Feb 12;105(6):707-13. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 1064
Target 2 Name DNA (cytosine-5)-methyltransferase 1
Target 2 Synonyms
  1. DNA MTase HsaI
  2. DNA methyltransferase HsaI
  3. Dnmt1
  4. EC 2.1.1.37
  5. M.HsaI
  6. MCMT
Target 2 Gene Name DNMT1
Target 2 Protein Sequence >DNA (cytosine-5)-methyltransferase 1 
MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQ
LCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRV
GMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKP
QEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEK
EEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPE
EKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYL
DDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLC
PIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFS
TSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGL
NLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQAR
RQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQ
QPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQ
GKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVT
ALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPS
ENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLA
EMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPR
KEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNK
FYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGP
NRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLR
TLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMA
GETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRP
RFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAP
GEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNG
ASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLP
NIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCL
PHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFP
DTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD
Target 2 Number of Residues 1642
Target 2 Molecular Weight 183167
Target 2 Theoretical pI 7.81
Target 2 GO Classification
Function
ion binding
cation binding
transition metal ion binding
zinc ion binding
protein binding
transcription factor binding
binding
nucleic acid binding
DNA binding
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA modification
DNA alkylation
DNA methylation
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 2 General Function Replication, recombination and repair
Target 2 Specific Function Methylates CpG residues. Preferentially methylates hemimethylated DNA. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2
Target 2 Pathways
Name SMPDB Link KEGG Link
Methionine metabolism SMP00033 Link Image map00271 Link Image
Target 2 Reactions
  • S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 1632819 Link Image
Target 2 UniProtKB/Swiss-Prot ID P26358 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name DNMT1_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Nucleus
Target 2 Gene Sequence >4851 bp 
ATGCCGGCGCGTACCGCCCCAGCCCGGGTGCCCACACTGGCCGTCCCGGCCATCTCGCTG
CCCGACGATGTCCGCAGGCGGCTCAAAGATTTGGAAAGAGACAGCTTAACAGAAAAGGAA
TGTGTGAAGGAGAAATTGAATCTCTTGCACGAATTTCTGCAAACAGAAATAAAGAATCAG
TTATGTGACTTGGAAACCAAATTACGTAAAGAAGAATTATCCGAGGAGGGCTACCTGGCT
AAAGTCAAATCCCTTTTAAATAAAGATTTGTCCTTGGAGAACGGTGCTCATGCTTACAAC
CGGGAAGTGAATGGACGTCTAGAAAACGGGAACCAAGCAAGAAGTGAAGCCCGTAGAGTG
GGAATGGCAGATGCCAACAGCCCCCCCAAACCCCTTTCCAAACCTCGCACGCCCAGGAGG
AGCAAGTCCGATGGAGAGGCTAAGCCTGAACCTTCACCTAGCCCCAGGATTACAAGGAAA
AGCACCAGGCAAACCACCATCACATCTCATTTTGCAAAGGGCCCTGCCAAACGGAAACCT
CAGGAAGAGTCTGAAAGAGCCAAATCGGATGAGTCCATCAAGGAAGAAGACAAAGACCAG
GATGAGAAGAGACGTAGAGTTACATCCAGAGAACGAGTTGCTAGACCGCTTCCTGCAGAA
GAACCTGAAAGAGCAAAATCAGGAACGCGCACTGAAAAGGAAGAAGAAAGAGATGAAAAA
GAAGAAAAGAGACTCCGAAGTCAAACCAAAGAACCAACACCCAAACAGAAACTGAAGGAG
GAGCCGGACAGAGAAGCCAGGGCAGGCGTGCAGGCTGACGAGGACGAAGATGGAGACGAG
AAAGATGAGAAGAAGCACAGAAGTCAACCCAAAGATCTAGCTGCCAAACGGAGGCCCGAA
GAAAAAGAACCTGAAAAAGTAAATCCACAGATTTCTGATGAAAAAGACGAGGATGAAAAG
GAGGAGAAGAGACGCAAAACGACCCCCAAAGAACCAACGGAGAAAAAAATGGCTCGCGCC
AAAACAGTCATGAACTCCAAGACCCACCCTCCCAAGTGCATTCAGTGCGGGCAGTACCTG
GACGACCCTGACCTCAAATATGGGCAGCACCCACCAGACGCGGTGGATGAGCCACAGATG
CTGACAAATGAGAAGCTGTCCATCTTTGATGCCAACGAGTCTGGCTTTGAGAGTTATGAG
GCGCTTCCCCAGCACAAACTGACCTGCTTCAGTGTGTACTGTAAGCACGGTCACCTGTGT
CCCATCGACACCGGCCTCATCGAGAAGAATATCGAACTCTTCTTTTCTGGTTCAGCAAAA
CCAATCTATGATGATGACCCGTCTCTTGAAGGTGGTGTTAATGGCAAAAATCTTGGCCCC
ATAAATGAATGGTGGATCACTGGCTTTGATGGAGGTGAAAAGGCCCTCATCGGCTTCAGC
ACCTCATTTGCCGAATACATTCTGATGGATCCCAGTCCCGAGTATGCGCCCATATTTGGG
CTGATGCAGGAGAAGATCTACATCAGCAAGATTGTGGTGGAGTTCCTGCAGAGCAATTCC
GACTCGACCTATGAGGACCTGATCAACAAGATCGAGACCACGGTTCCTCCTTCTGGCCTC
AACTTGAACCGCTTCACAGAGGACTCCCTCCTGCGACACGCGCAGTTTGTGGTGGAGCAG
GTGGAGAGTTATGACGAGGCCGGGGACAGTGATGAGCAGCCCATCTTCCTGACGCCCTGC
ATGCGGGACCTGATCAAGCTGGCTGGGGTCACGCTGGGACAGAGGCGAGCCCAGGCGAGG
CGGCAGACCATCAGGCATTCTACCAGGGAGAAGGACAGGGGACCCACGAAAGCCACCACC
ACCAAGCTGGTCTACCAGATCTTCGATACTTTCTTCGCAGAGCAAATTGAAAAGGATGAC
AGAGAAGACAAGGAGAACGCCTTTAAGCGCCGGCGATGTGGCGTCTGTGAGGTGTGTCAG
CAGCCTGAGTGTGGGAAATGTAAAGCCTGCAAGGACATGGTTAAATTTGGTGGCAGTGGA
CGGAGCAAGCAGGCTTGCCAAGAGCGGAGGTGTCCCAATATGGCCATGAAGGAGGCAGAT
GACGATGAGGAAGTCGATGATAACATCCCAGAGATGCCGTCACCCAAAAAAATGCACCAG
GGGAAGAAGAAGAAACAGAACAAGAATCGCATCTCTTGGGTCGGAGAAGCCGTCAAGACT
GATGGGAAGAAGAGTTACTATAAGAAGGTGTGCATTGATGCGGAAACCCTGGAAGTGGGG
GACTGTGTCTCTGTTATTCCAGATGATTCCTCAAAACCGCTGTATCTAGCAAGGGTCACG
GCGCTGTGGGAGGACAGCAGCAACGGGCAGATGTTTCACGCCCACTGGTTCTGCGCTGGG
ACAGACACAGTCCTCGGGGCCACGTCGGACCCTCTGGAGCTGTTCTTGGTGGATGAATGT
GAGGACATGCAGCTTTCATATATCCACAGCAAAGTGAAAGTCATCTACAAAGCCCCCTCC
GAAAACTGGGCCATGGAGGGAGGCATGGATCCCGAGTCCCTGCTGGAGGGGGACGACGGG
AAGACCTACTTCTACCAGCTGTGGTATGATCAAGACTACGCGAGATTCGAGTCCCCTCCA
AAAACCCAGCCAACAGAGGACAACAAGTTCAAATTCTGTGTGAGCTGTGCCCGTCTGGCT
GAGATGAGGCAAAAAGAAATCCCCAGGGTCCTGGAGCAGCTCGAGGACCTGGATAGCCGG
GTCCTCTACTACTCAGCCACCAAGAACGGCATCCTGTACCGAGTTGGTGATGGTGTGTAC
CTGCCCCCTGAGGCCTTCACGTTCAACATCAAGCTGTCCAGTCCCGTGAAACGCCCACGG
AAGGAGCCCGTGGATGAGGACCTGTACCCAGAGCACTACCGGAAATACTCCGACTACATC
AAAGGCAGCAACCTGGATGCCCCTGAGCCCTACCGAATTGGCCGGATCAAAGAGATCTTC
TGTCCCAAGAAGAGCAACGGCAGGCCCAATGAGACTGACATCAAAATCCGGGTCAACAAG
TTCTACAGGCCTGAGAACACCCACAAGTCCACTCCAGCGAGCTACCACGCAGACATCAAC
CTGCTCTACTGGAGCGACGAGGAGGCCGTGGTGGACTTCAAGGCTGTGCAGGGCCGCTGC
ACCGTGGAGTATGGGGAGGACCTGCCCGAGTGCGTCCAGGTGTACTCCATGGGCGGCCCC
AACCGCTTCTACTTCCTCGAGGCCTATAATGCAAAGAGCAAAAGCTTTGAAGATCCTCCC
AACCATGCCCGTAGCCCTGGAAACAAAGGGAAGGGCAAGGGAAAAGGGAAGGGCAAGCCC
AAGTCCCAAGCCTGTGAGCCGAGCGAGCCAGAGATAGAGATCAAGCTGCCCAAGCTGCGG
ACCCTGGATGTGTTTTCTGGCTGCGGGGGGTTGTCGGAGGGATTCCACCAAGCAGGCATC
TCTGACACGCTGTGGGCCATCGAGATGTGGGACCCTGCGGCCCAGGCGTTCCGGCTGAAC
AACCCCGGCTCCACAGTGTTCACAGAGGACTGCAACATCCTGCTGAAGCTGGTCATGGCT
GGGGAGACCACCAACTCCCGCGGCCAGCGGCTGCCCCAGAAGGGAGACGTGGAGATGCTG
TGCGGCGGGCCGCCCTGCCAGGGCTTCAGCGGCATGAACCGCTTCAATTCGCGCACCTAC
TCCAAGTTCAAAAACTCTCTGGTGGTTTCCTTCCTCAGCTACTGCGACTACTACCGGCCC
CGGTTCTTCCTCCTGGAGAATGTCAGGAACTTTGTCTCCTTCAAGCGCTCCATGGTCCTG
AAGCTCACCCTCCGCTGCCTGGTCCGCATGGGCTATCAGTGCACCTTCGGCGTGCTGCAG
GCCGGTCAGTACGGCGTGGCCCAGACTAGGAGGCGGGCCATCATCCTGGCCGCGGCCCCT
GGAGAGAAGCTCCCTCTGTTCCCGGAGCCACTGCACGTGTTTGCTCCCCGGGCCTGCCAG
CTGAGCGTGGTGGTGGATGACAAGAAGTTTGTGAGCAACATAACCAGGTTGAGCTCGGGT
CCTTTCCGGACCATCACGGTGCGAGACACGATGTCCGACCTGCCGGAGGTGCGGAATGGA
GCCTCGGCACTGGAGATCTCCTACAACGGGGAGCCTCAGTCCTGGTTCCAGAGGCAGCTC
CGGGGCGCACAGTACCAGCCCATCCTCAGGGACCACATCTGTAAGGACATGAGTGCATTG
GTGGCTGCCCGCATGCGGCACATCCCCTTGGCCCCAGGGTCAGACTGGCGCGATCTGCCC
AACATCGAGGTGCGGCTCTCAGACGGCACCATGGCCAGGAAGCTGCGGTATACCCACCAT
GACAGGAAGAACGGCCGCAGCAGCTCTGGGGCCCTCCGTGGGGTCTGCTCCTGCGTGGAA
GCCGGCAAAGCCTGCGACCCCGCAGCCAGGCAGTTCAACACCCTCATCCCCTGGTGCCTG
CCCCACACCGGGAACCGGCACAACCACTGGGCTGGCCTCTATGGAAGGCTCGAGTGGGAC
GGCTTCTTCAGCACAACCGTCACCAACCCCGAGCCCATGGGCAAGCAGGGCCGCGTGCTC
CACCCAGAGCAGCACCGTGTGGTGAGCGTGCGGGAGTGTGCCCGCTCCCAGGGCTTCCCT
GACACCTACCGGCTCTTCGGCAACATCCTGGACAAGCACCGGCAGGTGGGCAATGCCGTG
CCACCGCCCCTGGCCAAAGCCATTGGCTTGGAGATCAAGCTTTGTATGTTGGCCAAAGCC
CGAGAGAGTGCCTCAGCTAAAATAAAGGAGGAGGAAGCTGCTAAGGACTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID DNMT1 Link Image
Target 2 GenAtlas ID DNMT1 Link Image
Target 2 HGNC ID HGNC:2976 Link Image
Target 2 Chromosome Location 19
Target 2 Locus 19p13.2
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Robertson KD, Uzvolgyi E, Liang G, Talmadge C, Sumegi J, Gonzales FA, Jones PA: The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors. Nucleic Acids Res. 1999 Jun 1;27(11):2291-8. [PubMed Link Image]
  2. Hsu DW, Lin MJ, Lee TL, Wen SC, Chen X, Shen CK: Two major forms of DNA (cytosine-5) methyltransferase in human somatic tissues. Proc Natl Acad Sci U S A. 1999 Aug 17;96(17):9751-6. [PubMed Link Image]
  3. Bonfils C, Beaulieu N, Chan E, Cotton-Montpetit J, MacLeod AR: Characterization of the human DNA methyltransferase splice variant Dnmt1b. J Biol Chem. 2000 Apr 14;275(15):10754-60. [PubMed Link Image]
  4. Rountree MR, Bachman KE, Baylin SB: DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. Nat Genet. 2000 Jul;25(3):269-77. [PubMed Link Image]
  5. Robertson KD, Ait-Si-Ali S, Yokochi T, Wade PA, Jones PL, Wolffe AP: DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. Nat Genet. 2000 Jul;25(3):338-42. [PubMed Link Image]
  6. Tatematsu KI, Yamazaki T, Ishikawa F: MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase. Genes Cells. 2000 Aug;5(8):677-88. [PubMed Link Image]
  7. Yen RW, Vertino PM, Nelkin BD, Yu JJ, el-Deiry W, Cumaraswamy A, Lennon GG, Trask BJ, Celano P, Baylin SB: Isolation and characterization of the cDNA encoding human DNA methyltransferase. Nucleic Acids Res. 1992 May 11;20(9):2287-91. [PubMed Link Image]
  8. Yoder JA, Yen RW, Vertino PM, Bestor TH, Baylin SB: New 5' regions of the murine and human genes for DNA (cytosine-5)-methyltransferase. J Biol Chem. 1996 Dec 6;271(49):31092-7. [PubMed Link Image]
  9. Chuang LS, Ian HI, Koh TW, Ng HH, Xu G, Li BF: Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1. Science. 1997 Sep 26;277(5334):1996-2000. [PubMed Link Image]
Target 2 Drug References
  1. Oelke K, Lu Q, Richardson D, Wu A, Deng C, Hanash S, Richardson B: Overexpression of CD70 and overstimulation of IgG synthesis by lupus T cells and T cells treated with DNA methylation inhibitors. Arthritis Rheum. 2004 Jun;50(6):1850-60. [PubMed Link Image]
  2. Januchowski R, Jagodzinski PP: Effect of 5-azacytidine and procainamide on CD3-zeta chain expression in Jurkat T cells. Biomed Pharmacother. 2005 Apr;59(3):122-6. [PubMed Link Image]
  3. Lee BH, Yegnasubramanian S, Lin X, Nelson WG: Procainamide is a specific inhibitor of DNA methyltransferase 1. J Biol Chem. 2005 Dec 9;280(49):40749-56. Epub 2005 Oct 17. [PubMed Link Image]
  4. Scheinbart LS, Johnson MA, Gross LA, Edelstein SR, Richardson BC: Procainamide inhibits DNA methyltransferase in a human T cell line. J Rheumatol. 1991 Apr;18(4):530-4. [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.