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Showing drug card for Chlorzoxazone (DB00356)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:42
Primary Accession Number DB00356
Secondary Accession Number
  • APRD00308
Name Chlorzoxazone
Drug Type
  • Approved
  • Small Molecule
Description A centrally acting central muscle relaxant with sedative properties. It is claimed to inhibit muscle spasm by exerting an effect primarily at the level of the spinal cord and subcortical areas of the brain. (From Martindale, The Extra Pharmacopoea, 30th ed, p1202)
Synonyms
  1. Chloroxazone
  2. Chlorzoxane
  3. Chlorzoxazon
Brand Names
  1. Biomioran
  2. EZE-DS
  3. Escoflex
  4. Flexazone
  5. Mioran
  6. Miotran
  7. Myoflexin
  8. Myoflexine
  9. Neoflex
  10. Paraflex
  11. Parafon Forte Dsc
  12. Pathorysin
  13. Relaxazone
  14. Remular
  15. Remular-S
  16. Solaxin
  17. Strifon Forte Dsc
  18. Usaf Ma-10
Brand Mixtures
  1. Acetazone Forte (Acetaminophen + Chlorzoxazone)
  2. Acetazone Forte C8 (Acetaminophen + Chlorzoxazone + Codeine Phosphate)
  3. Back-Aid Forte - Tab (Acetaminophen + Chlorzoxazone)
  4. Extra Strength Tylenol Aches and Strains (Acetaminophen + Chlorzoxazone)
  5. Gin Pain Pills - Tab (Acetaminophen + Chlorzoxazone)
  6. Gin Pain Pills- Chlorzoxazone & Acetamin.Tab (Acetaminophen + Chlorzoxazone)
  7. Parafon Forte (Acetaminophen + Chlorzoxazone)
  8. Parafon Forte C8 W Codeine Tab (Acetaminophen + Chlorzoxazone + Codeine Phosphate)
  9. Parafon Forte Tablets (Acetaminophen + Chlorzoxazone)
Chemical IUPAC Name 5-chloro-3H-1,3-benzoxazol-2-one
Chemical Formula C7H4ClNO2
Chemical Structure Structure
CAS Registry Number 95-25-0
InChI Identifier InChI=1/C7H4ClNO2/c8-4-1-2-6-5(3-4)9-7(10)11-6/h1-3H,(H,9,10)/f/h9H
InChI Key TZFWDZFKRBELIQ-BGGKNDAXCM
KEGG Drug D00771 Link Image
KEGG Compound C07931 Link Image
PubChem Compound 2733 Link Image
PubChem Substance 7847836 Link Image
ChEBI ID Not Available
PharmGKB ID PA448971 Link Image
HET ID CLW Link Image
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link http://www.rxlist.com/cgi/generic2/chlorzox.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/par1317.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Chlorzoxazone Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 169.5650
Monoisotopic Molecular Weight 168.9931
State Solid
Melting Point 191.5 oC
Experimental Water Solubility 1000 mg/L Source: PhysProp
Predicted Water Solubility 2.96e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 1.6 Source: PhysProp
Predicted LogP 2.09 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -1.76 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 ClC1=CC2=C(OC(=O)N2)C=C1
Canonical SMILES ClC1=CC2=C(OC(=O)N2)C=C1
Drug Category
  • Muscle Relaxants, Central
ATC Codes
AHFS Codes Not Available
Indication For the relief of discomfort associated with acute painful musculoskeletal conditions.
Pharmacology Chlorzoxazone, a synthetic compound, inhibits antigen-induced bronchospasms and, hence, is used to treat asthma and allergic rhinitis. Chlorzoxazone is used as an ophthalmic solution to treat conjunctivitis and is taken orally to treat systemic mastocytosis and ulcerative colitis. Chlorzoxazone is also a centrally-acting agent for painful musculoskeletal conditions. Data available from animal experiments as well as human study indicate that chlorzoxazone acts primarily at the level of the spinal cord and subcortical areas of the brain where it inhibits multisynaptic reflex a.c. involved in producing and maintaining skeletal muscle spasm of varied etiology. The clinical result is a reduction of the skeletal muscle spasm with relief of pain and increased mobility of the involved muscles.
Mechanism of Action Chlorzoxazone inhibits degranulation of mast cells, subsequently preventing the release of histamine and slow-reacting substance of anaphylaxis (SRS-A), mediators of type I allergic reactions. Chlorzoxazone also may reduce the release of inflammatory leukotrienes. Chlorzoxazone may act by inhibiting calcium influx.
Absorption Not Available
Toxicity Oral, mouse: LD50 = 440 mg/kg; Oral, rat: LD50 = 763 mg/kg; Symptoms of overdose include diarrhea, dizziness, drowsiness, headache, light-headedness, nausea, and vomiting.
Protein Binding 13-18%
Biotransformation Chlorzoxazone is rapidly metabolized in the liver and is excreted in the urine, primarily in a conjugated form as the glucuronide.
Half Life Not Available
Dosage Forms
Form Route
Capsule Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Disulfiram Disulfiram increases chlorzoxazone levels
Food Interactions
  • Avoid alcohol.
  • Take without regard to meals.
Pathways Not Available
General References
  1. Wan J, Ernstgard L, Song BJ, Shoaf SE: Chlorzoxazone metabolism is increased in fasted Sprague-Dawley rats. J Pharm Pharmacol. 2006 Jan;58(1):51-61. [PubMed Link Image]
  2. Park JY, Kim KA, Park PW, Ha JM: Effect of high-dose aspirin on CYP2E1 activity in healthy subjects measured using chlorzoxazone as a probe. J Clin Pharmacol. 2006 Jan;46(1):109-14. [PubMed Link Image]
  3. Dong DL, Luan Y, Feng TM, Fan CL, Yue P, Sun ZJ, Gu RM, Yang BF: Chlorzoxazone inhibits contraction of rat thoracic aorta. Eur J Pharmacol. 2006 Sep 18;545(2-3):161-6. Epub 2006 Jun 29. [PubMed Link Image]
  4. Drugs.com Link Image
  5. Wikipedia Link Image
  6. RxList Link Image
  7. PDRhealth Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 2A6 (CYP2A6)
  2. Cytochrome P450 2E1 (CYP2E1)
  3. Cytochrome P450 2C19 (CYP2C19)
  4. Cytochrome P450 1A2 (CYP1A2)
  5. Cytochrome P450 2D6 (CYP2D6)
  6. Cytochrome P450 1A1 (CYP1A1)
Targets
  1. Calcium-activated potassium channel subunit alpha 1
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 2A6 (CYP2A6)
Enzyme 1 Gene Name CYP2A6
Enzyme 1 SwissProt ID P11509 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P11509|CP2A6_HUMAN Cytochrome P450 2A6 (EC 1.14.14.1) 
MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSN
GERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDAHRGTGGANIDPTFFLSRTVSN
VISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQL
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFI
GGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEK
GQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Cytochrome P450 2E1 (CYP2E1)
Enzyme 2 Gene Name CYP2E1
Enzyme 2 SwissProt ID P05181 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P05181|CP2E1_HUMAN Cytochrome P450 2E1 (EC 1.14.14.1) 
MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS
Phase 1 Metabolizing Enzyme 3 [top]
Enzyme 3 Name Cytochrome P450 2C19 (CYP2C19)
Enzyme 3 Gene Name CYP2C19
Enzyme 3 SwissProt ID P33261 Link Image
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 Protein Sequence >sp|P33261|CP2CJ_HUMAN Cytochrome P450 2C19 (EC 1.14.13.80) 
MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKI
YGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFM
ESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVVGRNRSPCMQDRGHMPYTDAVVHEVQRYID
LIPTSLPHAVTCDVKFRNYLIPKGTTILTSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFK
KSNYFMPFSAGKRICVGEGLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVP
PFYQLCFIPV
Phase 1 Metabolizing Enzyme 4 [top]
Enzyme 4 Name Cytochrome P450 1A2 (CYP1A2)
Enzyme 4 Gene Name CYP1A2
Enzyme 4 SwissProt ID P05177 Link Image
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 Protein Sequence >P05177|CP1A2_HUMAN Cytochrome P450 1A2 - Homo sapiens (Human). 
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
Phase 1 Metabolizing Enzyme 5 [top]
Enzyme 5 Name Cytochrome P450 2D6 (CYP2D6)
Enzyme 5 Gene Name CYP2D6
Enzyme 5 SwissProt ID P10635 Link Image
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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 6 [top]
Enzyme 6 Name Cytochrome P450 1A1 (CYP1A1)
Enzyme 6 Gene Name CYP1A1
Enzyme 6 SwissProt ID P04798 Link Image
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 Protein Sequence >sp|P04798|CP1A1_HUMAN Cytochrome P450 1A1 (EC 1.14.14.1) 
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
Drug Target 1 [top]
Target 1 ID 610
Target 1 Name Calcium-activated potassium channel subunit alpha 1
Target 1 Synonyms
  1. BK channel
  2. BKCA alpha
  3. Calcium-activated potassium channel, subfamily M subunit alpha 1
  4. K(VCA)alpha
  5. KCa1.1
  6. Maxi K channel
  7. MaxiK
  8. Slo homolog
  9. Slo-alpha
  10. Slo1
  11. Slowpoke homolog
  12. hSlo
Target 1 Gene Name KCNMA1
Target 1 Protein Sequence >Calcium-activated potassium channel subunit alpha 1 
MANGGGGGGGSSGGGGGGGGSSLRMSSNIHANHLSLDASSSSSSSSSSSSSSSSSSSSSS
VHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCH
CGGKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVL
VVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKL
WFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKL
VNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYA
KTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLES
VSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVK
IESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSW
NWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNE
MYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLG
FFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRPKMSIYKRMRRACCFDCGRSERD
CSCMSGRVRGNVDTLERAFPLSSVSVNDCSTSFRAFEDEQPSTLSPKKKQRNGGMRNSPN
TSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSG
HVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVS
ILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIG
VLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDD
DPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEEN
ALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRL
RDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSS
KKSSSVHSIPSTANRQNRPKSRESRDKQKYVQEERL
Target 1 Number of Residues 1256
Target 1 Molecular Weight 137561
Target 1 Theoretical pI 7.07
Target 1 GO Classification
Function
voltage-gated ion channel activity
voltage-gated potassium channel activity
transporter activity
ion transporter activity
ion channel activity
cation channel activity
potassium channel activity
calcium-activated potassium channel activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
potassium ion transport
Component
protein complex
voltage-gated potassium channel complex
cell
membrane
Target 1 General Function Inorganic ion transport and metabolism
Target 1 Specific Function Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX)
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 87-107
  • 179-199
  • 215-235
  • 240-260
  • 265-285
  • 301-321
  • 368-388
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 537439 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q12791 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name KCMA1_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 1 Gene Sequence >3639 bp 
ATGAGTAGCAATATCCACGCGAACCATCTCAGCCTAGACGCGTCCTCCTCCTCCTCCTCC
TCCTCTTCCTCTTCTTCTTCTTCCTCCTCCTCTTCCTCCTCGTCCTCGGTCCACGAGCCC
AAGATGGATGCGCTCATCATCCCGGTGACCATGGAGGTGCCGTGCGACAGCCGGGGCCAA
CGCATGTGGTGGGCTTTCCTGGCCTCCTCCATGGTGACTTTCTTCGGGGGCCTCTTCATC
ATCTTGCTCTGGCGGACGCTCAAGTACCTGTGGACCGTGTGCTGCCACTGCGGGGGCAAG
ACGAAGGAGGCCCAGAAGATTAACAATGGCTCAAGCCAGGCGGATGGCACTCTCAAACCA
GTGGATGAAAAAGAGGAGGCAGTGGCCGCCGAGGTCGGCTGGATGACCTCCGTGAAGGAC
TGGGCGGGGGTGATGATATCCGCCCAGACACTGACTGGCAGAGTCCTGGTTGTCTTAGTC
TTTGCTCTCAGCATCGGTGCACTTGTAATATACTTCATAGATTCATCAAACCCAATAGAA
TCCTGCCAGAATTTCTACAAAGATTTCACATTACAGATCGACATGGCTTTCAACGTGTTC
TTCCTTCTCTACTTCGGCTTGCGGTTTATTGCAGCCAACGATAAATTGTGGTTCTGGCTG
GAAGTGAACTCTGTAGTGGATTTCTTCACGGTGCCCCCCGTGTTTGTGTCTGTGTACTTA
AACAGAAGTTGGCTTGGTTTGAGATTTTTAAGAGCTCTGAGACTGATACAGTTTTCAGAA
ATTTTGCAGTTTCTGAATATTCTTAAAACAAGTAATTCCATCAAGCTGGTGAATCTGCTC
TCCATATTTATCAGCACGTGGCTGACTGCAGCCGGGTTCATCCATTTGGTGGAGAATTCA
GGGGACCCATGGGAAAATTTCCAAAACAACCAGGCTCTCACCTACTGGGAATGTGTCTAT
TTACTCATGGTCACAATGTCCACCGTTGGTTATGGGGATGTTTATGCAAAAACCACACTT
GGGCGCCTCTTCATGGTCTTCTTCATCCTCGGGGGACTGGCCATGTTTGCCAGCTACGTC
CCTGAAATCATAGAGTTAATAGGAAACCGCAAGAAATACGGGGGCTCCTATAGTGCGGTT
AGTGGAAGAAAGCACATTGTGGTCTGCGGACACATCACTCTGGAGAGTGTTTCCAACTTC
CTGAAGGACTTTCTGCACAAGGACCGGGATGACGTCAATGTGGAGATCGTTTTTCTTCAC
AACATCTCCCCCAACCTGGAGCTTGAAGCTCTGTTCAAACGACATTTTACTCAGGTGGAA
TTTTATCAGGGTTCCGTCCTCAATCCACATGATCTTGCAAGAGTCAAGATAGAGTCAGCA
GATGCATGCCTGATCCTTGCCAACAAGTACTGCGCTGACCCGGATGCGGAGGATGCCTCG
AATATCATGAGAGTAATCTCCATAAAGAACTACCATCCGAAGATAAGAATCATCACTCAA
ATGCTGCAGTATCACAACAAGGCCCATCTGCTAAACATCCCGAGCTGGAATTGGAAAGAA
GGTGATGACGCAATCTGCCTCGCAGAGTTGAAGTTGGGCTTCATAGCCCAGAGCTGCCTG
GCTCAAGGCCTCTCCACCATGCTTGCCAACCTCTTCTCCATGAGGTCATTCATAAAGATT
GAGGAAGACACATGGCAGAAATACTACTTGGAAGGAGTCTCAAATGAAATGTACACAGAA
TATCTCTCCAGTGCCTTCGTGGGTCTGTCCTTCCCTACTGTTTGTGAGCTGTGTTTTGTG
AAGCTCAAGCTCCTAATGATAGCCATTGAGTACAAGTCTGCCAACCGAGAGAGCCGTATA
TTAATTAATCCTGGAAACCATCTTAAGATCCAAGAAGGTACTTTAGGATTTTTCATCGCA
AGTGATGCCAAAGAAGTTAAAAGGGCATTTTTTTACTGCAAGGCCTGTCATGATGACATC
ACAGATCCCAAAAGAATAAAAAAATGTGGCTGCAAACGGCCCAAGATGTCCATCTACAAG
AGAATGAGACGGGCATGTTGTTTTGATTGCGGACGTTCTGAGCGTGACTGCTCATGCATG
TCAGGCCGTGTGCGTGGTAACGTGGACACCCTTGAGAGAGCCTTCCCACTTTCTTCTGTC
TCTGTTAATGATTGCTCCACCAGTTTCCGTGCCTTTGAAGATGAGCAGCCGTCAACACTA
TCACCAAAAAAAAAGCAACGGAATGGAGGCATGCGGAACTCACCCAACACCTCGCCTAAG
CTGATGAGGCATGACCCCTTGTTAATTCCTGGCAATGATCAGATTGACAACATGGACTCC
AATGTGAAGAAGTACGACTCTACTGGGATGTTTCACTGGTGTGCACCCAAGGAGATAGAG
AAAGTCATCCTGACTCGAAGTGAAGCTGCCATGACCGTCCTGAGTGGCCATGTCGTGGTC
TGCATCTTTGGCGACGTCAGCTCAGCCCTGATCGGCCTCCGGAACCTGGTGATGCCGCTC
CGTGCCAGCAACTTTCATTACCATGAGCTCAAGCACATTGTGTTTGTGGGCTCTATTGAG
TACCTCAAGCGGGAATGGGAGACGCTTCATAACTTCCCCAAAGTGTCCATATTGCCTGGT
ACGCCATTAAGTCGGGCTGATTTAAGGGCTGTCAACATCAACCTCTGTGACATGTGCGTT
ATCCTGTCAGCCAATCAGAATAATATTGATGATACTTCGCTGCAGGACAAGGAATGCATC
TTGGCGTCACTCAACATCAAATCTATGCAGTTTGATGACAGCATCGGAGTCTTGCAGGCT
AATTCCCAAGGGTTCACACCTCCAGGAATGGATAGATCCTCTCCAGATAACAGCCCAGTG
CACGGGATGTTACGTCAACCATCCATCACAACTGGGGTCAACATCCCCATCATCACTGAA
CTAGTGAACGATACTAATGTTCAGTTTTTGGACCAAGACGATGATGATGACCCTGATACA
GAACTGTACCTCACGCAGCCCTTTGCCTGTGGGACAGCATTTGCCGTCAGTGTCCTGGAC
TCACTCATGAGCGCGACGTACTTCAATGACAATATCCTCACCCTGATACGGACCCTGGTG
ACCGGAGGAGCCACGCCGGAGCTGGAGGCTCTGATTGCTGAGGAAAACGCCCTTAGAGGT
GGCTACAGCACCCCGCAGACACTGGCCAATAGGGACCGCTGCCGCGTGGCCCAGTTAGCT
CTGCTCGATGGGCCATTTGCGGACTTAGGGGATGGTGGTTGTTATGGTGATCTGTTCTGC
AAAGCTCTGAAAACATATAATATGCTTTGTTTTGGAATTTACCGGCTGAGAGATGCTCAC
CTCAGCACCCCCAGTCAGTGCACAAAGAGGTATGTCATCACCAACCCGCCCTATGAGTTT
GAGCTCGTGCCGACGGACCTGATCTTCTGCTTAATGCAGTTTGACCACAATGCCGGCCAG
TCCCGGGCCAGCCTGTCCCATTCCTCCCACTCGTCGCAGTCCTCCAGCAAGAAGAGCTCC
TCTGTTCACTCCATCCCATCCACAGCAAACCGACAGAACCGGCCCAAGTCCAGGGAGTCC
CGGGACAAACAGAAGTACGTGCAGGAAGAGCGGCTTTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID KCNMA1 Link Image
Target 1 GenAtlas ID KCNMA1 Link Image
Target 1 HGNC ID HGNC:6284 Link Image
Target 1 Chromosome Location 10
Target 1 Locus 10q22.3
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Wallner M, Meera P, Toro L: Molecular basis of fast inactivation in voltage and Ca2+-activated K+ channels: a transmembrane beta-subunit homolog. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):4137-42. [PubMed Link Image]
  2. Brenner R, Jegla TJ, Wickenden A, Liu Y, Aldrich RW: Cloning and functional characterization of novel large conductance calcium-activated potassium channel beta subunits, hKCNMB3 and hKCNMB4. J Biol Chem. 2000 Mar 3;275(9):6453-61. [PubMed Link Image]
  3. McCobb DP, Fowler NL, Featherstone T, Lingle CJ, Saito M, Krause JE, Salkoff L: A human calcium-activated potassium channel gene expressed in vascular smooth muscle. Am J Physiol. 1995 Sep;269(3 Pt 2):H767-77. [PubMed Link Image]
  4. Dworetzky SI, Trojnacki JT, Gribkoff VK: Cloning and expression of a human large-conductance calcium-activated potassium channel. Brain Res Mol Brain Res. 1994 Nov;27(1):189-93. [PubMed Link Image]
  5. Pallanck L, Ganetzky B: Cloning and characterization of human and mouse homologs of the Drosophila calcium-activated potassium channel gene, slowpoke. Hum Mol Genet. 1994 Aug;3(8):1239-43. [PubMed Link Image]
  6. Tseng-Crank J, Foster CD, Krause JD, Mertz R, Godinot N, DiChiara TJ, Reinhart PH: Cloning, expression, and distribution of functionally distinct Ca(2+)-activated K+ channel isoforms from human brain. Neuron. 1994 Dec;13(6):1315-30. [PubMed Link Image]
  7. Wallner M, Meera P, Ottolia M, Kaczorowski GJ, Latorre R, Garcia ML, Stefani E, Toro L: Characterization of and modulation by a beta-subunit of a human maxi KCa channel cloned from myometrium. Receptors Channels. 1995;3(3):185-99. [PubMed Link Image]
  8. Wallner M, Meera P, Toro L: Determinant for beta-subunit regulation in high-conductance voltage-activated and Ca(2+)-sensitive K+ channels: an additional transmembrane region at the N terminus. Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14922-7. [PubMed Link Image]
  9. Meera P, Wallner M, Song M, Toro L: Large conductance voltage- and calcium-dependent K+ channel, a distinct member of voltage-dependent ion channels with seven N-terminal transmembrane segments (S0-S6), an extracellular N terminus, and an intracellular (S9-S10) C terminus. Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):14066-71. [PubMed Link Image]
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]

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.