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Record Information
Version2.0
Creation Date2009-07-21 20:28:24 UTC
Update Date2014-12-24 20:25:54 UTC
Accession NumberT3D2988
Identification
Common NameMiconazole
ClassSmall Molecule
DescriptionMiconazole is only found in individuals that have used or taken this drug. It is an imidazole antifungal agent that is used topically and by intravenous infusion. [PubChem] Miconazole interacts with 14-α demethylase, a cytochrome P-450 enzyme necessary to convert lanosterol to ergosterol. As ergosterol is an essential component of the fungal cell membrane, inhibition of its synthesis results in increased cellular permeability causing leakage of cellular contents. Miconazole may also inhibit endogenous respiration, interact with membrane phospholipids, inhibit the transformation of yeasts to mycelial forms, inhibit purine uptake, and impair triglyceride and/or phospholipid biosynthesis.
Compound Type
  • 14-alpha Demethylase Inhibitor
  • Amine
  • Antifungal Agent
  • Drug
  • Ether
  • Metabolite
  • Organic Compound
  • Organochloride
  • Synthetic Compound
Chemical Structure
Thumb
Synonyms
Synonym
1-(2,4-Dichloro-beta-((2,4-dichlorobenzyl)oxy)phenethyl)imidazole
1-[2-(2,4-Dichloro-benzyloxy)-2-(2,4-dichloro-phenyl)-ethyl]-1H-imidazole
Daktarin
Decocort
Desenex
Femizol-M
Gyno-Daktarin
MCZ
Micatin
Miconazex
Monistat
Monistat-Derm
Oravig
Zeasorb-AF
Zimycan
Chemical FormulaC18H14Cl4N2O
Average Molecular Mass416.129 g/mol
Monoisotopic Mass413.986 g/mol
CAS Registry Number22916-47-8
IUPAC Name1-[2-(2,4-dichlorophenyl)-2-[(2,4-dichlorophenyl)methoxy]ethyl]-1H-imidazole
Traditional Namemiconazole
SMILESClC1=CC(Cl)=C(COC(CN2C=CN=C2)C2=C(Cl)C=C(Cl)C=C2)C=C1
InChI IdentifierInChI=1/C18H14Cl4N2O/c19-13-2-1-12(16(21)7-13)10-25-18(9-24-6-5-23-11-24)15-4-3-14(20)8-17(15)22/h1-8,11,18H,9-10H2
InChI KeyInChIKey=BYBLEWFAAKGYCD-UHFFFAOYNA-N
Chemical Taxonomy
Description belongs to the class of organic compounds known as benzylethers. These are aromatic ethers with the general formula ROCR' (R = alkyl, aryl; R'=benzene).
KingdomOrganic compounds
Super ClassBenzenoids
ClassBenzene and substituted derivatives
Sub ClassBenzylethers
Direct ParentBenzylethers
Alternative Parents
Substituents
  • Benzylether
  • 1,3-dichlorobenzene
  • Chlorobenzene
  • Halobenzene
  • Aryl chloride
  • Aryl halide
  • N-substituted imidazole
  • Imidazole
  • Azole
  • Heteroaromatic compound
  • Ether
  • Dialkyl ether
  • Organoheterocyclic compound
  • Azacycle
  • Organooxygen compound
  • Organonitrogen compound
  • Organochloride
  • Organohalogen compound
  • Hydrocarbon derivative
  • Organopnictogen compound
  • Organic oxygen compound
  • Organic nitrogen compound
  • Aromatic heteromonocyclic compound
Molecular FrameworkAromatic heteromonocyclic compounds
External Descriptors
Biological Properties
StatusDetected and Not Quantified
OriginExogenous
Cellular Locations
  • Cytoplasm
  • Membrane
Biofluid LocationsNot Available
Tissue LocationsNot Available
PathwaysNot Available
Applications
Biological Roles
Chemical RolesNot Available
Physical Properties
StateSolid
AppearanceWhite powder.
Experimental Properties
PropertyValue
Melting Point159-163°C
Boiling PointNot Available
Solubility1g/100mL (20°C)
LogP6.1
Predicted Properties
PropertyValueSource
Water Solubility0.00076 g/LALOGPS
logP5.86ALOGPS
logP5.96ChemAxon
logS-5.7ALOGPS
pKa (Strongest Basic)6.77ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area27.05 ŲChemAxon
Rotatable Bond Count6ChemAxon
Refractivity103.07 m³·mol⁻¹ChemAxon
Polarizability39.54 ųChemAxon
Number of Rings3ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-001i-9233000000-cf671d00eb6cf2e83a70JSpectraViewer
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-qTof , Positivesplash10-02t9-0501900000-40f5928152d84e02deefJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-qTof , Positivesplash10-015c-4900000000-628ede89a2ff3a714388JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - , positivesplash10-02t9-0501900000-40f5928152d84e02deefJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - , positivesplash10-0bt9-2900000000-1921b08c2de7bbf0624dJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QFT , positivesplash10-0bt9-0900500000-1a5805da9606edbe7e9aJSpectraViewer | MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-03di-0010900000-fdb45193fda5b55b51fbJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-029i-8196600000-0688ca27d69a2b799e4eJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-014i-9231000000-36d36a480a365220e479JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-03di-1001900000-6bf34660d27cb9682f77JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-014i-9001100000-646beb070226cf30103fJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-014l-9200000000-cddc446725179619915fJSpectraViewer
MSMass Spectrum (Electron Ionization)splash10-0bt9-4900000000-3f143064c2acde7e15a4JSpectraViewer | MoNA
Toxicity Profile
Route of ExposureTopical
Mechanism of ToxicityMiconazole interacts with 14-α demethylase, a cytochrome P-450 enzyme necessary to convert lanosterol to ergosterol. As ergosterol is an essential component of the fungal cell membrane, inhibition of its synthesis results in increased cellular permeability causing leakage of cellular contents. Miconazole may also inhibit endogenous respiration, interact with membrane phospholipids, inhibit the transformation of yeasts to mycelial forms, inhibit purine uptake, and impair triglyceride and/or phospholipid biosynthesis.
MetabolismNot Available
Toxicity ValuesLD50: 3800 mg/kg (Oral, Mouse) (1) LD50: 3 gm/kg (Oral, Rat) (1)
Lethal DoseNot Available
Carcinogenicity (IARC Classification)No indication of carcinogenicity to humans (not listed by IARC).
Uses/SourcesFor topical application in the treatment of tinea pedis (athlete’s foot), tinea cruris, and tinea corporis caused by Trichophyton rubrum, Trichophyton mentagrophytes, and Epidermophyton floccosum, in the treatment of cutaneous candidiasis (moniliasis), and in the treatment of tinea versicolor.
Minimum Risk LevelNot Available
Health EffectsNot Available
SymptomsIngestion of the amounts of the components contained in a tube of cream are unlikely to produce overdosage and toxic effects.
TreatmentNot Available
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDDB01110
HMDB IDHMDB15242
PubChem Compound ID4189
ChEMBL IDCHEMBL91
ChemSpider ID4044
KEGG IDC08070
UniProt IDNot Available
OMIM ID
ChEBI ID6923
BioCyc IDCPD-4501
CTD IDNot Available
Stitch IDMiconazole
PDB IDNot Available
ACToR IDNot Available
Wikipedia LinkMiconazole
References
Synthesis Reference

DrugSyn.org

MSDSLink
General References
  1. Wishart DS, Knox C, Guo AC, Cheng D, Shrivastava S, Tzur D, Gautam B, Hassanali M: DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6. Epub 2007 Nov 29. [18048412 ]
Gene Regulation
Up-Regulated GenesNot Available
Down-Regulated Genes
GeneGene SymbolGene IDInteractionChromosomeDetails

Targets

General Function:
Tetrahydrobiopterin binding
Specific Function:
Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.Isoform eNOS13C: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.
Gene Name:
NOS3
Uniprot ID:
P29474
Molecular Weight:
133287.62 Da
References
  1. Wolff DJ, Datto GA, Samatovicz RA: The dual mode of inhibition of calmodulin-dependent nitric-oxide synthase by antifungal imidazole agents. J Biol Chem. 1993 May 5;268(13):9430-6. [7683652 ]
  2. Bogle RG, Whitley GS, Soo SC, Johnstone AP, Vallance P: Effect of anti-fungal imidazoles on mRNA levels and enzyme activity of inducible nitric oxide synthase. Br J Pharmacol. 1994 Apr;111(4):1257-61. [7518297 ]
  3. Sennequier N, Wolan D, Stuehr DJ: Antifungal imidazoles block assembly of inducible NO synthase into an active dimer. J Biol Chem. 1999 Jan 8;274(2):930-8. [9873034 ]
  4. Dudek RR, Conforto A, Pinto V, Wildhirt S, Suzuki H: Inhibition of endothelial nitric oxide synthase by cytochrome P-450 reductase inhibitors. Proc Soc Exp Biol Med. 1995 May;209(1):60-4. [7536941 ]
General Function:
Tetrahydrobiopterin binding
Specific Function:
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH on 'Cys-247' implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM.
Gene Name:
NOS2
Uniprot ID:
P35228
Molecular Weight:
131116.3 Da
References
  1. Wolff DJ, Datto GA, Samatovicz RA: The dual mode of inhibition of calmodulin-dependent nitric-oxide synthase by antifungal imidazole agents. J Biol Chem. 1993 May 5;268(13):9430-6. [7683652 ]
  2. Bogle RG, Whitley GS, Soo SC, Johnstone AP, Vallance P: Effect of anti-fungal imidazoles on mRNA levels and enzyme activity of inducible nitric oxide synthase. Br J Pharmacol. 1994 Apr;111(4):1257-61. [7518297 ]
  3. Sennequier N, Wolan D, Stuehr DJ: Antifungal imidazoles block assembly of inducible NO synthase into an active dimer. J Biol Chem. 1999 Jan 8;274(2):930-8. [9873034 ]
  4. Dudek RR, Conforto A, Pinto V, Wildhirt S, Suzuki H: Inhibition of endothelial nitric oxide synthase by cytochrome P-450 reductase inhibitors. Proc Soc Exp Biol Med. 1995 May;209(1):60-4. [7536941 ]
General Function:
Voltage-gated potassium channel activity
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).
Gene Name:
KCNMA1
Uniprot ID:
Q12791
Molecular Weight:
137558.115 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General Function:
Potassium channel regulator activity
Specific Function:
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and alters its pharmacological properties. It slows down the activation and the deactivation kinetics of the channel. Acts as a negative regulator of smooth muscle contraction by enhancing the calcium sensitivity to KCNMA1. Its presence is also a requirement for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external binding of the agonist hormone 17-beta-estradiol (E2). Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1 peptide blocker by increasing the CTX association rate and decreasing the dissociation rate.
Gene Name:
KCNMB1
Uniprot ID:
Q16558
Molecular Weight:
21797.27 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General Function:
Potassium channel regulator activity
Specific Function:
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Acts as a negative regulator that confers rapid and complete inactivation of KCNMA1 channel complex. May participate in KCNMA1 inactivation in chromaffin cells of the adrenal gland or in hippocampal CA1 neurons.
Gene Name:
KCNMB2
Uniprot ID:
Q9Y691
Molecular Weight:
27129.37 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General Function:
Potassium channel regulator activity
Specific Function:
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Alters the functional properties of the current expressed by the KCNMA1 channel. Isoform 2, isoform 3 and isoform 4 partially inactivate the current of KCNBMA. Isoform 4 induces a fast and incomplete inactivation of KCNMA1 channel that is detectable only at large depolarizations. In contrast, isoform 1 does not induce detectable inactivation of KCNMA1. Two or more subunits of KCNMB3 are required to block the KCNMA1 tetramer.
Gene Name:
KCNMB3
Uniprot ID:
Q9NPA1
Molecular Weight:
31603.26 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General Function:
Potassium channel regulator activity
Specific Function:
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Decreases the gating kinetics and calcium sensitivity of the KCNMA1 channel, but with fast deactivation kinetics. May decrease KCNMA1 channel openings at low calcium concentrations but increases channel openings at high calcium concentrations. Makes KCNMA1 channel resistant to 100 nM charybdotoxin (CTX) toxin concentrations.
Gene Name:
KCNMB4
Uniprot ID:
Q86W47
Molecular Weight:
23948.465 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General Function:
Protein phosphatase binding
Specific Function:
Forms a voltage-independent potassium channel that is activated by intracellular calcium (PubMed:26148990). Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells. The channel is blocked by clotrimazole and charybdotoxin but is insensitive to apamin (PubMed:17157250, PubMed:18796614).
Gene Name:
KCNN4
Uniprot ID:
O15554
Molecular Weight:
47695.12 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General Function:
Voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization
Specific Function:
Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr). Isoforms USO have no channel activity by themself, but modulates channel characteristics by forming heterotetramers with other isoforms which are retained intracellularly and undergo ubiquitin-dependent degradation.
Gene Name:
KCNH2
Uniprot ID:
Q12809
Molecular Weight:
126653.52 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Kikuchi K, Nagatomo T, Abe H, Kawakami K, Duff HJ, Makielski JC, January CT, Nakashima Y: Blockade of HERG cardiac K+ current by antifungal drug miconazole. Br J Pharmacol. 2005 Mar;144(6):840-8. [15778703 ]
General Function:
Voltage-gated potassium channel activity
Specific Function:
Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, rectifying current (By similarity). Channel properties may be modulated by cAMP and subunit assembly.
Gene Name:
KCNH6
Uniprot ID:
Q9H252
Molecular Weight:
109923.705 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Kikuchi K, Nagatomo T, Abe H, Kawakami K, Duff HJ, Makielski JC, January CT, Nakashima Y: Blockade of HERG cardiac K+ current by antifungal drug miconazole. Br J Pharmacol. 2005 Mar;144(6):840-8. [15778703 ]
General Function:
Voltage-gated potassium channel activity
Specific Function:
Pore-forming (alpha) subunit of voltage-gated potassium channel. Channel properties may be modulated by cAMP and subunit assembly.
Gene Name:
KCNH7
Uniprot ID:
Q9NS40
Molecular Weight:
134998.525 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Kikuchi K, Nagatomo T, Abe H, Kawakami K, Duff HJ, Makielski JC, January CT, Nakashima Y: Blockade of HERG cardiac K+ current by antifungal drug miconazole. Br J Pharmacol. 2005 Mar;144(6):840-8. [15778703 ]
General Function:
Small conductance calcium-activated potassium channel activity
Specific Function:
Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin (By similarity).
Gene Name:
KCNN1
Uniprot ID:
Q92952
Molecular Weight:
59986.87 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General Function:
Small conductance calcium-activated potassium channel activity
Specific Function:
Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.
Gene Name:
KCNN2
Uniprot ID:
Q9H2S1
Molecular Weight:
63759.03 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General Function:
Small conductance calcium-activated potassium channel activity
Specific Function:
Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.
Gene Name:
KCNN3
Uniprot ID:
Q9UGI6
Molecular Weight:
82025.305 Da
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General Function:
Signal transducer activity
Specific Function:
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium.
Gene Name:
ATP2C1
Uniprot ID:
P98194
Molecular Weight:
100576.42 Da
References
  1. Wishart DS, Knox C, Guo AC, Cheng D, Shrivastava S, Tzur D, Gautam B, Hassanali M: DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6. Epub 2007 Nov 29. [18048412 ]
General Function:
Titin binding
Specific Function:
Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins 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. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.
Gene Name:
CALM1
Uniprot ID:
P0DP23
Molecular Weight:
16837.47 Da
References
  1. Wishart DS, Knox C, Guo AC, Cheng D, Shrivastava S, Tzur D, Gautam B, Hassanali M: DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6. Epub 2007 Nov 29. [18048412 ]
General Function:
Sterol 14-demethylase activity
Specific Function:
Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.
Gene Name:
CYP51A1
Uniprot ID:
Q16850
Molecular Weight:
56805.26 Da
References
  1. Wishart DS, Knox C, Guo AC, Cheng D, Shrivastava S, Tzur D, Gautam B, Hassanali M: DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6. Epub 2007 Nov 29. [18048412 ]