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Showing drug card for Triamterene (DB00384)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-27 00:16:22
Primary Accession Number DB00384
Secondary Accession Number
  • APRD00079
Name Triamterene
Drug Type
  • Small Molecule
Description A pteridine that is used as a mild diuretic. [PubChem]
Synonyms
  1. Triamteren
Brand Names
  1. Ademin
  2. Ademine
  3. Diren
  4. Ditak
  5. Diucelpin
  6. Diurene
  7. Dyazide
  8. Dyren
  9. Dyrenium
  10. Dytac
  11. Jatropur
  12. Maxzide
  13. Maxzide-25
  14. Noridil
  15. Noridyl
  16. Pterofen
  17. Pterophene
  18. Taturil
  19. Teriam
  20. Teridin
  21. Tri-Span
  22. Triampur
  23. Triamteril
  24. Triamteril Complex
  25. Trispan
  26. Triteren
  27. Urocaudal
Brand Mixtures
  1. Apo Triazide Tab (Hydrochlorothiazide + Triamterene)
  2. Dyazide Tab (Hydrochlorothiazide + Triamterene)
  3. Novo-Triamzide (Hydrochlorothiazide + Triamterene)
  4. Nu-Triazide Tab 50 Mg/25 Mg (Hydrochlorothiazide + Triamterene)
  5. Penta-Triamterene HCTZ Tablets (Hydrochlorothiazide + Triamterene)
  6. Pro-Triazide (Hydrochlorothiazide + Triamterene)
  7. Riva-Zide 50/25mg Tablets (Hydrochlorothiazide + Triamterene)
Chemical IUPAC Name 6-phenylpteridine-2,4,7-triamine
Chemical Formula C12H11N7
Chemical Structure Structure
CAS Registry Number 396-01-0
InChI Identifier InChI=1/C12H11N7/c13-9-7(6-4-2-1-3-5-6)16-8-10(14)18-12(15)19-11(8)17-9/h1-5H,(H6,13,14,15,17,18,19)/f/h13-15H2
InChI Key FNYLWPVRPXGIIP-VLYIBAHHCJ
KEGG Drug D00386 Link Image
KEGG Compound Not Available
PubChem Compound 5546 Link Image
PubChem Substance 153028 Link Image
ChEBI ID Not Available
PharmGKB ID PA451752 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 01919563 Link Image
RxList Link http://www.rxlist.com/cgi/generic/triamterine.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Triamterene Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Spickett, Timmis, J. Chem.. Soc. 1954, 2887 (1958)
Average Molecular Weight 253.2626
Monoisotopic Molecular Weight 253.1076
State Solid
Melting Point 316 oC
Experimental Water Solubility 48.2 mg/L Source: PhysProp
Predicted Water Solubility 9.63e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 0.3 Source: PhysProp
Predicted LogP 1.21 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.42 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 NC1=NC(N)=C2N=C(C3=CC=CC=C3)C(N)=NC2=N1
Canonical SMILES NC1=NC(N)=C2N=C(C3=CC=CC=C3)C(N)=NC2=N1
Drug Category
  • Diuretics
  • Potassium-sparing Diuretics
ATC Codes
AHFS Codes Not Available
Indication For the treatment of edema associated with congestive heart failure, cirrhosis of the liver, and the nephrotic syndrome; also in steroid-induced edema, idiopathic edema, and edema due to secondary hyperaldosteronism.
Pharmacology Triamterene, a relatively weak, potassium-sparing diuretic and antihypertensive, is used in the management of hypokalemia. Triamterene is similar in action to amiloride but, unlike amiloride, increases the urinary excretion of magnesium.
Mechanism of Action Triamterene inhibits the epithelial sodium channels on principal cells in the late distal convoluted tubule and collecting tubule, which are responsible for 1-2% of total sodium reabsorption. As sodium reabsorption is inhibited, this increases the osmolarity in the nephron lumen and decreases the osmolarity of the interstitium. Since sodium concentration is the main driving force for water reabsorption, triamterene can achieve a modest amount of diuresis by decreasing the osmotic gradient necessary for water reabsorption from lumen to interstitium. Triamterene also has a potassium-sparing effect. Normally, the process of potassium excretion is driven by the electrochemical gradient produced by sodium reabsorption. As sodium is reabsorbed, it leaves a negative potential in the lumen, while producing a positive potential in the principal cell. This potential promotes potassium excretion through apical potassium channels. By inhibiting sodium reabsorption, triamterene also inhibits potassium excretion.
Absorption Rapidly absorbed, with somewhat less than 50% of the oral dose reaching the urine.
Toxicity In the event of overdosage it can be theorized that electrolyte imbalance would be the major concern, with particular attention to possible hyperkalemia. Other symptoms that might be seen would be nausea and vomiting, other G.I. disturbances, and weakness. It is conceivable that some hypotension could occur. The oral LD50 in mice is 380 mg/kg.
Protein Binding 97%
Biotransformation Triamterene is primarily metabolized to the sulfate conjugate of hydroxytriamterene. Both the plasma and urine levels of this metabolite greatly exceed triamterene levels.
Half Life Not Available
Dosage Forms
Form Route
Capsule Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Amantadine The diuretic increases the adverse effects of amantadine
Benazepril Increased risk of hyperkaliemia
Candesartan Increased risk of hyperkaliemia
Captopril Increased risk of hyperkaliemia
Cilazapril Increased risk of hyperkaliemia
Drospirenone Increased risk of hyperkaliemia
Enalapril Increased risk of hyperkaliemia
Eplerenone This association presents an increased risk of hyperkaliemia
Eprosartan Increased risk of hyperkaliemia
Forasartan Increased risk of hyperkaliemia
Fosinopril Increased risk of hyperkaliemia
Indomethacin Risk of acute renal impairment with this combination
Irbesartan Increased risk of hyperkaliemia
Lisinopril Increased risk of hyperkaliemia
Losartan Increased risk of hyperkaliemia
Moexipril Increased risk of hyperkaliemia
Perindopril Increased risk of hyperkaliemia
Polystyrene sulfonate Antagonism of action
Potassium Increased risk of hyperkaliemia
Quinapril Increased risk of hyperkaliemia
Ramipril Increased risk of hyperkaliemia
Saprisartan Increased risk of hyperkaliemia
Spirapril Increased risk of hyperkaliemia
Tasosartan Increased risk of hyperkaliemia
Telmisartan Increased risk of hyperkaliemia
Trandolapril Increased risk of hyperkaliemia
Valsartan Increased risk of hyperkaliemia
Food Interactions Not Available
Pathways
Name SMPDB Link KEGG Link
Triamterene Pathway SMP00132 Link Image
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Amiloride-sensitive sodium channel subunit beta
  2. Amiloride-sensitive sodium channel subunit alpha
  3. Amiloride-sensitive sodium channel subunit delta
  4. Amiloride-sensitive sodium channel subunit gamma
Drug Target 1 [top]
Target 1 ID 27
Target 1 Name Amiloride-sensitive sodium channel subunit beta
Target 1 Synonyms
  1. Beta ENaC
  2. Beta NaCH
  3. ENaCB
  4. Epithelial Na(+) channel subunit beta
  5. Nonvoltage-gated sodium channel 1 subunit beta
  6. SCNEB
Target 1 Gene Name SCNN1B
Target 1 Protein Sequence >Amiloride-sensitive sodium channel subunit beta
MHVKKYLLKGLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIICEGPKKKAMWFLLTLLFA
ALVCWQWGIFIRTYLSWEVSVSLSVGFKTMDFPAVTICNASPFKYSKIKHLLKDLDELME
AVLERILAPELSHANATRNLNFSIWNHTPLVLIDERNPHHPMVLDLFGDNHNGLTSSSAS
EKICNAHGCKMAMRLCSLNRTQCTFRNFTSATQALTEWYILQATNIFAQVPQQELVEMSY
PGEQMILACLFGAEPCNYRNFTSIFYPHYGNCYIFNWGMTEKALPSANPGTEFGLKLILD
IGQEDYVPFLASTAGVRLMLHEQRSYPFIRDEGIYAMSGTETSIGVLVDKLQRMGEPYSP
CTVNGSEVPVQNFYSDYNTTYSIQACLRSCFQDHMIRNCNCGHYLYPLPRGEKYCNNRDF
PDWAHCYSDLQMSVAQRETCIGMCKESCNDTQYKMTISMADWPSEASEDWIFHVLSQERD
QSTNITLSRKGIVKLNIYFQEFNYRTIEESAANNIVWLLSNLGGQFGFWMGGSVLCLIEF
GEIIIDFVWITIIKLVALAKSLRQRRAQASYAGPPPTVAELVEAHTNFGFQPDTAPRSPN
TGPYPSEQALPIPGTPPPNYDSLRLQPLDVIESDSEGDAI
Target 1 Number of Residues 650
Target 1 Molecular Weight 72660
Target 1 Theoretical pI 6.26
Target 1 GO Classification
Function
transporter activity
ion transporter activity
ion channel activity
cation channel activity
sodium channel activity
amiloride-sensitive sodium channel activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
sodium ion transport
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 1 General Function Involved in amiloride-sensitive sodium channel activity
Target 1 Specific Function Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 51-71
  • 533-553
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 1004271 Link Image
Target 1 UniProtKB/Swiss-Prot ID P51168 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name SCNNB_HUMAN Link Image
Target 1 PDB ID 1I5H Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cell membrane
  • apical cell membrane
  • multi- pass membrane protein. Apical membrane of epithelial cel
Target 1 Gene Sequence >1923 bp
ATGCACGTGAAGAAGTACCTGCTGAAGGGCCTGCATCGGCTGCAGAAGGGCCCCGGCTAC
ACGTACAAGGAGCTGCTGGTGTGGTACTGCGACAACACCAACACCCACGGCCCCAAGCGC
ATCATCTGTGAGGGGCCCAAGAAGAAAGCCATGTGGTTCCTGCTCACCCTGCTCTTCGCC
GCCCTCGTCTGCTGGCAGTGGGGCATCTTCATCAGGACCTACTTGAGCTGGGAGGTCAGC
GTCTCCCTCTCCGTAGGCTTCAAGACCATGGACTTCCCCGCCGTCACCATCTGCAATGCT
AGCCCCTTCAAGTATTCCAAAATCAAGCATTTGCTGAAGGACCTGGATGAGCTGATGGAA
GCTGTCCTGGAGAGAATCCTGGCTCCTGAGCTAAGCCATGCCAATGCCACCAGGAACCTG
AACTTCTCCATCTGGAACCACACACCCCTGGTCCTTATTGATGAACGGAACCCCCACCAC
CCCATGGTCCTTGATCTCTTTGGAGACAACCACAATGGCTTAACAAGCAGCTCAGCATCA
GAAAAGATCTGTAATGCCCACGGGTGCAAAATGGCCATGAGACTATGTAGCCTCAACAGG
ACCCAGTGTACCTTCCGGAACTTCACCAGTGCTACCCAGGCATTGACAGAGTGGTACATC
CTGCAGGCCACCAACATCTTTGCACAGGTGCCACAGCAGGAGCTAGTAGAGATGAGCTAC
CCCGGCGAGCAGATGATCCTGGCCTGCCTATTCGGAGCTGAGCCCTGCAACTACCGGAAC
TTCACGTCCATCTTCTACCCTCACTATGGCAACTGTTACATCTTCAACTGGGGCATGACA
GAGAAGGCACTTCCTTCGGCCAACCCTGGAACTGAATTCGGCCTGAAGTTGATCCTGGAC
ATAGGCCAGGAAGACTACGTCCCCTTCCTTGCGTCCACGGGCGGGGTCAGGCTGATGCTT
CACGAGCAGAGGTCATACCCCTTCATCAGAGATGAGGGCATCTACGCCATGTCGGGGACA
GAGACGTCCATCGGGGTACTCGTGGATAAGCTTCAGCGCATGGGGGAGCCCTACAGCCCG
TGCACCGTGAATGGTTCTGAGGTCCCCGTCCAAAACTTCTACAGTGACTACAACACGACC
TACTCCATCCAGGCCTGTCTTCGCTCCTGCTTCCAAGACCACATGATCCGTAACTGCAAC
TGTGGCCACTACCTGTACCCACTGCCCCGTGGGGAGAAATACTGCAACAACCGGGACTTC
CCAGACTGGGCCCATTGCTACTCAGATCTACAGATGAGCGTGGCGCAGAGAGAGACCTGC
ATTGGCATGTGCAAGGAGTCCTGCAATGACACCCAGTACAAGATGACCATCTCCATGGCT
GACTGGCCTTCTGAGGCCTCCGAGGACTGGATTTTCCACGTCTTGTCTCAGGAGCGGGAC
CAAAGCACCAATATCACCCTGAGCAGGAAGGGAATTGTCAAGCTCAACATCTACTTCCAA
GAATTTAACTATCGCACCATTGAAGAATCAGCAGCCAATAACATCGTCTGGCTGCTCTCG
AATCTGGGTGGCCAGTTTGGCTTCTGGATGGGGGGCTCTGTGCTGTGCCTCATCGAGTTT
GGGGAGATCATCATCGACTTTGTGTGGATCACCATCATCAAGCTGGTGGCCTTGGCCAAG
AGCCTACGGCAGCGGCGAGCCCAAGCCAGCTACGCTGGCCCACCGCCCACCGTGGCCGAG
CTGGTGGAGGCCCACACCAACTTTGGCTTCCAGCCTGACACGGCCCCCCGCAGCCCCAAC
ACTGGGCCCTACCCCAGTGAGCAGGCCCTGCCCATCCCAGGCACCCCGCCCCCCAACTAT
GACTCCCTGCGTCTGCAGCCGCTGGACGTCATCGAGTCTGACAGTGAGGGTGATGCCATC
TAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID SCNN1B Link Image
Target 1 GenAtlas ID SCNN1B Link Image
Target 1 HGNC ID HGNC:10600 Link Image
Target 1 Chromosome Location 16
Target 1 Locus 16p12.2-p12.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Arai K, Zachman K, Shibasaki T, Chrousos GP: Polymorphisms of amiloride-sensitive sodium channel subunits in five sporadic cases of pseudohypoaldosteronism: do they have pathologic potential? J Clin Endocrinol Metab. 1999 Jul;84(7):2434-7. [PubMed Link Image]
  2. Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [PubMed Link Image]
  3. McDonald FJ, Western AH, McNeil JD, Thomas BC, Olson DR, Snyder PM: Ubiquitin-protein ligase WWP2 binds to and downregulates the epithelial Na(+) channel. Am J Physiol Renal Physiol. 2002 Sep;283(3):F431-6. [PubMed Link Image]
  4. Voilley N, Bassilana F, Mignon C, Merscher S, Mattei MG, Carle GF, Lazdunski M, Barbry P: Cloning, chromosomal localization, and physical linkage of the beta and gamma subunits (SCNN1B and SCNN1G) of the human epithelial amiloride-sensitive sodium channel. Genomics. 1995 Aug 10;28(3):560-5. [PubMed Link Image]
  5. Hansson JH, Nelson-Williams C, Suzuki H, Schild L, Shimkets R, Lu Y, Canessa C, Iwasaki T, Rossier B, Lifton RP: Hypertension caused by a truncated epithelial sodium channel gamma subunit: genetic heterogeneity of Liddle syndrome. Nat Genet. 1995 Sep;11(1):76-82. [PubMed Link Image]
  6. McDonald FJ, Price MP, Snyder PM, Welsh MJ: Cloning and expression of the beta- and gamma-subunits of the human epithelial sodium channel. Am J Physiol. 1995 May;268(5 Pt 1):C1157-63. [PubMed Link Image]
  7. Shimkets RA, Warnock DG, Bositis CM, Nelson-Williams C, Hansson JH, Schambelan M, Gill JR Jr, Ulick S, Milora RV, Findling JW, et al.: Liddle's syndrome: heritable human hypertension caused by mutations in the beta subunit of the epithelial sodium channel. Cell. 1994 Nov 4;79(3):407-14. [PubMed Link Image]
  8. Hansson JH, Schild L, Lu Y, Wilson TA, Gautschi I, Shimkets R, Nelson-Williams C, Rossier BC, Lifton RP: A de novo missense mutation of the beta subunit of the epithelial sodium channel causes hypertension and Liddle syndrome, identifying a proline-rich segment critical for regulation of channel activity. Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11495-9. [PubMed Link Image]
  9. Chang SS, Grunder S, Hanukoglu A, Rosler A, Mathew PM, Hanukoglu I, Schild L, Lu Y, Shimkets RA, Nelson-Williams C, Rossier BC, Lifton RP: Mutations in subunits of the epithelial sodium channel cause salt wasting with hyperkalaemic acidosis, pseudohypoaldosteronism type 1. Nat Genet. 1996 Mar;12(3):248-53. [PubMed Link Image]
  10. Pirozzi G, McConnell SJ, Uveges AJ, Carter JM, Sparks AB, Kay BK, Fowlkes DM: Identification of novel human WW domain-containing proteins by cloning of ligand targets. J Biol Chem. 1997 Jun 6;272(23):14611-6. [PubMed Link Image]
  11. 9674649 Persu A, Barbry P, Bassilana F, Houot AM, Mengual R, Lazdunski M, Corvol P, Jeunemaitre X: Genetic analysis of the beta subunit of the epithelial Na+ channel in essential hypertension. Hypertension. 1998 Jul;32(1):129-37.
  12. 9794716 Uehara Y, Sasaguri M, Kinoshita A, Tsuji E, Kiyose H, Taniguchi H, Noda K, Ideishi M, Inoue J, Tomita K, Arakawa K: Genetic analysis of the epithelial sodium channel in Liddle's syndrome. J Hypertens. 1998 Aug;16(8):1131-5.
  13. 9813171 Saxena A, Hanukoglu I, Strautnieks SS, Thompson RJ, Gardiner RM, Hanukoglu A: Gene structure of the human amiloride-sensitive epithelial sodium channel beta subunit. Biochem Biophys Res Commun. 1998 Nov 9;252(1):208-13.
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]
Drug Target 2 [top]
Target 2 ID 213
Target 2 Name Amiloride-sensitive sodium channel subunit alpha
Target 2 Synonyms
  1. Alpha ENaC
  2. Alpha NaCH
  3. Epithelial Na(+) channel subunit alpha
  4. Nonvoltage-gated sodium channel 1 subunit alpha
  5. SCNEA
Target 2 Gene Name SCNN1A
Target 2 Protein Sequence >Amiloride-sensitive sodium channel subunit alpha
MEGNKLEEQDSSPPQSTPGLMKGNKREEQGLGPEPAAPQQPTAEEEALIEFHRSYRELFE
FFCNNTTIHGAIRLVCSQHNRMKTAFWAVLWLCTFGMMYWQFGLLFGEYFSYPVSLNINL
NSDKLVFPAVTICTLNPYRYPEIKEELEELDRITEQTLFDLYKYSSFTTLVAGSRSRRDL
RGTLPHPLQRLRVPPPPHGARRARSVASSLRDNNPQVDWKDWKIGFQLCNQNKSDCFYQT
YSSGVDAVREWYRFHYINILSRLPETLPSLEEDTLGNFIFACRFNQVSCNQANYSHFHHP
MYGNCYTFNDKNNSNLWMSSMPGINNGLSLMLRAEQNDFIPLLSTVTGARVMVHGQDEPA
FMDDGGFNLRPGVETSISMRKETLDRLGGDYGDCTKNGSDVPVENLYPSKYTQQVCIHSC
FQESMIKECGCAYIFYPRPQNVEYCDYRKHSSWGYCYYKLQVDFSSDHLGCFTKCRKPCS
VTSYQLSAGYSRWPSVTSQEWVFQMLSRQNNYTVNNKRNGVAKVNIFFKELNYKTNSESP
SVTMVTLLSNLGSQWSLWFGSSVLSVVEMAELVFDLLVIMFLMLLRRFRSRYWSPGRGGR
GAQEVASTLASSPPSHFCPHPMSLSLSQPGPAPSPALTAPPPAYATLGPRPSPGGSAGAS
SSTCPLGGP
Target 2 Number of Residues 680
Target 2 Molecular Weight 75704
Target 2 Theoretical pI 7.54
Target 2 GO Classification
Function
transporter activity
ion transporter activity
ion channel activity
cation channel activity
sodium channel activity
amiloride-sensitive sodium channel activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
sodium ion transport
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 2 General Function Involved in amiloride-sensitive sodium channel activity
Target 2 Specific Function Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 86-106
  • 563-583
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 452650 Link Image
Target 2 UniProtKB/Swiss-Prot ID P37088 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name SCNNA_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Cell membrane
  • apical cell membrane
  • multi- pass membrane protein. Apical membrane of epithelial cel
Target 2 Gene Sequence >2010 bp
ATGGAGGGGAACAAGCTGGAGGAGCAGGACTCTAGCCCTCCACAGTCCACTCCAGGGCTC
ATGAAGGGGAACAAGCGTGAGGAGCAGGGGCTGGGCCCCGAACCTGCGGCGCCCCAGCAG
CCCACGGCGGAGGAGGAGGCCCTGATCGAGTTCCACCGCTCCTACCGAGAGCTCTTCGAG
TTCTTCTGCAACAACACCACCATCCACGGCGCCATCCGCCTGGTGTGCTCCCAGCACAAC
CGCATGAAGACGGCCTTCTGGGCAGTGCTGTGGCTCTGCACCTTTGGCATGATGTACTGG
CAATTCGGCCTGCTTTTCGGAGAGTACTTCAGCTACCCCGTCAGCCTCAACATCAACCTC
AACTCGGACAAGCTCGTCTTCCCCGCAGTGACCATCTGCACCCTCAATCCCTACAGGTAC
CCGGAAATTAAAGAGGAGCTGGAGGAGCTGGACCGCATCACAGAGCAGACGCTCTTTGAC
CTGTACAAATACAGCTCCTTCACCACTCTCGTGGCCGGCTCCCGCAGCCGTCGCGACCTG
CGGGGGACTCTGCCGCACCCCTTGCAGCGCCTGAGGGTCCCGCCCCCGCCTCACGGGGCC
CGTCGAGCCCGTAGCGTGGCCTCCAGCTTGCGGGACAACAACCCCCAGGTGGACTGGAAG
GACTGGAAGATCGGCTTCCAGCTGTGCAACCAGAACAAATCGGACTGCTTCTACCAGACA
TACTCATCAGGGGTGGATGCGGTGAGGGAGTGGTACCGCTTCCACTACATCAACATCCTG
TCGAGGCTGCCAGAGACTCTGCCATCCCTGGAGGAGGACACGCTGGGCAACTTCATCTTC
GCCTGCCGCTTCAACCAGGTCTCCTGCAACCAGGCGAATTACTCTCACTTCCACCACCCG
ATGTATGGAAACTGCTATACTTTCAATGACAAGAACAACTCCAACCTCTGGATGTCTTCC
ATGCCTGGAATCAACAACGGTCTGTCCCTGATGCTGCGCGCAGAGCAGAATGACTTCATT
CCCCTGCTGTCCACAGTGACTGGGGCCCGGGTAATGGTGCACGGGCAGGATGAACCTGCC
TTTATGGATGATGGTGGCTTTAACTTGCGGCCTGGCGTGGAGACCTCCATCAGCATGAGG
AAGGAAACCCTGGACAGACTTGGGGGCGATTATGGCGACTGCACCAAGAATGGCAGTGAT
GTTCCTGTTGAGAACCTTTACCCTTCAAAGTACACACAGCAGGTGTGTATTCACTCCTGC
TTCCAGGAGAGCATGATCAAGGAGTGTGGCTGTGCCTACATCTTCTATCCGCGGCCCCAG
AACGTGGAGTACTGTGACTACAGAAAGCACAGTTCCTGGGGGTACTGCTACTATAAGCTC
CAGGTTGACTTCTCCTCAGACCACCTGGGCTGTTTCACCAAGTGCCGGAAGCCATGCAGC
GTGACCAGCTACCAGCTCTCTGCTGGTTACTCACGATGGCCCTCGGTGACATCCCAGGAA
TGGGTCTTCCAGATGCTATCGCGACAGAACAATTACACCGTCAACAACAAGAGAAATGGA
GTGGCCAAAGTCAACATCTTCTTCAAGGAGCTGAACTACAAAACCAATTCTGAGTCTCCC
TCTGTCACGATGGTCACCCTCCTGTCCAACCTGGGCAGCCAGTGGAGCCTGTGGTTCGGC
TCCTCGGTGTTGTCTGTGGTGGAGATGGCTGAGCTCGTCTTTGACCTGCTGGTCATCATG
TTCCTCATGCTGCTCCGAAGGTTCCGAAGCCGATACTGGTCTCCAGGCCGAGGGGGCAGG
GGTGCTCAGGAGGTAGCCTCCACCCTGGCATCCTCCCCTCCTTCCCACTTCTGCCCCCAC
CCCATGTCTCTGTCCTTGTCCCAGCCAGGCCCTGCTCCCTCTCCAGCCTTGACAGCCCCT
CCCCCTGCCTATGCCACCCTGGGCCCCCGCCCATCTCCAGGGGGCTCTGCAGGGGCCAGT
TCCTCCACCTGTCCTCTGGGGGGGCCCTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID SCNN1A Link Image
Target 2 GenAtlas ID SCNN1A Link Image
Target 2 HGNC ID HGNC:10599 Link Image
Target 2 Chromosome Location 12
Target 2 Locus 12p13
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Arai K, Zachman K, Shibasaki T, Chrousos GP: Polymorphisms of amiloride-sensitive sodium channel subunits in five sporadic cases of pseudohypoaldosteronism: do they have pathologic potential? J Clin Endocrinol Metab. 1999 Jul;84(7):2434-7. [PubMed Link Image]
  2. Chow YH, Wang Y, Plumb J, O'Brodovich H, Hu J: Hormonal regulation and genomic organization of the human amiloride-sensitive epithelial sodium channel alpha subunit gene. Pediatr Res. 1999 Aug;46(2):208-14. [PubMed Link Image]
  3. Schaedel C, Marthinsen L, Kristoffersson AC, Kornfalt R, Nilsson KO, Orlenius B, Holmberg L: Lung symptoms in pseudohypoaldosteronism type 1 are associated with deficiency of the alpha-subunit of the epithelial sodium channel. J Pediatr. 1999 Dec;135(6):739-45. [PubMed Link Image]
  4. Mick VE, Itani OA, Loftus RW, Husted RF, Schmidt TJ, Thomas CP: The alpha-subunit of the epithelial sodium channel is an aldosterone-induced transcript in mammalian collecting ducts, and this transcriptional response is mediated via distinct cis-elements in the 5'-flanking region of the gene. Mol Endocrinol. 2001 Apr;15(4):575-88. [PubMed Link Image]
  5. McDonald FJ, Western AH, McNeil JD, Thomas BC, Olson DR, Snyder PM: Ubiquitin-protein ligase WWP2 binds to and downregulates the epithelial Na(+) channel. Am J Physiol Renal Physiol. 2002 Sep;283(3):F431-6. [PubMed Link Image]
  6. McDonald FJ, Snyder PM, McCray PB Jr, Welsh MJ: Cloning, expression, and tissue distribution of a human amiloride-sensitive Na+ channel. Am J Physiol. 1994 Jun;266(6 Pt 1):L728-34. [PubMed Link Image]
  7. Voilley N, Lingueglia E, Champigny G, Mattei MG, Waldmann R, Lazdunski M, Barbry P: The lung amiloride-sensitive Na+ channel: biophysical properties, pharmacology, ontogenesis, and molecular cloning. Proc Natl Acad Sci U S A. 1994 Jan 4;91(1):247-51. [PubMed Link Image]
  8. Pirozzi G, McConnell SJ, Uveges AJ, Carter JM, Sparks AB, Kay BK, Fowlkes DM: Identification of novel human WW domain-containing proteins by cloning of ligand targets. J Biol Chem. 1997 Jun 6;272(23):14611-6. [PubMed Link Image]
  9. Tucker JK, Tamba K, Lee YJ, Shen LL, Warnock DG, Oh Y: Cloning and functional studies of splice variants of the alpha-subunit of the amiloride-sensitive Na+ channel. Am J Physiol. 1998 Apr;274(4 Pt 1):C1081-9. [PubMed Link Image]
  10. Thomas CP, Auerbach S, Stokes JB, Volk KA: 5' heterogeneity in epithelial sodium channel alpha-subunit mRNA leads to distinct NH2-terminal variant proteins. Am J Physiol. 1998 May;274(5 Pt 1):C1312-23. [PubMed Link Image]
  11. 9654208 Ludwig M, Bolkenius U, Wickert L, Marynen P, Bidlingmaier F: Structural organisation of the gene encoding the alpha-subunit of the human amiloride-sensitive epithelial sodium channel. Hum Genet. 1998 May;102(5):576-81.
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 550
Target 3 Name Amiloride-sensitive sodium channel subunit delta
Target 3 Synonyms
  1. Delta ENaC
  2. Delta NaCH
  3. Epithelial Na(+) channel subunit delta
  4. Nonvoltage-gated sodium channel 1 subunit delta
  5. SCNED
Target 3 Gene Name SCNN1D
Target 3 Protein Sequence >Amiloride-sensitive sodium channel subunit delta
MAEHRSMDGRMEAATRGGSHLQAAAQTPPRPGPPSAPPPPPKEGHQEGLVELPASFRELL
TFFCTNATIHGAIRLVCSRGNRLKTTSWGLLSLGALVALCWQLGLLFERHWHRPVLMAVS
VHSERKLLPLVTLCDGNPRRPSPVLRHLELLDEFARENIDSLYNVNLSKGRAALSATVPR
HEPPFHLDREIRLQRLSHSGSRVRVGFRLCNSTGGDCFYRGYTSGVAAVQDWYHFHYVDI
LALLPAAWEDSHGSQDGHFVLSCSYDGLDCQARQFRTFHHPTYGSCYTVDGVWTAQRPGI
THGVGLVLRVEQQPHLPLLSTLAGIRVMVHGRNHTPFLGHHSFSVRPGTEATISIREDEV
HRLGSPYGHCTAGGEGVEVELLHNTSYTRQACLVSCFQQLMVETCSCGYYLHPLPAGAEY
CSSARHPAWGHCFYRLYQDLETHRLPCTSRCPRPCRESAFKLSTGTSRWPSAKSAGWTLA
TLGEQGLPHQSHRQRSSLAKINIVYQELNYRSVEEAPVYSVPQLLSAMGSLCSLWFGASV
LSLLELLELLLDASALTLVLGGRRLRRAWFSWPRASPASGASSIKPEASQMPPPAGGTSD
DPEPSGPHLPRVMLPGVLAGVSAEESWAGPQPLETLDT
Target 3 Number of Residues 648
Target 3 Molecular Weight 70216
Target 3 Theoretical pI 7.90
Target 3 GO Classification
Function
transporter activity
ion transporter activity
ion channel activity
cation channel activity
sodium channel activity
amiloride-sensitive sodium channel activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
sodium ion transport
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 3 General Function Involved in amiloride-sensitive sodium channel activity
Target 3 Specific Function Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • 87-107
  • 531-551
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 1066457 Link Image
Target 3 UniProtKB/Swiss-Prot ID P51172 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name SCNND_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 3 Gene Sequence >1917 bp
ATGGCTGAGCACCGAAGCATGGACGGGAGAATGGAAGCAGCCACACGGGGGGGCTCTCAC
CTCCAGGCTGCAGCCCAGACGCCCCCCAGGCCGGGGCCACCATCAGCACCACCACCACCA
CCCAAGGAGGGGCACCAGGAGGGGCTGGTGGAGCTGCCCGCCTCGTTCCGGGAGCTGCTC
ACCTTCTTCTGCACCAATGCCACCATCCACGGCGCCATCCGCCTGGTCTGCTCCCGCGGG
AACCGCCTCAAGACGACGTCCTGGGGGCTGCTGTCCCTGGGAGCCCTGGTCGCGCTCTGC
TGGCAGCTGGGGCTCCTCTTTGAGCGTCACTGGCACCGCCCGGTCCTCATGGCCGTCTCT
GTGCACTCGGAGCGCAAGCTGCTCCCGCTGGTCACCCTGTGTGACGGGAACCCACGTCGG
CCGAGTCCGGTCCTCCGCCATCTGGAGCTGCTGGACGAGTTTGCCAGGGAGAACATTGAC
TCCCTGTACAACGTCAACCTCAGCAAAGGCAGAGCCGCCCTCTCCGCCACTGTCCCCCGC
CACGAGCCCCCCTTCCACCTGGACCGGGAGATCCGTCTGCAGAGGCTGAGCCACTCGGGC
AGCCGGGTCAGAGTGGGGTTCAGACTGTGCAACAGCACGGGCGGCGACTGCTTTTACCGA
GGCTACACGTCAGGCGTGGCGGCTGTCCAGGACTGGTACCACTTCCACTATGTGGATATC
CTGGCCCTGCTGCCCGCGGCATGGGAGGACAGCCACGGGAGCCAGGACGGCCACTTCGTC
CTCTCCTGCAGTTACGATGGCCTGGACTGCCAGGCCCGACAGTTCCGGACCTTCCACCAC
CCCACCTACGGCAGCTGCTACACGGTCGATGGCGTCTGGACAGCTCAGCGCCCCGGCATC
ACCCACGGAGTCGGCCTGGTCCTCAGGGTTGAGCAGCAGCCTCACCTCCCTCTGCTGTCC
ACGCTGGCCGGCATCAGGGTCATGGTTCACGGCCGTAACCACACGCCCTTCCTGGGGCAC
CACAGCTTCAGCGTCCGGCCAGGGACGGAGGCCACCATCAGCATCCGAGAGGACGAGGTG
CACCGGCTCGGGAGCCCCTACGGCCACTGCACCGCCGGCGGGGAAGGCGTGGAGGTGGAG
CTGCTACACAACACCTCCTACACCAGGCAGGCCTGCCTGGTGTCCTGCTTCCAGCAGCTG
ATGGTGGAGACCTGCTCCTGTGGCTACTACCTCCACCCTCTGCCGGCGGGGGCTGAGTAC
TGCAGCTCTGCCCGGCACCCTGCCTGGGGACACTGCTTCTACCGCCTCTACCAGGACCTG
GAGACCCACCGGCTCCCCTGTACCTCCCGCTGCCCCAGGCCCTGCAGGGAGTCTGCATTC
AAGCTCTCCACTGGGACCTCCAGGTGGCCTTCCGCCAAGTCAGCTGGATGGACTCTGGCC
ACGCTAGGTGAACAGGGGCTGCCGCATCAGAGCCACAGACAGAGGAGCAGCCTGGCCAAA
ATCAACATCGTCTACCAGGAGCTCAACTACCGCTCAGTGGAGGAGGCGCCCGTGTACTCG
GTGCCGCAGCTGCTCTCCGCCATGGGCAGCCTCTACAGCCTGTGGTTTGGGGCCTCCGTC
CTCTCCCTCCTGGAGCTCCTGGAGCTGCTGCTCGATGCTTCTGCCCTCACCCTGGTGCTA
GGCGGCCGCCGGCTCCGCAGGGCGTGGTTCTCCTGGCCCAGAGCCAGCCCTGCCTCAGGG
GCGTCCAGCATCAAGCCAGAGGCCAGTCAGATGCCCCCGCCTGCAGGCGGCACGTCAGAT
GACCCGGAGCCCAGCGGGCCTCATCTCCCACGGGTGATGCTTCCAGGGGTTCTGGCGGGA
GTCTCAGCCGAAGAGAGCTGGGCTGGGCCCCAGCCCCTTGAGACTCTGGACACCTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID SCNN1D Link Image
Target 3 GenAtlas ID SCNN1D Link Image
Target 3 HGNC ID HGNC:10601 Link Image
Target 3 Chromosome Location 1
Target 3 Locus 1p36.3-p36.2
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Waldmann R, Champigny G, Bassilana F, Voilley N, Lazdunski M: Molecular cloning and functional expression of a novel amiloride-sensitive Na+ channel. J Biol Chem. 1995 Nov 17;270(46):27411-4. [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 552
Target 4 Name Amiloride-sensitive sodium channel subunit gamma
Target 4 Synonyms
  1. Epithelial Na(+) channel subunit gamma
  2. Gamma ENaC
  3. Gamma NaCH
  4. Nonvoltage-gated sodium channel 1 subunit gamma
  5. SCNEG
Target 4 Gene Name SCNN1G
Target 4 Protein Sequence >Amiloride-sensitive sodium channel gamma-subunit
MAPGEKIKAKIKKNLPVTGPQAPTIKELMRWYCLNTNTHGCRRIVVSRGRLRRLLWIGFT
LTAVALILWQCALLVFSFYTVSVSIKVHFRKLDFPAVTICNINPYKYSTVRHLLADLEQE
TREALKSLYGFPESRKRREAESWNSVSEGKQPRFSHRIPLLIFDQDEKGKARDFFTGRKR
KVGGSIIHKASNVMHIESKQVVGFQLCSNDTSDCATYTFSSGINAIQEWYKLHYMNIMAQ
VPLEKKINMSYSAEELLVTCFFDGVSCDARNFTLFHHPMHGNCYTFNNRENETILSTSMG
GSEYGLQVILYINEEEYNPFLVSSTGAKVIIHRQDEYPFVEDVGTEIETAMVTSIGMHLT
ESFKLSEPYSQCTEDGSDVPIRNIYNAAYSLQICLHSCFQTKMVEKCGCAQYSQPLPPAA
NYCNYQQHPNWMYCYYQLHRAFVQEELGCQSVCKEACSFKEWTLTTSLAQWPSVVSEKWL
LPVLTWDQGRQVNKKLNKTDLAKLLIFYKDLNQRSIMESPANSIEMLLSNFGGQLGLWMS
CSVVCVIEIIEVFFIDFFSIIARRQWQKAKEWWAWKQAPPCPEAPRSPQGQDNPALDIDD
DLPTFNSALHLPPALGTQVPGTPPPKYNTLRLERAFSNQLTDTQMLDEL
Target 4 Number of Residues 659
Target 4 Molecular Weight 74271
Target 4 Theoretical pI 7.54
Target 4 GO Classification
Function
transporter activity
ion transporter activity
ion channel activity
cation channel activity
sodium channel activity
amiloride-sensitive sodium channel activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
sodium ion transport
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 4 General Function Involved in amiloride-sensitive sodium channel activity
Target 4 Specific Function Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • 56-76
  • 542-562
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 1004273 Link Image
Target 4 UniProtKB/Swiss-Prot ID P51170 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name SCNNG_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Cell membrane
  • apical cell membrane
  • multi- pass membrane protein. Apical membrane of epithelial cel
Target 4 Gene Sequence >1950 bp
ATGGCCCCCGGGGAGAAGATCAAAGCCAAAATCAAGAAGAATCTGCCCGTGACGGGCCCT
CAGGCGCCGACCATTAAAGAGCTGATGCGGTGGTACTGCCTCAACACCAACACCCATGGC
TGTCGCCGCATCGTGGTGTCCCGCGGCCGTCTGCGCCGCCTCCTCTGGATCGGGTTCACA
CTGACTGCCGTGGCCCTCATCCTCTGGCAGTGCGCCCTCCTCGTCTTCTCCTTCTATACT
GTCTCAGTTTCCATCAAAGTCCACTTCCGGAAGCTGGATTTTCCTGCAGTCACCATCTGC
AACATCAACCCCTACAAGTACAGCACCGTTCGCCACCTTCTAGCTGACTTGGAACAGGAG
ACCAGAGAGGCCCTGAAGTCCCTGTATGGCTTTCCAGAGTCCCGGAAGCGCCGAGAGGCG
GAGTCCTGGAACTCCGTCTCAGAGGGAAAGCAGCCTAGATTCTCCCACCGGATTCCGCTG
CTGATCTTTGATCAGGATGAGAAGGGCAAGGCCAGGGACTTCTTCACAGGGAGGAAGCGG
AAAGTCGGCGGTAGCATCATTCACAAGGCTTCAAATGTCATGCACATCGAGTCCAAGCAA
GTGGTGGGATTCCAACTGTGCTCAAATGACACCTCCGACTGTGCCACCTACACCTTCAGC
TCGGGAATCAATGCCATTCAGGAGTGGTATAAGCTACACTACATGAACATCATGGCACAG
GTGCCTCTGGAGAAGAAAATCAACATGAGCTATTCTGCTGAGGAGCTGCTGGTGACCTGC
TTCTTTGATGGAGTGTCCTGTGATGCCAGGAATTTCACGCTTTTCCACCACCCGATGCAT
GGGAATTGCTATACTTTCAACAACAGAGAAAATGAGACCATTCTCAGCACCTCCATGGGG
GGCAGCGAATATGGGCTGCAAGTCATTTTGTACATAAACGAAGAGGAATACAACCCATTC
CTCGTGTCCTCCACTGGAGCTAAGGTGATCATCCATCGGCAGGATGAGTATCCCTCCGTC
GAAGATGTGGGAACAGAGATTGAGACAACAATGGTCACCTCTATAGGAATGCACCTGACA
GAGTCCTTCAAGCTGAGTGAGCCCTCCAGTCAGTGCACGGAGGGCGGGAGTGACGTGCCA
ATCAGGAACATCTACAACGCTGCCTACTCGCTCCAGATCTGCCTTCATTCATGCTTCCAG
ACAAAGATGGTGGAGAAATGTGGGTGTGCCCAGTACAGCCAGCCTCTACCTCCTGCAGCC
AACTACTGCAACTACCAGCAGCACCCCAACTGGATGTATTGTTACTACCAACTGCATCGA
GCCTTTGTCCAGGAAGAGCTGGGCTGCCAGTCTGTGTGCAAGGAAGCCTGCCGCTTTAAA
GAGTGGACACTAACCACAAGCCTGGCACAATGGCCATCTGTGGTTTCGGAGAAGTGGTTG
CTGCCTGTTCTCACTTGGGACCAAGGCCGGCAAGTAAACAAAAAGCTCAACAAGACAGAC
TTGGCCAAACTCTTGATATTCTACAAAGACCTGAACCAGAGATCCATCATGGAGAGCCCA
GCCAACAGTATTGAGATGCTTCTGTCCAACTTCGGCGGTCAGCTGGGCCTGTGGATGAGC
TGCTCTGTTGTCTGCGTCATCGAGATCATCGAGGTCTTCTTCATTGACTTCTTCTCTATC
ATTGCCCGCCGCCAGTGGCAGAAAGCCAAGGAGTGGTGGGCCTGGAAACAGGCTCCCCCA
TGTCCAGAAGCTCCCCGTAGCCCACAGGGCCAGGACAATCCAGCCCTGGATATAGACGAT
GACCTACCCACTTTCAACTCTGCTTTGCACCTGCCTCCAGCCCTAGGAACCCAAGTGCCC
GGCACACCGCCCCCCAAATACAATACCTTGCGCTTGGAGAGGGCCTTTTCCAACCAGCTC
ACAGATACCCAGATGCTGGATGAGCTCTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID SCNN1G Link Image
Target 4 GenAtlas ID SCNN1G Link Image
Target 4 HGNC ID HGNC:10602 Link Image
Target 4 Chromosome Location 16
Target 4 Locus 16p12
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
  2. Arai K, Zachman K, Shibasaki T, Chrousos GP: Polymorphisms of amiloride-sensitive sodium channel subunits in five sporadic cases of pseudohypoaldosteronism: do they have pathologic potential? J Clin Endocrinol Metab. 1999 Jul;84(7):2434-7. [PubMed Link Image]
  3. McDonald FJ, Western AH, McNeil JD, Thomas BC, Olson DR, Snyder PM: Ubiquitin-protein ligase WWP2 binds to and downregulates the epithelial Na(+) channel. Am J Physiol Renal Physiol. 2002 Sep;283(3):F431-6. [PubMed Link Image]
  4. Voilley N, Bassilana F, Mignon C, Merscher S, Mattei MG, Carle GF, Lazdunski M, Barbry P: Cloning, chromosomal localization, and physical linkage of the beta and gamma subunits (SCNN1B and SCNN1G) of the human epithelial amiloride-sensitive sodium channel. Genomics. 1995 Aug 10;28(3):560-5. [PubMed Link Image]
  5. Hansson JH, Nelson-Williams C, Suzuki H, Schild L, Shimkets R, Lu Y, Canessa C, Iwasaki T, Rossier B, Lifton RP: Hypertension caused by a truncated epithelial sodium channel gamma subunit: genetic heterogeneity of Liddle syndrome. Nat Genet. 1995 Sep;11(1):76-82. [PubMed Link Image]
  6. McDonald FJ, Price MP, Snyder PM, Welsh MJ: Cloning and expression of the beta- and gamma-subunits of the human epithelial sodium channel. Am J Physiol. 1995 May;268(5 Pt 1):C1157-63. [PubMed Link Image]
  7. Thomas CP, Doggett NA, Fisher R, Stokes JB: Genomic organization and the 5' flanking region of the gamma subunit of the human amiloride-sensitive epithelial sodium channel. J Biol Chem. 1996 Oct 18;271(42):26062-6. [PubMed Link Image]
  8. Pirozzi G, McConnell SJ, Uveges AJ, Carter JM, Sparks AB, Kay BK, Fowlkes DM: Identification of novel human WW domain-containing proteins by cloning of ligand targets. J Biol Chem. 1997 Jun 6;272(23):14611-6. [PubMed Link Image]
Target 4 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]

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.