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Showing drug card for Trichlormethiazide (DB01021)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:03:50
Primary Accession Number DB01021
Secondary Accession Number
  • APRD00031
Name Trichlormethiazide
Drug Type
  • Approved
  • Small Molecule
Description A thiazide diuretic with properties similar to those of hydrochlorothiazide. (From Martindale, The Extra Pharmacopoeia, 30th ed, p830)
Synonyms Not Available
Brand Names
  1. Achletin
  2. Anatran
  3. Anistadin
  4. Aponorin
  5. Carvacron
  6. Chlopolidine
  7. Cretonin
  8. Diu-Hydrin
  9. Diurazida
  10. Diurese
  11. Diuroral
  12. Esmarin
  13. Eurinol
  14. Fluitran
  15. Flurese
  16. Flutra
  17. Gangesol
  18. Hydrotrichlorothiazide
  19. Intromene
  20. Isestran
  21. Kubacron
  22. Metahydrin
  23. Metatensin
  24. Nakva
  25. Naqua
  26. Naquasone
  27. Salurin
  28. Schebitran
  29. Tachionin
  30. Tolcasone
  31. Trichlorex
  32. Trichlormas
  33. Trichlormetazid
  34. Trichlormethiazid
  35. Trichlormethiazide W/ Reserpine
  36. Trichloromethiadiazide
  37. Trichloromethiazide
  38. Triclordiuride
  39. Triclormetiazide
  40. Triflumen
Brand Mixtures Not Available
Chemical IUPAC Name 6-chloro-3-(dichloromethyl)-1,1-dioxo-3,4-dihydro-2H-benzo[e][1,2,4]thiadiazine-7-sulfonamide
Chemical Formula C8H8Cl3N3O4S2
Chemical Structure Structure
CAS Registry Number 133-67-5
InChI Identifier InChI=1/C8H8Cl3N3O4S2/c9-3-1-4-6(2-5(3)19(12,15)16)20(17,18)14-8(13-4)7(10)11/h1-2,7-8,13-14H,(H2,12,15,16)/f/h12H2
InChI Key LMJSLTNSBFUCMU-GAJRPKRDCL
KEGG Drug D00658 Link Image
KEGG Compound C07767 Link Image
PubChem Compound 5560 Link Image
PubChem Substance 9969 Link Image
ChEBI ID Not Available
PharmGKB ID PA451754 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link Not Available
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 380.6560
Monoisotopic Molecular Weight 378.9022
State Solid
Melting Point Not Available
Experimental Water Solubility 0.8 mg/mL at 25 oC [MERCK (1989)] Source: PhysProp
Predicted Water Solubility 4.15e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 0.7 Source: PhysProp
Predicted LogP 0.86 Calculated using ALOGPS
Experimental LogS -2.68 [ADME Research, USCD]
Predicted LogS -2.96 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 8.6
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 NS(=O)(=O)C1=C(Cl)C=C2N[C@@H](NS(=O)(=O)C2=C1)C(Cl)Cl
Canonical SMILES NS(=O)(=O)C1=C(Cl)C=C2NC(NS(=O)(=O)C2=C1)C(Cl)Cl
Drug Category
  • Antihypertensive Agents
  • Diuretics
  • Sodium Chloride Symporter Inhibitors
ATC Codes
AHFS Codes Not Available
Indication Used in the treatment of oedema (including that associated with heart failure) and hypertension.
Pharmacology Trichloromethiazide is indicated as adjunctive therapy in edema associated with congestive heart failure, hepatic cirrhosis, and corticosteroid and estrogen therapy. Trichloromethiazide has also been found useful in edema due to various forms of renal dysfunction such as nephrotic syndrome, acute glomer-ulonephritis, and chronic renal failure. Trichloromethiazide is also indicated in the management of hypertension either as the sole therapeutic agent or to enhance the effectiveness of other antihypertensive drugs in the more severe forms of hypertension. Like other thiazides, Trichloromethiazide promotes water loss from the body (diuretics). They inhibit Na+/Cl- reabsorption from the distal convoluted tubules in the kidneys. Thiazides also cause loss of potassium and an increase in serum uric acid. Thiazides are often used to treat hypertension, but their hypotensive effects are not necessarily due to their diuretic activity. Thiazides have been shown to prevent hypertension-related morbidity and mortality although the mechanism is not fully understood. Thiazides cause vasodilation by activating calcium-activated potassium channels (large conductance) in vascular smooth muscles and inhibiting various carbonic anhydrases in vascular tissue.
Mechanism of Action Trichlormethiazide appears to block the active reabsorption of chloride and possibly sodium in the ascending loop of Henle, altering electrolyte transfer in the proximal tubule. This results in excretion of sodium, chloride, and water and, hence, diuresis. As a diuretic, Trichloromethiazide inhibits active chloride reabsorption at the early distal tubule via the Na-Cl cotransporter, resulting in an increase in the excretion of sodium, chloride, and water. Thiazides like Trichloromethiazide also inhibit sodium ion transport across the renal tubular epithelium through binding to the thiazide sensitive sodium-chloride transporter. This results in an increase in potassium excretion via the sodium-potassium exchange mechanism. The antihypertensive mechanism of Trichloromethiazide is less well understood although it may be mediated through its action on carbonic anhydrases in the smooth muscle or through its action on the large-conductance calcium-activated potassium (KCa) channel, also found in the smooth muscle.
Absorption Not Available
Toxicity Oral Rat LD50 = 5600 mg/kg, oral Mouse LD50 = 2600 mg/kg
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms Not Available
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions
Drug Interaction
Amifostine Trichlormethiazide may increase the hypotensive effect of Amifostine. At chemotherapeutic doses of Amifostine, Trichlomethiazide should be withheld for 24 hours prior to Amifostine administration. Use caution at lower doses of Amifostine.
Cholestyramine The bile acid sequestrant, Cholestyramine resin, may inhibit the absorption of Trichlormethiazide.
Colesevelam The bile acid sequestrant, Colesevelam, may inhibit the absorption of Trichlormethiazide.
Colestipol The bile acid sequestrant, Colestipol, may inhibit the absorption of Trichlormethiazide.
Dofetilide Trichlormethiazide may increase Dofetilide serum concentrations and increase the QTc-prolonging effect of Dofetilide. Increased risk of ventricular arrhythmias.
Lithium Trichlormethiazide may increase the serum concentration of Lithium by decreasing Lithium excretion. Monitor for changes in the therapeutic/adverse effects of Lithium if Trichlorthiazide is initiated, discontinued or dose changed.
Rituximab Additive antihypertensive effects may occur. Increased risk of hypotension. Consider withholding Trichlormethiazide for 12 hours prior to administration of Rituximab.
Food Interactions Not Available
Pathways
Name SMPDB Link KEGG Link
Trichlormethiazide Pathway SMP00121 Link Image
General References
  1. Drugs.com Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Carbonic anhydrase 1
  2. Carbonic anhydrase 2
  3. Solute carrier family 12 member 1
  4. Carbonic anhydrase 4
  5. Calcium-activated potassium channel subunit alpha 1
  6. Sodium/potassium-transporting ATPase alpha-1 chain
Drug Target 1 [top]
Target 1 ID 295
Target 1 Name Carbonic anhydrase 1
Target 1 Synonyms
  1. CA-I
  2. Carbonate dehydratase I
  3. Carbonic anhydrase I
  4. EC 4.2.1.1
Target 1 Gene Name CA1
Target 1 Protein Sequence >Carbonic anhydrase 1 
ASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEII
NVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHV
AHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFD
PSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVP
MQHNNRPTQPLKGRTVRASF
Target 1 Number of Residues 264
Target 1 Molecular Weight 28739
Target 1 Theoretical pI 7.14
Target 1 GO Classification
Function
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
carbonate dehydratase activity
Process
physiological process
metabolism
cellular metabolism
one-carbon compound metabolism
Component
Not Available
Target 1 General Function Inorganic ion transport and metabolism
Target 1 Specific Function Reversible hydration of carbon dioxide
Target 1 Pathways
Name SMPDB Link KEGG Link
Nitrogen metabolism map00910 Link Image
Target 1 Reactions
  • H2CO3 = CO2 + H2O
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 29600 Link Image
Target 1 UniProtKB/Swiss-Prot ID P00915 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name CAH1_HUMAN Link Image
Target 1 PDB ID 1CZM Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cytoplasm
Target 1 Gene Sequence >786 bp 
ATGGCAAGTCCAGACTGGGGATATGATGACAAAAATGGTCCTGAACAATGGAGCAAGCTG
TATCCCATTGCCAATGGAAATAACCAATCCCCTGTTGATATTAAAACCAGTGAAACCAAA
CATGACACCTCTCTGAAACCTATTAGTGTCTCCTACAACCCAGCCACAGCCAAAGAAATT
ATCAATGTGGGGCATTCTTTCCATGTAAATTTTGAGGACAACGATAACCGATCAGTGCTG
AAAGGTGGTCCTTTCTCTGACAGCTACAGGCTCTTTCAGTTTCATTTTCACTGGGGCAGT
ACAAATGAGCATGGTTCAGAACATACAGTGGATGGAGTCAAATATTCTGCCGAGCTTCAC
GTAGCTCACTGGAATTCTGCAAAGTACTCCAGCCTTGCTGAAGCTGCCTCAAAGGCTGAT
GGTTTGGCAGTTATTGGTGTTTTGATGAAGGTTGGTGAGGCCAACCCAAAGCTGCAGAAA
GTACTTGATGCCCTCCAAGCAATTAAAACCAAGGGCAAACGAGCCCCATTCACAAATTTT
GACCCCTCTACTCTCCTTCCTTCATCCCTGGATTTCTGGACCTACCCTGGCTCTCTGACT
CATCCTCCTCTTTATGAGAGTGTAACTTGGATCATCTGTAAGGAGAGCATCAGTGTCAGC
TCAGAGCAGCTGGCACAATTCCGCAGCCTTCTATCAAATGTTGAAGGTGATAACGCTGTC
CCCATGCAGCACAACAACCGCCCAACCCAACCTCTGAAGGGCAGAACAGTGAGAGCTTCA
TTTTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID CA1 Link Image
Target 1 GenAtlas ID CA1 Link Image
Target 1 HGNC ID HGNC:1368 Link Image
Target 1 Chromosome Location 8
Target 1 Locus 8q13-q22.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Lowe N, Brady HJ, Barlow JH, Sowden JC, Edwards M, Butterworth PH: Structure and methylation patterns of the gene encoding human carbonic anhydrase I. Gene. 1990 Sep 14;93(2):277-83. [PubMed Link Image]
  2. Barlow JH, Lowe N, Edwards YH, Butterworth PH: Human carbonic anhydrase I cDNA. Nucleic Acids Res. 1987 Mar 11;15(5):2386. [PubMed Link Image]
  3. Lin KT, Deutsch HF: Human carbonic anhydrases. XII. The complete primary structure of the C isozyme. J Biol Chem. 1974 Apr 25;249(8):2329-37. [PubMed Link Image]
  4. Giraud N, Marriq C, Laurent-Tabusse G: [Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260)] Biochimie. 1974;56(8):1031-43. [PubMed Link Image]
  5. Andersson B, Nyman PO, Strid L: Amino acid sequence of human erythrocyte carbonic anhydrase B. Biochem Biophys Res Commun. 1972 Aug 7;48(3):670-7. [PubMed Link Image]
  6. Lin KT, Deutsch HF: Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B. J Biol Chem. 1973 Mar 25;248(6):1885-93. [PubMed Link Image]
  7. Omoto K, Ueda S, Goriki K, Takahashi N, Misawa S, Pagaran IG: Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam. Am J Hum Genet. 1981 Jan;33(1):105-11. [PubMed Link Image]
  8. Chegwidden WR, Wagner LE, Venta PJ, Bergenhem NC, Yu YS, Tashian RE: Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I. Hum Mutat. 1994;4(4):294-6. [PubMed Link Image]
  9. Kannan KK, Notstrand B, Fridborg K, Lovgren S, Ohlsson A, Petef M: Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution. Proc Natl Acad Sci U S A. 1975 Jan;72(1):51-5. [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]
Drug Target 2 [top]
Target 2 ID 357
Target 2 Name Carbonic anhydrase 2
Target 2 Synonyms
  1. CA-II
  2. Carbonate dehydratase II
  3. Carbonic anhydrase C
  4. Carbonic anhydrase II
  5. EC 4.2.1.1
Target 2 Gene Name CA2
Target 2 Protein Sequence >Carbonic anhydrase 2 
SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILN
NGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLV
HWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPR
GLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV
DNWRPAQPLKNRQIKASFK
Target 2 Number of Residues 263
Target 2 Molecular Weight 29115
Target 2 Theoretical pI 7.47
Target 2 GO Classification
Function
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
carbonate dehydratase activity
Process
physiological process
metabolism
cellular metabolism
one-carbon compound metabolism
Component
Not Available
Target 2 General Function Inorganic ion transport and metabolism
Target 2 Specific Function Reversible hydration of carbon dioxide
Target 2 Pathways
Name SMPDB Link KEGG Link
Nitrogen metabolism map00910 Link Image
Target 2 Reactions
  • H2CO3 = CO2 + H2O
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 179780 Link Image
Target 2 UniProtKB/Swiss-Prot ID P00918 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CAH2_HUMAN Link Image
Target 2 PDB ID 1T9N Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasm
Target 2 Gene Sequence >783 bp 
ATGTCCCATCACTGGGGGTACGGCAAACACAACGGACCTGAGCACTGGCATAAGGACTTC
CCCATTGCCAAGGGAGAGCGCCAGTCCCCTGTTGACATCGACACTCATACAGCCAAGTAT
GACCCTTCCCTGAAGCCCCTGTCTGTTTCCTATGATCAAGCAACTTCCCTGAGGATCCTC
AACAATGGTCATGCTTTCAACGTGGAGTTTGATGACTCTCAGGACAAAGCAGTGCTCAAG
GGAGGACCCCTGGATGGCACTTACAGATTGATTCAGTTTCACTTTCACTGGGGTTCACTT
GATGGACAAGGTTCAGAGCATACTGTGGATAAAAAGAAATATGCTGCAGAACTTCACTTG
GTTCACTGGAACACCAAATATGGGGATTTTGGGAAAGCTGTGCAGCAACCTGATGGACTG
GCCGTTCTAGGTATTTTTTTGAAGGTTGGCAGCGCTAAACCGGGCCTTCAGAAAGTTGTT
GATGTGCTGGATTCCATTAAAACAAAGGGCAAGAGTGCTGACTTCACTAACTTCGATCCT
CGTGGCCTCCTTCCTGAATCCTTGGATTACTGGACCTACCCAGGCTCACTGACCACCCCT
CCTCTTCTGGAATGTGTGACCTGGATTGTGCTCAAGGAACCCATCAGCGTCAGCAGCGAG
CAGGTGTTGAAATTCCGTAAACTTAACTTCAATGGGGAGGGTGAACCCGAAGAACTGATG
GTGGACAACTGGCGCCCAGCTCAGCCACTGAAGAACAGGCAAATCAAAGCTTCCTTCAAA
TAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID CA2 Link Image
Target 2 GenAtlas ID CA2 Link Image
Target 2 HGNC ID HGNC:1373 Link Image
Target 2 Chromosome Location 8
Target 2 Locus 8q22
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Cox JD, Hunt JA, Compher KM, Fierke CA, Christianson DW: Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II. Biochemistry. 2000 Nov 14;39(45):13687-94. [PubMed Link Image]
  2. Roth DE, Venta PJ, Tashian RE, Sly WS: Molecular basis of human carbonic anhydrase II deficiency. Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1804-8. [PubMed Link Image]
  3. Venta PJ, Welty RJ, Johnson TM, Sly WS, Tashian RE: Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His----Tyr): complete structure of the normal human CA II gene. Am J Hum Genet. 1991 Nov;49(5):1082-90. [PubMed Link Image]
  4. Venta PJ, Montgomery JC, Hewett-Emmett D, Tashian RE: Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements. Biochim Biophys Acta. 1985 Dec 18;826(4):195-201. [PubMed Link Image]
  5. Montgomery JC, Venta PJ, Tashian RE, Hewett-Emmett D: Nucleotide sequence of human liver carbonic anhydrase II cDNA. Nucleic Acids Res. 1987 Jun 11;15(11):4687. [PubMed Link Image]
  6. Murakami H, Marelich GP, Grubb JH, Kyle JW, Sly WS: Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II. Genomics. 1987 Oct;1(2):159-66. [PubMed Link Image]
  7. Eriksson AE, Jones TA, Liljas A: Refined structure of human carbonic anhydrase II at 2.0 A resolution. Proteins. 1988;4(4):274-82. [PubMed Link Image]
  8. Eriksson AE, Kylsten PM, Jones TA, Liljas A: Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH. Proteins. 1988;4(4):283-93. [PubMed Link Image]
  9. Lin KT, Deutsch HF: Human carbonic anhydrases. XII. The complete primary structure of the C isozyme. J Biol Chem. 1974 Apr 25;249(8):2329-37. [PubMed Link Image]
  10. Liljas A, Kannan KK, Bergsten PC, Waara I, Fridborg K, Strandberg B, Carlbom U, Jarup L, Lovgren S, Petef M: Crystal structure of human carbonic anhydrase C. Nat New Biol. 1972 Feb 2;235(57):131-7. [PubMed Link Image]
  11. 6407977 Jones GL, Shaw DC: A chemical and enzymological comparison of the common major human erythrocyte carbonic anhydrase II, its minor component, and a new genetic variant, CA II Melbourne (237 Pro leads to His). Hum Genet. 1983;63(4):392-9.
  12. 6817747 Jones GL, Sofro AS, Shaw DC: Chemical and enzymological characterization of an Indonesian variant of human erythrocyte carbonic anhydrase II, CAII Jogjakarta (17 Lys leads to Glu). Biochem Genet. 1982 Oct;20(9-10):979-1000.
  13. 823150 Henderson LE, Henriksson D, Nyman PO: Primary structure of human carbonic anhydrase C. J Biol Chem. 1976 Sep 25;251(18):5457-63.
  14. 8834238 Soda H, Yukizane S, Yoshida I, Koga Y, Aramaki S, Kato H: A point mutation in exon 3 (His 107-->Tyr) in two unrelated Japanese patients with carbonic anhydrase II deficiency with central nervous system involvement. Hum Genet. 1996 Apr;97(4):435-7.
  15. 9143915 Hu PY, Lim EJ, Ciccolella J, Strisciuglio P, Sly WS: Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis. Hum Mutat. 1997;9(5):383-7.
  16. 9541386 Stams T, Chen Y, Boriack-Sjodin PA, Hurt JD, Liao J, May JA, Dean T, Laipis P, Silverman DN, Christianson DW: Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: molecular basis of isozyme-drug discrimination. Protein Sci. 1998 Mar;7(3):556-63.
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 558
Target 3 Name Solute carrier family 12 member 1
Target 3 Synonyms
  1. Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 2
  2. Kidney-specific Na-K-Cl symporter
Target 3 Gene Name SLC12A1
Target 3 Protein Sequence >Solute carrier family 12 member 1 
MSLNNSSNVFLDSVPSNTNRFQVSVINENHESSAAADDNTDPPHYEETSFGDEAQKRLRI
SFRPGNQECYDNFLHSGETAKTDASFHAYDSHTNTYYLQTFGHNTMDAVPKIEYYRNTGS
ISGPKVNRPSLLEIHEQLAKNVAVTPSSADRVANGDGIPGDEQAENKEDDQAGVVKFGWV
KGVLVRCMLNIWGVMLFIRLSWIVGEAGIGLGVIIIGLSTIVTTITGMSTSAIATNGVVR
GGGAYYLISRSLGPEFGGSIGLIFAFANAVAVAMYVVGFAETVVDLLKESDSMMVDPTND
IRIIGSITVVILLGISVAGMEWEAKAQVILLVILLIAIANFFIGTVIPSNNEKKSRGFFN
YQASIFAENFGPRFTKGEGFFSVFAIFFPAATGILAGANISGDLEDPQDAIPRGTMLAIF
ITTVAYLGVAICVGACVVRDATGNMNDTIISGMNCNGSAACGLGYDFSRCRHEPCQYGLM
NNFQVMSMVSGFGPLITAGIFSATLSSALASLVSAPKVFQALCKDNIYKALQFFAKGYGK
NNEPLRGYILTFLIAMAFILIAELNTIAPIISNFFLASYALINFSCFHASYAKSPGWRPA
YGIYNMWVSLFGAVLCCAVMFVINWWAAVITYVIEFFLYVYVTCKKPDVNWGSSTQALSY
VSALDNALELTTVEDHVKNFRPQCIVLTGGPMTRPALLDITHAFTKNSGLCICCEVFVGP
RKLCVKEMNSGMAKKQAWLIKNKIKAFYAAVAADCFRDGVRSLLQASGLGRMKPNTLVIG
YKKNWRKAPLTEIENYVGIIHDAFDFEIGVVIVRISQGFDISQVLQVQEELERLEQERLA
LEATIKDNECEEESGGIRGLFKKAGKLNITKTTPKKDGSINTSQSMHVGEFNQKLVEAST
QFKKKQEKGTIDVWWLFDDGGLTLLIPYILTLRKKWKDCKLRIYVGGKINRIEEEKIAMA
SLLSKFRIKFADIHIIGDINIRPNKESWKVFEEMIEPYRLHESCKDLTTAEKLKRETPWK
ITDAELEAVKEKSYRQVRLNELLQEHSRAANLIVLSLPVARKGSISDLLYMAWLEILTKN
LPPVLLVRGNHKNVLTFYS
Target 3 Number of Residues 1117
Target 3 Molecular Weight 121342
Target 3 Theoretical pI 7.42
Target 3 GO Classification
Function
ion transporter activity
cation transporter activity
anion:cation symporter activity
cation:chloride symporter activity
transporter activity
Process
anion transport
inorganic anion transport
chloride transport
cation transport
monovalent inorganic cation transport
sodium ion transport
physiological process
cellular physiological process
transport
ion transport
Component
intrinsic to membrane
integral to membrane
cell
membrane
Target 3 General Function Involved in sodium/potassium transporter activity
Target 3 Specific Function Electrically silent transporter system. Mediates sodium and chloride reabsorption. Plays a vital role in the regulation of ionic balance and cell volume
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • 178-198
  • 202-222
  • 260-280
  • 303-323
  • 328-348
  • 380-400
  • 418-438
  • 485-505
  • 551-571
  • 572-592
  • 610-630
  • 793-813
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 1373425 Link Image
Target 3 UniProtKB/Swiss-Prot ID Q13621 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name S12A1_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 3 Gene Sequence >3300 bp 
ATGTCACTGAACAACTCTTCCAATGTATTTCTGGATTCAGTGCCCAGTAATACCAATCGC
TTTCAAGTTAGTGTCATAAATGAGAACCATGAGAGCAGTGCAGCTGCAGATGACAATACT
GACCCACCACATTATGAAGAAACCTCTTTTGGGGATGAAGCTCAGAAAAGACTCAGAATC
AGCTTTAGGCCTGGGAATCAGGAGTGCTATGACAATTTCCTCCACAGTGGAGAAACTGCT
AAAACAGATGCCAGTTTTCACGCTTATGATTCTCACACAAACACATACTATCTACAAACT
TTTGGCCACAACACCATGGATGCCGTTCCCAAGATAGAGTACTATCGTAACACCGGCAGC
ATCAGTGGGCCCAAGGTCAACCGACCCAGCCTGCTTGAGATTCACGAGCAACTCGCAAAG
AATGTGGCAGTCACCCCAAGTTCAGCTGACAGAGTTGCTAACGGTGATGGGATACCTGGA
GATGAACAAGCTGAAAATAAGGAAGATGATCAAGCTGGTGTTGTGAAGTTTGGATGGGTG
AAAGGTGTGCTGGTAAGATGCATGCTGAACATCTGGGGAGTCATGCTCTTCATTCGCCTC
TCCTGGATTGTTGGAGAAGCTGGAATTGGTCTTGGAGTTATCATCATTGGCCTATCCACC
ATAGTAACGACAATCACAGGTATGTCCACGTCTGCTATTGCCACGAACGGAGTTGTTAGA
GGAGGTGGGGCCTACTATCTTATTTCCAGAAGTTTAGGGCCCGAGTTCGGTGGGTCAATA
GGCCTGATCTTTGCTTTTGCTAATGCAGTGGCTGTTGCTATGTATGTGGTGGGATTCGCT
GAAACTGTAGTAGATCTACTTAAGGAGAGTGATTCGATGATGGTGGATCCAACCAATGAC
ATCCGGATTATAGGCTCCATCACAGTGGTGATTCTTCTAGGAATTTCAGTAGCTGGAATG
GAATGGGAGGCAAAGGCCCAAGTCATTCTTCTGGTCATTCTTCTAATTGCTATTGCAAAC
TTCTTCATTGGAACTGTCATTCCATCCAACAATGAGAAAAAGTCCAGAGGTTTCTTTAAT
TACCAAGCATCAATATTTGCAGAAAACTTTGGGCCACGCTTCACAAAGGGTGAAGGCTTC
TTCTCTGTCTTTGCCATTTTTTTCCCAGCAGCTACTGGGATTCTTGCTGGTGCCAATATC
TCAGGAGATTTGGAGGATCCCCAAGATGCCATCCCCAGAGGAACCATGCTGGCCATTTTC
ATCACCACTGTTGCCTACTTAGGGGTTGCAATTTGTGTAGGGGCCTGTGTGGTCCGAGAT
GCCACCGGGAACATGAATGACACCATCATTTCTGGGATGAACTGCAATGGTTCAGCAGCA
TGTGGGTTGGGCTATGACTTCTCAAGATGTCGACATGAACCATGTCAGTACGGGCTGATG
AACAATTTCCAGGTCATGAGCATGGTATCAGGGTTCGGCCCCCTCATCACTGCGGGAATC
TTTTCTGCAACACTCTCCTCCGCCCTGGCCTCCCTTGTCAGCGCACCCAAAGTGTTCCAG
GCTCTGTGCAAGGACAACATCTACAAAGCCCTGCAGTTTTTTGCAAAGGGATATGGGAAA
AACAATGAACCCCTGAGAGGATATATTCTCACTTTTCTTATAGCCATGGCATTTATTCTT
ATTGCGGAACTGAACACCATTGCTCCCATCATCTCCAACTTTTTCCTGGCCTCATATGCA
CTTATTAATTTCTCCTGCTTCCATGCCTCTTATGCCAAATCTCCAGGATGGAGACCTGCG
TATGGAATTTACAACATGTGGGTATCTCTTTTTGGAGCTGTTTTGTGCTGTGCAGTCATG
TTTGTCATCAACTGGTGGGCAGCTGTCATCACCTATGTCATTGAATTCTTCCTTTACGTC
TATGTGACTTGTAAGAAGCCAGATGTGAACTGGGGCTCCTCCACACAGGCTCTTTCCTAC
GTGAGTGCTTTAGACAATGCTCTGGAATTAACCACAGTGGAAGACCACGTAAAAAACTTC
AGGCCCCAGTGCATTGTCTTAACAGGGGGACCCATGACAAGACCTGCTCTCCTGGACATA
ACTCACGCCTTTACCAAGAACAGTGGCCTTTGCATCTGCTGTGAAGTCTTTGTGGGACCG
CGCAAACTGTGTGTTAAGGAGATGAACAGTGGCATGGCGAAAAAACAGGCCTGGCTTATA
AAGAACAAAATCAAGGCTTTTTATGCTGCAGTGGCGGCAGACTGTTTCAGGGATGGTGTC
CGAAGTCTTCTTCAGGCCTCAGGCTTAGGAAGAATGAAACCAAACACTCTGGTGATTGGA
TATAAGAAAAACTGGAGGAAAGCTCCCTTGACAGAGATTGAGAACTACGTGGGAATCATA
CATGATGCATTTGATTTTGAGATTGGCGTGGTTATAGTCAGAATCAGCCAAGGATTTGAC
ATCTCTCAGGTTCTTCAGGTGCAAGAGGAATTAGAGAGATTAGAACAGGAGAGACTAGCA
TTGGAAGCGACTATCAAAGATAATGAGTGTGAAGAGGAAAGTGGAGGCATCCGAGGCTTG
TTTAAAAAAGCTGGCAAGTTGAACATTACTAAGACAACGCCTAAAAAAGATGGCAGCATT
AACACAAGCCAGTCGATGCATGTGGGAGAGTTCAACCAGAAACTGGTGGAAGCCAGCACT
CAATTTAAAAAGAAACAAGAAAAAGGCACAATTGATGTTTGGTGGTTGTTTGATGATGGA
GGGTTAACACTTCTTATCCCCTATATCTTAACTCTCAGAAAAAAATGGAAAGACTGTAAA
TTAAGAATCTATGTGGGAGGGAAGATCAACCGCATTGAAGAAGAAAAAATTGCAATGGCT
TCCCTTCTGAGCAAATTTAGGATAAAATTTGCAGACATCCATATCATCGGTGACATCAAC
ATTAGGCCAAACAAAGAGAGCTGGAAAGTCTTTGAAGAGATGATTGAACCATATCGTCTC
CATGAAAGCTGCAAAGATTTAACAACTGCTGAGAAATTAAAAAGAGAAACTCCGTGGAAA
ATTACAGATGCAGAACTGGAAGCAGTCAAGGAAAAGAGTTACCGCCAAGTTCGACTGAAT
GAACTCTTACAGGAGCACTCCAGAGCTGCTAATCTCATTGTCCTGAGCCTTCCCGTGGCA
AGAAAGGGATCCATATCGGATTTGTTGTATATGGCTTGGTTGGAAATCCTCACAAAGAAC
CTCCCACCTGTCTTACTAGTTAGAGGAAATCACAAAAATGTCTTGACATTTTACTCTTAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID SLC12A1 Link Image
Target 3 GenAtlas ID SLC12A1 Link Image
Target 3 HGNC ID HGNC:10910 Link Image
Target 3 Chromosome Location 15
Target 3 Locus 15q15-q21.1
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Simon DB, Karet FE, Hamdan JM, DiPietro A, Sanjad SA, Lifton RP: Bartter's syndrome, hypokalaemic alkalosis with hypercalciuria, is caused by mutations in the Na-K-2Cl cotransporter NKCC2. Nat Genet. 1996 Jun;13(2):183-8. [PubMed Link Image]
Target 3 Drug References
  1. Li J, Wang DH: Function and regulation of epithelial sodium transporters in the kidney of a salt-sensitive hypertensive rat model. J Hypertens. 2007 May;25(5):1065-72. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 592
Target 4 Name Carbonic anhydrase 4
Target 4 Synonyms
  1. CA-IV
  2. Carbonate dehydratase IV
  3. Carbonic anhydrase 4 precursor
  4. Carbonic anhydrase IV
  5. EC 4.2.1.1
Target 4 Gene Name CA4
Target 4 Protein Sequence >Carbonic anhydrase 4 precursor 
MRMLLALLALSAARPSASAESHWCYEVQAESSNYPCLVPVKWGGNCQKDRQSPINIVTTK
AKVDKKLGRFFFSGYDKKQTWTVQNNGHSVMMLLENKASISGGGLPAPYQAKQLHLHWSD
LPYKGSEHSLDGEHFAMEMHIVHEKEKGTSRNVKEAQDPEDEIAVLAFLVEAGTQVNEGF
QPLVEALSNIPKPEMSTTMAESSLLDLLPKEEKLRHYFRYLGSLTTPTCDEKVVWTVFRE
PIQLHREQILAFSQKLYYDKEQTVSMKDNVRPLQQLGQRTVIKSGAPGRPLPWALPALLG
PMLACLLAGFLR
Target 4 Number of Residues 317
Target 4 Molecular Weight 35033
Target 4 Theoretical pI 7.94
Target 4 GO Classification
Function
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
carbonate dehydratase activity
Process
physiological process
metabolism
cellular metabolism
one-carbon compound metabolism
Component
Not Available
Target 4 General Function Inorganic ion transport and metabolism
Target 4 Specific Function Reversible hydration of carbon dioxide. May stimulate the sodium/bicarbonate transporter activity of SLC4A4
Target 4 Pathways
Name SMPDB Link KEGG Link
Nitrogen metabolism map00910 Link Image
Target 4 Reactions
  • H2CO3 = CO2 + H2O
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-18
Target 4 Transmembrane Regions
  • 292-311
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 179791 Link Image
Target 4 UniProtKB/Swiss-Prot ID P22748 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name CAH4_HUMAN Link Image
Target 4 PDB ID 1ZNC Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Cell membrane
  • GPI-anchor
  • lipid-anchor
Target 4 Gene Sequence >939 bp 
ATGCGGATGCTGCTGGCGCTCCTGGCCCTCTCCGCGGCGCGGCCATCGGCCAGTGCAGAG
TCACACTGGTGCTACGAGGTTCAAGCCGAGTCCTCCAACTACCCCTGCTTGGTGCCAGTC
AAGTGGGGTGGAAACTGCCAGAAGGACCGCCAGTCCCCCATCAACATCGTCACCACCAAG
GCAAAGGTGGACAAAAAACTGGGACGCTTCTTCTTCTCTGGCTACGATAAGAAGCAAACG
TGGACTGTCCAAAATAACGGGCACTCAGTGATGATGTTGCTGGAGAACAAGGCCAGCATT
TCTGGAGGAGGACTGCCTGCCCCATACCAGGCCAAACAGTTGCACCTGCACTGGTCCGAC
TTGCCATATAAGGGCTCGGAGCACAGCCTCGATGGGGAGCACTTTGCCATGGAGATGCAC
ATAGTACATGAGAAAGAGAAGGGGACATCGAGGAATGTGAAAGAGGCCCAGGACCCTGAA
GACGAAATTGCGGTGCTGGCCTTTCTGGTGGAGGCTGGAACCCAGGTGAACGAGGGCTTC
CAGCCACTGGTGGAGGCACTGTCTAATATCCCCAAACCTGAGATGAGCACTACGATGGCA
GAGAGCAGCCTGTTGGACCTGCTCCCCAAGGAGGAGAAACTGAGGCACTACTTCCGCTAC
CTGGGCTCACTCACCACACCGACCTGCGATGAGAAGGTCGTCTGGACTGTGTTCCGGGAG
CCCATTCAGCTTCACAGAGAACAGATCCTGGCATTCTCTCAGAAGCTGTACTACGACAAG
GAACAGACAGTGAGCATGAAGGACAATGTCAGGCCCCTGCAGCAGCTGGGGCAGCGCACG
GTGATAAAGTCCGGGGCCCCGGGTCGGCCGCTGCCCTGGGCCCTGCCTGCCCTGCTGGGC
CCCATGCTGGCCTGCCTGCTGGCCGGCTTCCTGCGATGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID CA4 Link Image
Target 4 GenAtlas ID CA4 Link Image
Target 4 HGNC ID HGNC:1375 Link Image
Target 4 Chromosome Location 17
Target 4 Locus 17q23
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Okuyama T, Sato S, Zhu XL, Waheed A, Sly WS: Human carbonic anhydrase IV: cDNA cloning, sequence comparison, and expression in COS cell membranes. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1315-9. [PubMed Link Image]
  2. Zhu XL, Sly WS: Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney. J Biol Chem. 1990 May 25;265(15):8795-801. [PubMed Link Image]
  3. Okuyama T, Waheed A, Kusumoto W, Zhu XL, Sly WS: Carbonic anhydrase IV: role of removal of C-terminal domain in glycosylphosphatidylinositol anchoring and realization of enzyme activity. Arch Biochem Biophys. 1995 Jul 10;320(2):315-22. [PubMed Link Image]
  4. Okuyama T, Batanian JR, Sly WS: Genomic organization and localization of gene for human carbonic anhydrase IV to chromosome 17q. Genomics. 1993 Jun;16(3):678-84. [PubMed Link Image]
  5. Waheed A, Okuyama T, Heyduk T, Sly WS: Carbonic anhydrase IV: purification of a secretory form of the recombinant human enzyme and identification of the positions and importance of its disulfide bonds. Arch Biochem Biophys. 1996 Sep 15;333(2):432-8. [PubMed Link Image]
  6. Stams T, Nair SK, Okuyama T, Waheed A, Sly WS, Christianson DW: Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution. Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13589-94. [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]
Drug Target 5 [top]
Target 5 ID 610
Target 5 Name Calcium-activated potassium channel subunit alpha 1
Target 5 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 5 Gene Name KCNMA1
Target 5 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 5 Number of Residues 1256
Target 5 Molecular Weight 137561
Target 5 Theoretical pI 7.07
Target 5 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 5 General Function Inorganic ion transport and metabolism
Target 5 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 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • 87-107
  • 179-199
  • 215-235
  • 240-260
  • 265-285
  • 301-321
  • 368-388
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 537439 Link Image
Target 5 UniProtKB/Swiss-Prot ID Q12791 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name KCMA1_HUMAN Link Image
Target 5 PDB ID Not Available
Target 5 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 5 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 5 GenBank Gene ID
Target 5 GeneCard ID KCNMA1 Link Image
Target 5 GenAtlas ID KCNMA1 Link Image
Target 5 HGNC ID HGNC:6284 Link Image
Target 5 Chromosome Location 10
Target 5 Locus 10q22.3
Target 5 SNPs SNPJam Report Link Image
Target 5 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 5 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 6 [top]
Target 6 ID 806
Target 6 Name Sodium/potassium-transporting ATPase alpha-1 chain
Target 6 Synonyms
  1. EC 3.6.3.9
  2. Na(+)/K(+) ATPase alpha-1 subunit
  3. Sodium pump subunit alpha 1
  4. Sodium/potassium-transporting ATPase alpha-1 chain precursor
Target 6 Gene Name ATP1A1
Target 6 Protein Sequence >Sodium/potassium-transporting ATPase alpha-1 chain precursor 
MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLS
RGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAA
TEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSI
NAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETR
NIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAV
FLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKN
LEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLA
LSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEI
PFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQN
AYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVP
DAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDA
KACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVN
DSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTL
TSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPK
TDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVED
SYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFE
ETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKE
TYY
Target 6 Number of Residues 1040
Target 6 Molecular Weight 112897
Target 6 Theoretical pI 5.15
Target 6 GO Classification
Function
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
catalytic activity
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
monovalent inorganic cation transporter activity
transporter activity
ion transporter activity
cation transporter activity
ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
Process
metabolism
monovalent inorganic cation transport
physiological process
cellular physiological process
transport
ion transport
cation transport
Component
intrinsic to membrane
integral to membrane
cell
membrane
Target 6 General Function Inorganic ion transport and metabolism
Target 6 Specific Function This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients
Target 6 Pathways Not Available
Target 6 Reactions
  • ATP + H2O + Na+in + K+out = ADP + phosphate + Na+out + K+in
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • 88-108
  • 132-152
  • 289-308
  • 321-338
  • 773-792
  • 803-823
  • 844-866
  • 919-938
  • 952-970
  • 986-1006
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 219942 Link Image
Target 6 UniProtKB/Swiss-Prot ID P05023 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name AT1A1_HUMAN Link Image
Target 6 PDB ID 1MO8 Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 6 Gene Sequence >3072 bp 
ATGGGGAAGGGGGTTGGACGTGATAAGTATGAGCCTGCAGCTGTTTCAGAACAAGGTGAT
AAAAAGGGCAAAAAGGGCAAAAAAGACAGGGACATGGATGAACTGAAGAAAGAAGTTTCT
ATGGATGATCATAAACTTAGCCTTGATGAACTTCATCGTAAATATGGAACAGACTTGAGC
CGGGGATTAACATCTGCTCGTGCAGCTGAGATCCTGGCGCGAGATGGTCCCAACGCCCTC
ACTCCCCCTCCCACTACTCCTGAATGGATCAAGTTTTGTCGGCAGCTCTTTGGGGGGTTC
TCAATGTTACTGTGGATTGGAGCGATTCTTTGTTTCTTGGCTTATAGCATCCAAGCTGCT
ACAGAAGAGGAACCTCAAAACGATAATCTGTACCTGGGTGTGGTGCTATCAGCCGTTGTA
ATCATAACTGGTTGCTTCTCCTACTATCAAGAAGCTAAAAGTTCAAAGATCATGGAATCC
TTCAAAAACATGGTCCCTCAGCAAGCCCTTGTGATTCGAAATGGTGAGAAAATGAGCATA
AATGCGGAGGAAGTTGTGGTTGGGGATCTGGTGGAAGTAAAAGGAGGAGACCGAATTCCT
GCTGACCTCAGAATCATATCTGCAAATGGCTGCAAGGTGGATAACTCCTCGCTCACTGGT
GAATCAGAACCCCAGACTAGGTCTCCAGATTTCACAAATGAAAACCCCCTGGAGACGAGG
AACATTGCCTTCTTTTCAACAAATTGTGTTGAAGGCACCGCACGTGGTATTGTTGTCTAC
ACTGGGGATCGCACTGTGATGGGAAGAATTGCCACACTTGCTTCTGGGCTGGAAGGAGGC
CAGACCCCCATTGCTGCAGAAATTGAACATTTTATCCACATCATCACGGGTGTGGCTGTG
TTCCTGGGTGTGTCTTTCTTCATCCTTTCTCTCATCCTTGAGTACACCTGGCTTGAGGCT
GTCATCTTCCTCATCGGTATCATCGTAGCCAATGTGCCGGAAGGTTTGCTGGCCACTGTC
ACGGTCTGTCTGACACTTACTGCCAAACGCATGGCAAGGAAAAACTGCTTAGTGAAGAAC
TTAGAAGCTGTGGAGACCTTGGGGTCCACGTCCACCATCTGCTCTGATAAAACTGGAACT
CTGACTCAGAACCGGATGACAGTGGCCCACATGTGGTTTGACAATCAAATCCATGAAGCT
GATACGACAGAGAATCAGAGTGGTGTCTCTTTTGACAAGACTTCAGCTACCTGGCTTGCT
CTGTCCAGAATTGCAGGTCTTTGTAACAGGGCAGTGTTTCAGGCTAACCAGGAAAACCTA
CCTATTCTTAAGCGGGCAGTTGCAGGAGATGCCTCTGAGTCAGCACTCTTAAAGTGCATA
GAGCTGTGCTGTGGTTCCGTGAAGGAGATGAGAGAAAGATACGCCAAAATCGTCGAGATA
CCCTTCAACTCCACCAACAAGTACCAGTTGTCTATTCATAAGAACCCCAACACATCGGAG
CCCCAACACCTGTTGGTGATGAAGGGCGCCCCAGAAAGGATCCTAGACCGTTGCAGCTCT
ATCCTCCTCCACGGCAAGGAGCAGCCCCTGGATGAGGAGCTGAAAGACGCCTTTCAGAAC
GCCTATTTGGAGCTGGGGGGCCTCGGAGAACGAGTCCTAGGTTTCTGCCACCTCTTTCTG
CCAGATGAACAGTTTCCTGAAGGGTTCCAGTTTGACACTGACGATGTGAATTTCCCTATC
GATAATCTGTGCTTTGTTGGGCTCATCTCCATGATTGACCCTCCACGGGCGGCCGTTCCT
GATGCCGTGGGCAAATGTCGAAGTGCTGGAATTAAGGTCATCATGGTCACAGGAGACCAT
CCAATCACAGCTAAAGCTATTGCCAAAGGTGTGGGCATCATCTCAGAAGGCAATGAGACC
GTGGAAGACATTGCTGCCCGCCTCAACATCCCAGTCAGCCAGGTGAACCCCAGGGATGCC
AAGGCCTGCGTAGTACACGGCAGTGATCTAAAGGACATGACCTCCGAGCAGCTGGATGAC
ATTTTGAAGTACCACACTGAGATAGTGTTTGCCAGGACCTCCCCTCAGCAGAAGCTCATC
ATTGTGGAAGGCTGCCAAAGACAGGGTGCTATCGTGGCTGTGACTGGTGACGGTGTGAAT
GACTCTCCAGCTTTGAAGAAAGCAGACATTGGGGTTGCTATGGGGATTGCTGGCTCAGAT
GTGTCCAAGCAAGCTGCTGACATGATTCTTCTGGATGACAACTTTGCCTCAATTGTGACT
GGAGTAGAGGAAGGTCGTCTGATCTTTGATAACTTGAAGAAATCCATTGCTTATACCTTA
ACCAGTAACATTCCCGAGATCACCCCGTTCCTGATATTTATTATTGCAAACATTCCACTA
CCACTGGGGACTGTCACCATCCTCTGCATTGACTTGGGCACTGACATGGTTCCTGCCATC
TCCCTGGCTTATGAGCAGGCTGAGAGTGACATCATGAAGAGACAGCCCAGAAATCCCAAA
ACAGACAAACTTGTGAATGAGCGGCTGATCAGCATGGCCTATGGGCAGATTGGAATGATC
CAGGCCCTGGGAGGCTTCTTTACTTACTTTGTGATTCTGGCTGAGAACGGCTTCCTCCCA
ATTCACCTGTTGGGCCTCCGAGTGGACTGGGATGACCGCTGGATCAACGATGTGGAAGAC
AGCTACGGGCAGCAGTGGACCTATGAGCAGAGGAAAATCGTGGAGTTCACCTGCCACACA
GCCTTCTTCGTCAGTATCGTGGTGGTGCAGTGGGCCGACTTGGTCATCTGTAAGACCAGG
AGGAATTCGGTCTTCCAGCAGGGGATGAAGAACAAGATCTTGATATTTGGCCTCTTTGAA
GAGACAGCCCTGGCTGCTTTCCTTTCCTACTGCCCTGGAATGGGTGTTGCTCTTAGGATG
TATCCCCTCAAACCTACCTGGTGGTTCTGTGCCTTCCCCTACTCTCTTCTCATCTTCGTA
TATGACGAAGTCAGAAAACTCATCATCAGGCGACGCCCTGGCGGCTGGGTGGAGAAGGAA
ACCTACTATTAG
Target 6 GenBank Gene ID
Target 6 GeneCard ID ATP1A1 Link Image
Target 6 GenAtlas ID ATP1A1 Link Image
Target 6 HGNC ID HGNC:799 Link Image
Target 6 Chromosome Location 1
Target 6 Locus 1p21
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Shull MM, Pugh DG, Lingrel JB: The human Na, K-ATPase alpha 1 gene: characterization of the 5'-flanking region and identification of a restriction fragment length polymorphism. Genomics. 1990 Mar;6(3):451-60. [PubMed Link Image]
  2. Kawakami K, Ohta T, Nojima H, Nagano K: Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence. J Biochem (Tokyo). 1986 Aug;100(2):389-97. [PubMed Link Image]
  3. Chehab FF, Kan YW, Law ML, Hartz J, Kao FT, Blostein R: Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue expression, DNA polymorphism, and chromosomal localization. Proc Natl Acad Sci U S A. 1987 Nov;84(22):7901-5. [PubMed Link Image]
  4. Shull MM, Lingrel JB: Multiple genes encode the human Na+,K+-ATPase catalytic subunit. Proc Natl Acad Sci U S A. 1987 Jun;84(12):4039-43. [PubMed Link Image]
  5. Sverdlov ED, Monastyrskaya GS, Broude NE, Ushkaryov YuA, Allikmets RL, Melkov AM, Smirnov YuV, Malyshev IV, Dulobova IE, Petrukhin KE, et al.: The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit. FEBS Lett. 1987 Jun 15;217(2):275-8. [PubMed Link Image]
  6. Ruiz A, Bhat SP, Bok D: Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium. Gene. 1995 Apr 3;155(2):179-84. [PubMed Link Image]
Target 6 Drug References
  1. Takahashi N, Kondo Y, Fujiwara I, Ito O, Igarashi Y, Abe K: Characterization of Na+ transport across the cell membranes of the ascending thin limb of Henle's loop. Kidney Int. 1995 Mar;47(3):789-94. [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.