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Showing drug card for Esomeprazole (DB00736)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:48
Primary Accession Number DB00736
Secondary Accession Number
  • APRD00363
Name Esomeprazole
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description A highly effective inhibitor of gastric acid secretion used in the therapy of stomach ulcers and zollinger-ellison syndrome. The drug inhibits the H(+)-K(+)-ATPase (H(+)-K(+)-exchanging ATPase) in the proton pump of gastric parietal cells. [PubChem]
Synonyms
  1. Esomeprazole Sodium
  2. Esomperazole
  3. esomeprazole
Brand Names
  1. Axagon
  2. Esopral
  3. Lucen
  4. Nexiam
  5. Nexium
  6. Nexium IV
Brand Mixtures Not Available
Chemical IUPAC Name 6-methoxy-2-[(4-methoxy-3,5-dimethylpyridin-2-yl)methylsulfinyl]-1H-benzimidazole
Chemical Formula C17H19N3O3S
Chemical Structure Structure
CAS Registry Number 161796-78-7
InChI Identifier InChI=1/C17H19N3O3S/c1-10-8-18-15(11(2)16(10)23-4)9-24(21)17-19-13-6-5-12(22-3)7-14(13)20-17/h5-8H,9H2,1-4H3,(H,19,20)/f/h20H
InChI Key SUBDBMMJDZJVOS-UYBDAZJACN
KEGG Drug D01984 Link Image
KEGG Compound Not Available
PubChem Compound 4594 Link Image
PubChem Substance 3865629 Link Image
ChEBI ID Not Available
PharmGKB ID PA10075 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02244521 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/esomeprazole.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Esomeprazole Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 345.4160
Monoisotopic Molecular Weight 345.1147
State Solid
Melting Point 155 oC
Experimental Water Solubility Very slightly soluble in water Source: PhysProp
Predicted Water Solubility 3.59e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 0.6 Source: PhysProp
Predicted LogP 1.91 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.98 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 COC1=CC2=C(C=C1)N=C(N2)[S@@](=O)CC1=NC=C(C)C(OC)=C1C
Canonical SMILES COC1=CC2=C(C=C1)N=C(N2)S(=O)CC1=NC=C(C)C(OC)=C1C
Drug Category
  • Anti-Ulcer Agents
  • Antihistamines
  • Enzyme Inhibitors
  • Proton-pump Inhibitors
ATC Codes
AHFS Codes
  • 56:28.36
Indication For the treatment of acid-reflux disorders (GERD) and peptic ulcer disease
Pharmacology Esomeprazole is a compound that inhibits gastric acid secretion and is indicated in the treatment of gastroesophageal reflux disease (GERD), the healing of erosive esophagitis, and H. pylori eradication to reduce the risk of duodenal ulcer recurrence. Esomeprazole belongs to a new class of antisecretory compounds, the substituted benzimidazoles, that do not exhibit anticholinergic or H2 histamine antagonistic properties, but that suppress gastric acid secretion by specific inhibition of the H+/K+ ATPase enzyme system at the secretory surface of the gastric parietal cell. Because this enzyme system is regarded as the acid (proton) pump within the gastric mucosa, Esomeprazole has been characterized as a gastric acid-pump inhibitor, in that it blocks the final step of acid production. This effect is dose-related and leads to inhibition of both basal and stimulated acid secretion irrespective of the stimulus.
Mechanism of Action Esomeprazole is a proton pump inhibitor that suppresses gastric acid secretion by specific inhibition of the H+/K+-ATPase in the gastric parietal cell. By acting specifically on the proton pump, Esomeprazole blocks the final step in acid production, thus reducing gastric acidity.
Absorption 90%
Toxicity Blurred vision, confusion, drowsiness, dry mouthflushingheadache, nausea, rapid heartbeat, sweating
Protein Binding 97%
Biotransformation Hepatic
Half Life 1-1.5 hours
Dosage Forms
Form Route
Capsule Oral
Capsule, delayed release Oral
Tablet, delayed release Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Atazanavir This gastric pH modifier decreases the levels/effects of atazanavir
Enoxacin The agent decreases the absorption of enoxacin
Indinavir Omeprazole decreases the absorption of indinavir
Itraconazole The proton pump inhibitor decreases the absorption of imidazole
Ketoconazole The proton pump inhibitor decreases the absorption of imidazole
Food Interactions
  • Take without regard to meals.
Pathways
Name SMPDB Link KEGG Link
Esomeprazole Pathway SMP00225 Link Image
General References
  1. Lind T, Rydberg L, Kyleback A, Jonsson A, Andersson T, Hasselgren G, Holmberg J, Rohss K: Esomeprazole provides improved acid control vs. omeprazole In patients with symptoms of gastro-oesophageal reflux disease. Aliment Pharmacol Ther. 2000 Jul;14(7):861-7. [PubMed Link Image]
  2. Drugs.com Link Image
  3. Wikipedia Link Image
  4. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 2C19 (CYP2C19)
  2. Cytochrome P450 3A4 (CYP3A4)
  3. Cytochrome P450 1A2 (CYP1A2)
  4. Cytochrome P450 2C9 (CYP2C9)
  5. Cytochrome P450 2D6 (CYP2D6)
  6. Cytochrome P450 1A1 (CYP1A1)
Targets
  1. Potassium-transporting ATPase alpha chain 1
  2. Sodium/potassium-transporting ATPase alpha-1 chain
  3. Potassium-transporting ATPase alpha chain 2
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 2C19 (CYP2C19)
Enzyme 1 Gene Name CYP2C19
Enzyme 1 SwissProt ID P33261 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P33261|CP2CJ_HUMAN Cytochrome P450 2C19 (EC 1.14.13.80) 
MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKI
YGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFM
ESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVVGRNRSPCMQDRGHMPYTDAVVHEVQRYID
LIPTSLPHAVTCDVKFRNYLIPKGTTILTSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFK
KSNYFMPFSAGKRICVGEGLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVP
PFYQLCFIPV
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 2 Gene Name CYP3A4
Enzyme 2 SwissProt ID P08684 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67) 
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Phase 1 Metabolizing Enzyme 3 [top]
Enzyme 3 Name Cytochrome P450 1A2 (CYP1A2)
Enzyme 3 Gene Name CYP1A2
Enzyme 3 SwissProt ID P05177 Link Image
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 Protein Sequence >P05177|CP1A2_HUMAN Cytochrome P450 1A2 - Homo sapiens (Human). 
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
Phase 1 Metabolizing Enzyme 4 [top]
Enzyme 4 Name Cytochrome P450 2C9 (CYP2C9)
Enzyme 4 Gene Name CYP2C9
Enzyme 4 SwissProt ID P11712 Link Image
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 Protein Sequence >sp|P11712|CP2C9_HUMAN Cytochrome P450 2C9 (EC 1.14.13.80) 
MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKV
YGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFM
KSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYID
LLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFK
KSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVP
PFYQLCFIPV
Phase 1 Metabolizing Enzyme 5 [top]
Enzyme 5 Name Cytochrome P450 2D6 (CYP2D6)
Enzyme 5 Gene Name CYP2D6
Enzyme 5 SwissProt ID P10635 Link Image
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 Protein Sequence >sp|P10635|CP2D6_HUMAN Cytochrome P450 2D6 (EC 1.14.14.1) 
MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQ
LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVF
LARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDK
AVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV
LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVA
DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI
HEVQRFGDIVPLGMTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF
LDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGV
FAFLVSPSPYELCAVPR
Phase 1 Metabolizing Enzyme 6 [top]
Enzyme 6 Name Cytochrome P450 1A1 (CYP1A1)
Enzyme 6 Gene Name CYP1A1
Enzyme 6 SwissProt ID P04798 Link Image
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 Protein Sequence >sp|P04798|CP1A1_HUMAN Cytochrome P450 1A1 (EC 1.14.14.1) 
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
Drug Target 1 [top]
Target 1 ID 385
Target 1 Name Potassium-transporting ATPase alpha chain 1
Target 1 Synonyms
  1. EC 3.6.3.10
  2. Gastric H(+)/K(+) ATPase subunit alpha
  3. Proton pump
Target 1 Gene Name ATP4A
Target 1 Protein Sequence >Potassium-transporting ATPase alpha chain 1 
GKAENYELYSVELGPGPGGDMAAKMSKKKKAGGGGGKRKEKLENMKKEMEINDHQLSVAE
LEQKYQTSATKGLSASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAI
CLIAFAIQASEGDLTTDDNLYLAIALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQAT
VIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILAAQGCKVDNSSLTGESEPQTRSPE
CTHESPLETRNIAFFSTMCLEGTAQGLVVNTGDRTIIGRIASLASGVENEKTPIAIEIEH
FVDIIAGLAILFGATFFIVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKR
LASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQT
FDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGY
RDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPL
DEQWREAFQTAYLSLGGLGERVLGFCQLYLNEKDYPPGYAFDVEAMNFPSSGLCFAGLVS
MIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRV
PVDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGA
IVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFD
NLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESD
IMHLRPRNPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEGWFPLLCVGLRAQW
EDHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEVCQIADVLIRKTRRLSAFQQGFF
RNKILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPLPYGILIFVYDEIRKLGV
RCCPGSWWDQELYY
Target 1 Number of Residues 1051
Target 1 Molecular Weight 113961
Target 1 Theoretical pI 5.54
Target 1 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 1 General Function Inorganic ion transport and metabolism
Target 1 Specific Function Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for acid production in the stomach
Target 1 Pathways
Name SMPDB Link KEGG Link
Oxidative phosphorylation map00190 Link Image
Target 1 Reactions
  • ATP + H2O + H+in + K+out = ADP + phosphate + H+out + K+in
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 98-118
  • 142-162
  • 299-318
  • 331-348
  • 783-802
  • 813-833
  • 854-876
  • 929-948
  • 963-981
  • 997-1017
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 561634 Link Image
Target 1 UniProtKB/Swiss-Prot ID P20648 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ATP4A_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 1 Gene Sequence >3108 bp 
ATGGGGAAGGCCGAGAACTATGAGCTCTACTCGGTGGAGCTGGGTCCTGGCCCTGGCGGG
GACATGGCTGCCAAGATGAGCAAGAAGAAGAAGGCGGGTGGCGGGGGTGGCAAGAGGAAG
GAGAAGCTGGAGAACATGAAGAAGGAGATGGAGATTAACGACCACCAGCTGTCAGTGGCG
GAGCTGGAACAGAAATACCAGACCAGTGCCACCAAGGGCCTCTCTGCGAGCCTGGCTGCT
GAGCTGCTGCTGCGGGATGGGCCCAACGCACTGCGGCCACCACGGGGCACCCCAGAGTAC
GTCAAGTTCGCGAGGCAGCTGGCCGGGGGCCTGCAGTGCCTCATGTGGGTTGCCGCCGCC
ATCTGCCTCATCGCCTTTGCCATCCAGGCTAGTGAGGGGGACCTCACCACCGACGACAAT
CTGTACCTGGCAATCGCTCTCATTGCTGTGGTTGTCGTCACCGGCTGCTTTGGCTACTAC
CAGGAATTCAAGAGCACCAACATCATCGCCAGCTTTAAGAACCTTGTGCCACAGCAAGCC
ACTGTCATCCGCGATGGAGACAAATTCCAGATCAACGCTGACCAACTGGTGGTGGGCGAC
CTGGTGGAGATGAAAGGTGGGGACAGAGTGCCCGCCGACATCCGCATCCTGGCGGCCCAG
GGCTGCAAGGTGGACAACTCCTCGCTGACAGGGGAGTCTGAGCCACAGACCCGCTCACCC
GAGTGCACGCACGAGAGCCCTCTGGAGACCCGCAACATCGCCTTCTTCTCCACCATGTGC
CTTGAGGGCACCGCGCAGGGCCTGGTGGTGAACACGGGCGACCGCACCATCATTGGGCGC
ATCGCATCGCTGGCGTCGGGGGTGGAAAACGAGAAGACACCCATCGCTATCGAGATCGAG
CATTTTGTGGACATCATCGCGGGCCTGGCCATTCTCTTCGGTGCCACATTTTTTATTGTG
GCCATGTGCATTGGCTACACCTTCCTGCGGGCCATGGTCTTCTTCATGGCCATCGTGGTG
GCCTATGTGCCTGAGGGGCTGCTGGCCACTGTCACAGTCTGCCTGTCCCTGACAGCCAAG
CGCCTGGCCAGTAAGAACTGCGTGGTCAAGAACCTGGAGGCGGTGGAGACATTGGGCTCC
ACTTCGGTGATCTGCTCGGACAAGACAGGGACTCTCACTCAGAACCGCATGACTGTGTCC
CATCTTTGGTTTGACAACCACATCCACACAGCTGACACCACGGAAGACCAGTCAGGGCAG
ACGTTTGACCAGTCCTCGGAGACGTGGCGGGCGCTGTGCCGGGTGCTCACCCTGTGCAAC
CGCGCCGCCTTCAAGTCCGGCCAGGATGCAGTGCCTGTGCCCAAGCGCATCGTGATTGGA
GACGCATCGGAGACGGCGCTGCTCAAGTTCTCGGAGCTGACGCTGGGCAACGCCATGGGC
TACCGGGACCGCTTCCCAAAAGTCTGCGAGATACCCTTCAACTCCACCAACAAGTTCCAG
CTGTCCATACATACGCTGGAGGACCCGCGGGACCCGCGACACTTGCTGGTGATGAAGGGC
GCCCCCGAGCGCGTGCTGGAGCGCTGCAGCTCCATCCTTATCAAGGGCCAGGAGCTGCCG
CTGGACGAGCAGTGGCGCGAGGCCTTCCAGACCGCCTACCTCAGCCTGGGAGGCCTGGGC
GAACGCGTGCTCGGCTTCTGCCAGCTCTACCTGAATGAGAAGGACTACCCGCCTGGCTAT
GCCTTCGACGTAGAGGCCATGAACTTTCCATCTAGCGGCCTCTGCTTTGCGGGACTTGTA
TCCATGATTGACCCACCCCGGGCCACCGTCCCTGATGCTGTGCTCAAGTGTCGCACCGCA
GGCATCCGGGTGATCATGGTAACGGGTGACCACCCCATCACCGCCAAGGCCATTGCAGCC
AGTGTGGGCATCATCTCGGAAGGCAGCGAGACAGTGGAGGACATCGCTGCCCGCCTCCGT
GTGCCCGTAGACCAGGTTAATCGCAAGGATGCCCGTGCCTGTGTGATCAATGGCATGCAG
CTGAAGGACATGGACCCATCGGAACTGGTCGAGGCCCTGCGCACCCACCCCGAGATGGTG
TTTGCGCGCACCAGCCCCCAGCAGAAGCTGGTGATCGTGGAGAGCTGCCAGCGGCTGGGT
GCGATTGTGGCCGTCACGGGGGATGGTGTGAATGACTCCCCAGCTCTGAAGAAGGCAGAC
ATCGGAGTAGCCATGGGCATCGCTGGCTCAGATGCTGCCAAAAATGCAGCTGACATGATC
CTGCTGGATGACAACTTTGCCTCCATTGTGACAGGCGTGGAGCAGGGTCGACTGATCTTC
GACAACCTGAAGAAGTCTATTGCCTACACATTGACCAAGAACATCCCAGAGCTGACACCC
TACCTCATCTACATCACCGTCAGCGTGCCCCTGCCCCTCGGGTGCATCACCATCCTCTTC
ATCGAACTCTGCACTGACATTTTCCCATCTGTGTCCCTGGCATATGAAAAGGCCGAGAGT
GACATCATGCACCTGCGTCCACGCAACCCAAAGCGTGACAGATTGGTCAACGAGCCCCTG
GCTGCCTACTCCTACTTCCAGATTGGTGCCATTCAGTCCTTTGCTGGCTTCACTGACTAC
TTCACGGCAATGGCCCAGGAGGGCTGGTTCCCACTGCTGTGCGTGGGGCTGCGGGCGCAG
TGGGAGGACCACCACCTACAAGATCTGCAGGACAGCTACGGCCAGGAGTGGACATTCGGG
CAGCGCCTGTACCAGCAGTACACCTGCTACACCGTGTTCTTCATCAGCATTGAGGTGTGC
CAGATCGCCGATGTCCTCATCCGCAAGACGCGCCGTCTCTCTGCCTTCCAGCAAGGCTTC
TTCAGGAATAAGATCCTGGTGATCGCCATCGTGTTCCAGGTCTGCATCGGCTGCTTCCTG
TGCTACTGCCCCGGCATGCCCAACATCTTCAACTTCATGCCCATTCGGTTCCAGTGGTGG
CTGGTCCCCCTGCCCTACGGCATCCTCATCTTCGTCTATGATGAGATCCGGAAGCTTGGA
GTTCGCTGTTGCCCAGGGAGCTGGTGGGACCAGGAACTCTACTATTAG
Target 1 GenBank Gene ID
Target 1 GeneCard ID ATP4A Link Image
Target 1 GenAtlas ID ATP4A Link Image
Target 1 HGNC ID HGNC:819 Link Image
Target 1 Chromosome Location 19
Target 1 Locus 19q13.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Maeda M, Oshiman K, Tamura S, Futai M: Human gastric (H+ + K+)-ATPase gene. Similarity to (Na+ + K+)-ATPase genes in exon/intron organization but difference in control region. J Biol Chem. 1990 Jun 5;265(16):9027-32. [PubMed Link Image]
  2. Newman PR, Greeb J, Keeton TP, Reyes AA, Shull GE: Structure of the human gastric H,K-ATPase gene and comparison of the 5'-flanking sequences of the human and rat genes. DNA Cell Biol. 1990 Dec;9(10):749-62. [PubMed Link Image]
  3. 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]
Target 1 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 806
Target 2 Name Sodium/potassium-transporting ATPase alpha-1 chain
Target 2 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 2 Gene Name ATP1A1
Target 2 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 2 Number of Residues 1040
Target 2 Molecular Weight 112897
Target 2 Theoretical pI 5.15
Target 2 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 2 General Function Inorganic ion transport and metabolism
Target 2 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 2 Pathways Not Available
Target 2 Reactions
  • ATP + H2O + Na+in + K+out = ADP + phosphate + Na+out + K+in
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 88-108
  • 132-152
  • 289-308
  • 321-338
  • 773-792
  • 803-823
  • 844-866
  • 919-938
  • 952-970
  • 986-1006
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 219942 Link Image
Target 2 UniProtKB/Swiss-Prot ID P05023 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name AT1A1_HUMAN Link Image
Target 2 PDB ID 1MO8 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 2 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 2 GenBank Gene ID
Target 2 GeneCard ID ATP1A1 Link Image
Target 2 GenAtlas ID ATP1A1 Link Image
Target 2 HGNC ID HGNC:799 Link Image
Target 2 Chromosome Location 1
Target 2 Locus 1p21
Target 2 SNPs SNPJam Report Link Image
Target 2 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 2 Drug References
  1. Bendsoe N, Ronquist G: Inhibition of the L-dopa transport system in human epidermal Langerhans cells by omeprazole and its analogues. Amino Acids. 2004 Feb;26(1):19-26. Epub 2003 Dec 18. [PubMed Link Image]
  2. Shin JM, Sachs G: Differences in binding properties of two proton pump inhibitors on the gastric H+,K+-ATPase in vivo. Biochem Pharmacol. 2004 Dec 1;68(11):2117-27. [PubMed Link Image]
  3. Dufner MM, Kirchhoff P, Remy C, Hafner P, Muller MK, Cheng SX, Tang LQ, Hebert SC, Geibel JP, Wagner CA: The calcium-sensing receptor acts as a modulator of gastric acid secretion in freshly isolated human gastric glands. Am J Physiol Gastrointest Liver Physiol. 2005 Dec;289(6):G1084-90. Epub 2005 Aug 18. [PubMed Link Image]
  4. Kukanich B, Lascelles BD, Aman AM, Mealey KL, Papich MG: The effects of inhibiting cytochrome P450 3A, p-glycoprotein, and gastric acid secretion on the oral bioavailability of methadone in dogs. J Vet Pharmacol Ther. 2005 Oct;28(5):461-6. [PubMed Link Image]
  5. Sharara AI: Rabeprazole: the role of proton pump inhibitors in Helicobacter pylori eradication. Expert Rev Anti Infect Ther. 2005 Dec;3(6):863-70. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 1370
Target 3 Name Potassium-transporting ATPase alpha chain 2
Target 3 Synonyms
  1. EC 3.6.3.10
  2. Non-gastric H(+)/K(+) ATPase subunit alpha
  3. Proton pump
Target 3 Gene Name ATP12A
Target 3 Protein Sequence >Potassium-transporting ATPase alpha chain 2 
MHQLFQKTPEIYSVELSGTKDIVKTDKGDGKEKYRGLKNNCLELKKKNHKEEFQKELHLD
DHKLSNRELEEKYGTDIIMGLSSTRAAELLARDGPNSLTPPKQTPEIVKFLKQMVGGFSI
LLWVGAFLCWIAYGIQYSSDKSASLNNVYLGCVLGLVVILTGIFAYYQEAKSTNIMSSFN
KMIPQQALVIRDSEKKTIPSEQLVVGDIVEVKGGDQIPADIRVLSSQGCRVDNSSLTGES
EPQPRSSEFTHENPLETKNICFYSTTCLEGTVTGMVINTGDRTIIGHIASLASGVGNEKT
PIAIEIEHFVHIVAGVAVSIGILFFIIAVSLKYQVLDSIIFLIGIIVANVPEGLLATVTV
TLSLTAKRMAKKNCLVKNLEAVETLGSTSIICSDKTGTLTQNRMTVAHLWFDNQIFVADT
SEDHSNQVFDQSSRTWASLSKIITLCNRAEFKPGQENVPIMKKAVIGDASETALLKFSEV
ILGDVMEIRKRNRKVAEIPFNSTNKFQLSIHEMDDPHGKRFLMVMKGAPERILEKCSTIM
INGEEHPLDKSTAKTFHTAYMELGGLGERVLGFCHLYLPADEFPETYSFDIDAMNFPTSN
LCFVGLLSMIDPPRSTVPDAVTKCRSAGIKVIMVTGDHPITAKAIAKSVGIISANSETVE
DIAHRLNIAVEQVNKRDAKAAVVTGMELKDMSSEQLDEILANYQEIVFARTSPQQKLIIV
EGCQRQDAVVAVTGDGVNDSPALKKADIGIAMGIAGSDAAKNAADMVLLDDNFASIVTGV
EEGRLIFDNLKKTIAYSLTKNIAELCPFLIYIIVGLPLPIGTITILFIDLGTDIIPSIAL
AYEKAESDIMNRKPRHKNKDRLVNQPLAVYSYLHIGLMQALGAFLVYFTVYAQEGFLPRT
LINLRVEWEKDYVNDLKDSYGQEWTRYQREYLEWTGYTAFFVGILVQQIADLIIRKTRRN
SIFQQGLFRNKVIWVGITSQIIIGLILSYGLGSVTALSFTMLRAQYWFVAVPHAILIWVY
DEVRKLFIRLYPGSWWDKNMYY
Target 3 Number of Residues 1059
Target 3 Molecular Weight 115900
Target 3 Theoretical pI 6.52
Target 3 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 3 General Function Inorganic ion transport and metabolism
Target 3 Specific Function Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for potassium absorption in various tissues
Target 3 Pathways
Name SMPDB Link KEGG Link
Oxidative phosphorylation map00190 Link Image
Target 3 Reactions
  • ATP + H2O + H+in + K+out = ADP + phosphate + H+out + K+in
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • 106-126
  • 150-170
  • 307-326
  • 339-356
  • 791-810
  • 821-841
  • 862-884
  • 937-956
  • 971-989
  • 1005-1025
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 404017 Link Image
Target 3 UniProtKB/Swiss-Prot ID P54707 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name AT12A_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 3 Gene Sequence >3120 bp 
ATGCACCAGAAAACCCCAGAAATTTACTCCGTGGAGCTCAGCGGAACTAAGGACATCGTG
AAAACAGACAAGGGGGATGGCAAGGAGAAGTATAGGGGTCTGAAGAACAACTGCCTGGAA
CTCAAAAAGAAAAATCACAAAGAGGAGTTTCAGAAAGAACTCCATCTGGATGACCACAAA
CTCAGCAATAGGGAATTGGAAGAGAAATATGGCACAGACATCATTATGGGTCTCTCCAGC
ACCAGAGCTGCCGAGCTCCTGGCCCGGGATGGGCCCAACTCCCTCACCCCTCCCAAGCAG
ACGCCTGAGATCGTCAAGTTCCTCAAGCAGATGGTGGGGGGGTTCTCTATCCTCCTGTGG
GTGGGCGCCTTTCTCTGTTGGATTGCATATGGGATTCAGTACTCCAGCGACAAGTCTGCA
TCCCTGAACAACGTGTACTTGGGCTGTGTGCTTGGTCTGGTGGTCATTTTAACGGGGATC
TTTGCTTATTACCAAGAGGCAAAAAGCACCAACATCATGTCCAGCTTCAATAAGATGATC
CCTCAGCAAGCTCTCGTCATCCGAGATTCCGAGAAGAAGACCATCCCTTCAGAGCAGCTG
GTGGTGGGGGACATTGTGGAGGTCAAAGGAGGAGACCAGATCCCTGCAGACATCAGGGTG
CTGTCTTCTCAGGGGTGTCGGGTGGATAACTCATCTCTCACGGGGGAGTCTGAGCCCCAG
CCCCGCTCCTCTGAGTTTACCCATGAAAACCCCCTGGAAACAAAGAACATCTGCTTCTAT
TCCACAACGTGTCTGGAAGGCACTGTCACCGGCATGGTTATCAACACGGGTGACCGCACC
ATCATTGGCCATATTGCCTCATTGGCCTCAGGAGTTGGAAATGAGAAGACGCCCATTGCC
ATTGAGATCGAGCACTTTGTTCACATTGTGGCAGGAGTGGCTGTCTCCATCGGCATCCTT
TTCTTCATCATCGCTGTGTCCCTGAAGTATCAAGTCCTGGACTCCATCATCTTCCTCATT
GGCATCATTGTGGCCAATGTGCCCGAGGGCCTCCTGGCCACTGTCACTGTGACCCTGTCG
CTGACAGCAAAACGGATGGCCAAGAAGAACTGCCTGGTGAAGAACCTGGAGGCTGTGGAG
ACCCTCGGCTCCACCTCCATCATCTGCTCGGACAAGACTGGGACACTGACCCAGAACAGG
ATGACAGTGGCCCATCTGTGGTTCGACAATCAGATCTTTGTGGCTGACACCAGTGAGGAC
CATTCAAACCAAGTCTTTGACCAAAGCTCTAGGACTTGGGCCTCCTTATCCAAGATAATA
ACATTGTGTAACCGAGCAGAGTTCAAGCCAGGACAGGAAAATGTCCCCATCATGAAGAAA
GCTGTGATTGGAGATGCCTCAGAAACTGCTCTTTTAAAATTCTCAGAGGTCATTTTGGGT
GATGTGATGGAAATTAGAAAAAGAAACCGCAAAGTAGCTGAAATCCCTTTTAACTCTACT
AATAAATTTCAGCTCTCCATCCACGAGATGGATGACCCCCACGGCAAGCGCTTCCTCATG
GTGATGAAGGGGGCCCCTGAGCGCATTCTAGAGAAATGCAGCACCATCATGATCAACGGC
GAGGAGCACCCACTGGACAAGAGCACTGCCAAGACCTTCCACACAGCCTACATGGAGCTG
GGCGGGTTGGGCGAGCGTGTGCTGGGTTTCTGTCATCTCTACCTGCCAGCAGACGAGTTT
CCAGAAACCTACTCATTTGACATAGACGCTATGAACTTTCCGACCTCCAACCTCTGTTTT
GTGGGACTCTTGTCAATGATCGATCCCCCTCGGTCCACCGTGCCAGATGCAGTCACCAAA
TGCCGGAGTGCAGGGATCAAGGTTATTATGGTTACTGGTGATCATCCCATCACAGCCAAA
GCTATTGCCAAGAGTGTGGGGATCATTTCAGCCAACAGTGAAACAGTGGAAGACATTGCA
CATCGCCTCAACATTGCTGTGGAGCAAGTTAACAAACGGGATGCCAAGGCCGCTGTGGTG
ACTGGCATGGAGCTGAAGGACATGAGCTCAGAACAGCTGGATGAGATCTTAGCCAACTAC
CAGGAGATTGTCTTTGCCCGGACATCCCCCCAGCAGAAGCTGATCATTGTGGAGGGCTGT
CAGAGGCAGGATGCTGTTGTTGCTGTGACCGGGGATGGAGTTAATGACTCTCCGGCTCTA
AAGAAGGCAGACATTGGGATTGCCATGGGGATAGCAGGTTCTGATGCAGCCAAAAATGCA
GCCGACATGGTCTTGCTGGACGACAACTTCGCATCCATCGTCACAGGGGTGGAGGAAGGT
CGCCTGATCTTTGACAACCTCAAGAAGACTATTGCTTATTCCCTGACCAAGAACATTGCC
GAGCTGTGCCCCTTTCTGATCTACATCATTGTCGGGCTCCCCCTGCCCATTGGCACCATC
ACCATTCTGTTCATTGACTTGGGGACAGACATTATCCCCTCCATTGCCTTGGCGTACGAG
AAAGCTGAAAGTGACATCATGAACAGGAAGCCTCGCCACAAGAATAAGGACAGGCTGGTG
AACCAGCCGCTCGCTGTGTACTCATACCTGCACATTGGCCTCATGCAAGCCCTGGGAGCT
TTCCTTGTGTATTTCACCGTCTATGCACAAGAGGGCTTTCTGCCCCGCACTCTCATTAAC
CTGCGGGTAGAATGGGAGAAGGACTACGTGAATGACTTGAAAGACAGCTATGGGCAGGAA
TGGACAAGGTACCAGAGGGAATACCTAGAATGGACGGGCTACACGGCTTTCTTTGTTGGC
ATCCTAGTCCAGCAAATAGCAGATCTGATCATCAGGAAAACCCGGAGGAATTCCATCTTC
CAGCAGGGTCTCTTCAGAAATAAAGTCATCTGGGTGGGGATCACCTCACAGATCATCATT
GGTCTGATCCTCTCCTATGGCCTCGGAAGTGTCACAGCCTTGAGTTTCACCATGCTTAGG
GCTCAGTACTGGTTTGTGGCTGTGCCGCACGCCATCCTGATCTGGGTGTATGATGAGGTG
CGGAAGCTCTTCATCAGGCTCTACCCTGGAAGCTGGTGGGATAAGAACATGTATTATTAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID ATP12A Link Image
Target 3 GenAtlas ID ATP12A Link Image
Target 3 HGNC ID HGNC:13816 Link Image
Target 3 Chromosome Location 13
Target 3 Locus 13q12.12|13q12.1-q12.3
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. 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]
  2. 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]
  3. Grishin AV, Sverdlov VE, Kostina MB, Modyanov NN: Cloning and characterization of the entire cDNA encoded by ATP1AL1--a member of the human Na,K/H,K-ATPase gene family. FEBS Lett. 1994 Jul 25;349(1):144-50. [PubMed Link Image]
  4. Sverdlov VE, Kostina MB, Modyanov NN: Genomic organization of the human ATP1AL1 gene encoding a ouabain-sensitive H,K-ATPase. Genomics. 1996 Mar 15;32(3):317-27. [PubMed Link Image]
  5. Pestov NB, Romanova LG, Korneenko TV, Egorov MV, Kostina MB, Sverdlov VE, Askari A, Shakhparonov MI, Modyanov NN: Ouabain-sensitive H,K-ATPase: tissue-specific expression of the mammalian genes encoding the catalytic alpha subunit. FEBS Lett. 1998 Dec 4;440(3):320-4. [PubMed Link Image]
Target 3 Drug References
  1. Li XQ, Andersson TB, Ahlstrom M, Weidolf L: Comparison of inhibitory effects of the proton pump-inhibiting drugs omeprazole, esomeprazole, lansoprazole, pantoprazole, and rabeprazole on human cytochrome P450 activities. Drug Metab Dispos. 2004 Aug;32(8):821-7. [PubMed Link Image]
  2. Miner P: Review article: relief of symptoms in gastric acid-related diseases--correlation with acid suppression in rabeprazole treatment. Aliment Pharmacol Ther. 2004 Nov;20 Suppl 6:20-9. [PubMed Link Image]
  3. Capendeguy O, Horisberger JD: The role of the third extracellular loop of the Na+,K+-ATPase alpha subunit in a luminal gating mechanism. J Physiol. 2005 May 15;565(Pt 1):207-18. Epub 2005 Mar 17. [PubMed Link Image]
  4. Kiley CA, Cragin DJ, Roth BJ: Omeprazole-associated digoxin toxicity. South Med J. 2007 Apr;100(4):400-2. [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.