Drugbank Logo

Showing drug card for Pantoprazole (DB00213)

Legend: drug field target field enzyme field

for drugs
Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:47:32
Primary Accession Number DB00213
Secondary Accession Number
  • APRD00073
Name Pantoprazole
Drug Type
  • Approved
  • Small Molecule
Description Pantoprazole is a proton pump inhibitor drug used for short-term treatment of erosion and ulceration of the esophagus caused by gastroesophageal reflux disease.
Synonyms
  1. Pantoprazol [INN-Spanish]
  2. Pantoprazole Na
  3. Pantoprazole Sodium
  4. Pantoprazolum [INN-Latin]
  5. Pantoprozole
Brand Names
  1. Astropan
  2. Pantoloc
  3. Pantopan
  4. Pantor
  5. Pantozol
  6. Protium
  7. Protonix
  8. Protonix I.V.
  9. Protonix IV
Brand Mixtures Not Available
Chemical IUPAC Name 6-(difluoromethoxy)-2-[(3,4-dimethoxypyridin-2-yl)methylsulfinyl]-1H-benzimidazole
Chemical Formula C16H15F2N3O4S
Chemical Structure Structure
CAS Registry Number 102625-70-7
InChI Identifier InChI=1/C16H15F2N3O4S/c1-23-13-5-6-19-12(14(13)24-2)8-26(22)16-20-10-4-3-9(25-15(17)18)7-11(10)21-16/h3-7,15H,8H2,1-2H3,(H,20,21)/f/h21H
InChI Key IQPSEEYGBUAQFF-PKSOQXRJCT
KEGG Drug D05353 Link Image
KEGG Compound C11806 Link Image
PubChem Compound 4679 Link Image
PubChem Substance 213529 Link Image
ChEBI ID Not Available
PharmGKB ID PA450774 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02241804 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/protonix.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Pantoprazole Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 383.3700
Monoisotopic Molecular Weight 383.0751
State Solid
Melting Point Because of gradual degradation of pantoprazole sodium during heating, the melting point cannot be determined.
Experimental Water Solubility Freely soluble in water. Source: PhysProp
Predicted Water Solubility 4.95e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 0.5 Source: PhysProp
Predicted LogP 2.11 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.89 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=C(OC)C(C[S@@](=O)C2=NC3=C(N2)C=C(OC(F)F)C=C3)=NC=C1
Canonical SMILES COC1=C(OC)C(CS(=O)C2=NC3=C(N2)C=C(OC(F)F)C=C3)=NC=C1
Drug Category
  • Anti-Ulcer Agents
  • Proton-pump Inhibitors
ATC Codes
AHFS Codes
  • 56:28.36
Indication Short-term (up to 16 weeks) treatment of erosive esophagitis.
Pharmacology Pantoprazole is a substituted benzimidazole indicated for the short-term treatment (up to 16 weeks) in the healing and symptomatic relief of erosive esophagitis. Pantoprazole is a proton pump inhibitor (PPI) that suppresses the final step in gastric acid production.
Mechanism of Action Pantoprazole is a proton pump inhibitor (PPI) that suppresses the final step in gastric acid production by forming a covalent bond to two sites of the (H+,K+ )- ATPase enzyme system at the secretory surface of the gastric parietal cell. This effect is dose- related and leads to inhibition of both basal and stimulated gastric acid secretion irrespective of the stimulus.
Absorption Pantoprazole is well absorbed. It undergoes little first-pass metabolism resulting in an absolute bioavailability of approximately 77%.
Toxicity Single intravenous doses of pantoprazole at 378, 230, and 266 mg/kg (38, 46, and 177 times the recommended human dose based on body surface area) were lethal to mice, rats and dogs, respectively. The symptoms of toxicity included hypoactivity, ataxia, hunched sitting, limb-splay, lateral position, segregation, absence of ear reflex, and tremor. There is limited experience regarding cases of human overdosage, and treatment should be symptomatic and supportive.
Protein Binding 98%
Biotransformation Pantoprazole is extensively metabolized in the liver through the cytochrome P450 (CYP) system. The main metabolic pathway is demethylation, by CYP2C19, with subsequent sulfation; other metabolic pathways include oxidation by CYP3A4. There is no evidence that any of the pantoprazole metabolites have significant pharmacologic activity.
Half Life 1 hour
Dosage Forms
Form Route
Powder, for solution Intravenous
Tablet, coated Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Atazanavir This gastric pH modifier decreases the levels/effects of atazanavir
Dasatinib Possible decreased levels of dasatinib
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
Pantoprazole Pathway SMP00228 Link Image
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. 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)
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
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. Takeuchi K, Konaka A, Nishijima M, Kato S, Yasuhiro T: Effects of pantoprazole, a novel H+/K+-ATPase inhibitor, on duodenal ulcerogenic and healing responses in rats: a comparative study with omeprazole and lansoprazole. J Gastroenterol Hepatol. 1999 Mar;14(3):251-7. [PubMed Link Image]
  2. Nishioka K, Nagao T, Urushidani T: Correlation between acid secretion and proton pump activity during inhibition by the proton pump inhibitors omeprazole and pantoprazole. Biochem Pharmacol. 1999 Oct 15;58(8):1349-59. [PubMed Link Image]
  3. Bruni AT, Leite VB, Ferreira MM: Conformational analysis: a new approach by means of chemometrics. J Comput Chem. 2002 Jan 30;23(2):222-36. [PubMed Link Image]
  4. Metz DC, Ferron GM, Paul J, Turner MB, Soffer E, Pisegna JR, Bochenek WJ: Proton pump activation in stimulated parietal cells is regulated by gastric acid secretory capacity: a human study. J Clin Pharmacol. 2002 May;42(5):512-9. [PubMed Link Image]
  5. Beil W, Sewing KF, Kromer W: Basic aspects of selectivity of pantoprazole and its pharmacological actions. Drugs Today (Barc). 1999 Oct;35(10):753-64. [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. Van Rensburg CJ, Honiball PJ, Van Zyl JH, Grundling HD, Eloff FP, Spies SK, Simjee AE, Theron I, Fischer R, Louw JA: Safety and efficacy of pantoprazole 40 mg daily as relapse prophylaxis in patients with healed reflux oesophagitis-a 2-year follow-up. Aliment Pharmacol Ther. 1999 Aug;13(8):1023-8. [PubMed Link Image]
  2. Nishioka K, Nagao T, Urushidani T: Correlation between acid secretion and proton pump activity during inhibition by the proton pump inhibitors omeprazole and pantoprazole. Biochem Pharmacol. 1999 Oct 15;58(8):1349-59. [PubMed Link Image]
  3. Avner DL: Clinical experience with pantoprazole in gastroesophageal reflux disease. Clin Ther. 2000 Oct;22(10):1169-85; discussion 1149-50. [PubMed Link Image]
  4. Jungnickel PW: Pantoprazole: a new proton pump inhibitor. Clin Ther. 2000 Nov;22(11):1268-93. [PubMed Link Image]
  5. Ramdani A, Mignon M, Samoyeau R: Effect of pantoprazole versus other proton pump inhibitors on 24-hour intragastric pH and basal acid output in Zollinger-Ellison syndrome. Gastroenterol Clin Biol. 2002 Apr;26(4):355-9. [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.