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Identification
HMDB Protein ID HMDBP01534
Secondary Accession Numbers
  • 6830
Name Sodium/potassium-transporting ATPase subunit alpha-2
Synonyms
  1. Na(+)/K(+) ATPase alpha-2 subunit
  2. Sodium pump subunit alpha-2
Gene Name ATP1A2
Protein Type Unknown
Biological Properties
General Function Involved in ATP binding
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, providing the energy for active transport of various nutrients.
Pathways
  • 3-Methylthiofentanyl Action Pathway
  • Acebutolol Action Pathway
  • Aldosterone-regulated sodium reabsorption
  • Alfentanil Action Pathway
  • Alprenolol Action Pathway
  • Alvimopan Action Pathway
  • Amiloride Action Pathway
  • Amiodarone Action Pathway
  • Amlodipine Action Pathway
  • Anileridine Action Pathway
  • Arbutamine Action Pathway
  • Atenolol Action Pathway
  • Bendroflumethiazide Action Pathway
  • Benzocaine Action Pathway
  • Betaxolol Action Pathway
  • Bevantolol Action Pathway
  • Bile secretion
  • Bisoprolol Action Pathway
  • Blue diaper syndrome
  • Bopindolol Action Pathway
  • Bumetanide Action Pathway
  • Bupivacaine Action Pathway
  • Bupranolol Action Pathway
  • Buprenorphine Action Pathway
  • Carbohydrate digestion and absorption
  • Cardiac muscle contraction
  • Carfentanil Action Pathway
  • Carteolol Action Pathway
  • Carvedilol Action Pathway
  • Chloroprocaine Action Pathway
  • Chlorothiazide Action Pathway
  • Chlorthalidone Action Pathway
  • Citalopram Action Pathway
  • Cocaine Action Pathway
  • Codeine Action Pathway
  • Cyclothiazide Action Pathway
  • Cystinuria
  • Desipramine Action Pathway
  • Dezocine Action Pathway
  • Dibucaine Action Pathway
  • Dihydromorphine Action Pathway
  • Diltiazem Action Pathway
  • Dimethylthiambutene Action Pathway
  • Diphenoxylate Action Pathway
  • Disopyramide Action Pathway
  • Dobutamine Action Pathway
  • Endocrine and other factor-regulated calcium reabsorption
  • Epinephrine Action Pathway
  • Eplerenone Action Pathway
  • Escitalopram Action Pathway
  • Esmolol Action Pathway
  • Ethacrynic Acid Action Pathway
  • Ethylmorphine Action Pathway
  • Felodipine Action Pathway
  • Fentanyl Action Pathway
  • Flecainide Action Pathway
  • Fluoxetine Action Pathway
  • Fosphenytoin (Antiarrhythmic) Action Pathway
  • Furosemide Action Pathway
  • Gastric acid secretion
  • Glucose Transporter Defect (SGLT2)
  • Hartnup Disorder
  • Heroin Action Pathway
  • Hydrochlorothiazide Action Pathway
  • Hydrocodone Action Pathway
  • Hydroflumethiazide Action Pathway
  • Hydromorphone Action Pathway
  • Ibutilide Action Pathway
  • Iminoglycinuria
  • Imipramine Action Pathway
  • Indapamide Action Pathway
  • Insulin secretion
  • Isoprenaline Action Pathway
  • Isradipine Action Pathway
  • Ketobemidone Action Pathway
  • Kidney Function
  • Labetalol Action Pathway
  • Lactose Degradation
  • Lactose Intolerance
  • Levallorphan Action Pathway
  • Levobunolol Action Pathway
  • Levobupivacaine Action Pathway
  • Levomethadyl Acetate Action Action Pathway
  • Levorphanol Action Pathway
  • Lidocaine (Antiarrhythmic) Action Pathway
  • Lidocaine (Local Anaesthetic) Action Pathway
  • Lysinuric Protein Intolerance
  • Lysinuric protein intolerance (LPI)
  • Mepivacaine Action Pathway
  • Methadone Action Pathway
  • Methadyl Acetate Action Pathway
  • Methyclothiazide Action Pathway
  • Metipranolol Action Pathway
  • Metolazone Action Pathway
  • Metoprolol Action Pathway
  • Mexiletine Action Pathway
  • Mineral absorption
  • Morphine Action Pathway
  • Muscle/Heart Contraction
  • Nadolol Action Pathway
  • Nalbuphine Action Pathway
  • Naloxone Action Pathway
  • Naltrexone Action Pathway
  • Nebivolol Action Pathway
  • Nicotine Action Pathway
  • Nifedipine Action Pathway
  • Nimodipine Action Pathway
  • Nisoldipine Action Pathway
  • Nitrendipine Action Pathway
  • Oxprenolol Action Pathway
  • Oxybuprocaine Action Pathway
  • Oxycodone Action Pathway
  • Oxymorphone Action Pathway
  • Pancreatic secretion
  • Penbutolol Action Pathway
  • Pentazocine Action Pathway
  • Phenytoin (Antiarrhythmic) Action Pathway
  • Pindolol Action Pathway
  • Polythiazide Action Pathway
  • Practolol Action Pathway
  • Prilocaine Action Pathway
  • Procainamide (Antiarrhythmic) Action Pathway
  • Procaine Action Pathway
  • Proparacaine Action Pathway
  • Propoxyphene Action Pathway
  • Propranolol Action Pathway
  • Protein digestion and absorption
  • Proximal tubule bicarbonate reclamation
  • Quinethazone Action Pathway
  • Quinidine Action Pathway
  • Remifentanil Action Pathway
  • Ropivacaine Action Pathway
  • Salivary secretion
  • Sotalol Action Pathway
  • Spironolactone Action Pathway
  • Sufentanil Action Pathway
  • Timolol Action Pathway
  • Tocainide Action Pathway
  • Torsemide Action Pathway
  • Tramadol Action Action Pathway
  • Trehalose Degradation
  • Triamterene Action Pathway
  • Trichlormethiazide Action Pathway
  • Verapamil Action Pathway
Reactions Not Available
GO Classification
Biological Process
ATP biosynthetic process
regulation of vasoconstriction
negative regulation of heart contraction
regulation of the force of heart contraction
adult locomotory behavior
ATP hydrolysis coupled proton transport
locomotion
neurotransmitter uptake
reduction of cytosolic calcium ion concentration
regulation of respiratory gaseous exchange by neurological system process
regulation of smooth muscle contraction
regulation of striated muscle contraction
visual learning
regulation of blood pressure
negative regulation of striated muscle contraction
Cellular Component
cytoplasm
sodium:potassium-exchanging ATPase complex
caveola
dendritic spine
synapse
endosome
sarcolemma
Component
membrane
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
binding
catalytic activity
hydrolase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
transmembrane transporter activity
substrate-specific transmembrane transporter activity
ion transmembrane transporter activity
cation transmembrane transporter activity
inorganic cation transmembrane transporter activity
monovalent inorganic cation transmembrane transporter activity
transporter activity
atpase activity, coupled to transmembrane movement of ions
atpase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
hydrolase activity, acting on acid anhydrides
Molecular Function
metal ion binding
ATP binding
sodium:potassium-exchanging ATPase activity
cation-transporting ATPase activity
Process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
purine nucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate biosynthetic process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
establishment of localization
transport
monovalent inorganic cation transport
ion transport
atp biosynthetic process
cation transport
Cellular Location
  1. Membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location 1
Locus 1q23.2
SNPs ATP1A2
Gene Sequence
>3063 bp
ATGGGCCGTGGGGCTGGCCGTGAGTACTCACCTGCCGCCACCACGGCAGAGAATGGGGGC
GGCAAGAAGAAACAGAAGGAGAAGGAACTGGATGAGCTGAAGAAGGAGGTGGCAATGGAT
GACCACAAGCTGTCCTTGGATGAGCTGGGCCGCAAATACCAAGTGGACCTGTCCAAGGGC
CTCACCAACCAGCGGGCTCAGGACGTTCTGGCTCGAGATGGGCCCAACGCCCTCACACCA
CCTCCCACAACCCCTGAGTGGGTCAAGTTCTGCCGTCAGCTTTTCGGGGGGTTCTCCATC
CTGCTGTGGATTGGGGCTATCCTCTGCTTCCTGGCCTACGGCATCCAGGCTGCCATGGAG
GATGAACCATCCAACGACAATCTATATCTGGGTGTGGTGCTGGCAGCTGTGGTCATTGTC
ACTGGCTGCTTCTCCTACTACCAGGAGGCCAAGAGCTCCAAGATCATGGATTCCTTCAAG
AACATGGTACCTCAGCAAGCCCTTGTGATCCGGGAGGGAGAGAAGATGCAGATCAACGCA
GAGGAAGTGGTGGTGGGAGACCTGGTGGAGGTGAAGGGTGGAGACCGCGTCCCTGCTGAC
CTCCGGATCATCTCTTCTCATGGCTGTAAGGTGGATAACTCATCCTTAACAGGAGAGTCG
GAGCCCCAGACCCGCTCCCCCGAGTTCACCCATGAGAACCCCCTGGAGACCCGCAATATC
TGTTTCTTCTCCACCAACTGTGTTGAAGGCACTGCCAGGGGCATTGTGATTGCCACAGGA
GACCGGACGGTGATGGGCCGCATAGCTACTCTCGCCTCAGGCCTGGAGGTTGGGCGGACA
CCCATAGCAATGGAGATTGAACACTTCATCCAGCTGATCACAGGGGTCGCTGTATTCCTG
GGGGTCTCCTTCTTCGTGCTCTCCCTCATCCTGGGCTACAGCTGGCTGGAGGCAGTCATC
TTCCTCATCGGCATCATAGTGGCCAACGTGCCTGAGGGGCTTCTGGCCACTGTCACTGTG
TGCCTGACCCTGACAGCCAAGCGCATGGCACGGAAGAACTGCCTGGTGAAGAACCTGGAG
GCGGTGGAGACGCTGGGCTCCACGTCCACCATCTGCTCGGACAAGACGGGCACCCTCACC
CAGAACCGCATGACCGTCGCCCACATGTGGTTCGACAACCAAATCCATGAGGCTGACACC
ACCGAAGATCAGTCTGGGGCCACTTTTGACAAACGATCCCCTACGTGGACGGCCCTGTCT
CGAATTGCTGGTCTCTGCAACCGCGCCGTCTTCAAGGCAGGACAGGAGAACATCTCCGTG
TCTAAGCGGGACACAGCTGGTGATGCCTCTGAGTCAGCTCTGCTCAAGTGCATTGAGCTC
TCCTGTGGCTCAGTGAGGAAAATGAGAGACAGAAACCCCAAGGTGGCAGAGATTCCTTTC
AACTCTACCAACAAGTACCAGCTGTCTATCCACGAGCGAGAAGACAGCCCCCAGAGCCAC
GTGCTGGTGATGAAGGGGGCCCCAGAGCGCATTCTGGACCGGTGCTCCACCATCCTGGTG
CAGGGCAAGGAGATCCCGCTCGACAAGGAGATGCAAGATGCCTTTCAAAATGCCTACATG
GAGCTGGGGGGACTTGGGGAGCGTGTGCTGGGATTCTGTCAACTGAATCTGCCATCTGGA
AAGTTTCCTCGGGGCTTCAAATTCGACACGGATGAGCTGAACTTTCCCACGGAGAAGCTT
TGCTTTGTGGGGCTCATGTCTATGATTGACCCTCCCCGGGCTGCTGTGCCAGATGCTGTG
GGCAAGTGCCGAAGCGCAGGCATCAAGGTGATCATGGTAACCGGGGATCACCCTATCACA
GCCAAGGCCATTGCCAAAGGCGTGGGCATCATATCAGAGGGTAACGAGACTGTGGAGGAC
ATTGCAGCCCGGCTCAACATTCCCATGAGTCAAGTCAACCCCAGAGAAGCCAAGGCATGC
GTGGTGCACGGCTCTGACCTGAAGGACATGACATCGGAGCAGCTCGATGAGATCCTCAAG
AACCACACAGAGATCGTCTTTGCTCGAACGTCTCCCCAGCAGAAGCTCATCATTGTGGAG
GGATGTCAGAGGCAGGGAGCCATTGTGGCCGTGACGGGTGACGGGGTGAACGACTCCCCT
GCATTGAAGAAGGCTGACATTGGCATTGCCATGGGCATCTCTGGCTCTGACGTCTCTAAG
CAGGCAGCCGACATGATCCTGCTGGATGACAACTTTGCCTCCATCGTCACGGGGGTGGAG
GAGGGCCGCCTGATCTTTGACAACTTGAAGAAATCCATCGCCTACACCCTGACCAGCAAC
ATCCCCGAGATCACCCCCTTCCTGCTGTTCATCATTGCCAACATCCCCCTACCTCTGGGC
ACTGTGACCATCCTTTGCATTGACCTGGGCACAGATATGGTCCCTGCCATCTCCTTGGCC
TATGAGGCAGCTGAGAGTGATATCATGAAGCGGCAGCCACGAAACTCCCAGACGGACAAG
CTGGTGAATGAGAGGCTCATCAGCATGGCCTACGGACAGATCGGGATGATCCAGGCACTG
GGTGGCTTCTTCACCTACTTTGTGATCCTGGCAGAGAACGGTTTCCTGCCATCACGGCTA
CTGGGAATCCGCCTCGACTGGGATGACCGGACCATGAATGATCTGGAGGACAGCTATGGA
CAGGAGTGGACCTATGAGCAGCGGAAGGTGGTGGAGTTCACGTGCCACACGGCATTCTTT
GCCAGCATCGTGGTGGTGCAGTGGGCTGACCTCATCATCTGCAAGACCCGCCGCAACTCA
GTCTTCCAGCAGGGCATGAAGAACAAGATCCTGATTTTTGGGCTCCTGGAGGAGACGGCG
TTGGCTGCCTTTCTCTCTTACTGCCCAGGCATGGGTGTAGCCCTCCGCATGTACCCGCTC
AAAGTCACCTGGTGGTTCTGCGCCTTCCCCTACAGCCTCCTCATCTTCATCTATGATGAG
GTCCGAAAGCTCATCCTGCGGCGGTATCCTGGTGGCTGGGTGGAGAAGGAGACATACTAC
TGA
Protein Properties
Number of Residues 1020
Molecular Weight 112264.385
Theoretical pI 5.651
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Sodium/potassium-transporting ATPase subunit alpha-2
MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKG
LTNQRAQDVLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAME
DEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINA
EEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNI
CFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFL
GVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLE
AVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALS
RIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPF
NSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYM
ELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAV
GKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPMSQVNPREAKAC
VVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSP
ALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSN
IPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDK
LVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTMNDLEDSYG
QEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETA
LAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
GenBank ID Protein 4502271
UniProtKB/Swiss-Prot ID P50993
UniProtKB/Swiss-Prot Entry Name AT1A2_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_000702.3
GeneCard ID ATP1A2
GenAtlas ID ATP1A2
HGNC ID HGNC:800
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
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  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed:9872452 ]
  5. 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:3035563 ]
  6. 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:3036582 ]
  7. Shull MM, Pugh DG, Lingrel JB: Characterization of the human Na,K-ATPase alpha 2 gene and identification of intragenic restriction fragment length polymorphisms. J Biol Chem. 1989 Oct 15;264(29):17532-43. [PubMed:2477373 ]
  8. Sverdlov ED, Bessarab DA, Malyshev IV, Petrukhin KE, Smirnov YuV, Ushkaryov YuA, Monastyrskaya GS, Broude NE, Modyanov NN: Family of human Na+,K+-ATPase genes. Structure of the putative regulatory region of the alpha+-gene. FEBS Lett. 1989 Feb 27;244(2):481-3. [PubMed:2537767 ]
  9. Vanmolkot KR, Kors EE, Hottenga JJ, Terwindt GM, Haan J, Hoefnagels WA, Black DF, Sandkuijl LA, Frants RR, Ferrari MD, van den Maagdenberg AM: Novel mutations in the Na+, K+-ATPase pump gene ATP1A2 associated with familial hemiplegic migraine and benign familial infantile convulsions. Ann Neurol. 2003 Sep;54(3):360-6. [PubMed:12953268 ]
  10. De Fusco M, Marconi R, Silvestri L, Atorino L, Rampoldi L, Morgante L, Ballabio A, Aridon P, Casari G: Haploinsufficiency of ATP1A2 encoding the Na+/K+ pump alpha2 subunit associated with familial hemiplegic migraine type 2. Nat Genet. 2003 Feb;33(2):192-6. Epub 2003 Jan 21. [PubMed:12539047 ]
  11. Swoboda KJ, Kanavakis E, Xaidara A, Johnson JE, Leppert MF, Schlesinger-Massart MB, Ptacek LJ, Silver K, Youroukos S: Alternating hemiplegia of childhood or familial hemiplegic migraine? A novel ATP1A2 mutation. Ann Neurol. 2004 Jun;55(6):884-7. [PubMed:15174025 ]