Sodium/potassium-transporting ATPase subunit alpha-2
Details
- Name
- Sodium/potassium-transporting ATPase subunit alpha-2
- Synonyms
- 3.6.3.9
- KIAA0778
- Na(+)/K(+) ATPase alpha-2 subunit
- Sodium pump subunit alpha-2
- Gene Name
- ATP1A2
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0008801|Sodium/potassium-transporting ATPase subunit alpha-2 MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKG LTNQRAQDVLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAME DEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINA EEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNI CFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFL GVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLE AVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALS RIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPF NSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYM ELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAV GKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPMSQVNPREAKAC VVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSP ALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSN IPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDK LVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTMNDLEDSYG QEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETA LAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
- Number of residues
- 1020
- Molecular Weight
- 112264.385
- Theoretical pI
- Not Available
- GO Classification
- FunctionsATP binding / chaperone binding / metal ion binding / sodium / steroid hormone bindingProcessesadult locomotory behavior / ATP hydrolysis coupled proton transport / ATP metabolic process / cardiac muscle contraction / cell communication by electrical coupling involved in cardiac conduction / cellular potassium ion homeostasis / cellular response to mechanical stimulus / cellular response to steroid hormone stimulus / cellular sodium ion homeostasis / establishment or maintenance of transmembrane electrochemical gradient / ion transmembrane transport / locomotion / membrane depolarization during cardiac muscle cell action potential / membrane repolarization / negative regulation of calcium / negative regulation of calcium ion transmembrane transport / negative regulation of cytosolic calcium ion concentration / negative regulation of heart contraction / negative regulation of striated muscle contraction / neurotransmitter uptake / potassium ion import / potassium ion import across plasma membrane / potassium ion transport / regulation of blood pressure / regulation of cardiac muscle cell contraction / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / regulation of glutamate uptake involved in transmission of nerve impulse / regulation of respiratory gaseous exchange by neurological system process / regulation of smooth muscle contraction / regulation of striated muscle contraction / regulation of synaptic transmission, glutamatergic / regulation of the force of heart contraction / regulation of vasoconstriction / relaxation of cardiac muscle / response to glycoside / response to nicotine / sodium ion export from cell / sodium ion transport / transmembrane transport / visual learningComponentscaveola / cytoplasm / cytosol / dendritic spine / endosome / extracellular vesicle / intercalated disc / intracellular membrane-bounded organelle / membrane / myelin sheath / plasma membrane / sodium / T-tubule
- General Function
- Steroid hormone 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.
- Pfam Domain Function
- Transmembrane Regions
- 86-106 130-150 287-306 319-336 770-789 800-820 841-863 916-935 949-967 983-1003
- Cellular Location
- Membrane
- Gene sequence
>lcl|BSEQ0013423|Sodium/potassium-transporting ATPase subunit alpha-2 (ATP1A2) 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
- Chromosome Location
- 1
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P50993 UniProtKB Entry Name AT1A2_HUMAN HGNC ID HGNC:800 - General References
- 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. [Article]
- 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. [Article]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- Hundal HS, Maxwell DL, Ahmed A, Darakhshan F, Mitsumoto Y, Klip A: Subcellular distribution and immunocytochemical localization of Na,K-ATPase subunit isoforms in human skeletal muscle. Mol Membr Biol. 1994 Oct-Dec;11(4):255-62. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- De Sanctis S, Grieco GS, Breda L, Casali C, Nozzi M, Del Torto M, Chiarelli F, Verrotti A: Prolonged sporadic hemiplegic migraine associated with a novel de novo missense ATP1A2 gene mutation. Headache. 2011 Mar;51(3):447-50. doi: 10.1111/j.1526-4610.2010.01793.x. Epub 2010 Nov 4. [Article]
- Pisano T, Spiller S, Mei D, Guerrini R, Cianchetti C, Friedrich T, Pruna D: Functional characterization of a novel C-terminal ATP1A2 mutation causing hemiplegic migraine and epilepsy. Cephalalgia. 2013 Dec;33(16):1302-10. doi: 10.1177/0333102413495116. Epub 2013 Jul 9. [Article]
- Costa C, Prontera P, Sarchielli P, Tonelli A, Bassi MT, Cupini LM, Caproni S, Siliquini S, Donti E, Calabresi P: A novel ATP1A2 gene mutation in familial hemiplegic migraine and epilepsy. Cephalalgia. 2014 Jan;34(1):68-72. doi: 10.1177/0333102413498941. Epub 2013 Aug 5. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01092 Ouabain approved unknown inhibitor Details DB09479 Rubidium Rb-82 approved, investigational no substrate Details DB09020 Bisacodyl approved unknown inhibitor Details DB16690 Tegoprazan investigational yes inhibitor Details DB01250 Olsalazine approved unknown inhibitor Details