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Sodium/potassium-transporting ATPase subunit alpha-2 (Na( )/K( ) ATPase alpha-2 subunit) (EC 3.6.3.9) (Sodium pump subunit alpha-2)

 AT1A2_HUMAN             Reviewed;        1020 AA.
P50993; D3DVE4; Q07059; Q5JW74; Q86UZ5; Q9UQ25;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 183.
RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-2;
Short=Na(+)/K(+) ATPase alpha-2 subunit;
EC=3.6.3.9;
AltName: Full=Sodium pump subunit alpha-2;
Flags: Precursor;
Name=ATP1A2; Synonyms=KIAA0778;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2477373;
Shull M.M., Pugh D.G., Lingrel J.B.;
"Characterization of the human Na,K-ATPase alpha 2 gene and
identification of intragenic restriction fragment length
polymorphisms.";
J. Biol. Chem. 264:17532-17543(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
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. 5:277-286(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 211-249.
TISSUE=Leukocyte;
PubMed=3035563; DOI=10.1073/pnas.84.12.4039;
Shull M.M., Lingrel J.B.;
"Multiple genes encode the human Na+,K+-ATPase catalytic subunit.";
Proc. Natl. Acad. Sci. U.S.A. 84:4039-4043(1987).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 251-442.
TISSUE=Brain, and Placenta;
PubMed=3036582; DOI=10.1016/0014-5793(87)80677-4;
Sverdlov E.D., Monastyrskaya G.S., Broude N.E., Ushkaryov Y.A.,
Allikmets R.L., Melkov A.M., Smirnov Y.V., Malyshev I.V.,
Dulubova I.E., Petrukhin K.E., Gryshin A.V., Kiyatkin N.I.,
Kostina M.B., Sverdlov V.E., Modyanov N.N., Ovchinnikov Y.A.;
"The family of human Na+,K+-ATPase genes. No less than five genes
and/or pseudogenes related to the alpha-subunit.";
FEBS Lett. 217:275-278(1987).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-4.
PubMed=2537767; DOI=10.1016/0014-5793(89)80588-5;
Sverdlov E.D., Bessarab D.A., Malyshev I.V., Petrukhin K.E.,
Smirnov Y.V., Ushkaryov Y.A., Monastyrskaya G.S., Broude N.E.,
Modyanov N.N.;
"Family of human Na+,K+-ATPase genes. Structure of the putative
regulatory region of the alpha+-gene.";
FEBS Lett. 244:481-483(1989).
[9]
SUBCELLULAR LOCATION.
PubMed=7711835; DOI=10.3109/09687689409160435;
Hundal H.S., Maxwell D.L., 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. 11:255-262(1994).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-570 AND SER-587, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
VARIANTS FHM2 GLN-689 AND THR-731.
PubMed=12953268; DOI=10.1002/ana.10674;
Vanmolkot K.R.J., Kors E.E., Hottenga J.-J., Terwindt G.M., Haan J.,
Hoefnagels W.A.J., Black D.F., Sandkuijl L.A., Frants R.R.,
Ferrari M.D., van den Maagdenberg A.M.J.M.;
"Novel mutations in the Na+, K+-ATPase pump gene ATP1A2 associated
with familial hemiplegic migraine and benign familial infantile
convulsions.";
Ann. Neurol. 54:360-366(2003).
[12]
VARIANTS FHM2 PRO-764 AND ARG-887, AND CHARACTERIZATION OF VARIANTS
FMH2 PRO-764 AND ARG-887.
PubMed=12539047; DOI=10.1038/ng1081;
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. 33:192-196(2003).
[13]
VARIANT AHC1 ASN-378.
PubMed=15174025; DOI=10.1002/ana.20134;
Swoboda K.J., Kanavakis E., Xaidara A., Johnson J.E., Leppert M.F.,
Schlesinger-Massart M.B., Ptacek L.J., Silver K., Youroukos S.;
"Alternating hemiplegia of childhood or familial hemiplegic migraine?
A novel ATP1A2 mutation.";
Ann. Neurol. 55:884-887(2004).
[14]
VARIANT FHM2 ARG-715.
PubMed=21352219; DOI=10.1111/j.1526-4610.2010.01793.x;
De Sanctis S., Grieco G.S., 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 51:447-450(2011).
[15]
VARIANT FHM2 TRP-1007.
PubMed=23838748; DOI=10.1177/0333102413495116;
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 33:1302-1310(2013).
[16]
VARIANT FHM2 SER-874.
PubMed=23918834; DOI=10.1177/0333102413498941;
Costa C., Prontera P., Sarchielli P., Tonelli A., Bassi M.T.,
Cupini L.M., Caproni S., Siliquini S., Donti E., Calabresi P.;
"A novel ATP1A2 gene mutation in familial hemiplegic migraine and
epilepsy.";
Cephalalgia 34:68-72(2014).
[17]
VARIANTS ALA-366 AND TRP-593.
PubMed=27864847; DOI=10.1002/humu.23149;
Clinical Study Group;
Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D.,
Bigoni S., Barba C., Mari F., Montomoli M., Pisano T., Rosati A.,
Guerrini R.;
"Diagnostic targeted resequencing in 349 patients with drug-resistant
pediatric epilepsies identifies causative mutations in 30 different
genes.";
Hum. Mutat. 38:216-225(2017).
-!- 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.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Na(+)(In) + K(+)(Out) = ADP +
phosphate + Na(+)(Out) + K(+)(In).
-!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
catalytic alpha subunit, an auxiliary non-catalytic beta subunit
and an additional regulatory subunit. Interacts with regulatory
subunit FXYD1. {ECO:0000250|UniProtKB:A2VDL6}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7711835};
Multi-pass membrane protein {ECO:0000269|PubMed:7711835}. Cell
membrane {ECO:0000269|PubMed:7711835}; Multi-pass membrane protein
{ECO:0000269|PubMed:7711835}.
-!- DISEASE: Migraine, familial hemiplegic, 2 (FHM2) [MIM:602481]: A
subtype of migraine with aura associated with hemiparesis in some
families. Migraine is a disabling symptom complex of periodic
headaches, usually temporal and unilateral. Headaches are often
accompanied by irritability, nausea, vomiting and photophobia,
preceded by constriction of the cranial arteries. Migraine with
aura is characterized by recurrent attacks of reversible
neurological symptoms (aura) that precede or accompany the
headache. Aura may include a combination of sensory disturbances,
such as blurred vision, hallucinations, vertigo, numbness and
difficulty in concentrating and speaking.
{ECO:0000269|PubMed:12539047, ECO:0000269|PubMed:12953268,
ECO:0000269|PubMed:21352219, ECO:0000269|PubMed:23838748,
ECO:0000269|PubMed:23918834}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Alternating hemiplegia of childhood 1 (AHC1)
[MIM:104290]: A rare syndrome of episodic hemi- or quadriplegia
lasting minutes to days. Most cases are accompanied by dystonic
posturing, choreoathetoid movements, nystagmus, other ocular motor
abnormalities, autonomic disturbances, and progressive cognitive
impairment. It is typically distinguished from familial hemiplegic
migraine by infantile onset and high prevalence of associated
neurological deficits that become increasingly obvious with age.
{ECO:0000269|PubMed:15174025}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIC subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA34498.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; J05096; AAA51797.1; -; Genomic_DNA.
EMBL; AB018321; BAA34498.2; ALT_INIT; mRNA.
EMBL; AL121987; CAI15271.1; -; Genomic_DNA.
EMBL; CH471121; EAW52740.1; -; Genomic_DNA.
EMBL; CH471121; EAW52741.1; -; Genomic_DNA.
EMBL; BC052271; AAH52271.2; -; mRNA.
EMBL; M16795; AAA51799.1; -; mRNA.
EMBL; M27578; AAA35575.1; -; Genomic_DNA.
EMBL; M27571; AAA35575.1; JOINED; Genomic_DNA.
EMBL; M27576; AAA35575.1; JOINED; Genomic_DNA.
EMBL; Y07494; CAA68793.1; ALT_SEQ; mRNA.
CCDS; CCDS1196.1; -.
PIR; A34474; A34474.
RefSeq; NP_000693.1; NM_000702.3.
UniGene; Hs.34114; -.
ProteinModelPortal; P50993; -.
SMR; P50993; -.
BioGrid; 106967; 20.
IntAct; P50993; 2.
STRING; 9606.ENSP00000354490; -.
ChEMBL; CHEMBL2095186; -.
DrugBank; DB09479; Rubidium chloride Rb-82.
TCDB; 3.A.3.1.1; the p-type atpase (p-atpase) superfamily.
iPTMnet; P50993; -.
PhosphoSitePlus; P50993; -.
SwissPalm; P50993; -.
BioMuta; ATP1A2; -.
DMDM; 1703467; -.
EPD; P50993; -.
MaxQB; P50993; -.
PaxDb; P50993; -.
PeptideAtlas; P50993; -.
PRIDE; P50993; -.
Ensembl; ENST00000361216; ENSP00000354490; ENSG00000018625.
GeneID; 477; -.
KEGG; hsa:477; -.
UCSC; uc001fvc.4; human.
CTD; 477; -.
DisGeNET; 477; -.
EuPathDB; HostDB:ENSG00000018625.14; -.
GeneCards; ATP1A2; -.
GeneReviews; ATP1A2; -.
HGNC; HGNC:800; ATP1A2.
HPA; CAB022230; -.
MalaCards; ATP1A2; -.
MIM; 104290; phenotype.
MIM; 182340; gene.
MIM; 602481; phenotype.
neXtProt; NX_P50993; -.
OpenTargets; ENSG00000018625; -.
Orphanet; 2131; Alternating hemiplegia of childhood.
Orphanet; 569; Familial or sporadic hemiplegic migraine.
PharmGKB; PA30796; -.
eggNOG; KOG0203; Eukaryota.
eggNOG; COG0474; LUCA.
GeneTree; ENSGT00890000139334; -.
HOGENOM; HOG000265622; -.
HOVERGEN; HBG004298; -.
InParanoid; P50993; -.
KO; K01539; -.
OMA; CVVAFIP; -.
OrthoDB; EOG091G01BB; -.
PhylomeDB; P50993; -.
TreeFam; TF312838; -.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
ChiTaRS; ATP1A2; human.
GeneWiki; ATP1A2; -.
GenomeRNAi; 477; -.
PRO; PR:P50993; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000018625; -.
CleanEx; HS_ATP1A2; -.
ExpressionAtlas; P50993; baseline and differential.
Genevisible; P50993; HS.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
GO; GO:0030315; C:T-tubule; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; IDA:BHF-UCL.
GO; GO:1990239; F:steroid hormone binding; IDA:BHF-UCL.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:Ensembl.
GO; GO:0046034; P:ATP metabolic process; IMP:BHF-UCL.
GO; GO:0060048; P:cardiac muscle contraction; TAS:BHF-UCL.
GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; TAS:BHF-UCL.
GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:BHF-UCL.
GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0040011; P:locomotion; IEA:Ensembl.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; TAS:BHF-UCL.
GO; GO:0086009; P:membrane repolarization; TAS:BHF-UCL.
GO; GO:1903170; P:negative regulation of calcium ion transmembrane transport; ISS:BHF-UCL.
GO; GO:1903280; P:negative regulation of calcium:sodium antiporter activity; ISS:BHF-UCL.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
GO; GO:0045988; P:negative regulation of striated muscle contraction; IEA:Ensembl.
GO; GO:0001504; P:neurotransmitter uptake; IEA:Ensembl.
GO; GO:0010107; P:potassium ion import; IDA:BHF-UCL.
GO; GO:1990573; P:potassium ion import across plasma membrane; IC:BHF-UCL.
GO; GO:0006813; P:potassium ion transport; NAS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IEA:Ensembl.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; TAS:BHF-UCL.
GO; GO:0051946; P:regulation of glutamate uptake involved in transmission of nerve impulse; NAS:BHF-UCL.
GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IEA:Ensembl.
GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0006942; P:regulation of striated muscle contraction; NAS:UniProtKB.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; NAS:BHF-UCL.
GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
GO; GO:0019229; P:regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0055119; P:relaxation of cardiac muscle; TAS:BHF-UCL.
GO; GO:1903416; P:response to glycoside; ISS:BHF-UCL.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0036376; P:sodium ion export from cell; IDA:BHF-UCL.
GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
CDD; cd02608; P-type_ATPase_Na-K_like; 1.
Gene3D; 3.40.1110.10; -; 2.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_domN.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR005775; P-type_ATPase_IIC.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Disease mutation;
Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport;
Reference proteome; Sodium; Sodium transport;
Sodium/potassium transport; Transmembrane; Transmembrane helix;
Transport.
PROPEP 1 5 {ECO:0000250}.
/FTId=PRO_0000002503.
CHAIN 6 1020 Sodium/potassium-transporting ATPase
subunit alpha-2.
/FTId=PRO_0000002504.
TOPO_DOM 6 85 Cytoplasmic. {ECO:0000255}.
TRANSMEM 86 106 Helical. {ECO:0000255}.
TOPO_DOM 107 129 Extracellular. {ECO:0000255}.
TRANSMEM 130 150 Helical. {ECO:0000255}.
TOPO_DOM 151 286 Cytoplasmic. {ECO:0000255}.
TRANSMEM 287 306 Helical. {ECO:0000255}.
TOPO_DOM 307 318 Extracellular. {ECO:0000255}.
TRANSMEM 319 336 Helical. {ECO:0000255}.
TOPO_DOM 337 769 Cytoplasmic. {ECO:0000255}.
TRANSMEM 770 789 Helical. {ECO:0000255}.
TOPO_DOM 790 799 Extracellular. {ECO:0000255}.
TRANSMEM 800 820 Helical. {ECO:0000255}.
TOPO_DOM 821 840 Cytoplasmic. {ECO:0000255}.
TRANSMEM 841 863 Helical. {ECO:0000255}.
TOPO_DOM 864 915 Extracellular. {ECO:0000255}.
TRANSMEM 916 935 Helical. {ECO:0000255}.
TOPO_DOM 936 948 Cytoplasmic. {ECO:0000255}.
TRANSMEM 949 967 Helical. {ECO:0000255}.
TOPO_DOM 968 982 Extracellular. {ECO:0000255}.
TRANSMEM 983 1003 Helical. {ECO:0000255}.
TOPO_DOM 1004 1020 Cytoplasmic. {ECO:0000255}.
REGION 80 82 Interaction with phosphoinositide-3
kinase. {ECO:0000250}.
ACT_SITE 374 374 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 714 714 Magnesium. {ECO:0000250}.
METAL 718 718 Magnesium. {ECO:0000250}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PIE5}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000250|UniProtKB:P06686}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PIE5}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000250|UniProtKB:P06686}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PIE5}.
MOD_RES 570 570 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 587 587 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 672 672 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PIE5}.
MOD_RES 940 940 Phosphoserine; by PKA. {ECO:0000250}.
VARIANT 366 366 G -> A (probable disease-associated
mutation found in a patient with early
infantile epileptic encephalopathy).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078231.
VARIANT 378 378 T -> N (in AHC1; dbSNP:rs28934002).
{ECO:0000269|PubMed:15174025}.
/FTId=VAR_019934.
VARIANT 593 593 R -> W (found in a patient with early
infantile epileptic encephalopathy;
unknown pathological significance).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078232.
VARIANT 689 689 R -> Q (in FHM2; dbSNP:rs28933401).
{ECO:0000269|PubMed:12953268}.
/FTId=VAR_019935.
VARIANT 715 715 G -> R (in FHM2; de novo mutation in a
sporadic case).
{ECO:0000269|PubMed:21352219}.
/FTId=VAR_065685.
VARIANT 731 731 M -> T (in FHM2; dbSNP:rs28933400).
{ECO:0000269|PubMed:12953268}.
/FTId=VAR_019936.
VARIANT 764 764 L -> P (in FHM2; loss of function;
dbSNP:rs28933398).
{ECO:0000269|PubMed:12539047}.
/FTId=VAR_019937.
VARIANT 874 874 G -> S (in FHM2; some patients exhibit a
clinical overlap between migraine and
epilepsy). {ECO:0000269|PubMed:23918834}.
/FTId=VAR_069991.
VARIANT 887 887 W -> R (in FHM2; loss of function;
dbSNP:rs28933399).
{ECO:0000269|PubMed:12539047}.
/FTId=VAR_019938.
VARIANT 1007 1007 R -> W (in FHM2; some patients exhibit a
clinical overlap between migraine and
epilepsy). {ECO:0000269|PubMed:23838748}.
/FTId=VAR_069992.
SEQUENCE 1020 AA; 112265 MW; AFBD8EA94FFB4FC3 CRC64;
MGRGAGREYS PAATTAENGG GKKKQKEKEL DELKKEVAMD DHKLSLDELG RKYQVDLSKG
LTNQRAQDVL ARDGPNALTP PPTTPEWVKF CRQLFGGFSI LLWIGAILCF LAYGIQAAME
DEPSNDNLYL GVVLAAVVIV TGCFSYYQEA KSSKIMDSFK NMVPQQALVI REGEKMQINA
EEVVVGDLVE VKGGDRVPAD LRIISSHGCK VDNSSLTGES EPQTRSPEFT HENPLETRNI
CFFSTNCVEG TARGIVIATG DRTVMGRIAT LASGLEVGRT PIAMEIEHFI QLITGVAVFL
GVSFFVLSLI LGYSWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE
AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TEDQSGATFD KRSPTWTALS
RIAGLCNRAV FKAGQENISV SKRDTAGDAS ESALLKCIEL SCGSVRKMRD RNPKVAEIPF
NSTNKYQLSI HEREDSPQSH VLVMKGAPER ILDRCSTILV QGKEIPLDKE MQDAFQNAYM
ELGGLGERVL GFCQLNLPSG KFPRGFKFDT DELNFPTEKL CFVGLMSMID PPRAAVPDAV
GKCRSAGIKV IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPMS QVNPREAKAC
VVHGSDLKDM TSEQLDEILK NHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP
ALKKADIGIA MGISGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN
IPEITPFLLF IIANIPLPLG TVTILCIDLG TDMVPAISLA YEAAESDIMK RQPRNSQTDK
LVNERLISMA YGQIGMIQAL GGFFTYFVIL AENGFLPSRL LGIRLDWDDR TMNDLEDSYG
QEWTYEQRKV VEFTCHTAFF ASIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLLEETA
LAAFLSYCPG MGVALRMYPL KVTWWFCAFP YSLLIFIYDE VRKLILRRYP GGWVEKETYY


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