Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Sodium/potassium-transporting ATPase subunit alpha-3 (Na( )/K( ) ATPase alpha-3 subunit) (EC 3.6.3.9) (Na( )/K( ) ATPase alpha(III) subunit) (Sodium pump subunit alpha-3)

 AT1A3_HUMAN             Reviewed;        1013 AA.
P13637; B7Z2T0; B7Z401; F5H6J6; Q16732; Q16735; Q969K5;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
22-NOV-2017, entry version 199.
RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-3;
Short=Na(+)/K(+) ATPase alpha-3 subunit;
EC=3.6.3.9;
AltName: Full=Na(+)/K(+) ATPase alpha(III) subunit;
AltName: Full=Sodium pump subunit alpha-3;
Name=ATP1A3;
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] (ISOFORM 1).
PubMed=2838329; DOI=10.1016/0014-5793(88)81361-9;
Ovchinnikov Y.A., Monastyrskaya G.S., Broude N.E., Ushkaryov Y.A.,
Melkov A.M., Smirnov Y.V., Malyshev I.V., Allikmets R.L.,
Kostina M.B., Dulubova I.E., Kiyatkin N.I., Grishin A.V.,
Modyanov N.N., Sverdlov E.D.;
"Family of human Na+, K+-ATPase genes. Structure of the gene for the
catalytic subunit (alpha III-form) and its relationship with
structural features of the protein.";
FEBS Lett. 233:87-94(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=2834163;
Sverdlov E.D., Monastyrskaya G.S., Broude N.E., Ushkarev Y.A.,
Melkov A.M., Smirnov Y.V., Malyshev I.V., Allikmets R.L.,
Kostina M.B., Dulubova I.E., Kiyatkin N.I., Grishin A.V.,
Modyanov N.N., Ovchinnikov Y.A.;
"Family of human Na(+),K(+)-ATPase genes. Structure of the gene of
isoform alpha-III.";
Dokl. Akad. Nauk SSSR 297:1488-1494(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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 [GENOMIC DNA] OF 120-387; 494-538 AND 545-1013.
PubMed=3030810; DOI=10.1016/0014-5793(87)81467-9;
Ovchinnikov Y.A., Monastyrskaya G.S., Broude N.E., Allikmets R.L.,
Ushkaryov Y.A., Melkov A.M., Smirnov Y.V., Malyshev I.V.,
Dulubova I.E., Petrukhin K.E., Gryshin A.V., Sverdlov V.E.,
Kiyatkin N.I., Kostina M.B., Modyanov N.N., Sverdlov E.D.;
"The family of human Na+,K+-ATPase genes. A partial nucleotide
sequence related to the alpha-subunit.";
FEBS Lett. 213:73-80(1987).
[7]
ERRATUM.
Ovchinnikov Y.A., Monastyrskaya G.S., Broude N.E., Allikmets R.L.,
Ushkaryov Y.A., Melkov A.M., Smirnov Y.V., Malyshev I.V.,
Dulubova I.E., Petrukhin K.E., Gryshin A.V., Sverdlov V.E.,
Kiyatkin N.I., Kostina M.B., Modyanov N.N., Sverdlov E.D.;
FEBS Lett. 214:375-375(1987).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 243-434.
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).
[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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
VARIANTS DYT12 THR-274; LYS-277; MET-613; SER-758; LEU-780 AND
TYR-801.
PubMed=15260953; DOI=10.1016/j.neuron.2004.06.028;
de Carvalho Aguiar P., Sweadner K.J., Penniston J.T., Zaremba J.,
Liu L., Caton M., Linazasoro G., Borg M., Tijssen M.A.J.,
Bressman S.B., Dobyns W.B., Brashear A., Ozelius L.J.;
"Mutations in the Na(+)/K(+)-ATPase alpha-3 gene ATP1A3 are associated
with rapid-onset dystonia parkinsonism.";
Neuron 43:169-175(2004).
[12]
VARIANT DYT12 TYR-1013 EXT, AND CHARACTERIZATION OF VARIANT DYT12
TYR-1013 EXT.
PubMed=19351654; DOI=10.1093/hmg/ddp170;
Blanco-Arias P., Einholm A.P., Mamsa H., Concheiro C.,
Gutierrez-de-Teran H., Romero J., Toustrup-Jensen M.S., Carracedo A.,
Jen J.C., Vilsen B., Sobrido M.J.;
"A C-terminal mutation of ATP1A3 underscores the crucial role of
sodium affinity in the pathophysiology of rapid-onset dystonia-
parkinsonism.";
Hum. Mol. Genet. 18:2370-2377(2009).
[13]
VARIANT DYT12 ASN-923.
PubMed=19652145; DOI=10.1212/WNL.0b013e3181b04acd;
Anselm I.A., Sweadner K.J., Gollamudi S., Ozelius L.J., Darras B.T.;
"Rapid-onset dystonia-parkinsonism in a child with a novel atp1a3 gene
mutation.";
Neurology 73:400-401(2009).
[14]
VARIANTS AHC2 ASN-274; ASP-322; PRO-371; CYS-755; ARG-772; ILE-773;
ASN-801; LYS-815 AND TYR-923.
PubMed=22850527; DOI=10.1016/S1474-4422(12)70182-5;
Rosewich H., Thiele H., Ohlenbusch A., Maschke U., Altmuller J.,
Frommolt P., Zirn B., Ebinger F., Siemes H., Nurnberg P.,
Brockmann K., Gartner J.;
"Heterozygous de-novo mutations in ATP1A3 in patients with alternating
hemiplegia of childhood: a whole-exome sequencing gene-identification
study.";
Lancet Neurol. 11:764-773(2012).
[15]
VARIANTS AHC2 TYR-137; PHE-137; LEU-140; ASN-220; ASN-274; PHE-333;
SER-755; SER-773; ASN-801; ARG-806; SER-810; PRO-811; LYS-815; VAL-919
DEL; ARG-947; ASP-955 AND TYR-992, AND CHARACTERIZATION OF VARIANTS
AHC2 ASN-801; PRO-811 AND LYS-815.
PubMed=22842232; DOI=10.1038/ng.2358;
Heinzen E.L., Swoboda K.J., Hitomi Y., Gurrieri F., Nicole S.,
de Vries B., Tiziano F.D., Fontaine B., Walley N.M., Heavin S.,
Panagiotakaki E., Neri G., Koelewijn S., Kamphorst J.,
Geilenkirchen M., Pelzer N., Laan L., Haan J., Ferrari M.,
van den Maagdenberg A.M., Zucca C., Bassi M.T., Franchini F.,
Vavassori R., Giannotta M., Gobbi G., Granata T., Nardocci N.,
De Grandis E., Veneselli E., Stagnaro M., Vigevano F., Oechsler C.,
Arzimanoglou A., Ninan M., Neville B., Ebinger F., Fons C.,
Campistol J., Kemlink D., Nevsimalova S., Peeters-Scholte C.,
Casaer P., Casari G., Sange G., Spiel G., Martinelli Boneschi F.,
Schyns T., Crawley F., Poncelin D., Fiori S., Abiusi E., Di Pietro L.,
Sweney M.T., Newcomb T.M., Viollet L., Huff C., Jorde L.B.,
Reyna S.P., Murphy K.J., Shianna K.V., Gumbs C.E., Little L.,
Silver K., Ptacek L.J., Ferrari M.D., Bye A.M., Herkes G.K.,
Whitelaw C.M., Webb D., Lynch B.J., Uldall P., King M.D.,
Scheffer I.E., Sisodiya S.M., Mikati M.A., Goldstein D.B.;
"De novo mutations in ATP1A3 cause alternating hemiplegia of
childhood.";
Nat. Genet. 44:1030-1034(2012).
[16]
VARIANTS AHC2 CYS-755; ASN-801 AND LYS-815.
PubMed=23409136; DOI=10.1371/journal.pone.0056120;
Ishii A., Saito Y., Mitsui J., Ishiura H., Yoshimura J., Arai H.,
Yamashita S., Kimura S., Oguni H., Morishita S., Tsuji S., Sasaki M.,
Hirose S.;
"Identification of ATP1A3 mutations by exome sequencing as the cause
of alternating hemiplegia of childhood in Japanese patients.";
PLoS ONE 8:E56120-E56120(2013).
[17]
INVOLVEMENT IN CAPOS, AND VARIANT CAPOS LYS-818.
PubMed=24468074; DOI=10.1186/1750-1172-9-15;
Demos M.K., van Karnebeek C.D., Ross C.J., Adam S., Shen Y.,
Zhan S.H., Shyr C., Horvath G., Suri M., Fryer A., Jones S.J.,
Friedman J.M.;
"A novel recurrent mutation in ATP1A3 causes CAPOS syndrome.";
Orphanet J. Rare Dis. 9:15-15(2014).
[18]
VARIANT THR-320, AND VARIANT AHC2 ARG-947.
PubMed=26993267; DOI=10.1136/jmedgenet-2015-103263;
Trump N., McTague A., Brittain H., Papandreou A., Meyer E., Ngoh A.,
Palmer R., Morrogh D., Boustred C., Hurst J.A., Jenkins L.,
Kurian M.A., Scott R.H.;
"Improving diagnosis and broadening the phenotypes in early-onset
seizure and severe developmental delay disorders through gene panel
analysis.";
J. Med. Genet. 53:310-317(2016).
-!- 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.
-!- 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:P06687}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7711835};
Multi-pass membrane protein {ECO:0000269|PubMed:7711835}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P13637-1; Sequence=Displayed;
Name=2;
IsoId=P13637-2; Sequence=VSP_046956;
Name=3;
IsoId=P13637-3; Sequence=VSP_046957;
-!- DISEASE: Dystonia 12 (DYT12) [MIM:128235]: An autosomal dominant
dystonia-parkinsonism disorder. Dystonia is defined by the
presence of sustained involuntary muscle contractions, often
leading to abnormal postures. DYT12 patients develop dystonia and
parkinsonism between 15 and 45 years of age. The disease is
characterized by an unusually rapid evolution of signs and
symptoms. The sudden onset of symptoms over hours to a few weeks,
often associated with physical or emotional stress, suggests a
trigger initiating a nervous system insult resulting in permanent
neurologic disability. {ECO:0000269|PubMed:15260953,
ECO:0000269|PubMed:19351654, ECO:0000269|PubMed:19652145}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Alternating hemiplegia of childhood 2 (AHC2)
[MIM:614820]: 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:22842232, ECO:0000269|PubMed:22850527,
ECO:0000269|PubMed:23409136, ECO:0000269|PubMed:26993267}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Cerebellar ataxia, areflexia, pes cavus, optic atrophy,
and sensorineural hearing loss (CAPOS) [MIM:601338]: An autosomal
dominant neurologic disorder characterized by relapsing and
partially remitting, early-onset cerebellar ataxia following a
febrile illness. Other features include progressive optic atrophy
and sensorineural hearing loss, generalized hypotonia, areflexia
and pes cavus without evidence of a peripheral neuropathy on
neurophysiological studies. {ECO:0000269|PubMed:24468074}.
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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M37457; AAA51798.1; -; Genomic_DNA.
EMBL; M37436; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37437; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37438; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37462; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37439; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37440; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37441; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37442; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37443; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37444; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37445; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37447; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37448; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37449; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37450; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37451; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37452; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37453; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37454; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37455; AAA51798.1; JOINED; Genomic_DNA.
EMBL; M37456; AAA51798.1; JOINED; Genomic_DNA.
EMBL; X12910; CAA31390.1; -; Genomic_DNA.
EMBL; X12911; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12912; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12913; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12914; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12915; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12916; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12917; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12919; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12920; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12921; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12922; CAA31390.1; JOINED; Genomic_DNA.
EMBL; X12923; CAA31390.1; JOINED; Genomic_DNA.
EMBL; AK295078; BAH11966.1; -; mRNA.
EMBL; AK296557; BAH12387.1; -; mRNA.
EMBL; AC010616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009282; AAH09282.1; -; mRNA.
EMBL; BC009394; AAH09394.1; -; mRNA.
EMBL; BC015566; AAH15566.1; -; mRNA.
EMBL; M28286; AAA52285.1; -; Genomic_DNA.
EMBL; M28284; AAA52285.1; JOINED; Genomic_DNA.
EMBL; M28285; AAA52285.1; JOINED; Genomic_DNA.
EMBL; M28293; AAA52286.1; -; Genomic_DNA.
EMBL; M28287; AAA52286.1; JOINED; Genomic_DNA.
EMBL; M35821; AAA52286.1; JOINED; Genomic_DNA.
EMBL; M35822; AAA52286.1; JOINED; Genomic_DNA.
EMBL; M28289; AAA52286.1; JOINED; Genomic_DNA.
EMBL; M28290; AAA52286.1; JOINED; Genomic_DNA.
EMBL; M28291; AAA52286.1; JOINED; Genomic_DNA.
EMBL; M28292; AAA52286.1; JOINED; Genomic_DNA.
EMBL; M27577; AAA58380.1; -; Genomic_DNA.
EMBL; M27570; AAA58380.1; JOINED; Genomic_DNA.
EMBL; M27573; AAA58380.1; JOINED; Genomic_DNA.
CCDS; CCDS12594.1; -. [P13637-1]
CCDS; CCDS58663.1; -. [P13637-2]
CCDS; CCDS58664.1; -. [P13637-3]
PIR; S00801; S00801.
RefSeq; NP_001243142.1; NM_001256213.1. [P13637-2]
RefSeq; NP_001243143.1; NM_001256214.1. [P13637-3]
RefSeq; NP_689509.1; NM_152296.4. [P13637-1]
UniGene; Hs.515427; -.
ProteinModelPortal; P13637; -.
SMR; P13637; -.
BioGrid; 106968; 47.
IntAct; P13637; 6.
MINT; MINT-2857038; -.
STRING; 9606.ENSP00000302397; -.
ChEMBL; CHEMBL2095186; -.
DrugBank; DB09479; Rubidium chloride Rb-82.
TCDB; 3.A.3.1.1; the p-type atpase (p-atpase) superfamily.
iPTMnet; P13637; -.
PhosphoSitePlus; P13637; -.
SwissPalm; P13637; -.
BioMuta; ATP1A3; -.
DMDM; 116241260; -.
EPD; P13637; -.
MaxQB; P13637; -.
PaxDb; P13637; -.
PeptideAtlas; P13637; -.
PRIDE; P13637; -.
Ensembl; ENST00000302102; ENSP00000302397; ENSG00000105409. [P13637-1]
Ensembl; ENST00000543770; ENSP00000437577; ENSG00000105409. [P13637-2]
Ensembl; ENST00000545399; ENSP00000444688; ENSG00000105409. [P13637-3]
GeneID; 478; -.
KEGG; hsa:478; -.
UCSC; uc002osg.4; human. [P13637-1]
CTD; 478; -.
DisGeNET; 478; -.
EuPathDB; HostDB:ENSG00000105409.15; -.
GeneCards; ATP1A3; -.
GeneReviews; ATP1A3; -.
HGNC; HGNC:801; ATP1A3.
HPA; CAB033630; -.
HPA; HPA045367; -.
HPA; HPA056446; -.
MalaCards; ATP1A3; -.
MIM; 128235; phenotype.
MIM; 182350; gene.
MIM; 601338; phenotype.
MIM; 614820; phenotype.
neXtProt; NX_P13637; -.
OpenTargets; ENSG00000105409; -.
Orphanet; 2131; Alternating hemiplegia of childhood.
Orphanet; 1171; Cerebellar ataxia - areflexia - pes cavus - optic atrophy - sensorineural hearing loss.
Orphanet; 71517; Rapid-onset dystonia-parkinsonism.
PharmGKB; PA64; -.
eggNOG; KOG0203; Eukaryota.
eggNOG; COG0474; LUCA.
GeneTree; ENSGT00890000139334; -.
HOGENOM; HOG000265622; -.
HOVERGEN; HBG004298; -.
InParanoid; P13637; -.
KO; K01539; -.
OrthoDB; EOG091G01BB; -.
PhylomeDB; P13637; -.
TreeFam; TF312838; -.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
ChiTaRS; ATP1A3; human.
GeneWiki; ATP1A3; -.
GenomeRNAi; 478; -.
PRO; PR:P13637; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105409; -.
CleanEx; HS_ATP1A3; -.
ExpressionAtlas; P13637; baseline and differential.
Genevisible; P13637; HS.
GO; GO:0030424; C:axon; IDA:ARUK-UCL.
GO; GO:0044327; C:dendritic spine head; IEA:Ensembl.
GO; GO:0044326; C:dendritic spine neck; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0016020; C:membrane; ISS:ARUK-UCL.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
GO; GO:0032809; C:neuronal cell body membrane; IC:ARUK-UCL.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IDA:ARUK-UCL.
GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0031748; F:D1 dopamine receptor binding; IEA:Ensembl.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; IDA:BHF-UCL.
GO; GO:0086037; F:sodium:potassium-exchanging ATPase activity involved in regulation of cardiac muscle cell membrane potential; IEA:Ensembl.
GO; GO:1990239; F:steroid hormone binding; NAS:BHF-UCL.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
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:1904646; P:cellular response to amyloid-beta; ISS:ARUK-UCL.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; NAS:BHF-UCL.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:1990535; P:neuron projection maintenance; IGI:ARUK-UCL.
GO; GO:0010107; P:potassium ion import; IDA:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0060075; P:regulation of resting membrane potential; TAS:ARUK-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:1903416; P:response to glycoside; NAS:BHF-UCL.
GO; GO:0036376; P:sodium ion export from cell; IDA:BHF-UCL.
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_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
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; 3.
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;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Deafness; Disease mutation; Dystonia; Hydrolase; Ion transport;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Parkinsonism;
Phosphoprotein; Potassium; Potassium transport; Reference proteome;
Sodium; Sodium transport; Sodium/potassium transport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1013 Sodium/potassium-transporting ATPase
subunit alpha-3.
/FTId=PRO_0000046298.
TOPO_DOM 1 77 Cytoplasmic. {ECO:0000255}.
TRANSMEM 78 98 Helical. {ECO:0000255}.
TOPO_DOM 99 121 Extracellular. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255}.
TOPO_DOM 143 278 Cytoplasmic. {ECO:0000255}.
TRANSMEM 279 298 Helical. {ECO:0000255}.
TOPO_DOM 299 310 Extracellular. {ECO:0000255}.
TRANSMEM 311 328 Helical. {ECO:0000255}.
TOPO_DOM 329 762 Cytoplasmic. {ECO:0000255}.
TRANSMEM 763 782 Helical. {ECO:0000255}.
TOPO_DOM 783 792 Extracellular. {ECO:0000255}.
TRANSMEM 793 813 Helical. {ECO:0000255}.
TOPO_DOM 814 833 Cytoplasmic. {ECO:0000255}.
TRANSMEM 834 856 Helical. {ECO:0000255}.
TOPO_DOM 857 908 Extracellular. {ECO:0000255}.
TRANSMEM 909 928 Helical. {ECO:0000255}.
TOPO_DOM 929 941 Cytoplasmic. {ECO:0000255}.
TRANSMEM 942 960 Helical. {ECO:0000255}.
TOPO_DOM 961 975 Extracellular. {ECO:0000255}.
TRANSMEM 976 996 Helical. {ECO:0000255}.
TOPO_DOM 997 1013 Cytoplasmic. {ECO:0000255}.
REGION 72 74 Interaction with phosphoinositide-3
kinase. {ECO:0000250}.
ACT_SITE 366 366 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 707 707 Magnesium. {ECO:0000250}.
METAL 711 711 Magnesium. {ECO:0000250}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:P06687}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PIC6}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PIC6}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PIC6}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000250|UniProtKB:P06687}.
MOD_RES 548 548 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q6PIC6}.
MOD_RES 933 933 Phosphoserine; by PKA. {ECO:0000250}.
VAR_SEQ 1 2 MG -> MGGWEEERNRRAT (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046956.
VAR_SEQ 1 2 MG -> MGSGGSDSYRIATSQ (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046957.
VARIANT 137 137 S -> F (in AHC2; dbSNP:rs542652468).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068935.
VARIANT 137 137 S -> Y (in AHC2; dbSNP:rs542652468).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068936.
VARIANT 140 140 Q -> L (in AHC2; dbSNP:rs606231427).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068937.
VARIANT 220 220 D -> N (in AHC2).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068938.
VARIANT 274 274 I -> N (in AHC2; dbSNP:rs80356532).
{ECO:0000269|PubMed:22842232,
ECO:0000269|PubMed:22850527}.
/FTId=VAR_068939.
VARIANT 274 274 I -> T (in DYT12; dbSNP:rs80356532).
{ECO:0000269|PubMed:15260953}.
/FTId=VAR_026735.
VARIANT 277 277 E -> K (in DYT12; dbSNP:rs80356533).
{ECO:0000269|PubMed:15260953}.
/FTId=VAR_026736.
VARIANT 320 320 A -> T (probable disease-associated
mutation found in a patient with tonic-
clonic seizures associated with profound
developmental delay and paroxysmal
movement disorder; dbSNP:rs879255368).
{ECO:0000269|PubMed:26993267}.
/FTId=VAR_078699.
VARIANT 322 322 V -> D (in AHC2; dbSNP:rs606231428).
{ECO:0000269|PubMed:22850527}.
/FTId=VAR_070767.
VARIANT 333 333 C -> F (in AHC2; dbSNP:rs606231430).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068940.
VARIANT 371 371 L -> P (in AHC2; dbSNP:rs606231433).
{ECO:0000269|PubMed:22850527}.
/FTId=VAR_070768.
VARIANT 613 613 T -> M (in DYT12; dbSNP:rs80356534).
{ECO:0000269|PubMed:15260953}.
/FTId=VAR_026737.
VARIANT 755 755 G -> C (in AHC2; dbSNP:rs557052809).
{ECO:0000269|PubMed:22850527,
ECO:0000269|PubMed:23409136}.
/FTId=VAR_070769.
VARIANT 755 755 G -> S (in AHC2; dbSNP:rs557052809).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068941.
VARIANT 758 758 I -> S (in DYT12; dbSNP:rs80356535).
{ECO:0000269|PubMed:15260953}.
/FTId=VAR_026738.
VARIANT 772 772 S -> R (in AHC2; dbSNP:rs534926223).
{ECO:0000269|PubMed:22850527}.
/FTId=VAR_070770.
VARIANT 773 773 N -> I (in AHC2; dbSNP:rs606231437).
{ECO:0000269|PubMed:22850527}.
/FTId=VAR_070771.
VARIANT 773 773 N -> S (in AHC2; dbSNP:rs606231437).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068942.
VARIANT 780 780 F -> L (in DYT12; dbSNP:rs80356536).
{ECO:0000269|PubMed:15260953}.
/FTId=VAR_026739.
VARIANT 801 801 D -> N (in AHC2; protein levels is
similar to wild-type but the enzyme
activity is significantly decreased;
dbSNP:rs80356537).
{ECO:0000269|PubMed:22842232,
ECO:0000269|PubMed:22850527,
ECO:0000269|PubMed:23409136}.
/FTId=VAR_068943.
VARIANT 801 801 D -> Y (in DYT12; dbSNP:rs80356537).
{ECO:0000269|PubMed:15260953}.
/FTId=VAR_026740.
VARIANT 806 806 M -> R (in AHC2; dbSNP:rs549006436).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068944.
VARIANT 810 810 I -> S (in AHC2; dbSNP:rs536681257).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068945.
VARIANT 811 811 S -> P (in AHC2; protein levels is
similar to wild-type but the enzyme
activity is significantly decreased;
dbSNP:rs387907282).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068946.
VARIANT 815 815 E -> K (in AHC2; protein levels is
similar to wild-type but the enzyme
activity is significantly decreased;
dbSNP:rs387907281).
{ECO:0000269|PubMed:22842232,
ECO:0000269|PubMed:22850527,
ECO:0000269|PubMed:23409136}.
/FTId=VAR_068947.
VARIANT 818 818 E -> K (in CAPOS; dbSNP:rs587777771).
{ECO:0000269|PubMed:24468074}.
/FTId=VAR_070772.
VARIANT 919 919 Missing (in AHC2).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068948.
VARIANT 923 923 D -> N (in DYT12; dbSNP:rs267606670).
{ECO:0000269|PubMed:19652145}.
/FTId=VAR_068949.
VARIANT 923 923 D -> Y (in AHC2; dbSNP:rs267606670).
{ECO:0000269|PubMed:22850527}.
/FTId=VAR_070773.
VARIANT 927 927 C -> Y (in AHC2; dbSNP:rs606231444).
/FTId=VAR_070774.
VARIANT 947 947 G -> R (in AHC2; dbSNP:rs398122887).
{ECO:0000269|PubMed:22842232,
ECO:0000269|PubMed:26993267}.
/FTId=VAR_068950.
VARIANT 955 955 A -> D (in AHC2; dbSNP:rs606231446).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068951.
VARIANT 992 992 D -> Y (in AHC2; dbSNP:rs606231447).
{ECO:0000269|PubMed:22842232}.
/FTId=VAR_068952.
VARIANT 1013 1013 Y -> YY (in DYT12; there is a drastic 40-
to 50-fold reduction in Na(+) affinity in
the mutant protein).
{ECO:0000269|PubMed:19351654}.
/FTId=VAR_068953.
CONFLICT 1 2 MG -> MEIH (in Ref. 2; CAA31390).
{ECO:0000305}.
CONFLICT 144 144 S -> R (in Ref. 3; BAH12387).
{ECO:0000305}.
CONFLICT 336 336 L -> V (in Ref. 1; AAA51798, 2; CAA31390,
6; AAA52285 and 8; AAA58380).
{ECO:0000305}.
CONFLICT 380 380 H -> T (in Ref. 6; AAA52285).
{ECO:0000305}.
CONFLICT 421 421 A -> P (in Ref. 8; AAA58380).
{ECO:0000305}.
CONFLICT 430 430 I -> M (in Ref. 2; CAA31390).
{ECO:0000305}.
CONFLICT 555 557 FPK -> YPQ (in Ref. 1; AAA51798, 2;
CAA31390 and 6; AAA52286). {ECO:0000305}.
CONFLICT 577 577 G -> P (in Ref. 1; AAA51798).
{ECO:0000305}.
CONFLICT 583 583 D -> G (in Ref. 1; AAA51798, 2; CAA31390
and 6; AAA52286). {ECO:0000305}.
CONFLICT 919 919 V -> A (in Ref. 6; AAA52286).
{ECO:0000305}.
CONFLICT 944 944 L -> M (in Ref. 6; AAA52286).
{ECO:0000305}.
CONFLICT 982 982 F -> S (in Ref. 2; CAA31390).
{ECO:0000305}.
CONFLICT 1006 1006 W -> S (in Ref. 1; AAA51798).
{ECO:0000305}.
SEQUENCE 1013 AA; 111749 MW; BF28CD9F1E11AF48 CRC64;
MGDKKDDKDS PKKNKGKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV QGLTHSKAQE
ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SILLWIGAIL CFLAYGIQAG TEDDPSGDNL
YLGIVLAAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIREGEKMQV NAEEVVVGDL
VEIKGGDRVP ADLRIISAHG CKVDNSSLTG ESEPQTRSPD CTHDNPLETR NITFFSTNCV
EGTARGVVVA TGDRTVMGRI ATLASGLEVG KTPIAIEIEH FIQLITGVAV FLGVSFFILS
LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN LEAVETLGST
STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTEDQSGTS FDKSSHTWVA LSHIAGLCNR
AVFKGGQDNI PVLKRDVAGD ASESALLKCI ELSSGSVKLM RERNKKVAEI PFNSTNKYQL
SIHETEDPND NRYLLVMKGA PERILDRCST ILLQGKEQPL DEEMKEAFQN AYLELGGLGE
RVLGFCHYYL PEEQFPKGFA FDCDDVNFTT DNLCFVGLMS MIDPPRAAVP DAVGKCRSAG
IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA KACVIHGTDL
KDFTSEQIDE ILQNHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN DSPALKKADI
GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF
LLFIMANIPL PLGTITILCI DLGTDMVPAI SLAYEAAESD IMKRQPRNPR TDKLVNERLI
SMAYGQIGMI QALGGFFSYF VILAENGFLP GNLVGIRLNW DDRTVNDLED SYGQQWTYEQ
RKVVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE ETALAAFLSY
CPGMDVALRM YPLKPSWWFC AFPYSFLIFV YDEIRKLILR RNPGGWVEKE TYY


Related products :

Catalog number Product name Quantity
EIAAB45649 ATP6A1,ATP6V1A,ATP6V1A1,Homo sapiens,Human,Vacuolar ATPase isoform VA68,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,VPP2,V-type proton ATPase catalytic subunit A
EIAAB45652 Atp6a1,Atp6a2,Atp6v1a,Atp6v1a1,Mouse,Mus musculus,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45651 ATP6A1,ATP6V1A,ATP6V1A1,Bos taurus,Bovine,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45650 ATP6A1,ATP6V1A,ATP6V1A1,Pig,Sus scrofa,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45648 ATP6V1A,Chicken,Gallus gallus,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45577 ATP6V0E2,ATP6V0E2L,C7orf32,Homo sapiens,Human,Lysosomal 9 kDa H(+)-transporting ATPase V0 subunit e2,Vacuolar proton pump subunit e 2,V-ATPase subunit e 2,V-type proton ATPase subunit e 2
AT1A1_PIG Pig ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-1 96T
ER451 Sodium per potassium-transporting ATPase subunit alpha-3 Elisa Kit 96T
H1749 Sodium potassium-transporting ATPase subunit alpha-3 (ATP1A3), Rat, ELISA Kit 96T
H1744 Sodium potassium-transporting ATPase subunit alpha-2 (ATP1A2), Pig, ELISA Kit 96T
H1745 Sodium potassium-transporting ATPase subunit alpha-2 (ATP1A2), Rat, ELISA Kit 96T
H1752 Sodium potassium-transporting ATPase subunit alpha-4 (ATP1A4), Rat, ELISA Kit 96T
AT1A2_MOUSE Mouse ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-2 96T
AT1A1_RABIT Rabbit ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-1 96T
AT1A2_HUMAN Human ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-2 96T
CSB-EL002322RA Rat Sodium per potassium-transporting ATPase subunit alpha-1(ATP1A1) ELISA kit 96T
E1431r Bovine ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-1 96T
AT1A2_BOVIN Bovine ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-2 96T
AT1A1_HUMAN Human ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-1 96T
H1736 Sodium potassium-transporting ATPase subunit alpha-1 (ATP1A1), Pig, ELISA Kit 96T
H1732 Sodium potassium-transporting ATPase subunit alpha-1 (ATP1A1), Dog, ELISA Kit 96T
H1738 Sodium potassium-transporting ATPase subunit alpha-1 (ATP1A1), Rat, ELISA Kit 96T
15-288-22820 Vacuolar ATP synthase catalytic subunit A. ubiquitous isoform - EC 3.6.3.14; V-ATPase subunit A 1; Vacuolar proton pump alpha subunit 1; V-ATPase 69 kDa subunit 1; Isoform VA68 Polyclonal 0.05 mg
15-288-22820 Vacuolar ATP synthase catalytic subunit A. ubiquitous isoform - EC 3.6.3.14; V-ATPase subunit A 1; Vacuolar proton pump alpha subunit 1; V-ATPase 69 kDa subunit 1; Isoform VA68 Polyclonal 0.1 mg
EIAAB45573 ATP6H,ATP6V0E,ATP6V0E1,Homo sapiens,Human,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur