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Sodium/potassium-transporting ATPase subunit alpha-1 (Na( )/K( ) ATPase alpha-1 subunit) (EC 3.6.3.9) (Sodium pump subunit alpha-1)

 AT1A1_HUMAN             Reviewed;        1023 AA.
P05023; B2RBR6; B7Z2T5; B7Z3U6; F5H3A1; Q16689; Q6LDM4; Q9UCN1;
Q9UJ20; Q9UJ21;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
25-OCT-2017, entry version 212.
RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-1;
Short=Na(+)/K(+) ATPase alpha-1 subunit;
EC=3.6.3.9;
AltName: Full=Sodium pump subunit alpha-1;
Flags: Precursor;
Name=ATP1A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2430951;
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. 100:389-397(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Retinal pigment epithelium;
PubMed=7536695; DOI=10.1016/0378-1119(94)00812-7;
Ruiz A., Bhat S.P., 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 155:179-184(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
TISSUE=Cerebellum;
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=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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, Cervix, and Skin;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
PubMed=1970326; DOI=10.1016/0888-7543(90)90475-A;
Shull M.M., Pugh D.G., Lingrel J.B.;
"The human Na, K-ATPase alpha 1 gene: characterization of the 5'-
flanking region and identification of a restriction fragment length
polymorphism.";
Genomics 6:451-460(1990).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-148.
TISSUE=Placenta;
Zhang J.-S., Yang J.X., Fang M.W., Lu S.D.;
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 168-189 AND 213-244.
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 198-943 (ISOFORM 1).
TISSUE=Placenta;
PubMed=2891135; DOI=10.1073/pnas.84.22.7901;
Chehab F.F., Kan Y.W., Law M.L., Hartz J., Kao F.T., 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. 84:7901-7905(1987).
[11]
PROTEIN SEQUENCE OF 199-216, AND INTERACTION WITH HLA-DR1.
PubMed=1380674; DOI=10.1038/358764a0;
Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J.,
Vignali D.A.A., Strominger J.L.;
"Predominant naturally processed peptides bound to HLA-DR1 are derived
from MHC-related molecules and are heterogeneous in size.";
Nature 358:764-768(1992).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-341 AND 420-444.
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).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 471-619.
Ovchinnikov Y.A., Monastyrskaya G.S., Arsenyan S.G., Broude N.E.,
Petrukhin K.E., Grishin A.V., Arzamazova N.M., Severtsova I.V.,
Modyanov N.N.;
"Amino acid sequence of the 17-kilodalton fragment of the cytoplasmic
region of the alpha-subunit of NA+,K+-ATPase.";
Dokl. Biochem. 288:270-272(1986).
[14]
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).
[15]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[16]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-542, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
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).
[20]
INTERACTION WITH FXYD3.
PubMed=21454534; DOI=10.1074/jbc.M110.184101;
Bibert S., Liu C.C., Figtree G.A., Garcia A., Hamilton E.J.,
Marassi F.M., Sweadner K.J., Cornelius F., Geering K., Rasmussen H.H.;
"FXYD proteins reverse inhibition of the Na+-K+ pump mediated by
glutathionylation of its beta1 subunit.";
J. Biol. Chem. 286:18562-18572(2011).
[21]
INTERACTION WITH SLC35G1 AND STIM1.
PubMed=22084111; DOI=10.1073/pnas.1117231108;
Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.;
"POST, partner of stromal interaction molecule 1 (STIM1), targets
STIM1 to multiple transporters.";
Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- 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 (By similarity). Interacts with regulatory subunit
FXYD3 (PubMed:21454534). Interacts with SIK1 (By similarity).
Binds the HLA class II histocompatibility antigen DR1
(PubMed:1380674). Interacts with SLC35G1 and STIM1
(PubMed:22084111). {ECO:0000250|UniProtKB:P06685,
ECO:0000269|PubMed:1380674, ECO:0000269|PubMed:21454534,
ECO:0000269|PubMed:22084111}.
-!- INTERACTION:
P13693:TPT1; NbExp=5; IntAct=EBI-358778, EBI-1783169;
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
{ECO:0000269|PubMed:7711835}; Multi-pass membrane protein
{ECO:0000255}. Melanosome {ECO:0000269|PubMed:17081065}.
Note=Identified by mass spectrometry in melanosome fractions from
stage I to stage IV. {ECO:0000269|PubMed:17081065}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Long;
IsoId=P05023-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P05023-2; Sequence=VSP_000415, VSP_000416;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3;
IsoId=P05023-3; Sequence=VSP_044242;
Name=4;
IsoId=P05023-4; Sequence=VSP_047309;
-!- PTM: Phosphorylation on Tyr-10 modulates pumping activity.
Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1
to PKC. Dephosphorylation by protein phosphatase 2A (PP2A)
following increases in intracellular sodium, leading to increase
catalytic activity (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIC subfamily. {ECO:0000305}.
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EMBL; D00099; BAA00061.1; -; mRNA.
EMBL; X04297; CAA27840.1; -; mRNA.
EMBL; U16798; AAC50131.1; -; mRNA.
EMBL; AK295095; BAH11971.1; -; mRNA.
EMBL; AK296362; BAH12332.1; -; mRNA.
EMBL; AK314777; BAG37313.1; -; mRNA.
EMBL; AL136376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471122; EAW56644.1; -; Genomic_DNA.
EMBL; BC003077; AAH03077.1; -; mRNA.
EMBL; BC001330; AAH01330.1; -; mRNA.
EMBL; BC050359; AAH50359.1; -; mRNA.
EMBL; M30310; AAA51801.1; -; Genomic_DNA.
EMBL; M30309; AAA51801.1; JOINED; Genomic_DNA.
EMBL; L76938; AAA92713.1; -; Genomic_DNA.
EMBL; M16793; AAD56251.1; -; mRNA.
EMBL; M16794; AAD56252.1; -; mRNA.
EMBL; J03007; AAA51803.1; -; mRNA.
EMBL; M27572; AAA35573.1; -; Genomic_DNA.
EMBL; M27579; AAA35574.2; -; Genomic_DNA.
EMBL; X03757; CAA27390.1; -; mRNA.
CCDS; CCDS53351.1; -. [P05023-4]
CCDS; CCDS53352.1; -. [P05023-3]
CCDS; CCDS887.1; -. [P05023-1]
PIR; A24414; A24414.
RefSeq; NP_000692.2; NM_000701.7. [P05023-1]
RefSeq; NP_001153705.1; NM_001160233.1. [P05023-4]
RefSeq; NP_001153706.1; NM_001160234.1. [P05023-3]
RefSeq; XP_016856849.1; XM_017001360.1. [P05023-3]
RefSeq; XP_016856850.1; XM_017001361.1. [P05023-3]
UniGene; Hs.371889; -.
ProteinModelPortal; P05023; -.
SMR; P05023; -.
BioGrid; 106966; 122.
DIP; DIP-38196N; -.
IntAct; P05023; 61.
MINT; MINT-4998863; -.
STRING; 9606.ENSP00000295598; -.
BindingDB; P05023; -.
ChEMBL; CHEMBL1807; -.
DrugBank; DB00511; Acetyldigitoxin.
DrugBank; DB01430; Almitrine.
DrugBank; DB01370; Aluminium.
DrugBank; DB01244; Bepridil.
DrugBank; DB01158; Bretylium.
DrugBank; DB01188; Ciclopirox.
DrugBank; DB01078; Deslanoside.
DrugBank; DB01119; Diazoxide.
DrugBank; DB01396; Digitoxin.
DrugBank; DB00390; Digoxin.
DrugBank; DB00903; Etacrynic acid.
DrugBank; DB00774; Hydroflumethiazide.
DrugBank; DB01378; Magnesium.
DrugBank; DB01092; Ouabain.
DrugBank; DB01345; Potassium.
DrugBank; DB09479; Rubidium chloride Rb-82.
DrugBank; DB01021; Trichlormethiazide.
TCDB; 3.A.3.1.1; the p-type atpase (p-atpase) superfamily.
iPTMnet; P05023; -.
PhosphoSitePlus; P05023; -.
SwissPalm; P05023; -.
BioMuta; ATP1A1; -.
DMDM; 114374; -.
EPD; P05023; -.
MaxQB; P05023; -.
PaxDb; P05023; -.
PeptideAtlas; P05023; -.
PRIDE; P05023; -.
DNASU; 476; -.
Ensembl; ENST00000295598; ENSP00000295598; ENSG00000163399. [P05023-1]
Ensembl; ENST00000369496; ENSP00000358508; ENSG00000163399. [P05023-3]
Ensembl; ENST00000537345; ENSP00000445306; ENSG00000163399. [P05023-4]
GeneID; 476; -.
KEGG; hsa:476; -.
UCSC; uc001ege.5; human. [P05023-1]
CTD; 476; -.
DisGeNET; 476; -.
EuPathDB; HostDB:ENSG00000163399.15; -.
GeneCards; ATP1A1; -.
HGNC; HGNC:799; ATP1A1.
HPA; CAB018702; -.
HPA; CAB069993; -.
MIM; 182310; gene.
neXtProt; NX_P05023; -.
OpenTargets; ENSG00000163399; -.
Orphanet; 85142; Aldosterone-producing adenoma.
PharmGKB; PA62; -.
eggNOG; KOG0203; Eukaryota.
eggNOG; COG0474; LUCA.
GeneTree; ENSGT00890000139334; -.
HOGENOM; HOG000265622; -.
HOVERGEN; HBG004298; -.
InParanoid; P05023; -.
KO; K01539; -.
OMA; ARIMPEQ; -.
OrthoDB; EOG091G01BB; -.
PhylomeDB; P05023; -.
TreeFam; TF312838; -.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
ChiTaRS; ATP1A1; human.
GeneWiki; ATPase,_Na%2B/K%2B_transporting,_alpha_1; -.
GenomeRNAi; 476; -.
PRO; PR:P05023; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000163399; -.
CleanEx; HS_ATP1A1; -.
ExpressionAtlas; P05023; baseline and differential.
Genevisible; P05023; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0042383; C:sarcolemma; ISS:BHF-UCL.
GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
GO; GO:0030315; C:T-tubule; IEA:Ensembl.
GO; GO:0043531; F:ADP binding; IEA:Ensembl.
GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; ISS:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0016791; F:phosphatase activity; IEA:Ensembl.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
GO; GO:0030955; F:potassium ion binding; ISS:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0031402; F:sodium ion binding; ISS:BHF-UCL.
GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; IDA:BHF-UCL.
GO; GO:1990239; F:steroid hormone binding; IDA:BHF-UCL.
GO; GO:0086002; P:cardiac muscle cell action potential involved in 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:0060081; P:membrane hyperpolarization; IEA:Ensembl.
GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IC:BHF-UCL.
GO; GO:0031947; P:negative regulation of glucocorticoid biosynthetic process; IEA:Ensembl.
GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
GO; GO:0045823; P:positive regulation of heart contraction; IEA:Ensembl.
GO; GO:0045989; P:positive regulation of striated muscle contraction; IEA:Ensembl.
GO; GO:0010107; P:potassium ion import; IDA:BHF-UCL.
GO; GO:1990573; P:potassium ion import across plasma membrane; ISS:BHF-UCL.
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:0002028; P:regulation of sodium ion transport; ISS:UniProtKB.
GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
GO; GO:0055119; P:relaxation of cardiac muscle; TAS:BHF-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:1903416; P:response to glycoside; IDA:BHF-UCL.
GO; GO:0036376; P:sodium ion export from cell; IDA:BHF-UCL.
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; 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;
Acetylation; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Direct protein sequencing; Hydrolase;
Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Potassium; Potassium transport;
Reference proteome; Sodium; Sodium transport;
Sodium/potassium transport; Transmembrane; Transmembrane helix;
Transport.
PROPEP 1 5
/FTId=PRO_0000002483.
CHAIN 6 1023 Sodium/potassium-transporting ATPase
subunit alpha-1.
/FTId=PRO_0000002484.
TOPO_DOM 6 87 Cytoplasmic. {ECO:0000255}.
TRANSMEM 88 108 Helical. {ECO:0000255}.
TOPO_DOM 109 131 Extracellular. {ECO:0000255}.
TRANSMEM 132 152 Helical. {ECO:0000255}.
TOPO_DOM 153 288 Cytoplasmic. {ECO:0000255}.
TRANSMEM 289 308 Helical. {ECO:0000255}.
TOPO_DOM 309 320 Extracellular. {ECO:0000255}.
TRANSMEM 321 338 Helical. {ECO:0000255}.
TOPO_DOM 339 772 Cytoplasmic. {ECO:0000255}.
TRANSMEM 773 792 Helical. {ECO:0000255}.
TOPO_DOM 793 802 Extracellular. {ECO:0000255}.
TRANSMEM 803 823 Helical. {ECO:0000255}.
TOPO_DOM 824 843 Cytoplasmic. {ECO:0000255}.
TRANSMEM 844 866 Helical. {ECO:0000255}.
TOPO_DOM 867 918 Extracellular. {ECO:0000255}.
TRANSMEM 919 938 Helical. {ECO:0000255}.
TOPO_DOM 939 951 Cytoplasmic. {ECO:0000255}.
TRANSMEM 952 970 Helical. {ECO:0000255}.
TOPO_DOM 971 985 Extracellular. {ECO:0000255}.
TRANSMEM 986 1006 Helical. {ECO:0000255}.
TOPO_DOM 1007 1023 Cytoplasmic. {ECO:0000255}.
REGION 82 84 Phosphoinositide-3 kinase binding.
{ECO:0000250}.
ACT_SITE 376 376 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 717 717 Magnesium. {ECO:0000250}.
METAL 721 721 Magnesium. {ECO:0000250}.
BINDING 487 487 ATP. {ECO:0000250}.
MOD_RES 9 9 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 10 10 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06685}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 21 21 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000250|UniProtKB:P06685}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000250|UniProtKB:P06685}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 260 260 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000250|UniProtKB:P06685}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000250|UniProtKB:P06685}.
MOD_RES 542 542 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 661 661 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 668 668 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 943 943 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P06685}.
VAR_SEQ 1 31 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044242.
VAR_SEQ 2 4 GKG -> AFK (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047309.
VAR_SEQ 638 681 NETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQL
DDI -> SGPMSRGKSWSSPATQPSSSVSWWCSGPTWSSVR
PGGIRSSSRG (in isoform 2).
{ECO:0000303|PubMed:7536695}.
/FTId=VSP_000415.
VAR_SEQ 682 1023 Missing (in isoform 2).
{ECO:0000303|PubMed:7536695}.
/FTId=VSP_000416.
VARIANT 47 47 S -> I (in dbSNP:rs12564026).
/FTId=VAR_048374.
CONFLICT 248 248 N -> S (in Ref. 3; BAG37313).
{ECO:0000305}.
CONFLICT 323 323 F -> L (in Ref. 3; BAH11971).
{ECO:0000305}.
CONFLICT 475 475 A -> T (in Ref. 13; CAA27390).
{ECO:0000305}.
CONFLICT 499 499 S -> A (in Ref. 13; CAA27390).
{ECO:0000305}.
CONFLICT 502 502 Q -> R (in Ref. 13; CAA27390).
{ECO:0000305}.
CONFLICT 523 523 L -> I (in Ref. 13; CAA27390).
{ECO:0000305}.
CONFLICT 892 892 D -> G (in Ref. 3; BAH11971).
{ECO:0000305}.
SEQUENCE 1023 AA; 112896 MW; F3C6FDE04FB3F667 CRC64;
MGKGVGRDKY EPAAVSEQGD KKGKKGKKDR DMDELKKEVS MDDHKLSLDE LHRKYGTDLS
RGLTSARAAE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SMLLWIGAIL CFLAYSIQAA
TEEEPQNDNL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI
NAEEVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR
NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWLA
LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI ELCCGSVKEM RERYAKIVEI
PFNSTNKYQL SIHKNPNTSE PQHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN
AYLELGGLGE RVLGFCHLFL PDEQFPEGFQ FDTDDVNFPI DNLCFVGLIS MIDPPRAAVP
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA
KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN
DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL
TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK
TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP IHLLGLRVDW DDRWINDVED
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE
ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE
TYY


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