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P05023 (AT1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium/potassium-transporting ATPase subunit alpha-1

Short name=Na(+)/K(+) ATPase alpha-1 subunit
EC=3.6.3.9
Alternative name(s):
Sodium pump subunit alpha-1
Gene names
Name:ATP1A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1023 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 + H2O + Na+(In) + K+(Out) = ADP + phosphate + Na+(Out) + K+(In).

Subunit structure

Interacts with SIK1 By similarity. Composed of three subunits: alpha (catalytic), beta and gamma. Binds the HLA class II histocompatibility antigen, DR1. Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.14 Ref.16

Post-translational modification

Phosphorylation on Tyr-10 modulates pumping activity. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity By similarity.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Sodium transport
Sodium/potassium transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Potassium
Sodium
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement. Source: Reactome

membrane hyperpolarization

Inferred from electronic annotation. Source: Ensembl

negative regulation of glucocorticoid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of heart contraction

Inferred from electronic annotation. Source: Ensembl

positive regulation of heart contraction

Inferred from electronic annotation. Source: Ensembl

positive regulation of striated muscle contraction

Inferred from electronic annotation. Source: Ensembl

potassium ion import

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

regulation of cardiac muscle cell contraction

Inferred from electronic annotation. Source: Ensembl

regulation of sodium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of the force of heart contraction

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

sodium ion transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: BHF-UCL

T-tubule

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

caveola

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: BHF-UCL

endosome

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 12519789PubMed 19199708PubMed 20458337. Source: UniProt

integral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Traceable author statement PubMed 1975705. Source: ProtInc

plasma membrane

Inferred from direct assay Ref.14. Source: UniProtKB

sodium:potassium-exchanging ATPase complex

Traceable author statement PubMed 1975705. Source: ProtInc

   Molecular_functionADP binding

Inferred from electronic annotation. Source: Ensembl

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

chaperone binding

Inferred from sequence or structural similarity. Source: BHF-UCL

potassium ion binding

Inferred from electronic annotation. Source: Ensembl

sodium ion binding

Inferred from electronic annotation. Source: Ensembl

sodium:potassium-exchanging ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TPT1P136935EBI-358778,EBI-1783169

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05023-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P05023-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     638-681: NETVEDIAAR...DMTSEQLDDI → SGPMSRGKSW...PGGIRSSSRG
     682-1023: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: P05023-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.
Isoform 4 (identifier: P05023-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2-4: GKG → AFK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 55
PRO_0000002483
Chain6 – 10231018Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000002484

Regions

Topological domain6 – 8782Cytoplasmic Potential
Transmembrane88 – 10821Helical; Potential
Topological domain109 – 13123Extracellular Potential
Transmembrane132 – 15221Helical; Potential
Topological domain153 – 288136Cytoplasmic Potential
Transmembrane289 – 30820Helical; Potential
Topological domain309 – 32012Extracellular Potential
Transmembrane321 – 33818Helical; Potential
Topological domain339 – 772434Cytoplasmic Potential
Transmembrane773 – 79220Helical; Potential
Topological domain793 – 80210Extracellular Potential
Transmembrane803 – 82321Helical; Potential
Topological domain824 – 84320Cytoplasmic Potential
Transmembrane844 – 86623Helical; Potential
Topological domain867 – 91852Extracellular Potential
Transmembrane919 – 93820Helical; Potential
Topological domain939 – 95113Cytoplasmic Potential
Transmembrane952 – 97019Helical; Potential
Topological domain971 – 98515Extracellular Potential
Transmembrane986 – 100621Helical; Potential
Topological domain1007 – 102317Cytoplasmic Potential
Region82 – 843Phosphoinositide-3 kinase binding By similarity

Sites

Active site37614-aspartylphosphate intermediate By similarity
Metal binding7171Magnesium By similarity
Metal binding7211Magnesium By similarity
Binding site4871ATP By similarity

Amino acid modifications

Modified residue91N6-acetyllysine By similarity
Modified residue101Phosphotyrosine By similarity
Modified residue161Phosphoserine By similarity
Modified residue211N6-acetyllysine By similarity
Modified residue2601Phosphotyrosine By similarity
Modified residue5421Phosphotyrosine Ref.18
Modified residue6611N6-succinyllysine By similarity
Modified residue9431Phosphoserine; by PKA By similarity

Natural variations

Alternative sequence1 – 3131Missing in isoform 3.
VSP_044242
Alternative sequence2 – 43GKG → AFK in isoform 4.
VSP_047309
Alternative sequence638 – 68144NETVE…QLDDI → SGPMSRGKSWSSPATQPSSS VSWWCSGPTWSSVRPGGIRS SSRG in isoform 2.
VSP_000415
Alternative sequence682 – 1023342Missing in isoform 2.
VSP_000416
Natural variant471S → I.
Corresponds to variant rs12564026 [ dbSNP | Ensembl ].
VAR_048374

Experimental info

Sequence conflict2481N → S in BAG37313. Ref.3
Sequence conflict3231F → L in BAH11971. Ref.3
Sequence conflict4751A → T in CAA27390. Ref.13
Sequence conflict4991S → A in CAA27390. Ref.13
Sequence conflict5021Q → R in CAA27390. Ref.13
Sequence conflict5231L → I in CAA27390. Ref.13
Sequence conflict8921D → G in BAH11971. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: F3C6FDE04FB3F667

FASTA1,023112,896
        10         20         30         40         50         60 
MGKGVGRDKY EPAAVSEQGD KKGKKGKKDR DMDELKKEVS MDDHKLSLDE LHRKYGTDLS 

        70         80         90        100        110        120 
RGLTSARAAE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SMLLWIGAIL CFLAYSIQAA 

       130        140        150        160        170        180 
TEEEPQNDNL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI 

       190        200        210        220        230        240 
NAEEVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR 

       250        260        270        280        290        300 
NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV 

       310        320        330        340        350        360 
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN 

       370        380        390        400        410        420 
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWLA 

       430        440        450        460        470        480 
LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI ELCCGSVKEM RERYAKIVEI 

       490        500        510        520        530        540 
PFNSTNKYQL SIHKNPNTSE PQHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN 

       550        560        570        580        590        600 
AYLELGGLGE RVLGFCHLFL PDEQFPEGFQ FDTDDVNFPI DNLCFVGLIS MIDPPRAAVP 

       610        620        630        640        650        660 
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA 

       670        680        690        700        710        720 
KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN 

       730        740        750        760        770        780 
DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL 

       790        800        810        820        830        840 
TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK 

       850        860        870        880        890        900 
TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP IHLLGLRVDW DDRWINDVED 

       910        920        930        940        950        960 
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE 

       970        980        990       1000       1010       1020 
ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE 


TYY 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: B74A8E7E31E975AD
Show »

FASTA68174,140
Isoform 3 [UniParc].

Checksum: 6F607167FD03A23B
Show »

FASTA992109,550
Isoform 4 [UniParc].

Checksum: B5B35DE0B0650011
Show »

FASTA1,023113,000

References

« Hide 'large scale' references
[1]"Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence."
Kawakami K., Ohta T., Nojima H., Nagano K.
J. Biochem. 100:389-397(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium."
Ruiz A., Bhat S.P., Bok D.
Gene 155:179-184(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Retinal pigment epithelium.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
Tissue: Cerebellum.
[4]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain, Cervix and Skin.
[7]"The human Na, K-ATPase alpha 1 gene: characterization of the 5'-flanking region and identification of a restriction fragment length polymorphism."
Shull M.M., Pugh D.G., Lingrel J.B.
Genomics 6:451-460(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
[8]Zhang J.-S., Yang J.X., Fang M.W., Lu S.D.
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-148.
Tissue: Placenta.
[9]"Multiple genes encode the human Na+,K+-ATPase catalytic subunit."
Shull M.M., Lingrel J.B.
Proc. Natl. Acad. Sci. U.S.A. 84:4039-4043(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 168-189 AND 213-244.
[10]"Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue expression, DNA polymorphism, and chromosomal localization."
Chehab F.F., Kan Y.W., Law M.L., Hartz J., Kao F.T., Blostein R.
Proc. Natl. Acad. Sci. U.S.A. 84:7901-7905(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 198-943 (ISOFORM 1).
Tissue: Placenta.
[11]"Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size."
Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J., Vignali D.A.A., Strominger J.L.
Nature 358:764-768(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 199-216, INTERACTION WITH HLA-DR1.
[12]"The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit."
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.
FEBS Lett. 217:275-278(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-341 AND 420-444.
[13]"Amino acid sequence of the 17-kilodalton fragment of the cytoplasmic region of the alpha-subunit of NA+,K+-ATPase."
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.
Dokl. Biochem. 288:270-272(1986)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 471-619.
[14]"Subcellular distribution and immunocytochemical localization of Na,K-ATPase subunit isoforms in human skeletal muscle."
Hundal H.S., Maxwell D.L., Ahmed A., Darakhshan F., Mitsumoto Y., Klip A.
Mol. Membr. Biol. 11:255-262(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[16]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
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.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00099 mRNA. Translation: BAA00061.1.
X04297 mRNA. Translation: CAA27840.1.
U16798 mRNA. Translation: AAC50131.1.
AK295095 mRNA. Translation: BAH11971.1.
AK296362 mRNA. Translation: BAH12332.1.
AK314777 mRNA. Translation: BAG37313.1.
AL136376 Genomic DNA. No translation available.
CH471122 Genomic DNA. Translation: EAW56644.1.
BC003077 mRNA. Translation: AAH03077.1.
BC001330 mRNA. Translation: AAH01330.1.
BC050359 mRNA. Translation: AAH50359.1.
M30310, M30309 Genomic DNA. Translation: AAA51801.1.
L76938 Genomic DNA. Translation: AAA92713.1.
M16793 mRNA. Translation: AAD56251.1.
M16794 mRNA. Translation: AAD56252.1.
J03007 mRNA. Translation: AAA51803.1.
M27572 Genomic DNA. Translation: AAA35573.1.
M27579 Genomic DNA. Translation: AAA35574.2.
X03757 mRNA. Translation: CAA27390.1.
PIRA24414.
RefSeqNP_000692.2. NM_000701.7.
NP_001153705.1. NM_001160233.1.
NP_001153706.1. NM_001160234.1.
UniGeneHs.371889.

3D structure databases

ProteinModelPortalP05023.
SMRP05023. Positions 30-1023.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106966. 37 interactions.
DIPDIP-38196N.
IntActP05023. 24 interactions.
MINTMINT-4998863.
STRING9606.ENSP00000295598.

Chemistry

BindingDBP05023.
ChEMBLCHEMBL2095186.
DrugBankDB00511. Acetyldigitoxin.
DB01430. Almitrine.
DB01370. Aluminium.
DB01244. Bepridil.
DB01158. Bretylium.
DB01197. Captopril.
DB01078. Deslanoside.
DB01119. Diazoxide.
DB01396. Digitoxin.
DB00390. Digoxin.
DB00736. Esomeprazole.
DB00903. Ethacrynic acid.
DB00695. Furosemide.
DB00774. Hydroflumethiazide.
DB00232. Methyclothiazide.
DB01092. Ouabain.
DB00213. Pantoprazole.
DB01021. Trichlormethiazide.
GuidetoPHARMACOLOGY833.

Protein family/group databases

TCDB3.A.3.1.1. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteP05023.

Polymorphism databases

DMDM114374.

Proteomic databases

PaxDbP05023.
PeptideAtlasP05023.
PRIDEP05023.

Protocols and materials databases

DNASU476.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295598; ENSP00000295598; ENSG00000163399. [P05023-1]
ENST00000369496; ENSP00000358508; ENSG00000163399. [P05023-3]
ENST00000537345; ENSP00000445306; ENSG00000163399. [P05023-4]
GeneID476.
KEGGhsa:476.
UCSCuc001ege.3. human. [P05023-1]

Organism-specific databases

CTD476.
GeneCardsGC01P116915.
HGNCHGNC:799. ATP1A1.
HPACAB018702.
MIM182310. gene.
neXtProtNX_P05023.
Orphanet85142. Aldosterone-producing adenoma.
PharmGKBPA62.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOVERGENHBG004298.
InParanoidP05023.
KOK01539.
OMAQFPEGFQ.
OrthoDBEOG7327N0.
PhylomeDBP05023.
TreeFamTF312838.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP05023.
BgeeP05023.
CleanExHS_ATP1A1.
GenevestigatorP05023.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR005775. ATPase_P-typ_Na/K_IIC.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP1A1. human.
GeneWikiATPase,_Na%2B/K%2B_transporting,_alpha_1.
GenomeRNAi476.
NextBio1971.
PROP05023.
SOURCESearch...

Entry information

Entry nameAT1A1_HUMAN
AccessionPrimary (citable) accession number: P05023
Secondary accession number(s): B2RBR6 expand/collapse secondary AC list , B7Z2T5, B7Z3U6, F5H3A1, Q16689, Q6LDM4, Q9UCN1, Q9UJ20, Q9UJ21
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM