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P05023

- AT1A1_HUMAN

UniProt

P05023 - AT1A1_HUMAN

Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

ATP1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei376 – 37614-aspartylphosphate intermediateBy similarity
    Binding sitei487 – 4871ATPBy similarity
    Metal bindingi717 – 7171MagnesiumBy similarity
    Metal bindingi721 – 7211MagnesiumBy similarity

    GO - Molecular functioni

    1. ADP binding Source: Ensembl
    2. ATP binding Source: UniProtKB-KW
    3. chaperone binding Source: BHF-UCL
    4. potassium ion binding Source: Ensembl
    5. protein binding Source: UniProtKB
    6. sodium:potassium-exchanging ATPase activity Source: UniProtKB
    7. sodium ion binding Source: Ensembl

    GO - Biological processi

    1. ATP biosynthetic process Source: InterPro
    2. cellular response to mechanical stimulus Source: Ensembl
    3. ion transmembrane transport Source: Reactome
    4. membrane hyperpolarization Source: Ensembl
    5. negative regulation of glucocorticoid biosynthetic process Source: Ensembl
    6. negative regulation of heart contraction Source: Ensembl
    7. positive regulation of heart contraction Source: Ensembl
    8. positive regulation of striated muscle contraction Source: Ensembl
    9. potassium ion import Source: Ensembl
    10. regulation of blood pressure Source: Ensembl
    11. regulation of cardiac muscle cell contraction Source: Ensembl
    12. regulation of sodium ion transport Source: UniProtKB
    13. regulation of the force of heart contraction Source: Ensembl
    14. response to drug Source: Ensembl
    15. sodium ion transmembrane transport Source: GOC
    16. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Ion transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Sodium

    Enzyme and pathway databases

    ReactomeiREACT_25149. Ion transport by P-type ATPases.

    Protein family/group databases

    TCDBi3.A.3.1.1. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sodium/potassium-transporting ATPase subunit alpha-1 (EC:3.6.3.9)
    Short name:
    Na(+)/K(+) ATPase alpha-1 subunit
    Alternative name(s):
    Sodium pump subunit alpha-1
    Gene namesi
    Name:ATP1A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:799. ATP1A1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. caveola Source: Ensembl
    3. endoplasmic reticulum Source: BHF-UCL
    4. endosome Source: Ensembl
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi apparatus Source: BHF-UCL
    7. integral component of membrane Source: UniProtKB
    8. melanosome Source: UniProtKB-SubCell
    9. membrane Source: ProtInc
    10. plasma membrane Source: UniProtKB
    11. protein complex Source: MGI
    12. sodium:potassium-exchanging ATPase complex Source: ProtInc
    13. T-tubule Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti85142. Aldosterone-producing adenoma.
    PharmGKBiPA62.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 55PRO_0000002483
    Chaini6 – 10231018Sodium/potassium-transporting ATPase subunit alpha-1PRO_0000002484Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91N6-acetyllysineBy similarity
    Modified residuei10 – 101PhosphotyrosineBy similarity
    Modified residuei16 – 161PhosphoserineBy similarity
    Modified residuei21 – 211N6-acetyllysineBy similarity
    Modified residuei260 – 2601PhosphotyrosineBy similarity
    Modified residuei542 – 5421Phosphotyrosine1 Publication
    Modified residuei661 – 6611N6-succinyllysineBy similarity
    Modified residuei943 – 9431Phosphoserine; by PKABy similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP05023.
    PaxDbiP05023.
    PeptideAtlasiP05023.
    PRIDEiP05023.

    PTM databases

    PhosphoSiteiP05023.

    Expressioni

    Gene expression databases

    ArrayExpressiP05023.
    BgeeiP05023.
    CleanExiHS_ATP1A1.
    GenevestigatoriP05023.

    Organism-specific databases

    HPAiCAB018702.

    Interactioni

    Subunit structurei

    Interacts with SIK1 By similarity. Composed of three subunits: alpha (catalytic), beta and gamma. Binds the HLA class II histocompatibility antigen, DR1. Interacts with SLC35G1 and STIM1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TPT1P136935EBI-358778,EBI-1783169

    Protein-protein interaction databases

    BioGridi106966. 36 interactions.
    DIPiDIP-38196N.
    IntActiP05023. 24 interactions.
    MINTiMINT-4998863.
    STRINGi9606.ENSP00000295598.

    Structurei

    3D structure databases

    ProteinModelPortaliP05023.
    SMRiP05023. Positions 30-1023.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini6 – 8782CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini109 – 13123ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini153 – 288136CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini309 – 32012ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini339 – 772434CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini793 – 80210ExtracellularSequence Analysis
    Topological domaini824 – 84320CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini867 – 91852ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini939 – 95113CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini971 – 98515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1007 – 102317CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei88 – 10821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei132 – 15221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei289 – 30820HelicalSequence AnalysisAdd
    BLAST
    Transmembranei321 – 33818HelicalSequence AnalysisAdd
    BLAST
    Transmembranei773 – 79220HelicalSequence AnalysisAdd
    BLAST
    Transmembranei803 – 82321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei844 – 86623HelicalSequence AnalysisAdd
    BLAST
    Transmembranei919 – 93820HelicalSequence AnalysisAdd
    BLAST
    Transmembranei952 – 97019HelicalSequence AnalysisAdd
    BLAST
    Transmembranei986 – 100621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni82 – 843Phosphoinositide-3 kinase bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    HOVERGENiHBG004298.
    InParanoidiP05023.
    KOiK01539.
    OMAiFLPTHLL.
    OrthoDBiEOG7327N0.
    PhylomeDBiP05023.
    TreeFamiTF312838.

    Family and domain databases

    Gene3Di1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProiIPR006068. 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]
    PfamiPF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SMARTiSM00831. Cation_ATPase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsiTIGR01106. ATPase-IIC_X-K. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P05023-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGKGVGRDKY EPAAVSEQGD KKGKKGKKDR DMDELKKEVS MDDHKLSLDE     50
    LHRKYGTDLS RGLTSARAAE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF 100
    SMLLWIGAIL CFLAYSIQAA TEEEPQNDNL YLGVVLSAVV IITGCFSYYQ 150
    EAKSSKIMES FKNMVPQQAL VIRNGEKMSI NAEEVVVGDL VEVKGGDRIP 200
    ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR NIAFFSTNCV 250
    EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV 300
    FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR 350
    MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA 400
    DTTENQSGVS FDKTSATWLA LSRIAGLCNR AVFQANQENL PILKRAVAGD 450
    ASESALLKCI ELCCGSVKEM RERYAKIVEI PFNSTNKYQL SIHKNPNTSE 500
    PQHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN AYLELGGLGE 550
    RVLGFCHLFL PDEQFPEGFQ FDTDDVNFPI DNLCFVGLIS MIDPPRAAVP 600
    DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI 650
    PVSQVNPRDA KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI 700
    IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIAGSD VSKQAADMIL 750
    LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LIFIIANIPL 800
    PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK TDKLVNERLI 850
    SMAYGQIGMI QALGGFFTYF VILAENGFLP IHLLGLRVDW DDRWINDVED 900
    SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK 950
    NKILIFGLFE ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV 1000
    YDEVRKLIIR RRPGGWVEKE TYY 1023
    Length:1,023
    Mass (Da):112,896
    Last modified:August 13, 1987 - v1
    Checksum:iF3C6FDE04FB3F667
    GO
    Isoform 2 (identifier: P05023-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:681
    Mass (Da):74,140
    Checksum:iB74A8E7E31E975AD
    GO
    Isoform 3 (identifier: P05023-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: Missing.

    Show »
    Length:992
    Mass (Da):109,550
    Checksum:i6F607167FD03A23B
    GO
    Isoform 4 (identifier: P05023-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,023
    Mass (Da):113,000
    Checksum:iB5B35DE0B0650011
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti248 – 2481N → S in BAG37313. (PubMed:14702039)Curated
    Sequence conflicti323 – 3231F → L in BAH11971. (PubMed:14702039)Curated
    Sequence conflicti475 – 4751A → T in CAA27390. 1 PublicationCurated
    Sequence conflicti499 – 4991S → A in CAA27390. 1 PublicationCurated
    Sequence conflicti502 – 5021Q → R in CAA27390. 1 PublicationCurated
    Sequence conflicti523 – 5231L → I in CAA27390. 1 PublicationCurated
    Sequence conflicti892 – 8921D → G in BAH11971. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471S → I.
    Corresponds to variant rs12564026 [ dbSNP | Ensembl ].
    VAR_048374

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3131Missing in isoform 3. 1 PublicationVSP_044242Add
    BLAST
    Alternative sequencei2 – 43GKG → AFK in isoform 4. 1 PublicationVSP_047309
    Alternative sequencei638 – 68144NETVE…QLDDI → SGPMSRGKSWSSPATQPSSS VSWWCSGPTWSSVRPGGIRS SSRG in isoform 2. 1 PublicationVSP_000415Add
    BLAST
    Alternative sequencei682 – 1023342Missing in isoform 2. 1 PublicationVSP_000416Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS53351.1. [P05023-4]
    CCDS53352.1. [P05023-3]
    CCDS887.1. [P05023-1]
    PIRiA24414.
    RefSeqiNP_000692.2. NM_000701.7. [P05023-1]
    NP_001153705.1. NM_001160233.1. [P05023-4]
    NP_001153706.1. NM_001160234.1. [P05023-3]
    XP_006710718.1. XM_006710655.1. [P05023-3]
    UniGeneiHs.371889.

    Genome annotation databases

    EnsembliENST00000295598; ENSP00000295598; ENSG00000163399. [P05023-1]
    ENST00000369496; ENSP00000358508; ENSG00000163399. [P05023-3]
    ENST00000537345; ENSP00000445306; ENSG00000163399. [P05023-4]
    GeneIDi476.
    KEGGihsa:476.
    UCSCiuc001ege.3. human. [P05023-1]

    Polymorphism databases

    DMDMi114374.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS53351.1. [P05023-4 ]
    CCDS53352.1. [P05023-3 ]
    CCDS887.1. [P05023-1 ]
    PIRi A24414.
    RefSeqi NP_000692.2. NM_000701.7. [P05023-1 ]
    NP_001153705.1. NM_001160233.1. [P05023-4 ]
    NP_001153706.1. NM_001160234.1. [P05023-3 ]
    XP_006710718.1. XM_006710655.1. [P05023-3 ]
    UniGenei Hs.371889.

    3D structure databases

    ProteinModelPortali P05023.
    SMRi P05023. Positions 30-1023.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106966. 36 interactions.
    DIPi DIP-38196N.
    IntActi P05023. 24 interactions.
    MINTi MINT-4998863.
    STRINGi 9606.ENSP00000295598.

    Chemistry

    BindingDBi P05023.
    ChEMBLi CHEMBL2095186.
    DrugBanki DB00511. Acetyldigitoxin.
    DB01430. Almitrine.
    DB01370. Aluminium.
    DB01244. Bepridil.
    DB01158. Bretylium.
    DB01188. Ciclopirox.
    DB01078. Deslanoside.
    DB01119. Diazoxide.
    DB01396. Digitoxin.
    DB00390. Digoxin.
    DB00903. Ethacrynic acid.
    DB00774. Hydroflumethiazide.
    DB01092. Ouabain.
    DB01021. Trichlormethiazide.
    GuidetoPHARMACOLOGYi 833.

    Protein family/group databases

    TCDBi 3.A.3.1.1. the p-type atpase (p-atpase) superfamily.

    PTM databases

    PhosphoSitei P05023.

    Polymorphism databases

    DMDMi 114374.

    Proteomic databases

    MaxQBi P05023.
    PaxDbi P05023.
    PeptideAtlasi P05023.
    PRIDEi P05023.

    Protocols and materials databases

    DNASUi 476.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295598 ; ENSP00000295598 ; ENSG00000163399 . [P05023-1 ]
    ENST00000369496 ; ENSP00000358508 ; ENSG00000163399 . [P05023-3 ]
    ENST00000537345 ; ENSP00000445306 ; ENSG00000163399 . [P05023-4 ]
    GeneIDi 476.
    KEGGi hsa:476.
    UCSCi uc001ege.3. human. [P05023-1 ]

    Organism-specific databases

    CTDi 476.
    GeneCardsi GC01P116915.
    HGNCi HGNC:799. ATP1A1.
    HPAi CAB018702.
    MIMi 182310. gene.
    neXtProti NX_P05023.
    Orphaneti 85142. Aldosterone-producing adenoma.
    PharmGKBi PA62.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0474.
    HOVERGENi HBG004298.
    InParanoidi P05023.
    KOi K01539.
    OMAi FLPTHLL.
    OrthoDBi EOG7327N0.
    PhylomeDBi P05023.
    TreeFami TF312838.

    Enzyme and pathway databases

    Reactomei REACT_25149. Ion transport by P-type ATPases.

    Miscellaneous databases

    ChiTaRSi ATP1A1. human.
    GeneWikii ATPase,_Na%2B/K%2B_transporting,_alpha_1.
    GenomeRNAii 476.
    NextBioi 1971.
    PROi P05023.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05023.
    Bgeei P05023.
    CleanExi HS_ATP1A1.
    Genevestigatori P05023.

    Family and domain databases

    Gene3Di 1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProi IPR006068. 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 ]
    Pfami PF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SMARTi SM00831. Cation_ATPase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsi TIGR01106. ATPase-IIC_X-K. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    16. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to multiple transporters."
      Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.
      Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC35G1 AND STIM1.

    Entry informationi

    Entry nameiAT1A1_HUMAN
    AccessioniPrimary (citable) accession number: P05023
    Secondary accession number(s): B2RBR6
    , B7Z2T5, B7Z3U6, F5H3A1, Q16689, Q6LDM4, Q9UCN1, Q9UJ20, Q9UJ21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 178 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3