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P06685

- AT1A1_RAT

UniProt

P06685 - AT1A1_RAT

Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

Atp1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      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 – 4871ATP1 Publication
    Metal bindingi717 – 7171MagnesiumBy similarity
    Metal bindingi721 – 7211MagnesiumBy similarity

    GO - Molecular functioni

    1. ADP binding Source: RGD
    2. ankyrin binding Source: BHF-UCL
    3. ATP binding Source: RGD
    4. chaperone binding Source: BHF-UCL
    5. phosphatidylinositol 3-kinase binding Source: RGD
    6. potassium ion binding Source: RGD
    7. protein binding Source: RGD
    8. protein domain specific binding Source: RGD
    9. protein kinase binding Source: UniProtKB
    10. sodium:potassium-exchanging ATPase activity Source: UniProtKB
    11. sodium ion binding Source: RGD

    GO - Biological processi

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

    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

    SABIO-RKP06685.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi2167. Atp1a1.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161S → A: Dopamine fails to increase phosphoinositide-3 kinase activity and to promote its interaction with Na(+)/K(+) ATPase. 1 Publication
    Mutagenesisi83 – 831P → R: Dopamine fails to increase phosphoinositide-3 kinase activity and to promote its interaction with Na(+)/K(+) ATPase. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 551 PublicationPRO_0000002489
    Chaini6 – 10231018Sodium/potassium-transporting ATPase subunit alpha-1PRO_0000002490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91N6-acetyllysineBy similarity
    Modified residuei10 – 101Phosphotyrosine1 Publication
    Modified residuei16 – 161Phosphoserine; by PKC1 Publication
    Modified residuei21 – 211N6-acetyllysineBy similarity
    Modified residuei23 – 231Phosphoserine; by PKC2 Publications
    Modified residuei260 – 2601PhosphotyrosineBy similarity
    Modified residuei542 – 5421PhosphotyrosineBy similarity
    Modified residuei661 – 6611N6-succinyllysineBy similarity
    Modified residuei943 – 9431Phosphoserine; by PKA1 Publication

    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.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP06685.
    PRIDEiP06685.

    PTM databases

    PhosphoSiteiP06685.

    Expressioni

    Gene expression databases

    GenevestigatoriP06685.

    Interactioni

    Subunit structurei

    Interacts with SLC35G1 and STIM1 By similarity. Composed of three subunits: alpha (catalytic), beta and gamma. Interacts with SIK1.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi246399. 10 interactions.
    IntActiP06685. 2 interactions.
    MINTiMINT-3089277.
    STRINGi10116.ENSRNOP00000045650.

    Structurei

    Secondary structure

    1
    1023
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi394 – 3963
    Beta strandi403 – 4053
    Helixi416 – 42712
    Beta strandi431 – 4355
    Beta strandi438 – 4403
    Helixi442 – 4443
    Beta strandi447 – 4493
    Turni451 – 4533
    Helixi454 – 4618
    Turni462 – 4643
    Helixi467 – 4737
    Beta strandi478 – 4803
    Turni483 – 4853
    Beta strandi489 – 4946
    Beta strandi496 – 5005
    Beta strandi502 – 5098
    Helixi511 – 5155
    Beta strandi518 – 5214
    Beta strandi526 – 5294
    Helixi532 – 54615
    Beta strandi556 – 5583
    Turni562 – 5643
    Turni572 – 5743

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MO7NMR-A386-595[»]
    1MO8NMR-A386-595[»]
    ProteinModelPortaliP06685.
    SMRiP06685. Positions 26-1023.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06685.

    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 binding

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    GeneTreeiENSGT00560000076866.
    HOVERGENiHBG004298.
    KOiK01539.
    OMAiFLPTHLL.
    OrthoDBiEOG7327N0.
    PhylomeDBiP06685.

    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. 1 hit.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P06685-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKGVGRDKY EPAAVSEHGD KKSKKAKKER DMDELKKEVS MDDHKLSLDE     50
    LHRKYGTDLS RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF 100
    SMLLWIGAIL CFLAYGIRSA TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ 150
    EAKSSKIMES FKNMVPQQAL VIRNGEKMSI NAEDVVVGDL VEVKGGDRIP 200
    ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR NIAFFSTNCV 250
    EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV 300
    FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR 350
    MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA 400
    DTTENQSGVS FDKTSATWFA LSRIAGLCNR AVFQANQENL PILKRAVAGD 450
    ASESALLKCI EVCCGSVMEM REKYTKIVEI PFNSTNKYQL SIHKNPNASE 500
    PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN AYLELGGLGE 550
    RVLGFCHLLL PDEQFPEGFQ FDTDEVNFPV DNLCFVGLIS MIDPPRAAVP 600
    DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI 650
    PVNQVNPRDA KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI 700
    IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIVGSD VSKQAADMIL 750
    LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LIFIIANIPL 800
    PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK TDKLVNERLI 850
    SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWINDVED 900
    SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK 950
    NKILIFGLFE ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV 1000
    YDEVRKLIIR RRPGGWVEKE TYY 1023
    Length:1,023
    Mass (Da):113,054
    Last modified:January 1, 1988 - v1
    Checksum:i85E98233EE6C18E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 692AA → PV in AAA41671. (PubMed:2822726)Curated
    Sequence conflicti175 – 1751G → E in AAA41671. (PubMed:2822726)Curated
    Sequence conflicti188 – 1881G → V in AAA41671. (PubMed:2822726)Curated
    Sequence conflicti335 – 3351G → V in AAA41671. (PubMed:2822726)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14511 mRNA. Translation: AAA40775.1.
    X05882 mRNA. Translation: CAA29306.1.
    M28647 mRNA. Translation: AAA41671.1.
    BC061968 mRNA. Translation: AAH61968.1.
    M11733 mRNA. Translation: AAA40783.1.
    X53233 Genomic DNA. Translation: CAA37325.1.
    X53234 Genomic DNA. Translation: CAA37326.1.
    PIRiA24639.
    RefSeqiNP_036636.1. NM_012504.1.
    UniGeneiRn.217534.
    Rn.2992.

    Genome annotation databases

    EnsembliENSRNOT00000040430; ENSRNOP00000045650; ENSRNOG00000030019.
    GeneIDi24211.
    KEGGirno:24211.
    UCSCiRGD:2167. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14511 mRNA. Translation: AAA40775.1 .
    X05882 mRNA. Translation: CAA29306.1 .
    M28647 mRNA. Translation: AAA41671.1 .
    BC061968 mRNA. Translation: AAH61968.1 .
    M11733 mRNA. Translation: AAA40783.1 .
    X53233 Genomic DNA. Translation: CAA37325.1 .
    X53234 Genomic DNA. Translation: CAA37326.1 .
    PIRi A24639.
    RefSeqi NP_036636.1. NM_012504.1.
    UniGenei Rn.217534.
    Rn.2992.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MO7 NMR - A 386-595 [» ]
    1MO8 NMR - A 386-595 [» ]
    ProteinModelPortali P06685.
    SMRi P06685. Positions 26-1023.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246399. 10 interactions.
    IntActi P06685. 2 interactions.
    MINTi MINT-3089277.
    STRINGi 10116.ENSRNOP00000045650.

    Chemistry

    BindingDBi P06685.

    PTM databases

    PhosphoSitei P06685.

    Proteomic databases

    PaxDbi P06685.
    PRIDEi P06685.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000040430 ; ENSRNOP00000045650 ; ENSRNOG00000030019 .
    GeneIDi 24211.
    KEGGi rno:24211.
    UCSCi RGD:2167. rat.

    Organism-specific databases

    CTDi 476.
    RGDi 2167. Atp1a1.

    Phylogenomic databases

    eggNOGi COG0474.
    GeneTreei ENSGT00560000076866.
    HOVERGENi HBG004298.
    KOi K01539.
    OMAi FLPTHLL.
    OrthoDBi EOG7327N0.
    PhylomeDBi P06685.

    Enzyme and pathway databases

    SABIO-RK P06685.

    Miscellaneous databases

    EvolutionaryTracei P06685.
    NextBioi 602617.

    Gene expression databases

    Genevestigatori P06685.

    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. 1 hit.
    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. "Molecular cloning of three distinct forms of the Na+,K+-ATPase alpha-subunit from rat brain."
      Shull G.E., Greeb J., Lingrel J.B.
      Biochemistry 25:8125-8132(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain and Kidney.
    2. "Primary structures of two types of alpha-subunit of rat brain Na+,K+,-ATPase deduced from cDNA sequences."
      Hara Y., Urayama O., Kawakami K., Nojima H., Nagamune H., Kojima T., Ohta T., Nagano K., Nakao M.
      J. Biochem. 102:43-58(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Three differentially expressed Na,K-ATPase alpha subunit isoforms: structural and functional implications."
      Herrera V.L.M., Emanuel J.R., Ruiz-Opazo N., Levenson R., Nadal-Ginard B.
      J. Cell Biol. 105:1855-1865(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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].
      Tissue: Prostate.
    5. Lubec G., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 157-162; 597-605; 630-647; 662-671 AND 744-773, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 489-533.
      Tissue: Brain.
    7. "Cloning and analysis of the 5'-flanking region of rat Na+/K(+)-ATPase alpha 1 subunit gene."
      Yagawa Y., Kawakami K., Nagano K.
      Biochim. Biophys. Acta 1049:286-292(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
    8. "Identification of the phosphorylation site for cAMP-dependent protein kinase on Na+,K(+)-ATPase and effects of site-directed mutagenesis."
      Fisone G., Cheng S.X.-J., Nairn A.C., Czernik A.J., Hemmings H.C. Jr., Hoeoeg J.-O., Bertorello A.M., Kaiser R., Bergman T., Joernvall H., Aperia A., Greengard P.
      J. Biol. Chem. 269:9368-9373(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CAMP-DEPENDENT KINASE.
    9. "Regulation of rat Na(+)-K(+)-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA."
      Cheng X.J., Hoeoeg J.O., Nairn A.C., Greengard P., Aperia A.
      Am. J. Physiol. 273:C1981-C1986(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-23 AND SER-943.
    10. "Insulin-induced stimulation of Na+,K(+)-ATPase activity in kidney proximal tubule cells depends on phosphorylation of the alpha-subunit at Tyr-10."
      Feraille E., Carranza M.L., Gonin S., Beguin P., Pedemonte C., Rousselot M., Caverzasio J., Geering K., Martin P.Y., Favre H.
      Mol. Biol. Cell 10:2847-2859(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-10.
    11. "Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C."
      Feschenko M.S., Sweadner K.J.
      J. Biol. Chem. 270:14072-14077(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PHOSPHORYLATION AT SER-16 AND SER-23 BY PROTEIN KINASE C.
    12. "Phosphoinositide-3 kinase binds to a proline-rich motif in the Na+, K+-ATPase alpha subunit and regulates its trafficking."
      Yudowski G.A., Efendiev R., Pedemonte C.H., Katz A.I., Berggren P.-O., Bertorello A.M.
      Proc. Natl. Acad. Sci. U.S.A. 97:6556-6561(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: BINDING SITE FOR PHOSPHOINOSITIDE-3 KINASE, MUTAGENESIS.
    13. "SIK1 is part of a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process."
      Sjostrom M., Stenstrom K., Eneling K., Zwiller J., Katz A.I., Takemori H., Bertorello A.M.
      Proc. Natl. Acad. Sci. U.S.A. 104:16922-16927(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION, INTERACTION WITH SIK1.
    14. "ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase."
      Hilge M., Siegal G., Vuister G.W., Guntert P., Gloor S.M., Abrahams J.P.
      Nat. Struct. Biol. 10:468-474(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 383-595 ALONE AND IN COMPLEX WITH ATP, ATP-BINDING SITE.

    Entry informationi

    Entry nameiAT1A1_RAT
    AccessioniPrimary (citable) accession number: P06685
    Secondary accession number(s): Q64609
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3