Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06685

- AT1A1_RAT

UniProt

P06685 - AT1A1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. phosphatase activity Source: Ensembl
  6. phosphatidylinositol 3-kinase binding Source: RGD
  7. potassium ion 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. cardiac muscle contraction Source: BHF-UCL
  4. cellular response to mechanical stimulus Source: RGD
  5. energy coupled proton transmembrane transport, against electrochemical gradient Source: RGD
  6. membrane hyperpolarization Source: RGD
  7. negative regulation of glucocorticoid biosynthetic process Source: Ensembl
  8. negative regulation of heart contraction Source: Ensembl
  9. positive regulation of heart contraction Source: Ensembl
  10. positive regulation of striated muscle contraction Source: Ensembl
  11. potassium ion import Source: RGD
  12. potassium ion transport Source: RGD
  13. regulation of blood pressure Source: Ensembl
  14. regulation of cardiac muscle cell contraction Source: RGD
  15. regulation of sodium ion transport Source: UniProtKB
  16. regulation of the force of heart contraction Source: Ensembl
  17. relaxation of cardiac muscle Source: BHF-UCL
  18. response to drug Source: Ensembl
  19. sodium ion transmembrane transport Source: GOC
  20. sodium ion transport Source: RGD
Complete GO annotation...

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. apical plasma membrane Source: Ensembl
  2. basolateral plasma membrane Source: Ensembl
  3. caveola Source: RGD
  4. endoplasmic reticulum Source: BHF-UCL
  5. endosome Source: RGD
  6. extracellular vesicular exosome Source: Ensembl
  7. Golgi apparatus Source: BHF-UCL
  8. integral component of membrane Source: UniProtKB
  9. intercalated disc Source: BHF-UCL
  10. membrane Source: RGD
  11. membrane raft Source: RGD
  12. plasma membrane Source: BHF-UCL
  13. sarcolemma Source: BHF-UCL
  14. sodium:potassium-exchanging ATPase complex Source: RGD
  15. T-tubule Source: BHF-UCL
Complete GO annotation...

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.
GeneTreeiENSGT00760000119003.
HOVERGENiHBG004298.
InParanoidiP06685.
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

        10         20         30         40         50
MGKGVGRDKY EPAAVSEHGD KKSKKAKKER DMDELKKEVS MDDHKLSLDE
60 70 80 90 100
LHRKYGTDLS RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF
110 120 130 140 150
SMLLWIGAIL CFLAYGIRSA TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ
160 170 180 190 200
EAKSSKIMES FKNMVPQQAL VIRNGEKMSI NAEDVVVGDL VEVKGGDRIP
210 220 230 240 250
ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR NIAFFSTNCV
260 270 280 290 300
EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV
310 320 330 340 350
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR
360 370 380 390 400
MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA
410 420 430 440 450
DTTENQSGVS FDKTSATWFA LSRIAGLCNR AVFQANQENL PILKRAVAGD
460 470 480 490 500
ASESALLKCI EVCCGSVMEM REKYTKIVEI PFNSTNKYQL SIHKNPNASE
510 520 530 540 550
PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN AYLELGGLGE
560 570 580 590 600
RVLGFCHLLL PDEQFPEGFQ FDTDEVNFPV DNLCFVGLIS MIDPPRAAVP
610 620 630 640 650
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI
660 670 680 690 700
PVNQVNPRDA KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI
710 720 730 740 750
IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIVGSD VSKQAADMIL
760 770 780 790 800
LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LIFIIANIPL
810 820 830 840 850
PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK TDKLVNERLI
860 870 880 890 900
SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWINDVED
910 920 930 940 950
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK
960 970 980 990 1000
NKILIFGLFE ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV
1010 1020
YDEVRKLIIR RRPGGWVEKE TYY
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 ENSGT00760000119003.
HOVERGENi HBG004298.
InParanoidi P06685.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 155 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