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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

ATP1A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 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. phosphatase activity Source: Ensembl
  5. potassium ion binding Source: Ensembl
  6. sodium:potassium-exchanging ATPase activity Source: UniProtKB
  7. sodium ion binding Source: Ensembl
  8. steroid hormone binding Source: BHF-UCL

GO - Biological processi

  1. cardiac muscle contraction Source: BHF-UCL
  2. cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
  3. cellular potassium ion homeostasis Source: BHF-UCL
  4. cellular response to mechanical stimulus Source: Ensembl
  5. cellular response to steroid hormone stimulus Source: BHF-UCL
  6. cellular sodium ion homeostasis Source: BHF-UCL
  7. ion transmembrane transport Source: Reactome
  8. membrane hyperpolarization Source: Ensembl
  9. membrane repolarization Source: BHF-UCL
  10. membrane repolarization during cardiac muscle cell action potential Source: BHF-UCL
  11. negative regulation of glucocorticoid biosynthetic process Source: Ensembl
  12. negative regulation of heart contraction Source: Ensembl
  13. positive regulation of heart contraction Source: Ensembl
  14. positive regulation of striated muscle contraction Source: Ensembl
  15. potassium ion import Source: BHF-UCL
  16. regulation of blood pressure Source: Ensembl
  17. regulation of cardiac muscle cell contraction Source: Ensembl
  18. regulation of sodium ion transport Source: UniProtKB
  19. regulation of the force of heart contraction Source: Ensembl
  20. relaxation of cardiac muscle Source: BHF-UCL
  21. response to drug Source: Ensembl
  22. response to glycoside Source: BHF-UCL
  23. sodium ion export from cell Source: BHF-UCL
  24. transmembrane transport Source: Reactome
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

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini6 – 8782CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei88 – 10821HelicalSequence AnalysisAdd
BLAST
Topological domaini109 – 13123ExtracellularSequence AnalysisAdd
BLAST
Transmembranei132 – 15221HelicalSequence AnalysisAdd
BLAST
Topological domaini153 – 288136CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei289 – 30820HelicalSequence AnalysisAdd
BLAST
Topological domaini309 – 32012ExtracellularSequence AnalysisAdd
BLAST
Transmembranei321 – 33818HelicalSequence AnalysisAdd
BLAST
Topological domaini339 – 772434CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei773 – 79220HelicalSequence AnalysisAdd
BLAST
Topological domaini793 – 80210ExtracellularSequence Analysis
Transmembranei803 – 82321HelicalSequence AnalysisAdd
BLAST
Topological domaini824 – 84320CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei844 – 86623HelicalSequence AnalysisAdd
BLAST
Topological domaini867 – 91852ExtracellularSequence AnalysisAdd
BLAST
Transmembranei919 – 93820HelicalSequence AnalysisAdd
BLAST
Topological domaini939 – 95113CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei952 – 97019HelicalSequence AnalysisAdd
BLAST
Topological domaini971 – 98515ExtracellularSequence AnalysisAdd
BLAST
Transmembranei986 – 100621HelicalSequence AnalysisAdd
BLAST
Topological domaini1007 – 102317CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

BgeeiP05023.
CleanExiHS_ATP1A1.
ExpressionAtlasiP05023. baseline and differential.
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. 42 interactions.
DIPiDIP-38196N.
IntActiP05023. 24 interactions.
MINTiMINT-4998863.
STRINGi9606.ENSP00000295598.

Structurei

3D structure databases

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

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.
GeneTreeiENSGT00760000119003.
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.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005775. P-type_ATPase_IIC.
IPR001757. P_typ_ATPase.
[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. AlignAdd to basket

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

        10         20         30         40         50
MGKGVGRDKY EPAAVSEQGD KKGKKGKKDR DMDELKKEVS MDDHKLSLDE
60 70 80 90 100
LHRKYGTDLS RGLTSARAAE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF
110 120 130 140 150
SMLLWIGAIL CFLAYSIQAA TEEEPQNDNL YLGVVLSAVV IITGCFSYYQ
160 170 180 190 200
EAKSSKIMES FKNMVPQQAL VIRNGEKMSI NAEEVVVGDL VEVKGGDRIP
210 220 230 240 250
ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR NIAFFSTNCV
260 270 280 290 300
EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV
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 FDKTSATWLA LSRIAGLCNR AVFQANQENL PILKRAVAGD
460 470 480 490 500
ASESALLKCI ELCCGSVKEM RERYAKIVEI PFNSTNKYQL SIHKNPNTSE
510 520 530 540 550
PQHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN AYLELGGLGE
560 570 580 590 600
RVLGFCHLFL PDEQFPEGFQ FDTDDVNFPI DNLCFVGLIS MIDPPRAAVP
610 620 630 640 650
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI
660 670 680 690 700
PVSQVNPRDA KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI
710 720 730 740 750
IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIAGSD 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 IHLLGLRVDW DDRWINDVED
910 920 930 940 950
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK
960 970 980 990 1000
NKILIFGLFE ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV
1010 1020
YDEVRKLIIR RRPGGWVEKE TYY
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 (Ref. 13) Curated
Sequence conflicti499 – 4991S → A in CAA27390 (Ref. 13) Curated
Sequence conflicti502 – 5021Q → R in CAA27390 (Ref. 13) Curated
Sequence conflicti523 – 5231L → I in CAA27390 (Ref. 13) Curated
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi106966. 42 interactions.
DIPiDIP-38196N.
IntActiP05023. 24 interactions.
MINTiMINT-4998863.
STRINGi9606.ENSP00000295598.

Chemistry

ChEMBLiCHEMBL2095186.
DrugBankiDB00511. 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.
GuidetoPHARMACOLOGYi833.

Protein family/group databases

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

PTM databases

PhosphoSiteiP05023.

Polymorphism databases

DMDMi114374.

Proteomic databases

MaxQBiP05023.
PaxDbiP05023.
PeptideAtlasiP05023.
PRIDEiP05023.

Protocols and materials databases

DNASUi476.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi476.
GeneCardsiGC01P116915.
HGNCiHGNC:799. ATP1A1.
HPAiCAB018702.
MIMi182310. gene.
neXtProtiNX_P05023.
Orphaneti85142. Aldosterone-producing adenoma.
PharmGKBiPA62.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOVERGENiHBG004298.
InParanoidiP05023.
KOiK01539.
OMAiFLPTHLL.
OrthoDBiEOG7327N0.
PhylomeDBiP05023.
TreeFamiTF312838.

Enzyme and pathway databases

ReactomeiREACT_25149. Ion transport by P-type ATPases.

Miscellaneous databases

ChiTaRSiATP1A1. human.
GeneWikiiATPase,_Na%2B/K%2B_transporting,_alpha_1.
GenomeRNAii476.
NextBioi1971.
PROiP05023.
SOURCEiSearch...

Gene expression databases

BgeeiP05023.
CleanExiHS_ATP1A1.
ExpressionAtlasiP05023. baseline and differential.
GenevestigatoriP05023.

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.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005775. P-type_ATPase_IIC.
IPR001757. P_typ_ATPase.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: March 4, 2015
This is version 182 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.