Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00136
Entry Name
UniProt Accession
Theoretical PI
5.33
Molecular Weight
112896.1
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Sodium/potassium-transporting ATPase subunit alpha-1
Protein Synonyms/Alias
Na(+)/K(+) ATPase alpha-1 subunit; 3.6.3.9; Sodium pump subunit alpha-1;
Gene Name
ATP1A1
Gene Synonyms/Alias
Created Date
13-AUG-1987
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
428
Canonical
LSRIAGLCNRAVFQA
[1]
S-Palmitoylation
464
Canonical
LKCIELCCGSVKEMR
[1]
S-Palmitoylation
606
Canonical
VPDAVGKCRSAGIKV
[1]
S-Palmitoylation
937
Canonical
QWADLVICKTRRNSV
[1]
S-Palmitoylation
990
Canonical
LKPTWWFCAFPYSLL
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
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.
Sequence Annotation
Topological domain: 6 87 Cytoplasmic.
Transmembrane: 88 108 Helical.
Topological domain: 109 131 Extracellular.
Transmembrane: 132 152 Helical.
Topological domain: 153 288 Cytoplasmic.
Transmembrane: 289 308 Helical.
Topological domain: 309 320 Extracellular.
Transmembrane: 321 338 Helical.
Topological domain: 339 772 Cytoplasmic.
Transmembrane: 773 792 Helical.
Topological domain: 793 802 Extracellular.
Transmembrane: 803 823 Helical.
Topological domain: 824 843 Cytoplasmic.
Transmembrane: 844 866 Helical.
Topological domain: 867 918 Extracellular.
Transmembrane: 919 938 Helical.
Topological domain: 939 951 Cytoplasmic.
Transmembrane: 952 970 Helical.
Topological domain: 971 985 Extracellular.
Transmembrane: 986 1006 Helical.
Topological domain: 1007 1023 Cytoplasmic.
Region: 82 84 Phosphoinositide-3 kinase binding.
Active site: 376 376 4-aspartylphosphate intermediate.
Metal binding site: 717 717 Magnesium.
Metal binding site: 721 721 Magnesium.
Binding site: 487 487 ATP.
Modified residue: 9 9 N6-acetyllysine.
Modified residue: 10 10 Phosphotyrosine.
Modified residue: 16 16 Phosphoserine.
Modified residue: 21 21 N6-acetyllysine.
Modified residue: 260 260 Phosphotyrosine.
Modified residue: 542 542 Phosphotyrosine.
Modified residue: 661 661 N6-succinyllysine.
Modified residue: 943 943 Phosphoserine; by PKA.
Protein Length
1023 AA.
Protein Sequence
(Canonical)
MGKGVGRDKY EPAAVSEQGD KKGKKGKKDR DMDELKKEVS MDDHKLSLDE LHRKYGTDLS  60
RGLTSARAAE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SMLLWIGAIL CFLAYSIQAA  120
TEEEPQNDNL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI  180
NAEEVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR  240
NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV  300
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN  360
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWLA  420
LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI ELCCGSVKEM RERYAKIVEI  480
PFNSTNKYQL SIHKNPNTSE PQHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN  540
AYLELGGLGE RVLGFCHLFL PDEQFPEGFQ FDTDDVNFPI DNLCFVGLIS MIDPPRAAVP  600
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA  660
KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN  720
DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL  780
TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK  840
TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP IHLLGLRVDW DDRWINDVED  900
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE  960
ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE  1020
TYY                                                                1023
FASTA
(Canonical)
>LipidDB-9606-00136|P05023
MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLS
RGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAA
TEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSI
NAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETR
NIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAV
FLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKN
LEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLA
LSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEI
PFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQN
AYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVP
DAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDA
KACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVN
DSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTL
TSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPK
TDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVED
SYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFE
ETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKE
TYY
Gene Ontology
GO:0016324; C:apical plasma membrane; IEA:Ensembl
GO:0016323; C:basolateral plasma membrane; IEA:Ensembl
GO:0005901; C:caveola; IEA:Ensembl
GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL
GO:0005768; C:endosome; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005794; C:Golgi apparatus; ISS:BHF-UCL
GO:0016021; C:integral component of membrane; ISS:UniProtKB
GO:0016020; C:membrane; TAS:ProtInc
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0043234; C:protein complex; IDA:MGI
GO:0042383; C:sarcolemma; ISS:BHF-UCL
GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL
GO:0030315; C:T-tubule; IEA:Ensembl
GO:0031982; C:vesicle; IDA:UniProtKB
GO:0043531; F:ADP binding; IEA:Ensembl
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0051087; F:chaperone binding; IPI:BHF-UCL
GO:0016791; F:phosphatase activity; IEA:Ensembl
GO:0030955; F:potassium ion binding; IEA:Ensembl
GO:0031402; F:sodium ion binding; IEA:Ensembl
GO:0005391; F:sodium:potassium-exchanging ATPase activity; ISS:UniProtKB
GO:1990239; F:steroid hormone binding; IDA:BHF-UCL
GO:0006754; P:ATP biosynthetic process; IEA:InterPro
GO:0060048; P:cardiac muscle contraction; TAS:BHF-UCL
GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; TAS:BHF-UCL
GO:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL
GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl
GO:0071383; P:cellular response to steroid hormone stimulus; IDA:BHF-UCL
GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL
GO:0034220; P:ion transmembrane transport; TAS:Reactome
GO:0060081; P:membrane hyperpolarization; IEA:Ensembl
GO:0086009; P:membrane repolarization; IDA:BHF-UCL
GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IC:BHF-UCL
GO:0031947; P:negative regulation of glucocorticoid biosynthetic process; IEA:Ensembl
GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl
GO:0045823; P:positive regulation of heart contraction; IEA:Ensembl
GO:0045989; P:positive regulation of striated muscle contraction; IEA:Ensembl
GO:0010107; P:potassium ion import; IDA:BHF-UCL
GO:0008217; P:regulation of blood pressure; IEA:Ensembl
GO:0086004; P:regulation of cardiac muscle cell contraction; IEA:Ensembl
GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB
GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl
GO:0055119; P:relaxation of cardiac muscle; TAS:BHF-UCL
GO:0042493; P:response to drug; IEA:Ensembl
GO:0036376; P:sodium ion export from cell; IDA:BHF-UCL
GO:0055085; P:transmembrane transport; TAS:Reactome
Interpro
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N
InterPro; IPR023299; ATPase_P-typ_cyto_domN
InterPro; IPR005775; ATPase_P-typ_Na/K_IIC
InterPro; IPR018303; ATPase_P-typ_P_site
InterPro; IPR023298; ATPase_P-typ_TM_dom
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A
InterPro; IPR001757; Cation_transp_P_typ_ATPase
InterPro; IPR023214; HAD-like_dom
Pfam
Pfam; PF00689; Cation_ATPase_C;
Pfam; PF00690; Cation_ATPase_N;
Pfam; PF00122; E1-E2_ATPase;
Pfam; PF00702; Hydrolase;
SMART
SMART; SM00831; Cation_ATPase_N;
PROSITE
PROSITE; PS00154; ATPASE_E1_E2;
PRINTS
PRINTS; PR00119; CATATPASE;