CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002086
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sodium/potassium-transporting ATPase subunit alpha-1 
Protein Synonyms/Alias
 Na(+)/K(+) ATPase alpha-1 subunit; Sodium pump subunit alpha-1 
Gene Name
 ATP1A1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Ovis aries (Sheep) 
NCBI Taxa ID
 9940 
Lysine Modification
Position
Peptide
Type
References
160SKIMESFKNMVPQQAubiquitination[1]
175LVIRNGEKMSINAEEubiquitination[2]
210IISANGCKVDNSSLTubiquitination[1, 3]
627ITAKAIAKGVGIISEubiquitination[1]
724VNDSPALKKADIGVAubiquitination[2]
725NDSPALKKADIGVAMubiquitination[2]
771RLIFDNLKKSIAYTLubiquitination[4]
1017RPGGWVEKETYY***ubiquitination[2, 4]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
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
 REGION 80 82 Phosphoinositide-3 kinase binding (By
 ACT_SITE 374 374 4-aspartylphosphate intermediate (By
 METAL 715 715 Magnesium (By similarity).
 METAL 719 719 Magnesium (By similarity).
 BINDING 485 485 ATP (By similarity).
 MOD_RES 10 10 Phosphotyrosine (By similarity).
 MOD_RES 16 16 Phosphoserine; by PKC (By similarity).
 MOD_RES 45 45 Phosphoserine (By similarity).
 MOD_RES 215 215 Phosphoserine (By similarity).
 MOD_RES 217 217 Phosphothreonine (By similarity).
 MOD_RES 226 226 Phosphoserine (By similarity).
 MOD_RES 258 258 Phosphotyrosine (By similarity).
 MOD_RES 450 450 Phosphoserine (By similarity).
 MOD_RES 540 540 Phosphotyrosine (By similarity).
 MOD_RES 941 941 Phosphoserine; by PKA (By similarity).  
Keyword
 ATP-binding; Cell membrane; Direct protein sequencing; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport; Sodium; Sodium transport; Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1021 AA 
Protein Sequence
MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH RKYGTDLNRG 60
LTTARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM LLWIGAVLCF LAYGIQAATE 120
EEPQNDNLYL GVVLSAVVII TGCFSYYQEA KSSKIMESFK NMVPQQALVI RNGEKMSINA 180
EEVVVGDLVE VKGGDRIPAD LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI 240
AFFSTNCVEG TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL 300
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE 360
AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TENQSGVSFD KTSATWLALS 420
RIAGLCNRAV FQANQDNLPI LKRAVAGDAS ESALLKCIEV CCGSVKEMRE RYAKIVEIPF 480
NSTNKYQLSI HKNANAGEPR HLLVMKGAPE RILDRCSSIL IHGKEQPLDE ELKDAFQNAY 540
LELGGLGERV LGFCHLMLPD EQFPEGFQFD TDDVNFPVDN LCFVGLISMI DPPRAAVPDA 600
VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISEGNETVE DIAARLNIPV SQVNPRDARA 660
CVVHGSDLKD MTPEQLDDIL KYHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS 720
PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS 780
NIPEITPFLI FIIANIPLPL GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPQTD 840
KLVNERLISM AYGQIGMIQA LGGFFTYFVI MAENGFLPNH LLGIRVTWDD RWINDVEDSY 900
GQQWTYEQRK IVEFTCHTAF FVSIVVVQWA DLVICKTRRN SVFQQGMKNK ILIFGLFEET 960
ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD EVRKLIIRRR PGGWVEKETY 1020
Y 1021 
Gene Ontology
 GO:0016021; C:integral to membrane; ISS:UniProtKB.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0005391; F:sodium:potassium-exchanging ATPase activity; ISS:UniProtKB.
 GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
 GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB. 
Interpro
 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. 
Pfam
 PF00689; Cation_ATPase_C
 PF00690; Cation_ATPase_N
 PF00122; E1-E2_ATPase
 PF00702; Hydrolase 
SMART
 SM00831; Cation_ATPase_N 
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.