CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002204
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9GKGVGRDKYEPAAVSacetylation[1]
9GKGVGRDKYEPAAVSubiquitination[2, 3, 4, 5, 6]
21AVSEQGDKKGKKGKKubiquitination[2, 5, 7]
22VSEQGDKKGKKGKKDubiquitination[7]
36DRDMDELKKEVSMDDubiquitination[2, 3, 5, 6, 7, 8]
37RDMDELKKEVSMDDHubiquitination[2, 5, 6]
45EVSMDDHKLSLDELHubiquitination[2, 5, 6, 7, 9, 10]
54SLDELHRKYGTDLSRubiquitination[6, 7, 9, 10]
91PTTPEWIKFCRQLFGubiquitination[3]
156YQEAKSSKIMESFKNubiquitination[2]
162SKIMESFKNMVPQQAubiquitination[2, 3, 5, 9]
177LVIRNGEKMSINAEEubiquitination[6, 7]
194VGDLVEVKGGDRIPAubiquitination[2]
212IISANGCKVDNSSLTubiquitination[2, 3, 6, 7, 8, 9, 11]
359ARKNCLVKNLEAVETubiquitination[9]
377TSTICSDKTGTLTQNubiquitination[2]
444QENLPILKRAVAGDAubiquitination[2, 3, 4, 5, 6, 7, 8, 9, 11, 12]
458ASESALLKCIELCCGubiquitination[3, 7]
468ELCCGSVKEMRERYAubiquitination[4, 6, 7, 8]
476EMRERYAKIVEIPFNubiquitination[7, 9, 10]
487IPFNSTNKYQLSIHKacetylation[1]
487IPFNSTNKYQLSIHKubiquitination[2, 4, 5, 9]
494KYQLSIHKNPNTSEPubiquitination[2, 4, 5, 6, 7, 9]
508PQHLLVMKGAPERILubiquitination[2, 3, 5, 6, 7, 9, 10]
526SSILLHGKEQPLDEEubiquitination[4, 5, 12]
535QPLDEELKDAFQNAYubiquitination[2, 5]
605AVPDAVGKCRSAGIKubiquitination[2, 4, 8]
612KCRSAGIKVIMVTGDubiquitination[2, 5]
625GDHPITAKAIAKGVGubiquitination[2, 5, 9]
629ITAKAIAKGVGIISEubiquitination[2, 5, 9, 13]
661QVNPRDAKACVVHGSubiquitination[6, 7]
671VVHGSDLKDMTSEQLubiquitination[3, 5, 6, 7, 11]
683EQLDDILKYHTEIVFubiquitination[2, 3, 5, 8, 9, 10]
698ARTSPQQKLIIVEGCubiquitination[4, 9]
726VNDSPALKKADIGVAubiquitination[2, 5]
727NDSPALKKADIGVAMubiquitination[2]
773RLIFDNLKKSIAYTLubiquitination[2, 5, 9]
840KRQPRNPKTDKLVNEubiquitination[2, 3, 4, 5, 6, 7, 8]
843PRNPKTDKLVNERLIubiquitination[2, 4, 6, 9]
950SVFQQGMKNKILIFGubiquitination[2, 5]
1019RPGGWVEKETYY***ubiquitination[2, 6, 7, 9]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] 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]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] 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]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [10] 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]
 [11] 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]
 [12] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [13] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048] 
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 82 84 Phosphoinositide-3 kinase binding (By
 ACT_SITE 376 376 4-aspartylphosphate intermediate (By
 METAL 717 717 Magnesium (By similarity).
 METAL 721 721 Magnesium (By similarity).
 BINDING 487 487 ATP (By similarity).
 MOD_RES 10 10 Phosphotyrosine (By similarity).
 MOD_RES 16 16 Phosphoserine (By similarity).
 MOD_RES 47 47 Phosphoserine (By similarity).
 MOD_RES 217 217 Phosphoserine (By similarity).
 MOD_RES 219 219 Phosphothreonine (By similarity).
 MOD_RES 228 228 Phosphoserine (By similarity).
 MOD_RES 260 260 Phosphotyrosine (By similarity).
 MOD_RES 452 452 Phosphoserine (By similarity).
 MOD_RES 542 542 Phosphotyrosine.
 MOD_RES 943 943 Phosphoserine; by PKA (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Direct protein sequencing; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Potassium; Potassium transport; Reference proteome; Sodium; Sodium transport; Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1023 AA 
Protein Sequence
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 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
 GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005890; C:sodium:potassium-exchanging ATPase complex; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051087; F:chaperone binding; ISS:BHF-UCL.
 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.