CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-045374
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Sodium/potassium-transporting ATPase subunit alpha-3 
Protein Synonyms/Alias
  
Gene Name
 ATP1A3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
172IISAHGCKVDNSSLTubiquitination[1, 2]
404QDNIPVLKRDVAGDAubiquitination[2]
418ASESALLKCIELSSGubiquitination[1]
428ELSSGSVKLMRERNKubiquitination[1, 2, 3, 4]
486STILLQGKEQPLDEEubiquitination[4]
686VNDSPALKKADIGVAubiquitination[4]
687NDSPALKKADIGVAMubiquitination[1, 5]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 983 AA 
Protein Sequence
MTEHKMSVEE VCRKYNTDCV QGLTHSKAQE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF 60
SILLWIGAIL CFLAYGIQAG TEDDPSGDNL YLGIVLAAVV IITGCFSYYQ EAKSSKIMES 120
FKNMVPQQAL VIREGEKMQV NAEEVVVGDL VEIKGGDRVP ADLRIISAHG CKVDNSSLTG 180
ESEPQTRSPD CTHDNPLETR NITFFSTNCV EGTARGVVVA TGDRTVMGRI ATLASGLEVG 240
KTPIAIEIEH FIQLITGVAV FLGVSFFILS LILGYTWLEA VIFLIGIIVA NVPEGLLATV 300
TVCLTLTAKR MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA 360
DTTEDQSGTS FDKSSHTWVA LSHIAGLCNR AVFKGGQDNI PVLKRDVAGD ASESALLKCI 420
ELSSGSVKLM RERNKKVAEI PFNSTNKYQL SIHETEDPND NRYLLVMKGA PERILDRCST 480
ILLQGKEQPL DEEMKEAFQN AYLELGGLGE RVLGFCHYYL PEEQFPKGFA FDCDDVNFTT 540
DNLCFVGLMS MIDPPRAAVP DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET 600
VEDIAARLNI PVSQVNPRDA KACVIHGTDL KDFTSEQIDE ILQNHTEIVF ARTSPQQKLI 660
IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT 720
GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LLFIMANIPL PLGTITILCI DLGTDMVPAI 780
SLAYEAAESD IMKRQPRNPR TDKLVNERLI SMAYGQIGMI QALGGFFSYF VILAENGFLP 840
GNLVGIRLNW DDRTVNDLED SYGQQWTYEQ RKVVEFTCHT AFFVSIVVVQ WADLIICKTR 900
RNSVFQQGMK NKILIFGLFE ETALAAFLSY CPGMDVALRM YPLKPSWWFC AFPYSFLIFV 960
YDEIRKLILR RNPGGWVEKE TYY 983 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:InterPro.
 GO:0015077; F:monovalent inorganic cation transmembrane transporter activity; IEA:InterPro.
 GO:0006754; P:ATP biosynthetic process; IEA:InterPro. 
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.