CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-044042
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 
Protein Synonyms/Alias
  
Gene Name
 ATP2A2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
46EYEPEMGKVYRQDRKubiquitination[1]
80GESVSVIKHTDPVPDubiquitination[1]
243TSVICSDKTGTLTTNubiquitination[2, 3, 4]
327EAKGVYEKVGEATETubiquitination[4]
342ALTCLVEKMNVFDTEubiquitination[4]
351NVFDTELKGLSKIERubiquitination[1, 2, 4, 5, 6]
355TELKGLSKIERANACacetylation[7]
355TELKGLSKIERANACubiquitination[4]
367NACNSVIKQLMKKEFubiquitination[4]
401PSRTSMSKMFVKGAPubiquitination[4]
405SMSKMFVKGAPEGVIubiquitination[1]
424HIRVGSTKVPMTSGVubiquitination[1, 4, 6]
432VPMTSGVKQKIMSVIubiquitination[6]
502IEVASSVKLCRQAGIubiquitination[2, 6, 8]
519IMITGDNKGTAVAICubiquitination[2, 4, 7]
541QDEDVTSKAFTGREFubiquitination[1, 2, 4, 5, 6, 7]
576VEPSHKSKIVEFLQSubiquitination[1]
602VNDAPALKKAEIGIAubiquitination[2, 6]
886RNYLEPGKECVQPATubiquitination[4, 6, 7]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Hydrolase; Membrane; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 933 AA 
Protein Sequence
XTITAFVEPF VILLILVANA IVGVWQERNA ENAIEALKEY EPEMGKVYRQ DRKSVQRIKA 60
KDIVPGDIVE IAGESVSVIK HTDPVPDPRA VNQDKKNMLF SGTNIAAGKA MGVVVATGVN 120
TEIGKIRDEM VATEQERTPL QQKLDEFGEQ LSKVISLICI AVWIINIGHF NDPVHGGSWI 180
RGAIYYFKIA VALAVAAIPE GLPAVITTCL ALGTRRMAKK NAIVRSLPSV ETLGCTSVIC 240
SDKTGTLTTN QMSVCRMFIL DRVEGDTCSL NEFTITGSTY APIGEVHKDD KPVNCHQYDG 300
LVELATICAL CNDSALDYNE AKGVYEKVGE ATETALTCLV EKMNVFDTEL KGLSKIERAN 360
ACNSVIKQLM KKEFTLEFSR DRKSMSVYCT PNKPSRTSMS KMFVKGAPEG VIDRCTHIRV 420
GSTKVPMTSG VKQKIMSVIR EWGSGSDTLR CLALATHDNP LRREEMHLED SANFIKYETN 480
LTFVGCVGML DPPRIEVASS VKLCRQAGIR VIMITGDNKG TAVAICRRIG IFGQDEDVTS 540
KAFTGREFDE LNPSAQRDAC LNARCFARVE PSHKSKIVEF LQSFDEITAM TGDGVNDAPA 600
LKKAEIGIAM GSGTAVAKTA SEMVLADDNF STIVAAVEEG RAIYNNMKQF IRYLISSNVG 660
EVVCIFLTAA LGFPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMNKP PRNPKEPLIS 720
GWLFFRYLAI GCYVGAATVG AAAWWFIAAD GGPRVSFYQL SHFLQCKEDN PDFEGVDCAI 780
FESPYPMTMA LSVLVTIEMC NALNSLSENQ SLLRMPPWEN IWLVGSICLS MSLHFLILYV 840
EPLPLIFQIT PLNVTQWLMV LKISLPVILM DETLKFVARN YLEPGKECVQ PATKSCSFSA 900
CTDGISWPFV LLIMPLVIWV YSTDTNFSDM FWS 933 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005388; F:calcium-transporting ATPase activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:InterPro. 
Interpro
 IPR005782; ATPase_P-typ_Ca-transp_IIA.
 IPR006068; ATPase_P-typ_cation-transptr_C.
 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.
 IPR001757; Cation_transp_P_typ_ATPase.
 IPR023214; HAD-like_dom. 
Pfam
 PF00689; Cation_ATPase_C
 PF00122; E1-E2_ATPase
 PF00702; Hydrolase 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.
 PR00120; HATPASE.