CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004482
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 
Protein Synonyms/Alias
 SERCA2; SR Ca(2+)-ATPase 2; Calcium pump 2; Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform; Endoplasmic reticulum class 1/2 Ca(2+) ATPase 
Gene Name
 ATP2A2 
Gene Synonyms/Alias
 ATP2B 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30GLSLEQVKKLKERWGubiquitination[1]
120ENAIEALKEYEPEMGubiquitination[1]
128EYEPEMGKVYRQDRKubiquitination[1]
135KVYRQDRKSVQRIKAglycation[2]
141RKSVQRIKAKDIVPGglycation[2]
169DIRLTSIKSTTLRVDubiquitination[1, 3]
205RAVNQDKKNMLFSGTubiquitination[4, 5]
252ERTPLQQKLDEFGEQubiquitination[1]
328LGTRRMAKKNAIVRSubiquitination[1]
329GTRRMAKKNAIVRSLubiquitination[1]
352TSVICSDKTGTLTTNubiquitination[3]
436EAKGVYEKVGEATETubiquitination[3]
451ALTCLVEKMNVFDTEubiquitination[3]
460NVFDTELKGLSKIERglycation[2]
460NVFDTELKGLSKIERubiquitination[1, 3, 4, 5, 6]
464TELKGLSKIERANACacetylation[7]
464TELKGLSKIERANACubiquitination[3]
476NACNSVIKQLMKKEFglycation[2]
476NACNSVIKQLMKKEFubiquitination[3, 6]
480SVIKQLMKKEFTLEFsumoylation[8]
481VIKQLMKKEFTLEFSglycation[2]
481VIKQLMKKEFTLEFSubiquitination[3]
510PSRTSMSKMFVKGAPubiquitination[3]
514SMSKMFVKGAPEGVIubiquitination[1, 3, 9]
533HIRVGSTKVPMTSGVubiquitination[1, 3]
541VPMTSGVKQKIMSVIubiquitination[1]
585EDSANFIKYETNLTFsumoylation[8]
611IEVASSVKLCRQAGIubiquitination[1]
628IMITGDNKGTAVAICubiquitination[3]
650QDEDVTSKAFTGREFubiquitination[1, 3, 4, 5, 10]
683ARVEPSHKSKIVEFLglycation[2]
685VEPSHKSKIVEFLQSubiquitination[1]
711VNDAPALKKAEIGIAubiquitination[1]
712NDAPALKKAEIGIAMubiquitination[1, 3]
757RAIYNNMKQFIRYLIubiquitination[1, 3, 4, 5]
824NKPPRNPKEPLISGWubiquitination[1]
995RNYLEPGKECVQPATubiquitination[1, 3]
Reference
 [1] 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]
 [2] Diabetes increases formation of advanced glycation end products on Sarco(endo)plasmic reticulum Ca2+-ATPase.
 Bidasee KR, Zhang Y, Shao CH, Wang M, Patel KP, Dincer UD, Besch HR Jr.
 Diabetes. 2004 Feb;53(2):463-73. [PMID: 14747299]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] SUMO1-dependent modulation of SERCA2a in heart failure.
 Kho C, Lee A, Jeong D, Oh JG, Chaanine AH, Kizana E, Park WJ, Hajjar RJ.
 Nature. 2011 Sep 7;477(7366):601-5. [PMID: 21900893]
 [9] 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]
 [10] 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] 
Functional Description
 This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle. 
Sequence Annotation
 REGION 370 400 Interacts with phospholamban 1 (By
 REGION 575 594 Interacts with HAX1.
 REGION 787 807 Interacts with phospholamban 2 (By
 ACT_SITE 351 351 4-aspartylphosphate intermediate (By
 METAL 304 304 Calcium 2; via carbonyl oxygen (By
 METAL 305 305 Calcium 2; via carbonyl oxygen (By
 METAL 307 307 Calcium 2; via carbonyl oxygen (By
 METAL 309 309 Calcium 2 (By similarity).
 METAL 702 702 Magnesium (By similarity).
 METAL 706 706 Magnesium (By similarity).
 METAL 767 767 Calcium 1 (By similarity).
 METAL 770 770 Calcium 1 (By similarity).
 METAL 795 795 Calcium 2 (By similarity).
 METAL 798 798 Calcium 1 (By similarity).
 METAL 799 799 Calcium 1 (By similarity).
 METAL 799 799 Calcium 2 (By similarity).
 METAL 907 907 Calcium 1 (By similarity).
 MOD_RES 294 294 Nitrated tyrosine.
 MOD_RES 295 295 Nitrated tyrosine.
 MOD_RES 537 537 Phosphothreonine (By similarity).
 MOD_RES 663 663 Phosphoserine.
 CROSSLNK 143 143 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Alternative splicing; ATP-binding; Calcium; Calcium transport; Complete proteome; Disease mutation; Endoplasmic reticulum; Epilepsy; Hydrolase; Ion transport; Isopeptide bond; Magnesium; Membrane; Metal-binding; Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome; Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1042 AA 
Protein Sequence
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL 60
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK 120
EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL 180
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV 240
ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV 300
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ 360
MSVCRMFILD RVEGDTCSLN EFTITGSTYA PIGEVHKDDK PVNCHQYDGL VELATICALC 420
NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK 480
KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTSGV 540
KQKIMSVIRE WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD 600
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL 660
NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKAEIGIAMG 720
SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL 780
GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG 840
CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL 900
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP 960
LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP ATKSCSFSAC TDGISWPFVL 1020
LIMPLVIWVY STDTNFSDMF WS 1042 
Gene Ontology
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0031095; C:platelet dense tubular network membrane; TAS:Reactome.
 GO:0033017; C:sarcoplasmic reticulum membrane; TAS:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0086039; F:calcium-transporting ATPase activity involved in regulation of cardiac muscle cell membrane potential; TAS:BHF-UCL.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0007155; P:cell adhesion; TAS:ProtInc.
 GO:0006874; P:cellular calcium ion homeostasis; TAS:BHF-UCL.
 GO:0008544; P:epidermis development; TAS:ProtInc.
 GO:0006984; P:ER-nucleus signaling pathway; IEA:Compara.
 GO:0045822; P:negative regulation of heart contraction; IEA:Compara.
 GO:0010460; P:positive regulation of heart rate; TAS:BHF-UCL.
 GO:0002026; P:regulation of the force of heart contraction; IEA:Compara.
 GO:0055119; P:relaxation of cardiac muscle; TAS:BHF-UCL.
 GO:0070296; P:sarcoplasmic reticulum calcium ion transport; TAS:BHF-UCL. 
Interpro
 IPR005782; ATPase_P-typ_Ca-transp_IIA.
 IPR006068; ATPase_P-typ_cation-transptr_C.
 IPR004014; ATPase_P-typ_cation-transptr_N.
 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
 PF00690; Cation_ATPase_N
 PF00122; E1-E2_ATPase
 PF00702; Hydrolase 
SMART
 SM00831; Cation_ATPase_N 
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.
 PR00120; HATPASE.