CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004823
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Plasma membrane calcium-transporting ATPase 1 
Protein Synonyms/Alias
 PMCA1; Plasma membrane calcium ATPase isoform 1; Plasma membrane calcium pump isoform 1 
Gene Name
 ATP2B1 
Gene Synonyms/Alias
 PMCA1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
19SGVKNSLKEANHDGDubiquitination[1, 2, 3]
62DVYGICTKLKTSPNEubiquitination[1, 3, 4]
64YGICTKLKTSPNEGLubiquitination[2]
193SRIEQEQKFTVIRGGubiquitination[1, 3, 4]
256HVKKSLDKDPLLLSGubiquitination[1, 2, 3, 4]
324IENRNKAKAQDGAAMubiquitination[2]
337AMEMQPLKSEEGGDGubiquitination[2]
347EGGDGDEKDKKKANLubiquitination[2]
365EKSVLQGKLTKLAVQacetylation[5]
452YSVKKMMKDNNLVRHubiquitination[2, 6]
533SKILPPEKEGGLPRHubiquitination[3, 6]
622LSANGEAKVFRPRDRubiquitination[1, 3]
634RDRDDIVKTVIEPMAubiquitination[1, 2, 3]
721TARAIATKCGILHPGubiquitination[4]
747NRRIRNEKGEIEQERubiquitination[2, 6]
757IEQERIDKIWPKLRVubiquitination[1, 3]
806TNDGPALKKADVGFAubiquitination[2, 3, 6]
921RKPYGRNKPLISRTMubiquitination[2, 6]
1172SLYEGLEKPESRSSIubiquitination[1, 2, 3, 4]
1212AEDDAPTKRNSSPPPubiquitination[2]
Reference
 [1] 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]
 [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] 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]
 [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] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [6] 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] 
Functional Description
 This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell. 
Sequence Annotation
 REGION 1100 1117 Calmodulin-binding subdomain A.
 REGION 1118 1127 Calmodulin-binding subdomain B.
 ACT_SITE 475 475 4-aspartylphosphate intermediate.
 METAL 797 797 Magnesium (By similarity).
 METAL 801 801 Magnesium (By similarity).
 MOD_RES 2 2 N-acetylglycine.
 MOD_RES 17 17 Phosphoserine.
 MOD_RES 1116 1116 Phosphothreonine; by PKC.
 MOD_RES 1193 1193 Phosphoserine.
 MOD_RES 1203 1203 Phosphothreonine.
 MOD_RES 1216 1216 Phosphoserine; by PKA.
 MOD_RES 1220 1220 Phosphoserine.
 MOD_RES 1246 1246 Phosphoserine.
 MOD_RES 1249 1249 Phosphoserine.
 MOD_RES 1253 1253 Phosphoserine.
 MOD_RES 1257 1257 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Calcium; Calcium transport; Calmodulin-binding; Cell membrane; Complete proteome; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1258 AA 
Protein Sequence
MGDMANNSVA YSGVKNSLKE ANHDGDFGIT LAELRALMEL RSTDALRKIQ ESYGDVYGIC 60
TKLKTSPNEG LSGNPADLER REAVFGKNFI PPKKPKTFLQ LVWEALQDVT LIILEIAAIV 120
SLGLSFYQPP EGDNALCGEV SVGEEEGEGE TGWIEGAAIL LSVVCVVLVT AFNDWSKEKQ 180
FRGLQSRIEQ EQKFTVIRGG QVIQIPVADI TVGDIAQVKY GDLLPADGIL IQGNDLKIDE 240
SSLTGESDHV KKSLDKDPLL LSGTHVMEGS GRMVVTAVGV NSQTGIIFTL LGAGGEEEEK 300
KDEKKKEKKN KKQDGAIENR NKAKAQDGAA MEMQPLKSEE GGDGDEKDKK KANLPKKEKS 360
VLQGKLTKLA VQIGKAGLLM SAITVIILVL YFVIDTFWVQ KRPWLAECTP IYIQYFVKFF 420
IIGVTVLVVA VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL 480
TMNRMTVVQA YINEKHYKKV PEPEAIPPNI LSYLVTGISV NCAYTSKILP PEKEGGLPRH 540
VGNKTECALL GLLLDLKRDY QDVRNEIPEE ALYKVYTFNS VRKSMSTVLK NSDGSYRIFS 600
KGASEIILKK CFKILSANGE AKVFRPRDRD DIVKTVIEPM ASEGLRTICL AFRDFPAGEP 660
EPEWDNENDI VTGLTCIAVV GIEDPVRPEV PDAIKKCQRA GITVRMVTGD NINTARAIAT 720
KCGILHPGED FLCLEGKDFN RRIRNEKGEI EQERIDKIWP KLRVLARSSP TDKHTLVKGI 780
IDSTVSDQRQ VVAVTGDGTN DGPALKKADV GFAMGIAGTD VAKEASDIIL TDDNFTSIVK 840
AVMWGRNVYD SISKFLQFQL TVNVVAVIVA FTGACITQDS PLKAVQMLWV NLIMDTLASL 900
ALATEPPTES LLLRKPYGRN KPLISRTMMK NILGHAFYQL VVVFTLLFAG EKFFDIDSGR 960
NAPLHAPPSE HYTIVFNTFV LMQLFNEINA RKIHGERNVF EGIFNNAIFC TIVLGTFVVQ 1020
IIIVQFGGKP FSCSELSIEQ WLWSIFLGMG TLLWGQLIST IPTSRLKFLK EAGHGTQKEE 1080
IPEEELAEDV EEIDHAEREL RRGQILWFRG LNRIQTQMDV VNAFQSGSSI QGALRRQPSI 1140
ASQHHDVTNI STPTHIRVVN AFRSSLYEGL EKPESRSSIH NFMTHPEFRI EDSEPHIPLI 1200
DDTDAEDDAP TKRNSSPPPS PNKNNNAVDS GIHLTIEMNK SATSSSPGSP LHSLETSL 1258 
Gene Ontology
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005388; F:calcium-transporting ATPase activity; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007596; P:blood coagulation; TAS:Reactome. 
Interpro
 IPR022141; ATP_Ca_trans_C.
 IPR006408; ATPase_P-typ_Ca-transp_plasma.
 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
 PF12424; ATP_Ca_trans_C
 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.