CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005205
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Plasma membrane calcium-transporting ATPase 4 
Protein Synonyms/Alias
 PMCA4; Matrix-remodeling-associated protein 1; Plasma membrane calcium ATPase isoform 4; Plasma membrane calcium pump isoform 4 
Gene Name
 ATP2B4 
Gene Synonyms/Alias
 ATP2B2; MXRA1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
31CTVMELRKLMELRSRubiquitination[1]
75GNPADLEKRRQVFGHubiquitination[1, 2]
189CRIEQEQKFSIIRNGubiquitination[1]
252HVKKSLDKDPMLLSGubiquitination[1, 2]
314PENRNKAKTQDGVALubiquitination[3]
339IDNEEKDKKAVKVPKubiquitination[1]
340DNEEKDKKAVKVPKKubiquitination[1]
355EKSVLQGKLTRLAVQubiquitination[1]
561RNEVPEEKLYKVYTFubiquitination[1, 3]
686PDAIAKCKQAGITVRubiquitination[1]
709TARAIATKCGILTPGubiquitination[1]
725DFLCLEGKEFNRLIRubiquitination[1]
735NRLIRNEKGEVEQEKubiquitination[1, 3]
1055AIPTRSLKFLKEAGHubiquitination[1]
1105NRIQTQIKVVKAFHSubiquitination[1, 2, 4, 5, 6]
1108QTQIKVVKAFHSSLHubiquitination[1]
1120SLHESIQKPYNQKSIubiquitination[2]
1158EEEENPDKASKFGTRubiquitination[3]
1161ENPDKASKFGTRVLLubiquitination[1]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [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] 
Functional Description
 This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell. 
Sequence Annotation
 REGION 1086 1103 Calmodulin-binding subdomain A.
 REGION 1104 1113 Calmodulin-binding subdomain B (By
 ACT_SITE 465 465 4-aspartylphosphate intermediate (By
 METAL 785 785 Magnesium (By similarity).
 METAL 789 789 Magnesium (By similarity).
 MOD_RES 1102 1102 Phosphothreonine; by PKC (By similarity).  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Calcium; Calcium transport; Calmodulin-binding; Cell membrane; Complete proteome; Direct protein sequencing; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1241 AA 
Protein Sequence
MTNPSDRVLP ANSMAESREG DFGCTVMELR KLMELRSRDA LTQINVHYGG VQNLCSRLKT 60
SPVEGLSGNP ADLEKRRQVF GHNVIPPKKP KTFLELVWEA LQDVTLIILE IAAIISLVLS 120
FYRPAGEENE LCGQVATTPE DENEAQAGWI EGAAILFSVI IVVLVTAFND WSKEKQFRGL 180
QCRIEQEQKF SIIRNGQLIQ LPVAEIVVGD IAQVKYGDLL PADGILIQGN DLKIDESSLT 240
GESDHVKKSL DKDPMLLSGT HVMEGSGRMV VTAVGVNSQT GIILTLLGVN EDDEGEKKKK 300
GKKQGVPENR NKAKTQDGVA LEIQPLNSQE GIDNEEKDKK AVKVPKKEKS VLQGKLTRLA 360
VQIGKAGLLM SALTVFILIL YFVIDNFVIN RRPWLPECTP IYIQYFVKFF IIGITVLVVA 420
VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL TMNRMTVVQA 480
YIGGIHYRQI PSPDVFLPKV LDLIVNGISI NSAYTSKILP PEKEGGLPRQ VGNKTECALL 540
GFVTDLKQDY QAVRNEVPEE KLYKVYTFNS VRKSMSTVIR NPNGGFRMYS KGASEIILRK 600
CNRILDRKGE AVPFKNKDRD DMVRTVIEPM ACDGLRTICI AYRDFDDTEP SWDNENEILT 660
ELTCIAVVGI EDPVRPEVPD AIAKCKQAGI TVRMVTGDNI NTARAIATKC GILTPGDDFL 720
CLEGKEFNRL IRNEKGEVEQ EKLDKIWPKL RVLARSSPTD KHTLVKGIID STVGEHRQVV 780
AVTGDGTNDG PALKKADVGF AMGIAGTDVA KEASDIILTD DNFTSIVKAV MWGRNVYDSI 840
SKFLQFQLTV NVVAVIVAFT GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTESLL 900
KRRPYGRNKP LISRTMMKNI LGHAFYQLIV IFILVFAGEK FFDIDSGRKA PLHSPPSQHY 960
TIVFNTFVLM QLFNEINSRK IHGEKNVFSG IYRNIIFCSV VLGTFICQIF IVEFGGKPFS 1020
CTSLSLSQWL WCLFIGIGEL LWGQFISAIP TRSLKFLKEA GHGTTKEEIT KDAEGLDEID 1080
HAEMELRRGQ ILWFRGLNRI QTQIKVVKAF HSSLHESIQK PYNQKSIHSF MTHPEFAIEE 1140
ELPRTPLLDE EEEENPDKAS KFGTRVLLLD GEVTPYANTN NNAVDCNQVQ LPQSDSSLQS 1200
LETSV 1205 
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.