CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005611
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein disulfide-isomerase A3 
Protein Synonyms/Alias
 58 kDa glucose-regulated protein; 58 kDa microsomal protein; p58; Disulfide isomerase ER-60; Endoplasmic reticulum resident protein 57; ER protein 57; ERp57; Endoplasmic reticulum resident protein 60; ER protein 60; ERp60 
Gene Name
 Pdia3 
Gene Synonyms/Alias
 Erp; Erp60; Grp58 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
104VSGYPTLKIFRDGEEubiquitination[1]
129DGIVSHLKKQAGPASacetylation[2, 3, 4, 5]
129DGIVSHLKKQAGPASsuccinylation[5]
146LRTEEEFKKFISDKDacetylation[4, 6]
147RTEEEFKKFISDKDAacetylation[3]
152FKKFISDKDASVVGFacetylation[3, 4, 5]
152FKKFISDKDASVVGFubiquitination[1]
173DGHSEFLKAASNLRDacetylation[3, 7]
173DGHSEFLKAASNLRDubiquitination[1]
214RPLHLANKFEDKTVAacetylation[3, 4]
218LANKFEDKTVAYTEKacetylation[3, 5]
218LANKFEDKTVAYTEKsuccinylation[5]
225KTVAYTEKKMTSGKIacetylation[4]
231EKKMTSGKIKKFIQDacetylation[6]
234MTSGKIKKFIQDSIFacetylation[3]
252PHMTEDNKDLIQGKDacetylation[3, 5]
271YYDVDYEKNAKGSNYacetylation[6]
274VDYEKNAKGSNYWRNubiquitination[1]
289RVMMVAKKFLDAGHKacetylation[3]
296KFLDAGHKLNFAVASacetylation[3]
305NFAVASRKTFSHELSubiquitination[1]
335IRTAKGEKFVMQEEFacetylation[3]
335IRTAKGEKFVMQEEFubiquitination[1]
362EYFDGNLKRYLKSEPacetylation[3, 5]
362EYFDGNLKRYLKSEPsuccinylation[5]
362EYFDGNLKRYLKSEPubiquitination[1]
366GNLKRYLKSEPIPESacetylation[3]
425ELGEKLSKDPNIVIAacetylation[3, 4, 7]
425ELGEKLSKDPNIVIAubiquitination[1]
460IYFSPANKKLTPKKYubiquitination[1]
494PPIIQEEKPKKKKKAacetylation[4, 5, 6]
494PPIIQEEKPKKKKKAsuccinylation[5]
496IIQEEKPKKKKKAQEacetylation[4, 6]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
  
Sequence Annotation
 DOMAIN 25 133 Thioredoxin 1.
 DOMAIN 343 485 Thioredoxin 2.
 MOTIF 502 505 Prevents secretion from ER (By
 ACT_SITE 57 57 Nucleophile (By similarity).
 ACT_SITE 60 60 Nucleophile (By similarity).
 ACT_SITE 406 406 Nucleophile (By similarity).
 ACT_SITE 409 409 Nucleophile (By similarity).
 DISULFID 57 60 Redox-active; alternate (By similarity).
 DISULFID 57 57 Interchain (with C-118 in TAPBP);
 DISULFID 85 92 By similarity.
 DISULFID 406 409 Redox-active (By similarity).  
Keyword
 Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Isomerase; Phosphoprotein; Redox-active center; Reference proteome; Repeat; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 505 AA 
Protein Sequence
MRFSCLALLP GVALLLASAR LAAASDVLEL TDENFESRVS DTGSAGLMLV EFFAPWCGHC 60
KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT 120
ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASVVGFF RDLFSDGHSE FLKAASNLRD 180
NYRFAHTNIE SLVKEYDDNG EGITIFRPLH LANKFEDKTV AYTEKKMTSG KIKKFIQDSI 240
FGLCPHMTED NKDLIQGKDL LTAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA 300
VASRKTFSHE LSDFGLESTT GEVPVVAIRT AKGEKFVMQE EFSRDGKALE QFLQEYFDGN 360
LKRYLKSEPI PESNEGPVKV VVAENFDDIV NEEDKDVLIE FYAPWCGHCK NLEPKYKELG 420
EKLSKDPNIV IAKMDATAND VPSPYEVKGF PTIYFSPANK KLTPKKYEGG RELNDFISYL 480
QREATNPPII QEEKPKKKKK AQEDL 505 
Gene Ontology
 GO:0009986; C:cell surface; IDA:MGI.
 GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0003756; F:protein disulfide isomerase activity; IEA:EC.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
 GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
 GO:0006457; P:protein folding; IEA:GOC. 
Interpro
 IPR005788; Disulphide_isomerase.
 IPR005792; Prot_disulphide_isomerase.
 IPR005746; Thioredoxin.
 IPR012336; Thioredoxin-like_fold.
 IPR017937; Thioredoxin_CS.
 IPR013766; Thioredoxin_domain. 
Pfam
 PF00085; Thioredoxin 
SMART
  
PROSITE
 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 
PRINTS
 PR00421; THIOREDOXIN.