CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002581
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein disulfide-isomerase A4 
Protein Synonyms/Alias
 Endoplasmic reticulum resident protein 72; ER protein 72; ERp-72; ERp72 
Gene Name
 Pdia4 
Gene Synonyms/Alias
 Cai; Erp72 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
96QFAPEYEKIASTLKDacetylation[1]
102EKIASTLKDNDPPIAacetylation[2]
102EKIASTLKDNDPPIAubiquitination[3]
124SASMLASKFDVSGYPacetylation[1]
124SASMLASKFDVSGYPubiquitination[3]
134VSGYPTIKILKKGQAacetylation[1]
134VSGYPTIKILKKGQAubiquitination[3]
211KLAPEYEKAAKELSKacetylation[4]
238TEQTDLAKRFDVSGYubiquitination[3]
249VSGYPTLKIFRKGRPacetylation[1]
249VSGYPTLKIFRKGRPubiquitination[3]
265DYNGPREKYGIVDYMacetylation[1]
287SKEILTLKQVQEFLKubiquitination[3]
339TFSPEIAKFLKVSLGacetylation[1]
342PEIAKFLKVSLGKLVacetylation[1]
347FLKVSLGKLVLTHPEacetylation[1]
347FLKVSLGKLVLTHPEubiquitination[3]
355LVLTHPEKFQSKYEPacetylation[1]
359HPEKFQSKYEPRFHVacetylation[1]
379STEASAIKDYVVKHAacetylation[1]
384AIKDYVVKHALPLVGacetylation[1]
478ILDESGKKFAMEPEEacetylation[1]
499REFVTAFKKGKLKPVacetylation[1]
508GKLKPVIKSQPVPKNacetylation[1]
526PVKVVVGKTFDAIVMacetylation[1]
563PIYTSLGKKYKGQKDacetylation[5]
569GKKYKGQKDLVIAKMubiquitination[3]
575QKDLVIAKMDATANDacetylation[1]
622RDLEHLSKFIDEHATacetylation[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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] 
Functional Description
  
Sequence Annotation
 DOMAIN 21 162 Thioredoxin 1.
 DOMAIN 162 294 Thioredoxin 2.
 DOMAIN 498 629 Thioredoxin 3.
 MOTIF 635 638 Prevents secretion from ER.
 MOD_RES 359 359 N6-acetyllysine (By similarity).
 CARBOHYD 36 36 N-linked (GlcNAc...) (Potential).
 DISULFID 84 87 Redox-active (By similarity).
 DISULFID 199 202 Redox-active (By similarity).
 DISULFID 548 551 Redox-active (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase; Redox-active center; Reference proteome; Repeat; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 638 AA 
Protein Sequence
MKLRKAWLLV LLLALTQLLA AASAGDAHED TSDTENATEE EEEEDDDDLE VKEENGVWVL 60
NDGNFDNFVA DKDTVLLEFY APWCGHCKQF APEYEKIAST LKDNDPPIAV AKIDATSASM 120
LASKFDVSGY PTIKILKKGQ AVDYDGSRTQ EEIVAKVREV SQPDWTPPPE VTLSLTKDNF 180
DDVVNNADII LVEFYAPWCG HCKKLAPEYE KAAKELSKRS PPIPLAKVDA TEQTDLAKRF 240
DVSGYPTLKI FRKGRPFDYN GPREKYGIVD YMIEQSGPPS KEILTLKQVQ EFLKDGDDVV 300
IIGLFQGDGD PAYLQYQDAA NNLREDYKFH HTFSPEIAKF LKVSLGKLVL THPEKFQSKY 360
EPRFHVMDVQ GSTEASAIKD YVVKHALPLV GHRKTSNDAK RYSKRPLVVV YYSVDFSFDY 420
RAATQFWRNK VLEVAKDFPE YTFAIADEED YATEVKDLGL SESGEDVNAA ILDESGKKFA 480
MEPEEFDSDT LREFVTAFKK GKLKPVIKSQ PVPKNNKGPV KVVVGKTFDA IVMDPKKDVL 540
IEFYAPWCGH CKQLEPIYTS LGKKYKGQKD LVIAKMDATA NDITNDQYKV EGFPTIYFAP 600
SGDKKNPIKF EGGNRDLEHL SKFIDEHATK RSRTKEEL 638 
Gene Ontology
 GO:0009986; C:cell surface; IDA:MGI.
 GO:0005783; C:endoplasmic reticulum; IDA:MGI.
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 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:0006457; P:protein folding; IEA:GOC. 
Interpro
 IPR005788; Disulphide_isomerase.
 IPR005792; Prot_disulphide_isomerase.
 IPR017068; Protein_diS-isomerase_A4.
 IPR005746; Thioredoxin.
 IPR012336; Thioredoxin-like_fold.
 IPR017937; Thioredoxin_CS.
 IPR013766; Thioredoxin_domain. 
Pfam
 PF00085; Thioredoxin 
SMART
  
PROSITE
 PS00014; ER_TARGET
 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 
PRINTS
 PR00421; THIOREDOXIN.