CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005298
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptidyl-prolyl cis-trans isomerase B 
Protein Synonyms/Alias
 PPIase B; CYP-S1; Cyclophilin B; Rotamase B; S-cyclophilin; SCYLP 
Gene Name
 Ppib 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
67VVFGLFGKTVPKTVDacetylation[1, 2]
67VVFGLFGKTVPKTVDsuccinylation[2]
71LFGKTVPKTVDNFVAacetylation[3]
84VALATGEKGFGYKNSacetylation[3]
84VALATGEKGFGYKNSubiquitination[4]
98SKFHRVIKDFMIQGGacetylation[3]
116RGDGTGGKSIYGERFacetylation[2, 3, 5]
116RGDGTGGKSIYGERFsuccinylation[2]
129RFPDENFKLKHYGPGacetylation[5, 6]
131PDENFKLKHYGPGWVacetylation[3]
165KTSWLDGKHVVFGKVacetylation[2, 3]
165KTSWLDGKHVVFGKVsuccinylation[2]
165KTSWLDGKHVVFGKVubiquitination[4]
171GKHVVFGKVLEGMDVacetylation[3]
186VRKVESTKTDSRDKPacetylation[5]
192TKTDSRDKPLKDVIIacetylation[2, 5]
192TKTDSRDKPLKDVIIsuccinylation[2]
209SGKIEVEKPFAIAKEacetylation[1, 2, 3, 5]
209SGKIEVEKPFAIAKEsuccinylation[2]
209SGKIEVEKPFAIAKEubiquitination[4]
215EKPFAIAKE******acetylation[1, 2, 5, 7]
Reference
 [1] 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]
 [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] 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] 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]
 [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]
 [6] 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]
 [7] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758
Functional Description
 PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. 
Sequence Annotation
 DOMAIN 47 204 PPIase cyclophilin-type.
 MOTIF 213 216 Prevents secretion from ER (By  
Keyword
 Complete proteome; Cyclosporin; Endoplasmic reticulum; Isomerase; Reference proteome; Rotamase; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 216 AA 
Protein Sequence
MLRLSERNMK VLFAAALIVG SVVFLLLPGP SVANDKKKGP KVTVKVYFDL QIGDESVGRV 60
VFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG 120
ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTS WLDGKHVVFG KVLEGMDVVR 180
KVESTKTDSR DKPLKDVIIV DSGKIEVEKP FAIAKE 216 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0042277; F:peptide binding; IEA:UniProtKB-KW.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
 GO:0006457; P:protein folding; IEA:UniProtKB-KW.
 GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC. 
Interpro
 IPR002130; Cyclophilin-like_PPIase_dom.
 IPR024936; Cyclophilin-type_PPIase.
 IPR020892; Cyclophilin-type_PPIase_CS. 
Pfam
 PF00160; Pro_isomerase 
SMART
  
PROSITE
 PS00170; CSA_PPIASE_1
 PS50072; CSA_PPIASE_2 
PRINTS
 PR00153; CSAPPISMRASE.