CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005154
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
 CYPB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67VIFGLFGKTVPKTVDubiquitination[1, 2, 3, 4]
84VALATGEKGFGYKNSubiquitination[1, 2, 3, 5]
98SKFHRVIKDFMIQGGubiquitination[1, 3, 5]
116RGDGTGGKSIYGERFubiquitination[5, 6]
131PDENFKLKHYGPGWVubiquitination[1, 3]
158QFFITTVKTAWLDGKubiquitination[1, 3]
165KTAWLDGKHVVFGKVacetylation[7]
165KTAWLDGKHVVFGKVubiquitination[1, 3, 5]
171GKHVVFGKVLEGMEVacetylation[8]
209CGKIEVEKPFAIAKEacetylation[9]
209CGKIEVEKPFAIAKEubiquitination[1, 3, 5, 6]
215EKPFAIAKE******acetylation[9, 10, 11]
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] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] 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]
 [9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [10] Aspirin acetylates multiple cellular proteins in HCT-116 colon cancer cells: Identification of novel targets.
 Marimuthu S, Chivukula RS, Alfonso LF, Moridani M, Hagen FK, Bhat GJ.
 Int J Oncol. 2011 Nov;39(5):1273-83. [PMID: 21743961]
 [11] 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
 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.
 CARBOHYD 148 148 N-linked (GlcNAc...) (Potential).  
Keyword
 3D-structure; Complete proteome; Cyclosporin; Direct protein sequencing; Disease mutation; Dwarfism; Endoplasmic reticulum; Glycoprotein; Isomerase; Osteogenesis imperfecta; Polymorphism; Reference proteome; Rotamase; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 216 AA 
Protein Sequence
MLRLSERNMK VLLAAALIAG SVFFLLLPGP SAADEKKKGP KVTVKVYFDL RIGDEDVGRV 60
IFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG 120
ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTA WLDGKHVVFG KVLEGMEVVR 180
KVESTKTDSR DKPLKDVIIA DCGKIEVEKP FAIAKE 216 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; NAS:UniProtKB.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0042277; F:peptide binding; IEA:UniProtKB-KW.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; NAS:UniProtKB.
 GO:0051082; F:unfolded protein binding; TAS:ProtInc.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0006457; P:protein folding; IEA:UniProtKB-KW. 
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.