CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023769
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptidyl-prolyl cis-trans isomerase-like 1 
Protein Synonyms/Alias
 PPIase; Rotamase PPIL1 
Gene Name
 PPIL1 
Gene Synonyms/Alias
 CYPL1; CGI-124; UNQ2425/PRO4984 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
37KHAPKTCKNFAELARubiquitination[1]
52RGYYNGTKFHRIIKDubiquitination[1]
58TKFHRIIKDFMIQGGubiquitination[1, 2, 3]
80GGASIYGKQFEDELHacetylation[4]
80GGASIYGKQFEDELHubiquitination[1, 2, 3, 5, 6]
161VDDVKIIKAYPSG**ubiquitination[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] 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]
 [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] 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]
 [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] 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
 PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing. 
Sequence Annotation
 DOMAIN 10 164 PPIase cyclophilin-type.
 REGION 54 65 Cyclosporin A binding.
 REGION 70 71 Cyclosporin A binding.
 REGION 99 104 Cyclosporin A binding.
 REGION 109 113 Cyclosporin A binding.
 BINDING 119 119 Cyclosporin A.
 BINDING 125 125 Cyclosporin A.  
Keyword
 3D-structure; Complete proteome; Isomerase; mRNA processing; mRNA splicing; Polymorphism; Reference proteome; Rotamase; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 166 AA 
Protein Sequence
MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF 60
MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ 120
WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSG 166 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
 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.