CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012072
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptidyl-prolyl cis-trans isomerase-like 2 
Protein Synonyms/Alias
 PPIase; Cyclophilin-60; Cyclophilin-like protein Cyp-60; Rotamase PPIL2 
Gene Name
 PPIL2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
82TNPSNGEKLDGRSLIubiquitination[1]
90LDGRSLIKLNFSKNSubiquitination[1]
95LIKLNFSKNSEGKYHubiquitination[1]
166QDPTNLDKFNVSNFYubiquitination[1, 2]
180YHVKNNMKIIDPDEEubiquitination[1]
198QDPSYYLKNTNAETRubiquitination[1]
213ETLQELYKEFKGDEIubiquitination[1]
232MKAPEKKKVDKLNAAubiquitination[1]
313NFIRLCKKHYYDGTIubiquitination[1]
462VAPETKVKSSQPQAGubiquitination[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] 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] 
Functional Description
 PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. 
Sequence Annotation
 DOMAIN 42 101 U-box.
 DOMAIN 278 433 PPIase cyclophilin-type.
 MOD_RES 482 482 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Coiled coil; Complete proteome; Isomerase; Nucleus; Reference proteome; Rotamase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 520 AA 
Protein Sequence
MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV 60
FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR 120
TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK 180
IIDPDEEKAK QDPSYYLKNT NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH 240
YSTGKVSASF TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT 300
PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH 360
TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD 420
RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV 480
GKYINPAATE QQRKSPQPVP LSPCPRRSPV GVLGTSAPGS SRLPDDH 527 
Gene Ontology
 GO:0005796; C:Golgi lumen; TAS:Reactome.
 GO:0005634; C:nucleus; TAS:UniProtKB.
 GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
 GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0050900; P:leukocyte migration; TAS:Reactome.
 GO:0006457; P:protein folding; IEA:UniProtKB-KW.
 GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
 GO:0000209; P:protein polyubiquitination; IDA:MGI. 
Interpro
 IPR002130; Cyclophilin-like_PPIase_dom.
 IPR020892; Cyclophilin-type_PPIase_CS.
 IPR026951; PPIL2.
 IPR003613; Ubox_domain.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00160; Pro_isomerase 
SMART
 SM00504; Ubox 
PROSITE
 PS00170; CSA_PPIASE_1
 PS50072; CSA_PPIASE_2 
PRINTS
 PR00153; CSAPPISMRASE.