Version 5.4
Homo sapiens Protein: PPIL1
Summary
InnateDB Protein IDBP-85092.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PPIL1
Protein Name peptidylprolyl isomerase (cyclophilin)-like 1
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000362803
InnateDB Gene IDBG-85090 (PPIL1)
Protein Structure
UniProt Annotation
Function 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. {ECO:0000269PubMed:16595688}.
Subcellular Localization
Disease Associations
Tissue Specificity Ubiquitous, with the most abundant expression in heart and skeletal muscle.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 34 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 34 [view]
Protein-Protein 31 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 2 [view]
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
Biological Process
GO:0000398 mRNA splicing, via spliceosome
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
Cellular Component
GO:0070062 extracellular vesicular exosome
GO:0071013 catalytic step 2 spliceosome
Protein Structure and Domains
PDB ID
InterPro IPR002130 Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain
IPR029000 Cyclophilin-like domain
PFAM PF00160
PRINTS PR00153
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9Y3C6
PhosphoSite PhosphoSite-Q9Y3C6
TrEMBL A0A024RCX8
UniProt Splice Variant
Entrez Gene 51645
UniGene Hs.27693
RefSeq NP_057143
HUGO HGNC:9260
OMIM 601301
CCDS CCDS4826
HPRD 03194
IMGT
EMBL AF151882 AL122034 AY359032 BC003048 CH471081 Z85996
GenPept AAD34119 AAH03048 AAQ89391 CAI20894 CAI23296 EAX03916 EAX03917

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca