Version 5.4
Mus musculus Protein: Ppil1
Summary
InnateDB Protein IDBP-160287.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ppil1
Protein Name peptidylprolyl isomerase (cyclophilin)-like 1
Synonyms 1110060O10Rik; AI327391; Cypl1;
Species Mus musculus
Ensembl Protein ENSMUSP00000024802
InnateDB Gene IDBG-160285 (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 (By similarity). {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
They are also associated with 21 interaction(s) predicted by orthology.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 21 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006397 mRNA processing
GO:0006457 protein folding
GO:0008380 RNA splicing
Cellular Component
GO:0070062 extracellular vesicular exosome
GO:0071013 catalytic step 2 spliceosome
Protein Structure and Domains
PDB ID MGI:1916066
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 Q9D0W5
PhosphoSite PhosphoSite-Q9D0W5
TrEMBL B9EJX8
UniProt Splice Variant
Entrez Gene 68816
UniGene Mm.416234
RefSeq NP_081121
MGI ID
MGI Symbol Ppil1
OMIM
CCDS CCDS28593
HPRD
IMGT
EMBL AK004331 AK150643 AK151572 BC058369 BC147647 BC147649 CH466606
GenPept AAH58369 AAI47648 AAI47650 BAB23265 BAE29731 BAE30513 EDL22612

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