Version 5.4
Mus musculus Protein: Ppil3
Summary
InnateDB Protein IDBP-251970.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ppil3
Protein Name peptidylprolyl isomerase (cyclophilin)-like 3
Synonyms 2310076N22Rik; 2510026K04Rik; Cyp10l;
Species Mus musculus
Ensembl Protein ENSMUSP00000109988
InnateDB Gene IDBG-156766 (Ppil3)
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 0 experimentally validated interaction(s) in this database.
They are also associated with 17 interaction(s) predicted by orthology.
Predicted by orthology
Total 17 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006397 mRNA processing
GO:0006457 protein folding
GO:0008380 RNA splicing
Cellular Component
GO:0071013 catalytic step 2 spliceosome
Protein Structure and Domains
PDB ID MGI:1917475
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 Q9D6L8
PhosphoSite PhosphoSite-Q9D6L8
TrEMBL
UniProt Splice Variant
Entrez Gene 70225
UniGene
RefSeq NP_001272756
MGI ID
MGI Symbol Ppil3
OMIM
CCDS CCDS35579
HPRD
IMGT
EMBL AF315803 AK010207 AK011000 BC060993 BC061645
GenPept AAH60993 AAH61645 AAO32944 BAB26768 BAB27319

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