Version 5.4
Mus musculus Protein: Ppia
Summary
InnateDB Protein IDBP-540628.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ppia
Protein Name peptidylprolyl isomerase A
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000117987
InnateDB Gene IDBG-147795 (Ppia)
Protein Structure
UniProt Annotation
Function PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Localization Cytoplasm. Secreted {ECO:0000250}. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation. {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 10 experimentally validated interaction(s) in this database.
They are also associated with 46 interaction(s) predicted by orthology.
Experimentally validated
Total 10 [view]
Protein-Protein 10 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 46 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0042277 peptide binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
GO:0045069 regulation of viral genome replication
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005829 cytosol
Protein Structure and Domains
PDB ID MGI:97749
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 P17742
PhosphoSite PhosphoSite-XP_001002180
TrEMBL Q9CZK9
UniProt Splice Variant
Entrez Gene 668548
UniGene Mm.5246
RefSeq NP_032933
MGI ID
MGI Symbol Ppia
OMIM
CCDS CCDS24419
HPRD
IMGT
EMBL AF171073 AK002236 AK007981 AK010649 AK012491 AK012531 AK012663 AK028210 AK131942 AK136788 AK151583 AK153030 AK160631 AK160780 AK168035 BC083076 BC087928 BC094272 BC094632 BC099478 CH466574 DQ985731 X52803
GenPept AAD50996 AAH83076 AAH87928 AAH94272 AAH94632 AAH99478 ABL77398 BAB21954 BAB25387 BAB27089 BAB28276 BAB28300 BAB28392 BAC25817 BAE20888 BAE23129 BAE30523 BAE31662 BAE35927 BAE36004 BAE40018 CAA36989 EDL40590 EDL40591

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