Version 5.4
Bos taurus Protein: PPIA
Summary
InnateDB Protein IDBP-685907.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PPIA
Protein Name Peptidyl-prolyl cis-trans isomerase A
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000015924
InnateDB Gene IDBG-634150 (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 0 experimentally validated interaction(s) in this database.
They are also associated with 49 interaction(s) predicted by orthology.
Predicted by orthology
Total 49 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0016853 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:0005737 cytoplasm
GO:0005829 cytosol
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 P62935
PhosphoSite PhosphoSite-
TrEMBL Q9N138
UniProt Splice Variant
Entrez Gene 786614
UniGene
RefSeq NP_847890
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL AF228021 AY911355 BC105173
GenPept AAF69142 AAI05174 AAW82121

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