Version 5.4
Homo sapiens Protein: PPIC
Summary
InnateDB Protein IDBP-39027.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PPIC
Protein Name peptidylprolyl isomerase C (cyclophilin C)
Synonyms CYPC;
Species Homo sapiens
Ensembl Protein ENSP00000303057
InnateDB Gene IDBG-39025 (PPIC)
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.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 5 experimentally validated interaction(s) in this database.
Experimentally validated
Total 5 [view]
Protein-Protein 4 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
GO:0016018 cyclosporin A binding
GO:0051082 unfolded protein binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
GO:0007165 signal transduction
Cellular Component
GO:0005737 cytoplasm
GO:0070062 extracellular vesicular exosome
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 P45877
PhosphoSite PhosphoSite-P45877
TrEMBL
UniProt Splice Variant
Entrez Gene 5480
UniGene Hs.110364
RefSeq NP_000934
HUGO HGNC:9256
OMIM 123842
CCDS CCDS4133
HPRD 00459
IMGT
EMBL BC002678 CH471086 EF506885 S71018
GenPept AAB31350 AAH02678 ABO43038 EAW48878

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