Version 5.4
Homo sapiens Protein: PPIG
Summary
InnateDB Protein IDBP-595077.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PPIG
Protein Name peptidylprolyl isomerase G (cyclophilin G)
Synonyms CARS-Cyp; CYP; SCAF10; SRCyp;
Species Homo sapiens
Ensembl Protein ENSP00000435987
InnateDB Gene IDBG-74530 (PPIG)
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 implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.
Subcellular Localization Nucleus matrix {ECO:0000269PubMed:15358154}. Nucleus speckle {ECO:0000269PubMed:15358154}. Note=Colocalizes with RNA splicing factors at nuclear speckles.
Disease Associations
Tissue Specificity Ubiquitous.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 27 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 27 [view]
Protein-Protein 27 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
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:0044822 poly(A) RNA binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
GO:0008380 RNA splicing
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0016363 nuclear matrix
GO:0016607 nuclear speck
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 Q13427
PhosphoSite PhosphoSite-Q13427
TrEMBL C9JT64
UniProt Splice Variant
Entrez Gene 9360
UniGene Hs.734172
RefSeq
HUGO HGNC:14650
OMIM 606093
CCDS
HPRD 12083
IMGT
EMBL AC016772 AC093899 BC001555 CH471058 U40763 X99717
GenPept AAB40347 AAH01555 AAY24119 AAY24233 CAA68053 EAX11267 EAX11268 EAX11269 EAX11270

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