Version 5.4
Mus musculus Protein: Ppig
Summary
InnateDB Protein IDBP-177126.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ppig
Protein Name peptidyl-prolyl isomerase G (cyclophilin G)
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000088370
InnateDB Gene IDBG-177120 (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 (By similarity). {ECO:0000250}.
Subcellular Localization Nucleus matrix. Nucleus speckle. Note=Colocalizes with splicing factors at nuclear speckles. {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 2 experimentally validated interaction(s) in this database.
They are also associated with 15 interaction(s) predicted by orthology.
Experimentally validated
Total 2 [view]
Protein-Protein 2 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 15 [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:0006457 protein folding
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0016363 nuclear matrix
GO:0016607 nuclear speck
Protein Structure and Domains
PDB ID MGI:2445173
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 A2AR02
PhosphoSite PhosphoSite-A2AR02
TrEMBL Q3UZ38
UniProt Splice Variant
Entrez Gene 228005
UniGene Mm.488936
RefSeq XP_006499247
MGI ID
MGI Symbol Ppig
OMIM
CCDS CCDS38137
HPRD
IMGT
EMBL AK134121 AK135713 AK164670 AL845261 U91923
GenPept AAC05726 BAE22023 BAE22623 BAE37869 CAM16370

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