Version 5.4
Mus musculus Protein: Pdia2
Summary
InnateDB Protein IDBP-532366.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Pdia2
Protein Name protein disulfide isomerase associated 2
Synonyms 1810041F13Rik; AI661267; Pdip; Pdipl;
Species Mus musculus
Ensembl Protein ENSMUSP00000116340
InnateDB Gene IDBG-154856 (Pdia2)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 3 experimentally validated interaction(s) in this database.
They are also associated with 23 interaction(s) predicted by orthology.
Experimentally validated
Total 3 [view]
Protein-Protein 3 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 23 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0016209 antioxidant activity
GO:0016491 oxidoreductase activity
GO:0016853 isomerase activity
Biological Process
GO:0045454 cell redox homeostasis
GO:0055114 oxidation-reduction process
Cellular Component
Protein Structure and Domains
PDB ID MGI:1916441
InterPro IPR000866 Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant
IPR005788 Disulphide isomerase
IPR012336 Thioredoxin-like fold
IPR013740 Redoxin
IPR013766 Thioredoxin domain
PFAM PF00578
PF13098
PF13192
PF13462
PF13905
PF08534
PF00085
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 69191
UniGene Mm.32631
RefSeq
MGI ID
MGI Symbol Pdia2
OMIM
CCDS
HPRD
IMGT
EMBL
GenPept

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