Version 5.4
Mus musculus Protein: Arg2
Summary
InnateDB Protein IDBP-152632.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Arg2
Protein Name arginase type II
Synonyms AII; AU022422;
Species Mus musculus
Ensembl Protein ENSMUSP00000021550
InnateDB Gene IDBG-152630 (Arg2)
Protein Structure
UniProt Annotation
Function May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. {ECO:0000250}.
Subcellular Localization Mitochondrion.
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 2 interaction(s) predicted by orthology.
Experimentally validated
Total 3 [view]
Protein-Protein 1 [view]
Protein-DNA 2 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004053 arginase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872 metal ion binding
Biological Process
GO:0000050 urea cycle
GO:0001657 ureteric bud development
GO:0006525 arginine metabolic process
GO:0006941 striated muscle contraction
Cellular Component
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID MGI:1330806
InterPro IPR006035 Ureohydrolase
IPR014033 Arginase
PFAM PF00491
PRINTS PR00116
PIRSF PIRSF036979
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt O08691
PhosphoSite PhosphoSite-O08691
TrEMBL
UniProt Splice Variant
Entrez Gene 11847
UniGene Mm.3506
RefSeq NP_033835
MGI ID
MGI Symbol Arg2
OMIM
CCDS CCDS26007
HPRD
IMGT
EMBL AF032466 AF044680 AF045959 AF045960 AF045961 AF045962 AF045963 AF045964 AF045965 U90886
GenPept AAB86959 AAC22548 AAC78460

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