Version 5.4
Mus musculus Protein: Ddah2
Summary
InnateDB Protein IDBP-176276.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ddah2
Protein Name dimethylarginine dimethylaminohydrolase 2
Synonyms 1110003M04Rik; AU019324; AW413173; Ddah; DDAH-2; DDAHII; G6a; NG30;
Species Mus musculus
Ensembl Protein ENSMUSP00000007255
InnateDB Gene IDBG-176274 (Ddah2)
Protein Structure
UniProt Annotation
Function Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation (By similarity). {ECO:0000250}.
Subcellular Localization Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Translocates from cytosol to mitochondrion upon IL-1beta stimulation in chondrocytes. {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 22 interaction(s) predicted by orthology.
Predicted by orthology
Total 22 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0016403 dimethylargininase activity
GO:0016597 amino acid binding
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
Biological Process
GO:0000052 citrulline metabolic process
GO:0006525 arginine metabolic process
GO:0006527 arginine catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:1859016
InterPro IPR003198 Amidinotransferase
PFAM PF02274
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q99LD8
PhosphoSite PhosphoSite-Q99LD8
TrEMBL G3UZR0
UniProt Splice Variant
Entrez Gene 51793
UniGene
RefSeq NP_001177378
MGI ID
MGI Symbol Ddah2
OMIM
CCDS CCDS50082
HPRD
IMGT
EMBL AC087117 BC003328
GenPept AAH03328

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