Version 5.4
Bos taurus Protein: BT.25930
Summary
InnateDB Protein IDBP-683105.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol BT.25930
Protein Name D-aspartate oxidase
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000013892
InnateDB Gene IDBG-631560 (BT.25930)
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 0 experimentally validated interaction(s) in this database.
They are also associated with 2 interaction(s) predicted by orthology.
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003884 D-amino-acid oxidase activity
GO:0005102 receptor binding
GO:0005515 protein binding
GO:0008445 D-aspartate oxidase activity
GO:0016491 oxidoreductase activity
GO:0016641 oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
GO:0048037 cofactor binding
Biological Process
GO:0006531 aspartate metabolic process
GO:0006533 aspartate catabolic process
GO:0007320 insemination
GO:0007625 grooming behavior
GO:0019478 D-amino acid catabolic process
GO:0042445 hormone metabolic process
GO:0055114 oxidation-reduction process
Cellular Component
Protein Structure and Domains
PDB ID
InterPro IPR006076 FAD dependent oxidoreductase
PFAM PF01266
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL F1MP99
UniProt Splice Variant
Entrez Gene 280763
UniGene Bt.25930
RefSeq NP_776333
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL DAAA02025904
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