Version 5.4
Mus musculus Protein: Aspdh
Summary
InnateDB Protein IDBP-178764.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Aspdh
Protein Name aspartate dehydrogenase domain containing
Synonyms 0610012D14Rik;
Species Mus musculus
Ensembl Protein ENSMUSP00000039202
InnateDB Gene IDBG-178762 (Aspdh)
Protein Structure
UniProt Annotation
Function Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. {ECO:0000250}.
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.
Experimentally validated
Total 3 [view]
Protein-Protein 3 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0016491 oxidoreductase activity
GO:0033735 aspartate dehydrogenase activity
GO:0050661 NADP binding
Biological Process
GO:0006742 NADP catabolic process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
GO:0055114 oxidation-reduction process
Cellular Component
GO:0005575 cellular_component
Protein Structure and Domains
PDB ID MGI:1915602
InterPro IPR002811 Aspartate dehydrogenase
IPR005106 Aspartate/homoserine dehydrogenase, NAD-binding
IPR011182 Aspartate dehydrogenase, NAD biosynthesis
PFAM PF01958
PF03447
PRINTS
PIRSF PIRSF005227
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9DCQ2
PhosphoSite PhosphoSite-Q9DCQ2
TrEMBL
UniProt Splice Variant
Entrez Gene 68352
UniGene
RefSeq NP_080966
MGI ID
MGI Symbol Aspdh
OMIM
CCDS CCDS21207
HPRD
IMGT
EMBL AK002587 BC019451
GenPept AAH19451 BAB22209

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