Version 5.4
Mus musculus Protein: Aasdh
Summary
InnateDB Protein IDBP-533241.4
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Aasdh
Protein Name aminoadipate-semialdehyde dehydrogenase
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000117639
InnateDB Gene IDBG-173517 (Aasdh)
Protein Structure
UniProt Annotation
Function Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA (By similarity). Putative 2-aminoadipic 6-semialdehyde dehydrogenase, which may be involved in lysine catabolism. {ECO:0000250}.
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.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0003824 catalytic activity
GO:0004043 L-aminoadipate-semialdehyde dehydrogenase activity
GO:0005524 ATP binding
GO:0016878 acid-thiol ligase activity
Biological Process
GO:0006631 fatty acid metabolic process
GO:0008150 biological_process
GO:0008152 metabolic process
GO:0055114 oxidation-reduction process
Cellular Component
GO:0005575 cellular_component
Protein Structure and Domains
PDB ID MGI:2442517
InterPro IPR000873 AMP-dependent synthetase/ligase
IPR009081 Acyl carrier protein-like
PFAM PF00501
PF00550
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q80WC9
PhosphoSite PhosphoSite-
TrEMBL D3YXV2
UniProt Splice Variant
Entrez Gene 231326
UniGene Mm.39271
RefSeq
MGI ID
MGI Symbol Aasdh
OMIM
CCDS
HPRD
IMGT
EMBL AB095954 AC114666 AC166328 AK038779 AK043807 BC094507 BC128330
GenPept AAH94507 AAI28331 BAC31660 BAC75954 BAE43303

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