Version 5.4
Mus musculus Protein: Acy1
Summary
InnateDB Protein IDBP-196002.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Acy1
Protein Name aminoacylase 1
Synonyms 1110014J22Rik; Acy-1;
Species Mus musculus
Ensembl Protein ENSMUSP00000024031
InnateDB Gene IDBG-196000 (Acy1)
Protein Structure
UniProt Annotation
Function Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). {ECO:0000250}.
Subcellular Localization Cytoplasm {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 2 experimentally validated interaction(s) in this database.
They are also associated with 10 interaction(s) predicted by orthology.
Experimentally validated
Total 2 [view]
Protein-Protein 2 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 10 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004046 aminoacylase activity
GO:0008237 metallopeptidase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0006520 cellular amino acid metabolic process
GO:0008152 metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:87913
InterPro IPR002933 Peptidase M20
IPR010159 N-acyl-L-amino-acid amidohydrolase
IPR011650 Peptidase M20, dimerisation domain
PFAM PF01546
PF07687
PRINTS
PIRSF PIRSF036696
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q99JW2
PhosphoSite PhosphoSite-Q99JW2
TrEMBL
UniProt Splice Variant
Entrez Gene 109652
UniGene Mm.7165
RefSeq NP_079647
MGI ID
MGI Symbol Acy1
OMIM
CCDS CCDS23477
HPRD
IMGT
EMBL AK002423 AK003703 BC005631
GenPept AAH05631 BAB22090 BAB22948

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