Version 5.4
Mus musculus Protein: Aga
Summary
InnateDB Protein IDBP-155093.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Aga
Protein Name aspartylglucosaminidase
Synonyms AW060726;
Species Mus musculus
Ensembl Protein ENSMUSP00000033920
InnateDB Gene IDBG-155091 (Aga)
Protein Structure
UniProt Annotation
Function Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.
Subcellular Localization Lysosome.
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:0003948 N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
GO:0008233 peptidase activity
GO:0016787 hydrolase activity
GO:0043621 protein self-association
Biological Process
GO:0006508 proteolysis
GO:0006517 protein deglycosylation
GO:0051604 protein maturation
Cellular Component
GO:0005764 lysosome
GO:0005783 endoplasmic reticulum
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:104873
InterPro IPR000246 Peptidase T2, asparaginase 2
IPR029055 Nucleophile aminohydrolases, N-terminal
PFAM PF01112
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q64191
PhosphoSite PhosphoSite-NP_001191983
TrEMBL B7ZNK6
UniProt Splice Variant
Entrez Gene 11593
UniGene
RefSeq NP_001191983
MGI ID
MGI Symbol Aga
OMIM
CCDS CCDS22304
HPRD
IMGT
EMBL BC132227 BC132229 BC145297 CH466554 S81393
GenPept AAB36101 AAI32228 AAI32230 AAI45298 EDL35636

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