Version 5.4
Bos taurus Protein: ASRGL1
Summary
InnateDB Protein IDBP-696122.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ASRGL1
Protein Name L-asparaginase
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000009073
InnateDB Gene IDBG-643561 (ASRGL1)
Protein Structure
UniProt Annotation
Function Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L- Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine (By similarity). {ECO:0000250}.
Subcellular Localization Cytoplasm {ECO:0000250}. Note=Midpiece of sperm tail. {ECO:0000250}.
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 4 interaction(s) predicted by orthology.
Predicted by orthology
Total 4 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004067 asparaginase activity
GO:0008233 peptidase activity
GO:0008798 beta-aspartyl-peptidase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006508 proteolysis
GO:0033345 asparagine catabolic process via L-aspartate
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID
InterPro IPR000246 Peptidase T2, asparaginase 2
IPR029055 Nucleophile aminohydrolases, N-terminal
PFAM PF01112
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q32LE5
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 767970
UniGene Bt.685
RefSeq NP_001070503
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC109621
GenPept AAI09622

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