Version 5.4
Mus musculus Protein: Asl
Summary
InnateDB Protein IDBP-542911.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Asl
Protein Name argininosuccinate lyase
Synonyms 2510006M18Rik;
Species Mus musculus
Ensembl Protein ENSMUSP00000124487
InnateDB Gene IDBG-202187 (Asl)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
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 7 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 7 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003824 catalytic activity
GO:0004056 argininosuccinate lyase activity
Biological Process
GO:0006520 cellular amino acid metabolic process
GO:0007626 locomotory behavior
GO:0009791 post-embryonic development
GO:0019676 ammonia assimilation cycle
GO:0042450 arginine biosynthetic process via ornithine
Cellular Component
Protein Structure and Domains
PDB ID MGI:88084
InterPro IPR000362 Fumarate lyase family
IPR008948 L-Aspartase-like
IPR009049 Argininosuccinate lyase
IPR022761 Fumarate lyase, N-terminal
PFAM PF00206
PRINTS PR00149
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL E0CY49
UniProt Splice Variant
Entrez Gene 109900
UniGene Mm.480857
RefSeq
MGI ID
MGI Symbol Asl
OMIM
CCDS
HPRD
IMGT
EMBL AC161345
GenPept

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