Version 5.4
Mus musculus Protein: Iars
Summary
InnateDB Protein IDBP-620460.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Iars
Protein Name isoleucine-tRNA synthetase
Synonyms 2510016L12Rik; AI327140; AU044614; E430001P04Rik; ILRS;
Species Mus musculus
Ensembl Protein ENSMUSP00000130058
InnateDB Gene IDBG-151359 (Iars)
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 3 experimentally validated interaction(s) in this database.
They are also associated with 54 interaction(s) predicted by orthology.
Experimentally validated
Total 3 [view]
Protein-Protein 3 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 54 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
Cellular Component
GO:0005634 nucleus
Protein Structure and Domains
PDB ID MGI:2145219
InterPro IPR002300 Aminoacyl-tRNA synthetase, class Ia
IPR015413 Methionyl/Leucyl tRNA synthetase
PFAM PF00133
PF09334
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL E9Q866
UniProt Splice Variant
Entrez Gene 105148
UniGene Mm.21118
RefSeq
MGI ID
MGI Symbol Iars
OMIM
CCDS
HPRD
IMGT
EMBL AC125070
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