Version 5.4
Mus musculus Protein: Yars2
Summary
InnateDB Protein IDBP-136780.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Yars2
Protein Name tyrosyl-tRNA synthetase 2 (mitochondrial)
Synonyms 2210023C10Rik; tyrRS;
Species Mus musculus
Ensembl Protein ENSMUSP00000055277
InnateDB Gene IDBG-136778 (Yars2)
Protein Structure
UniProt Annotation
Function Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr). {ECO:0000250}.
Subcellular Localization Mitochondrion matrix {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 7 interaction(s) predicted by orthology.
Predicted by orthology
Total 7 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0003723 RNA binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004831 tyrosine-tRNA ligase activity
GO:0005524 ATP binding
GO:0042803 protein homodimerization activity
GO:0044822 poly(A) RNA binding
GO:0072545 tyrosine binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006437 tyrosyl-tRNA aminoacylation
GO:0043039 tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
Protein Structure and Domains
PDB ID MGI:1917370
InterPro IPR002305 Aminoacyl-tRNA synthetase, class Ic
IPR002307 Tyrosine-tRNA ligase
PFAM PF00579
PRINTS PR01040
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8BYL4
PhosphoSite PhosphoSite-Q8BYL4
TrEMBL
UniProt Splice Variant
Entrez Gene 70120
UniGene Mm.37486
RefSeq NP_937889
MGI ID
MGI Symbol Yars2
OMIM
CCDS CCDS27983
HPRD
IMGT
EMBL AK039123 BC060295
GenPept AAH60295 BAC30245

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