Version 5.4
Homo sapiens Protein: YARS2
Summary
InnateDB Protein IDBP-26547.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol YARS2
Protein Name tyrosyl-tRNA synthetase 2, mitochondrial
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000320658
InnateDB Gene IDBG-26545 (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:0000269PubMed:15779907}.
Disease Associations Myopathy with lactic acidosis and sideroblastic anemia 2 (MLASA2) [MIM:613561]: A rare oxidative phosphorylation disorder specific to skeletal muscle and bone marrow. Affected individuals manifest sideroblastic anemia, progressive lethargy, muscle weakness, and exercise intolerance associated with persistent lactic acidemia. {ECO:0000269PubMed:20598274, ECO:0000269PubMed:22504945}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 11 experimentally validated interaction(s) in this database.
Experimentally validated
Total 11 [view]
Protein-Protein 11 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0000049 tRNA binding
GO:0000166 nucleotide 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:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006437 tyrosyl-tRNA aminoacylation
GO:0010467 gene expression
GO:0043039 tRNA aminoacylation
GO:0070184 mitochondrial tyrosyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
Protein Structure and Domains
PDB ID
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 Q9Y2Z4
PhosphoSite PhosphoSite-Q9Y2Z4
TrEMBL
UniProt Splice Variant
Entrez Gene 51067
UniGene Hs.505231
RefSeq NP_001035526
HUGO HGNC:24249
OMIM 610957
CCDS CCDS31770
HPRD 13025
IMGT
EMBL AC087588 AF132939 AK024057 BC015625 CH471116
GenPept AAD27714 AAH15625 BAB14806 EAW88517 EAW88518

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