Version 5.4
Mus musculus Protein: Qrsl1
Summary
InnateDB Protein IDBP-148253.7
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Qrsl1
Protein Name glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1
Synonyms 2700038P16Rik; C80053; GatA;
Species Mus musculus
Ensembl Protein ENSMUSP00000020012
InnateDB Gene IDBG-148251 (Qrsl1)
Protein Structure
UniProt Annotation
Function Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). {ECO:0000255HAMAP-Rule:MF_03150}.
Subcellular Localization Mitochondrion {ECO:0000255HAMAP- Rule:MF_03150}.
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 5 interaction(s) predicted by orthology.
Predicted by orthology
Total 5 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005524 ATP binding
GO:0016884 carbon-nitrogen ligase activity, with glutamine as amido-N-donor
GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Biological Process
GO:0006412 translation
GO:0032543 mitochondrial translation
GO:0070681 glutaminyl-tRNAGln biosynthesis via transamidation
Cellular Component
GO:0005739 mitochondrion
GO:0030956 glutamyl-tRNA(Gln) amidotransferase complex
Protein Structure and Domains
PDB ID MGI:1923813
InterPro IPR000120 Amidase
IPR004412 Glutamyl-tRNA(Gln) amidotransferase A subunit
IPR023631 Amidase signature domain
PFAM PF01425
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9CZN8
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 76563
UniGene Mm.5904
RefSeq NP_001074523
MGI ID
MGI Symbol Qrsl1
OMIM
CCDS CCDS35894
HPRD
IMGT
EMBL AK012351 AK170225 BC070459
GenPept AAH70459 BAB28181 BAE41646

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