Version 5.4
Mus musculus Gene: Farsa
Summary
InnateDB Gene IDBG-175011.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Farsa
Gene Name phenylalanyl-tRNA synthetase, alpha subunit
Synonyms 0610012A19Rik; Farsla
Species Mus musculus
Ensembl Gene ENSMUSG00000003808
Encoded Proteins
IDBP-175013
phenylalanyl-tRNA synthetase, alpha subunit
IDBP-261706
phenylalanyl-tRNA synthetase, alpha subunit
IDBP-541745
phenylalanyl-tRNA synthetase, alpha subunit
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This gene does not have any Entrez summary - the following is the summary from its human ortholog ENSG00000179115:
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. This gene encodes a product which is similar to the catalytic subunit of prokaryotic and Saccharomyces cerevisiae phenylalanyl-tRNA synthetases (PheRS). This gene product has been shown to be expressed in a tumor-selective and cell cycle stage- and differentiation-dependent manner, the first member of the tRNA synthetase gene family shown to exhibit this type of regulated expression [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 8:84856989-84869257
Strand Forward strand
Band C2
Transcripts
ENSMUST00000003906 ENSMUSP00000003906
ENSMUST00000109754 ENSMUSP00000105376
ENSMUST00000129595
ENSMUST00000144404
ENSMUST00000156970 ENSMUSP00000120609
ENSMUST00000141480
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 14 experimentally validated interaction(s) in this database.
They are also associated with 21 interaction(s) predicted by orthology.
Experimentally validated
Total 14 [view]
Protein-Protein 13 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 21 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004826 phenylalanine-tRNA ligase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0044822 poly(A) RNA binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006432 phenylalanyl-tRNA aminoacylation
GO:0008150 biological_process
GO:0043039 tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane
Orthologs
Species
Homo sapiens
Bos taurus
Gene ID
Gene Order
ENSG00000179115
View Gene Order
ENSBTAG00000021374
Not yet available
Pathways
NETPATH
REACTOME
KEGG
mmu00970
Aminoacyl-tRNA biosynthesis pathway
INOH
PID NCI
Pathway Predictions based on Human Orthology Data
NETPATH
REACTOME
REACT_15306
Cytosolic tRNA aminoacylation pathway
REACT_15482
tRNA Aminoacylation pathway
REACT_71
Gene Expression pathway
KEGG
hsa00970
Aminoacyl-tRNA biosynthesis pathway
INOH
PID NCI
Cross-References
SwissProt Q8C0C7
TrEMBL D6RIJ2 E9PWY9
UniProt Splice Variant
Entrez Gene 66590
UniGene Mm.292517 Mm.414759
RefSeq NM_025648 XM_006531288
OMIM
CCDS CCDS22480
HPRD
IMGT
MGI ID MGI:1913840
MGI Symbol Farsa
EMBL AC155163 AC161765 AK031697 AK154629 BC006862 BC013533
GenPept AAH06862 AAH13533 BAC27519 BAE32726
RNA Seq Atlas 66590

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