Version 5.4
Bos taurus Protein: SARS
Summary
InnateDB Protein IDBP-687355.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol SARS
Protein Name Seryl-tRNA synthetase, cytoplasmic
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000017232
InnateDB Gene IDBG-635511 (SARS)
Protein Structure
UniProt Annotation
Function Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (By similarity). {ECO:0000250}.
Subcellular Localization Cytoplasm {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 15 interaction(s) predicted by orthology.
Predicted by orthology
Total 15 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004828 serine-tRNA ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006434 seryl-tRNA aminoacylation
GO:0097056 selenocysteinyl-tRNA(Sec) biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR002314 Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain
IPR002317 Serine-tRNA ligase, type1
IPR006195 Aminoacyl-tRNA synthetase, class II
IPR010978 tRNA-binding arm
IPR015866 Serine-tRNA synthetase, type1, N-terminal
PFAM PF00587
PF02403
PRINTS PR00981
PIRSF PIRSF001529
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9GMB8
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 281476
UniGene Bt.1552
RefSeq NP_776600
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL AF297553
GenPept AAG03084

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