InnateDB: Systems Biology of the Innate Immune Response

Mus musculus Protein: Rars

Summary

InnateDB Protein

IDBP-162758.6

Last Modified

2014-10-13 [Report errors or provide feedback]

Gene Symbol

Rars

Protein Name

arginyl-tRNA synthetase

Synonyms

2610011N19Rik; 2610037E21Rik; AL033339; AW985894;

Species

Mus musculus

Ensembl Protein

ENSMUSP00000018992

InnateDB Gene

IDBG-162756 (Rars)

Protein Structure

UniProt Annotation

Function

Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 (By similarity). {ECO:0000250}.

Subcellular Localization

Cytoplasm.

Disease Associations

Tissue Specificity

Comments

Interactions

Number of Interactions

This gene and/or its encoded proteins are associated with 10 experimentally validated interaction(s) in this database.
They are also associated with 31 interaction(s) predicted by orthology.

Experimentally validated
Total	10 [view]
Protein-Protein	10 [view]
Protein-DNA	0
Protein-RNA	0
DNA-DNA	0
RNA-RNA	0
DNA-RNA	0

Predicted by orthology
Total	31 [view]

Gene Ontology

Molecular Function

Accession	GO Term
GO:0000049	tRNA binding
GO:0000166	nucleotide binding
GO:0004812	aminoacyl-tRNA ligase activity
GO:0004814	arginine-tRNA ligase activity
GO:0005515	protein binding
GO:0005524	ATP binding
GO:0034618	arginine binding

Biological Process

GO:0006418	tRNA aminoacylation for protein translation
GO:0006420	arginyl-tRNA aminoacylation

Cellular Component

GO:0005634	nucleus
GO:0005737	cytoplasm
GO:0005739	mitochondrion
GO:0016020	membrane
GO:0017101	aminoacyl-tRNA synthetase multienzyme complex
GO:0070062	extracellular vesicular exosome

Protein Structure and Domains

PDB ID

MGI:1914297

InterPro

IPR001278 Arginine-tRNA ligase
IPR005148 Arginyl tRNA synthetase N-terminal domain
IPR008909 DALR anticodon binding
IPR009080 Aminoacyl-tRNA synthetase, class 1a, anticodon-binding

PFAM

PF00750
PF03485
PF05746

PRINTS

PR01038

PIRSF

SMART

SM01016
SM00836

TIGRFAMs

Post-translational Modifications

Modification

Cross-References

SwissProt