InnateDB: Systems Biology of the Innate Immune Response

Mus musculus Protein: Sars2

Summary

InnateDB Protein

IDBP-164093.6

Last Modified

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

Gene Symbol

Sars2

Protein Name

seryl-aminoacyl-tRNA synthetase 2

Synonyms

2410015F05Rik; D7Ertd353e; SerRS; SerRSmt;

Species

Mus musculus

Ensembl Protein

ENSMUSP00000092216

InnateDB Gene

IDBG-164091 (Sars2)

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

Mitochondrion matrix {ECO:0000250}.

Disease Associations

Tissue Specificity

Comments

Interactions

Number of Interactions

This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
They are also associated with 20 interaction(s) predicted by orthology.

Experimentally validated
Total	1 [view]
Protein-Protein	1 [view]
Protein-DNA	0
Protein-RNA	0
DNA-DNA	0
RNA-RNA	0
DNA-RNA	0

Predicted by orthology
Total	20 [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

Biological Process

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:0005759	mitochondrial matrix

Protein Structure and Domains

PDB ID

MGI:1919234

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