BAIT

DPS1

aspartate--tRNA ligase DPS1, AspRS, L000002834, YLL018C
Aspartyl-tRNA synthetase, primarily cytoplasmic; homodimeric enzyme that catalyzes the specific aspartylation of tRNA(Asp); class II aminoacyl tRNA synthetase; binding to its own mRNA may confer autoregulation; shares five highly conserved amino acids with human that when mutated cause leukoencephalopathy characterized by hypomyelination with brain stem and spinal cord involvement and leg spasticity (HBSL)
GO Process (1)
GO Function (2)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

TD(GUC)I1

L000003873
Aspartate tRNA (tRNA-Asp), predicted by tRNAscan-SE analysis
GO Process (1)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Biochemical Activity

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

Yeast tRNA(Asp) charging accuracy is threatened by the N-terminal extension of aspartyl-tRNA synthetase.

Ryckelynck M, Giege R, Frugier M

This study evaluates the role of the N-terminal extension from yeast aspartyl-tRNA synthetase in tRNA aspartylation. The presence of an RNA-binding motif in this extension, conserved in eukaryotic class IIb aminoacyl-tRNA synthetases, provides nonspecific tRNA binding properties to this enzyme. Here, it is assumed that the additional contacts the 70 amino acid-long appendix of aspartyl-tRNA synthetase makes with tRNA could ... [more]

J. Biol. Chem. Mar. 14, 2003; 278(11);9683-90 [Pubmed: 12486031]

Throughput

  • Low Throughput

Additional Notes

  • aspartylation

Curated By

  • BioGRID