DPS1 aspartate--tRNA ligase DPS1 [Saccharomyces cerevisiae S288C] - Gene

Summary

Official Symbol: DPS1
Official Full Name: aspartate--tRNA ligase DPS1
Primary source: SGD:S000003941
Locus tag: YLL018C
See related: AllianceGenome:SGD:S000003941; FungiDB:YLL018C; VEuPathDB:YLL018C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables aspartate-tRNA ligase activity and sequence-specific mRNA binding activity. Involved in aspartyl-tRNA aminoacylation. Located in cytoplasm and nucleus. Orthologous to human DARS1 (aspartyl-tRNA synthetase 1). [provided by Alliance of Genome Resources, Nov 2024]
NEW: Try the new Gene table
Try the new Transcript table

Chromosome XII - NC_001144.5 Genomic Context describing neighboring genes

Go to nucleotide: Graphics FASTA GenBank

Submit: New GeneRIF Correction

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables RNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables RNA binding	IDA Inferred from Direct Assay more info	PubMed
enables aminoacyl-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables aspartate-tRNA ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables aspartate-tRNA ligase activity	IDA Inferred from Direct Assay more info	PubMed
enables aspartate-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables nucleic acid binding	IEA Inferred from Electronic Annotation more info
enables sequence-specific mRNA binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in aspartyl-tRNA aminoacylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in aspartyl-tRNA aminoacylation	IDA Inferred from Direct Assay more info	PubMed
involved_in aspartyl-tRNA aminoacylation	IEA Inferred from Electronic Annotation more info
involved_in tRNA aminoacylation for protein translation	IEA Inferred from Electronic Annotation more info
involved_in translation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of aminoacyl-tRNA synthetase multienzyme complex	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

NP_013083.1

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)