RARS1 arginyl-tRNA synthetase 1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: RARS1provided by HGNC
Official Full Name: arginyl-tRNA synthetase 1provided by HGNC
Primary source: HGNC:HGNC:9870
See related: Ensembl:ENSG00000113643 MIM:107820; AllianceGenome:HGNC:9870
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: HLD9; RARS; ArgRS; DALRD1
Summary: Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. [provided by RefSeq, Jul 2008]
Expression: Ubiquitous expression in duodenum (RPKM 28.0), small intestine (RPKM 25.9) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 5q34

Exon count:: 15

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	5	NC_000005.10 (168486471..168519301)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	5	NC_060929.1 (169021262..169054094)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	5	NC_000005.9 (167913476..167946306)

Chromosome 5 - NC_000005.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Distinct pathogenic mechanisms of various RARS1 mutations in Pelizaeus-Merzbacher-like disease.
Title: Distinct pathogenic mechanisms of various RARS1 mutations in Pelizaeus-Merzbacher-like disease.
RARS1-related hypomyelinating leukodystrophy: Expanding the spectrum.
Title: RARS1-related hypomyelinating leukodystrophy: Expanding the spectrum.
we demonstrated the presence of the recurrent RARS-MAD1L1 gene fusion in NPC. Furthermore, we provided the first evidence showing that the RARS-MAD1L1 fusion gene enhances tumorigenicity, CSC-like properties, and therapeutic resistance
Title: The RARS-MAD1L1 Fusion Gene Induces Cancer Stem Cell-like Properties and Therapeutic Resistance in Nasopharyngeal Carcinoma.
This study demonstrates that human mitochondrial AspRS, ArgRS, and LysRS, each have a specific sub-mitochondrial distribution, with ArgRS being exclusively localized in the membrane, LysRS exclusively in the soluble fraction, and AspRS being present in both.
Title: Three human aminoacyl-tRNA synthetases have distinct sub-mitochondrial localizations that are unaffected by disease-associated mutations.
Missense variant Ser456Leu and a de novo deletion Tyr616Leufs*6 cause disorder akin to Pelizaeus-Merzbacher disease.
Title: Mutations in RARS cause a hypomyelination disorder akin to Pelizaeus-Merzbacher disease.
Data indicate that the N terminus of Pro-EMAP II binds to its C terminus, arginyl-tRNA synthetase, and the neurofilament light subunit.
Title: The N terminus of pro-endothelial monocyte-activating polypeptide II (EMAP II) regulates its binding with the C terminus, arginyl-tRNA synthetase, and neurofilament light protein.
interactions between the N-terminal domains of ArgRS and AIMP1 are important for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC protein complex with ArgRS-GlnRS-AIMP1
Title: Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation.
The mRNA of human cytoplasmic arginyl-tRNA synthetase recruits prokaryotic ribosomes independently.
Title: The mRNA of human cytoplasmic arginyl-tRNA synthetase recruits prokaryotic ribosomes independently.
report describe 4 patients with hypomyelination and mutations in RARS
Title: Mutations in RARS cause hypomyelination.
The crystal structures of the L-arginine-complexed, and L-canavanine-complexed forms of arginyl-tRNA synthetase from Homo sapiens.
Title: The crystal structure of arginyl-tRNA synthetase from Homo sapiens.

Submit: New GeneRIF Correction See all GeneRIFs (14)

Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Hypomyelinating leukodystrophy 9 MedGen: C4015323 OMIM: 616140 GeneReviews: Not available	Compare labs

EBI GWAS Catalog

Description
Genome-wide meta-analysis identifies variants associated with platinating agent susceptibility across populations EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Pr55(Gag)	gag	Interaction of HIV-1 Gag with arginyl-tRNA synthetase (RARS) is identified in a series of six affinity purification/mass spectrometry screens	PubMed
matrix	gag	HIV-1 MA is identified to have a physical interaction with arginyl-tRNA synthetase (RARS) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH12410 (e-PCR)
- UniSTS:39170

RARS (e-PCR)
- UniSTS:504849

STS-AA011177 (e-PCR)
- UniSTS:8308

WI-16695 (e-PCR)
- UniSTS:7558

RH65982 (e-PCR)
- UniSTS:33964

RH10999 (e-PCR)
- UniSTS:53168

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables arginine binding	IEA Inferred from Electronic Annotation more info
enables arginine-tRNA ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables arginine-tRNA ligase activity	IDA Inferred from Direct Assay more info	PubMed
enables arginine-tRNA ligase activity	TAS Traceable Author Statement more info
enables cadherin binding	HDA more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables tRNA binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in arginyl-tRNA aminoacylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in arginyl-tRNA aminoacylation	IDA Inferred from Direct Assay more info	PubMed
involved_in tRNA aminoacylation for protein translation	TAS Traceable Author Statement more info

Component	Evidence Code	Pubs
part_of aminoacyl-tRNA synthetase multienzyme complex	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	TAS Traceable Author Statement more info
located_in extracellular exosome	HDA more info	PubMed
located_in membrane	HDA more info	PubMed
located_in nucleolus	IDA Inferred from Direct Assay more info
located_in nucleoplasm	IDA Inferred from Direct Assay more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: arginine--tRNA ligase, cytoplasmic

Names: arginine tRNA ligase 1, cytoplasmic; arginyl-tRNA synthetase, cytoplasmic

NP_002878.2

EC 6.1.1.19

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.