Wikiwand AI

Arginine–tRNA ligase, cytoplasmic

Enzyme found in humans From Wikipedia, the free encyclopedia

Arginine–tRNA ligase, cytoplasmic, or arginyl-tRNA synthetase 1, is an enzyme that in humans is encoded by the RARS1 gene (previously RARS).[5][6] This enzyme (like the mitochondrial form, RARS2) functions as a Arginine–tRNA ligase, which means it attaches the amino acid arginine to the corresponding transfer RNA (tRNAArg) as part of RNA-to-protein translation.[6]

AliasesRARS1, ArgRS, DALRD1, HLD9, arginyl-tRNA synthetase, arginyl-tRNA synthetase 1, RARS
PDBOrtholog search: PDBe RCSB
Quick facts RARS1, Identifiers ...
RARS1
Identifiers
AliasesRARS1, ArgRS, DALRD1, HLD9, arginyl-tRNA synthetase, arginyl-tRNA synthetase 1, RARS
External IDsOMIM: 107820; MGI: 1914297; GeneCards: RARS1
Available structures
PDBOrtholog search: PDBe RCSB
Enzyme activity
EC #BRENDAExPASyKEGGMetaCyc
6.1.1.19↗↗↗↗
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002887

NM_025936

RefSeq (protein)

NP_002878

NP_080212

Location (UCSC)Chr 5: 168.49 – 168.52 MbChr 11: 35.7 – 35.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Close

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.[6]

Medical significance

Mutations in RARS1 can cause hypomyelination.[7]

Interactions

RARS1 has been shown to interact with QARS1.[8]

References

Further reading

Related Articles

Timelines

Top Qs

Fact Checks