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RARS

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]
Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets

Predicted location

Intracellular

Single cell type specificity

Group enriched (Cytotrophoblasts, Extravillous trophoblasts, Syncytiotrophoblasts, Hofbauer cells, Cardiomyocytes)

Immune cell specificity

Low immune cell specificity

Cell line specificity

Low cell line specificity

Interaction

Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity (PubMed:10358004, PubMed:25288775). Interacts (via N-terminus) with LARS2 (via C-terminus) (PubMed:16055448, PubMed:17443684). Monomer (PubMed:24859084). Part of a multisubunit complex that groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:19131329, PubMed:19289464). Interacts with QARS1 (PubMed:24656866). Part of a complex composed of RARS1, QARS1 and AIMP1 (PubMed:25288775).

Molecular function

Aminoacyl-tRNA synthetase, Ligase

More Types Infomation

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