// Workers AI · dad joke modeWhy was Arginine–tRNA ligase, cytoplasmic lonely? It couldn't bond.

RARS1
Identifiers
Aliases	RARS1, ArgRS, DALRD1, HLD9, arginyl-tRNA synthetase, arginyl-tRNA synthetase 1, RARS
External IDs	OMIM: 107820; MGI: 1914297; GeneCards: RARS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4Q2T, 4Q2X, 4Q2Y, 4R3Z, 4ZAJ
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 6.1.1.19 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 5 (human) Band 5q34 Start 168,486,451 bp End 168,519,301 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 A4 Start 35,699,208 bp End 35,725,333 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon jejunal mucosa rectum islet of Langerhans duodenum body of pancreas gonad stromal cell of endometrium skin of leg skin of abdomen Top expressed in tail of embryo primitive streak genital tubercle hair follicle epiblast gastrula endothelial cell of lymphatic vessel yolk sac crypt of lieberkuhn of small intestine fetal liver hematopoietic progenitor cell More reference expression data BioGPS n/a
Gene ontology Molecular function aminoacyl-tRNA ligase activity nucleotide binding tRNA binding arginine binding ligase activity protein binding ATP binding cadherin binding arginine-tRNA ligase activity Cellular component membrane nucleoplasm mitochondrion extracellular exosome nucleus cytoplasm aminoacyl-tRNA synthetase multienzyme complex cytosol Biological process protein biosynthesis tRNA aminoacylation for protein translation arginyl-tRNA aminoacylation Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 5917 104458 Ensembl ENSG00000113643 ENSMUSG00000018848 UniProt P54136 Q9D0I9 RefSeq (mRNA) NM_002887 NM_025936 RefSeq (protein) NP_002878 NP_080212 Location (UCSC) Chr 5: 168.49 – 168.52 Mb Chr 11: 35.7 – 35.73 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Arginine–tRNA ligase, cytoplasmic, or arginyl-tRNA synthetase 1, is an enzyme that in humans is encoded by the RARS1 gene (previously RARS). 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 (tRNA^Arg) as part of RNA-to-protein translation.

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.

Medical significance

Mutations in RARS1 can cause hypomyelination.

Interactions

RARS1 has been shown to interact with QARS1.

Further reading

• McCune SA, Yu PL, Nance WE (1977). "A genetic study of erythrocyte arginine-tRNA synthetase activity in man". Acta Geneticae Medicae et Gemellologiae. 26 (1): 21–7. doi:10.1017/S0001566000010151. PMID 562050.
• Norcum MT (August 1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents". The Journal of Biological Chemistry. 266 (23): 15398–405. doi:10.1016/S0021-9258(18)98629-1. PMID 1651330.
• Wang HY, Pan F (1985). "Kinetic mechanism of arginyl-tRNA synthetase from human placenta". The International Journal of Biochemistry. 16 (12): 1379–85. doi:10.1016/0020-711X(84)90244-1. PMID 6530022.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Rho SB, Lee JS, Jeong EJ, Kim KS, Kim YG, Kim S (May 1998). "A multifunctional repeated motif is present in human bifunctional tRNA synthetase". The Journal of Biological Chemistry. 273 (18): 11267–73. doi:10.1074/jbc.273.18.11267. PMID 9556618.
• Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M (January 1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". Journal of Molecular Biology. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID 9878398.
• Park SG, Jung KH, Lee JS, Jo YJ, Motegi H, Kim S, Shiba K (June 1999). "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase". The Journal of Biological Chemistry. 274 (24): 16673–6. doi:10.1074/jbc.274.24.16673. PMID 10358004.
• Kim T, Park SG, Kim JE, Seol W, Ko YG, Kim S (July 2000). "Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex". The Journal of Biological Chemistry. 275 (28): 21768–72. doi:10.1074/jbc.M002404200. PMID 10801842.
• Kang J, Kim T, Ko YG, Rho SB, Park SG, Kim MJ, Kwon HJ, Kim S (October 2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". The Journal of Biological Chemistry. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. PMID 10913161.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
• Ling C, Yao YN, Zheng YG, Wei H, Wang L, Wu XF, Wang ED (October 2005). "The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex". The Journal of Biological Chemistry. 280 (41): 34755–63. doi:10.1074/jbc.M413511200. PMID 16055448.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Bottoni A, Vignali C, Piccin D, Tagliati F, Luchin A, Zatelli MC, Uberti EC (August 2007). "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines". Journal of Cellular Physiology. 212 (2): 293–7. doi:10.1002/jcp.21083. hdl:11392/521544. PMID 17443684. S2CID 27371659.

External links

• Overview of all the structural information available in the PDB for UniProt: P54136 (Human Arginine--tRNA ligase, cytoplasmic) at the PDBe-KB.