SARS (gene)

Seryl-tRNA synthetase
Identifiers
Symbols	SARS; FLJ36399; SERRS; SERS
External IDs	OMIM: 607529 MGI: 102809 HomoloGene: 4751 GeneCards: SARS Gene
EC number	6.1.1.11
Gene Ontology Molecular function • nucleotide binding • RNA binding • serine-tRNA ligase activity • protein binding • ATP binding • ligase activity Cellular component • cytoplasm • mitochondrion • cytosol Biological process • translation • tRNA aminoacylation for protein translation • seryl-tRNA aminoacylation • tRNA processing • gene expression Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6301	20226
Ensembl	ENSG00000031698	ENSMUSG00000068739
UniProt	P49591	Q3U6F6
RefSeq (mRNA)	NM_006513.3	NM_011319
RefSeq (protein)	NP_006504	NP_035449
Location (UCSC)	Chr 1: 109.76 – 109.78 Mb	Chr 3: 108.23 – 108.25 Mb
PubMed search	[1]	[2]

Seryl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the SARS gene.

This gene belongs to the class II amino-acyl tRNA family. The encoded enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts.

Further reading

• Härtlein M, Cusack S (1995). "Structure, function and evolution of seryl-tRNA synthetases: implications for the evolution of aminoacyl-tRNA synthetases and the genetic code". J. Mol. Evol. 40 (5): 519–30. doi:10.1007/BF00166620. PMID 7540217. 
• Maruyama K, Sugano S (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. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al (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. 
• Heckl M, Busch K, Gross HJ (1998). "Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA synthetase: contribution of tRNA domains to serylation and tertiary structure". FEBS Lett. 427 (3): 315–9. doi:10.1016/S0014-5793(98)00435-9. PMID 9637248. 
• Shah ZH, Toompuu M, Hakkinen T et al (2001). "Novel coding-region polymorphisms in mitochondrial seryl-tRNA synthetase (SARSM) and mitoribosomal protein S12 (RPMS12) genes in DFNA4 autosomal dominant deafness families". Hum. Mutat. 17 (5): 433–4. doi:10.1002/humu.1123. PMID 11317363. 
• Shimada N, Suzuki T, Watanabe K (2002). "Dual mode recognition of two isoacceptor tRNAs by mammalian mitochondrial seryl-tRNA synthetase". J. Biol. Chem. 276 (50): 46770–8. doi:10.1074/jbc.M105150200. PMID 11577083. 
• Rigler R, Cronvall E, Hirsch R et al (1970). "Interactions of seryl-tRNA synthetase with serine and phenylalanine specific tRNA". FEBS letters 11 (5): 320–323. doi:10.1016/0014-5793(70)80558-0. PMID 11945516. 
• Strausberg RL, Feingold EA, Grouse LH et al (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Ota T, Suzuki Y, Nishikawa T et al (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Gerhard DS, Wagner L, Feingold EA et al (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Ewing RM, Chu P, Elisma F et al (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.