HARS2

Histidyl-tRNA synthetase 2, mitochondrial
Identifiers
Symbols	HARS2 ; HARSL; HARSR; HO3; PRLTS2
External IDs	OMIM: 600783 MGI: 1918041 HomoloGene: 40819 GeneCards: HARS2 Gene
EC number	6.1.1.21
Gene ontology Molecular function • histidine-tRNA ligase activity • protein binding • ATP binding • protein homodimerization activity • poly(A) RNA binding Cellular component • cytoplasm • mitochondrion • mitochondrial matrix Biological process • translation • tRNA aminoacylation for protein translation • histidyl-tRNA aminoacylation • gene expression • mitochondrial translation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	23438	70791
Ensembl	ENSG00000112855	ENSMUSG00000019143
UniProt	P49590	Q99KK9
RefSeq (mRNA)	NM_001278731	NM_001305627
RefSeq (protein)	NP_001265660	NP_001292556
Location (UCSC)	Chr 5: 140.69 – 140.7 Mb	Chr 18: 36.78 – 36.79 Mb
PubMed search

Probable histidyl-tRNA synthetase, mitochondrial is an enzyme that in humans is encoded by the HARS2 gene.^[1][2]

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is an enzyme belonging to the class II family of aminoacyl-tRNA synthetases. Functioning in the synthesis of histidyl-transfer RNA, the enzyme plays an accessory role in the regulation of protein biosynthesis. The gene is located in a head-to-head orientation with HARS on chromosome five, where the homologous genes share a bidirectional promoter.^[2]

References

1. O'Hanlon TP, Raben N, Miller FW (Jun 1995). "A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS". Biochem Biophys Res Commun 210 (2): 556–66. doi:10.1006/bbrc.1995.1696. PMID 7755634.
2. "Entrez Gene: HARS2 histidyl-tRNA synthetase 2, mitochondrial (putative)".

Further reading

• Freist W, Verhey JF, Rühlmann A, et al. (1999). "Histidyl-tRNA synthetase.". Biol. Chem. 380 (6): 623–46. doi:10.1515/BC.1999.079. PMID 10430027.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• 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.
• 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.
• Lama J, Trono D (1998). "Human immunodeficiency virus type 1 matrix protein interacts with cellular protein HO3.". J. Virol. 72 (2): 1671–6. PMC 124654. PMID 9445076.
• Tsui HW, Mok S, de Souza L, et al. (1993). "Transcriptional analyses of the gene region that encodes human histidyl-tRNA synthetase: identification of a novel bidirectional regulatory element.". Gene 131 (2): 201–8. doi:10.1016/0378-1119(93)90294-D. PMID 8406012.
• Raben N, Borriello F, Amin J, et al. (1992). "Human histidyl-tRNA synthetase: recognition of amino acid signature regions in class 2a aminoacyl-tRNA synthetases.". Nucleic Acids Res. 20 (5): 1075–81. doi:10.1093/nar/20.5.1075. PMC 312093. PMID 1549469.