HARS

Not to be confused with Hamilton Anxiety Rating Scale.

HARS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1X59, 2LW7, 4G84, 4G85, 4PHC, 4X5O
Identifiers
Aliases	HARS1 , HRS, USH3B, CMT2W, histidyl-tRNA synthetase, HARS, histidyl-tRNA synthetase 1
External IDs	OMIM: 142810 MGI: 108087 HomoloGene: 1592 GeneCards: HARS1
Gene location (Human) Chr. Chromosome 5 (human) [1] Band 5q31.3 Start 140,673,035 bp [1] End 140,691,537 bp [1]
Gene location (Mouse) Chr. Chromosome 18 (mouse) [2] Band 18|18 B2 Start 36,766,528 bp [2] End 36,783,205 bp [2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • aminoacyl-tRNA ligase activity • nucleotide binding • ligase activity • ATP binding • histidine-tRNA ligase activity • identical protein binding Cellular component • cytoplasm • mitochondrion • cytosol Biological process • tRNA aminoacylation for protein translation • protein biosynthesis • mitochondrial translation • histidyl-tRNA aminoacylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3035	15115
Ensembl	ENSG00000170445	ENSMUSG00000001380
UniProt	P12081	Q61035
RefSeq (mRNA)	NM_002109 NM_001258040 NM_001258041 NM_001258042 NM_001289092 NM_001289093 NM_001289094	NM_008214
RefSeq (protein)	NP_001244969 NP_001244970 NP_001244971 NP_001276021 NP_001276022 NP_001276023 NP_002100	NP_032240
Location (UCSC)	Chr 5: 140.67 – 140.69 Mb	Chr 18: 36.77 – 36.78 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Histidyl-tRNA synthetase (HARS) also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene. ^{[5] [6]}

Function

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. ^[7] The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. ^[5]

Clinical significance

The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis. ^[7]

Interactions

HARS has been shown to interact with EEF1B2 ^[8] and EEF1G. ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000170445 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000001380 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: HARS histidyl-tRNA synthetase".
6. Wasmuth JJ, Carlock LR (1986). "Chromosomal localization of human gene for histidyl-tRNA synthetase: clustering of genes encoding aminoacyl-tRNA synthetases on human chromosome 5". Somat. Cell Mol. Genet. 12 (5): 513–7. doi:10.1007/BF01539922. PMID   3464104. S2CID   28520231.
7. Freist W, Verhey JF, Rühlmann A, Gauss DH, Arnez JG (1999). "Histidyl-tRNA synthetase". Biol. Chem. 380 (6): 623–46. doi: 10.1515/BC.1999.079 . PMID   10430027.
8. Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys. Res. Commun. 291 (1): 158–64. doi:10.1006/bbrc.2002.6398. PMID   11829477.

Further reading

• Raben N, Borriello F, Amin J, Horwitz R, Fraser D, Plotz P (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.
• Shi MH, Tsui FW, Rubin LA (1991). "Cellular localization of the target structures recognized by the anti-Jo-1 antibody: immunofluorescence studies on cultured human myoblasts". J. Rheumatol. 18 (2): 252–8. PMID   2023220.
• Carlock LR, Skarecky D, Dana SL, Wasmuth JJ (1985). "Deletion mapping of human chromosome 5 using chromosome-specific DNA probes". Am. J. Hum. Genet. 37 (5): 839–52. PMC   1684692 . PMID   2996334.
• Wasmuth JJ, Carlock LR (1986). "Chromosomal localization of human gene for histidyl-tRNA synthetase: clustering of genes encoding aminoacyl-tRNA synthetases on human chromosome 5". Somat. Cell Mol. Genet. 12 (5): 513–7. doi:10.1007/BF01539922. PMID   3464104. S2CID   28520231.
• Tsui FW, Siminovitch L (1987). "Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase". Nucleic Acids Res. 15 (8): 3349–67. doi:10.1093/nar/15.8.3349. PMC   340734 . PMID   3554142.
• O'Hanlon TP, Raben N, Miller FW (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.
• Ogata K, Kurahashi A, Nishiyama C, Terao K (1994). "Presence of role of the 5SrRNA-L5 protein complex (5SRNP) in the threonyl- and histidyl-tRNA synthetase complex in rat liver cytosol". Biochim. Biophys. Acta. 1218 (3): 388–400. doi:10.1016/0167-4781(94)90192-9. PMID   8049265.
• 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.
• Tsui HW, Mok S, de Souza L, Martin A, Tsui FW (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.
• Vázquez-Abad D, Carson JH, Rothfield N (1996). "Localization of histidyl-tRNA synthetase (Jo-1) in human laryngeal epithelial carcinoma cell line (HEp-2 cells)". Cell Tissue Res. 286 (3): 487–91. doi:10.1007/s004410050718. PMID   8929351. S2CID   1552865.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (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.
• Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys. Res. Commun. 291 (1): 158–64. doi:10.1006/bbrc.2002.6398. PMID   11829477.
• O'Hanlon TP, Miller FW (2002). "Genomic organization, transcriptional mapping, and evolutionary implications of the human bi-directional histidyl-tRNA synthetase locus (HARS/HARSL)". Biochem. Biophys. Res. Commun. 294 (3): 609–14. doi:10.1016/S0006-291X(02)00525-9. PMID   12056811.
• Ascherman DP, Oriss TB, Oddis CV, Wright TM (2002). "Critical requirement for professional APCs in eliciting T cell responses to novel fragments of histidyl-tRNA synthetase (Jo-1) in Jo-1 antibody-positive polymyositis". J. Immunol. 169 (12): 7127–34. doi: 10.4049/jimmunol.169.12.7127 . PMID   12471150.
• Lu Q, Hope LW, Brasch M, Reinhard C, Cohen SN (2003). "TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation". Proc. Natl. Acad. Sci. U.S.A. 100 (13): 7626–31. Bibcode:2003PNAS..100.7626L. doi: 10.1073/pnas.0932599100 . PMC   164637 . PMID   12802020.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Levine SM, Raben N, Xie D, Askin FB, Tuder R, Mullins M, Rosen A, Casciola-Rosen LA (2007). "Novel conformation of histidyl-transfer RNA synthetase in the lung: the target tissue in Jo-1 autoantibody-associated myositis". Arthritis Rheum. 56 (8): 2729–39. doi: 10.1002/art.22790 . PMID   17665459.