EPRS

EPRS1
Identifiers
Aliases	EPRS1, EARS, GLUPRORS, PARS, QARS, QPRS, PIG32, glutamyl-prolyl-tRNA synthetase, HLD15, glutamyl-prolyl-tRNA synthetase 1, EPRS
External IDs	OMIM: 138295; MGI: 97838; GeneCards: EPRS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1FYJ, 4HVC, 4K86, 4K87, 4K88, 5A34, 5BMU, 5A1N, 5A5H
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 6.1.1.15 ↗ ↗ ↗ ↗ 6.1.1.17 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 1 (human) Band 1q41 Start 219,968,600 bp End 220,046,530 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1|1 H5 Start 185,095,241 bp End 185,160,557 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in parotid gland optic nerve secondary oocyte Achilles tendon lateral nuclear group of thalamus ventricular zone tibia islet of Langerhans external globus pallidus Brodmann area 23 Top expressed in otic placode Rostral migratory stream parotid gland saccule maxillary prominence human fetus mandibular prominence tail of embryo genital tubercle otic vesicle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding protein binding RNA stem-loop binding ATP binding catalytic activity ligase activity aminoacyl-tRNA ligase activity GTPase binding RNA binding glutamate-tRNA ligase activity proline-tRNA ligase activity zinc ion binding protein homodimerization activity metal ion binding identical protein binding Cellular component membrane GAIT complex cytoplasm aminoacyl-tRNA synthetase multienzyme complex cytosol plasma membrane ribonucleoprotein complex Biological process regulation of translation tRNA aminoacylation metabolism protein biosynthesis tRNA aminoacylation for protein translation negative regulation of translation cellular response to interferon-gamma glutamyl-tRNA aminoacylation prolyl-tRNA aminoacylation cellular response to insulin stimulus long-chain fatty acid import into cell protein-containing complex assembly regulation of long-chain fatty acid import into cell Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 2058 107508 Ensembl ENSG00000136628 ENSMUSG00000026615 UniProt P07814 Q8CGC7 RefSeq (mRNA) NM_004446 NM_029735 NM_001357474 RefSeq (protein) NP_004437 NP_084011 NP_001344403 Location (UCSC) Chr 1: 219.97 – 220.05 Mb Chr 1: 185.1 – 185.16 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Not to be confused with European Parliamentary Research Service.

Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS1 gene (previously EPRS).

Gene

Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined.

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 multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species.

Phosphorylation of EPRS is reported to be essential for the formation of GAIT (Gamma-interferon Activated Inhibitor of Translation) complex that regulates the translation of multiple genes in monocytes and macrophages.

EPRS1 acts, in human cells, as a proviral factor in mammarenaviruses infection, including LCMV, JUNV, and LASV, and its inhibition using halofuginon compound, a prolyl domain inhibitor, completely abolishes the viral infection by interrupting viral assembly and budding.

Interactions

EPRS has been shown to interact with POU2F1, Heat shock protein 90kDa alpha (cytosolic), member A1 and IARS.

Further reading

• Kaiser E, Eberhard D, Knippers R (1992). "Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase". Journal of Molecular Evolution. 34 (1): 45–53. Bibcode:1992JMolE..34...45K. doi:10.1007/BF00163851. PMID 1556743. S2CID 6021527.
• 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): 15398–15405. doi:10.1016/S0021-9258(18)98629-1. PMID 1651330.
• Cerini C, Kerjan P, Astier M, Gratecos D, Mirande M, Sémériva M (December 1991). "A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase". The EMBO Journal. 10 (13): 4267–4277. doi:10.1002/j.1460-2075.1991.tb05005.x. PMC 453179. PMID 1756734.
• Kunze N, Bittler E, Fett R, Schray B, Hameister H, Wiedorn KH, et al. (October 1990). "The human QARS locus: assignment of the human gene for glutaminyl-tRNA synthetase to chromosome 1q32-42". Human Genetics. 85 (5): 527–530. doi:10.1007/BF00194231. PMID 2227938. S2CID 27487450.
• Thömmes P, Fett R, Schray B, Kunze N, Knippers R (June 1988). "The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes". Nucleic Acids Research. 16 (12): 5391–5406. doi:10.1093/nar/16.12.5391. PMC 336774. PMID 3290852.
• Kaiser E, Hu B, Becher S, Eberhard D, Schray B, Baack M, et al. (January 1994). "The human EPRS locus (formerly the QARS locus): a gene encoding a class I and a class II aminoacyl-tRNA synthetase". Genomics. 19 (2): 280–290. doi:10.1006/geno.1994.1059. PMID 8188258.
• Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, et al. (September 1996). "Generation and analysis of 280,000 human expressed sequence tags". Genome Research. 6 (9): 807–828. doi:10.1101/gr.6.9.807. PMID 8889549.
• 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): 183–195. doi:10.1006/jmbi.1998.2316. PMID 9878398.
• Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS (December 2000). "Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats". Biochemistry. 39 (51): 15775–15782. doi:10.1021/bi001393h. PMID 11123902. S2CID 25514243.
• Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (February 2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochemical and Biophysical Research Communications. 291 (1): 158–164. Bibcode:2002BBRC..291..158S. doi:10.1006/bbrc.2002.6398. PMID 11829477.
• Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, et al. (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, et al. (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–12135. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Sampath P, Mazumder B, Seshadri V, Gerber CA, Chavatte L, Kinter M, et al. (October 2004). "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation". Cell. 119 (2): 195–208. doi:10.1016/j.cell.2004.09.030. PMID 15479637. S2CID 18944876.
• Kato T, Daigo Y, Hayama S, Ishikawa N, Yamabuki T, Ito T, et al. (July 2005). "A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis". Cancer Research. 65 (13): 5638–5646. doi:10.1158/0008-5472.CAN-05-0600. PMID 15994936.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–1292. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (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.