Bifunctional aminoacyl-tRNA synthetase is an
enzyme that in humans is encoded by the EPRSgene.[5][6]
Gene
Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined.[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 multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species.[6]
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.[7]
Kunze N, Bittler E, Fett R, et al. (1990). "The human QARS locus: assignment of the human gene for glutaminyl-tRNA synthetase to chromosome 1q32-42". Hum. Genet. 85 (5): 527–30.
doi:
10.1007/BF00194231.
PMID2227938.
S2CID27487450.
Kaiser E, Hu B, Becher S, et al. (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): 280–90.
doi:
10.1006/geno.1994.1059.
PMID8188258.
Quevillon S, Robinson JC, Berthonneau E, et al. (1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". J. Mol. Biol. 285 (1): 183–95.
doi:
10.1006/jmbi.1998.2316.
PMID9878398.
Jeong EJ, Hwang GS, Kim KH, et al. (2001). "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): 15775–82.
doi:
10.1021/bi001393h.
PMID11123902.
S2CID25514243.
Sang Lee J, Gyu Park S, Park H, et al. (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.
PMID11829477.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105.
doi:
10.1038/ncb1086.
PMID14743216.
S2CID11683986.
Kato T, Daigo Y, Hayama S, et al. (2005). "A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis". Cancer Res. 65 (13): 5638–46.
doi:
10.1158/0008-5472.CAN-05-0600.
PMID15994936.
Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92.
doi:
10.1038/nbt1240.
PMID16964243.
S2CID14294292.
Bifunctional aminoacyl-tRNA synthetase is an
enzyme that in humans is encoded by the EPRSgene.[5][6]
Gene
Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined.[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 multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species.[6]
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.[7]
Kunze N, Bittler E, Fett R, et al. (1990). "The human QARS locus: assignment of the human gene for glutaminyl-tRNA synthetase to chromosome 1q32-42". Hum. Genet. 85 (5): 527–30.
doi:
10.1007/BF00194231.
PMID2227938.
S2CID27487450.
Kaiser E, Hu B, Becher S, et al. (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): 280–90.
doi:
10.1006/geno.1994.1059.
PMID8188258.
Quevillon S, Robinson JC, Berthonneau E, et al. (1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". J. Mol. Biol. 285 (1): 183–95.
doi:
10.1006/jmbi.1998.2316.
PMID9878398.
Jeong EJ, Hwang GS, Kim KH, et al. (2001). "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): 15775–82.
doi:
10.1021/bi001393h.
PMID11123902.
S2CID25514243.
Sang Lee J, Gyu Park S, Park H, et al. (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.
PMID11829477.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105.
doi:
10.1038/ncb1086.
PMID14743216.
S2CID11683986.
Kato T, Daigo Y, Hayama S, et al. (2005). "A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis". Cancer Res. 65 (13): 5638–46.
doi:
10.1158/0008-5472.CAN-05-0600.
PMID15994936.
Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92.
doi:
10.1038/nbt1240.
PMID16964243.
S2CID14294292.