EPRS

From Wikipedia, the free encyclopedia

Glutamyl-prolyl-tRNA synthetase

PDB rendering based on 1fyj.

Available structures: 1fyj

Identifiers

Symbol(s)

EPRS; DKFZp313B047; EARS; PARS; PIG32; QARS; QPRS

External IDs

OMIM: 138295 MGI: 97838 HomoloGene: 5870

Gene ontology
Molecular Function:	• nucleotide binding • glutamate-tRNA ligase activity • proline-tRNA ligase activity • ATP binding • ligase activity
Cellular Component:	• soluble fraction • cytoplasm
Biological Process:	• glutamyl-tRNA aminoacylation • prolyl-tRNA aminoacylation • protein complex assembly

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_004446 (mRNA)
NP_004437 (protein)

XM_001004369 (mRNA)
XP_001004369 (protein)

Location

Chr 1: 218.21 - 218.29 Mb

n/a

Pubmed search

[1]

[2]

Glutamyl-prolyl-tRNA synthetase, also known as EPRS, is a human gene.^[1]

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. Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined.^[1]

[edit] References

^ ^a ^b Entrez Gene: EPRS glutamyl-prolyl-tRNA synthetase.

[edit] Further reading

Kaiser E, Eberhard D, Knippers R (1992). "Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase.". J. Mol. Evol. 34 (1): 45–53. PMID 1556743.
Norcum MT (1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents.". J. Biol. Chem. 266 (23): 15398–405. PMID 1651330.
Cerini C, Kerjan P, Astier M, et al. (1992). "A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase.". EMBO J. 10 (13): 4267–77. PMID 1756734.
Fett R, Knippers R (1991). "The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors.". J. Biol. Chem. 266 (3): 1448–55. PMID 1988429.
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. PMID 2227938.
Thömmes P, Fett R, Schray B, et al. (1988). "The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes.". Nucleic Acids Res. 16 (12): 5391–406. PMID 3290852.
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. PMID 8188258.
Hillier LD, Lennon G, Becker M, et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags.". Genome Res. 6 (9): 807–28. PMID 8889549.
Rho SB, Lee JS, Jeong EJ, et al. (1998). "A multifunctional repeated motif is present in human bifunctional tRNA synthetase.". J. Biol. Chem. 273 (18): 11267–73. PMID 9556618.
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. PMID 9878398.
Kang J, Kim T, Ko YG, et al. (2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases.". J. Biol. Chem. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. PMID 10913161.
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. PMID 11123902.
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. PMID 11829477.
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. PMID 12477932.
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. PMID 14743216.
Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.
Sampath P, Mazumder B, Seshadri V, et al. (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.
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. PMID 15994936.
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. PMID 16964243.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.