EPRS

EPRS
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases EPRS, EARS, GLUPRORS, PARS, QARS, QPRS, PIG32, glutamyl-prolyl-tRNA synthetase
External IDs MGI: 97838 HomoloGene: 5870 GeneCards: EPRS
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

2058

107508

Ensembl

ENSG00000136628

ENSMUSG00000026615

UniProt

P07814

Q8CGC7

RefSeq (mRNA)

NM_004446

NM_029735

RefSeq (protein)

NP_004437.2

NP_084011.1

Location (UCSC) Chr 1: 219.97 – 220.05 Mb Chr 1: 185.36 – 185.43 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS gene.[3][4]

Gene

Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined.[4]

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.[4]

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.[5]

Interactions

EPRS has been shown to interact with POU2F1,[6] Heat shock protein 90kDa alpha (cytosolic), member A1[7] and IARS.[8]

References

  1. "Human PubMed Reference:".
  2. "Mouse PubMed Reference:".
  3. Fett R, Knippers R (February 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.
  4. 1 2 3 "Entrez Gene: EPRS glutamyl-prolyl-tRNA synthetase".
  5. Arif A, Jia J, Mukhopadhyay R, Willard B, Kinter M, Fox PL (July 2009). "Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity". Mol. Cell. 35 (2): 164–80. doi:10.1016/j.molcel.2009.05.028. PMC 2752289Freely accessible. PMID 19647514.
  6. Nie, J; Sakamoto S; Song D; Qu Z; Ota K; Taniguchi T (March 1998). "Interaction of Oct–1 and automodification domain of poly(ADP-ribose) synthetase". FEBS Lett. 424 (1–2): 27–32. doi:10.1016/S0014-5793(98)00131-8. PMID 9537509.
  7. Kang, J; Kim T; Ko Y G; Rho S B; Park S G; Kim M J; Kwon H J; Kim S (October 2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". J. Biol. Chem. UNITED STATES. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. ISSN 0021-9258. PMID 10913161.
  8. Rho, S B; Lee J S; Jeong E J; Kim K S; Kim Y G; Kim S (May 1998). "A multifunctional repeated motif is present in human bifunctional tRNA synthetase". J. Biol. Chem. UNITED STATES. 273 (18): 11267–73. doi:10.1074/jbc.273.18.11267. ISSN 0021-9258. PMID 9556618.

Further reading


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