EPRS

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Glutamyl-prolyl-tRNA synthetase
Protein EPRS PDB 1fyj.png
PDB rendering based on 1fyj.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols EPRS ; EARS; GLUPRORS; PARS; QARS; QPRS
External IDs OMIM138295 MGI97838 HomoloGene5870 ChEMBL: 3873 GeneCards: EPRS Gene
EC number 6.1.1.15, 6.1.1.17
RNA expression pattern
PBB GE EPRS 200843 s at tn.png
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 NP_084011
Location (UCSC) Chr 1:
220.14 – 220.22 Mb
Chr 1:
185.36 – 185.43 Mb
PubMed search [1] [2]

Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS gene.[1][2]

Gene[edit]

Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined.[2]

Function[edit]

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.[2]

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.[3]

Interactions[edit]

EPRS has been shown to interact with POU2F1,[4] Heat shock protein 90kDa alpha (cytosolic), member A1[5] and IARS.[6]

References[edit]

  1. ^ 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. 
  2. ^ a b c "Entrez Gene: EPRS glutamyl-prolyl-tRNA synthetase". 
  3. ^ 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 2752289. PMID 19647514. 
  4. ^ Nie, J; Sakamoto S; Song D; Qu Z; Ota K; Taniguchi T (March 1998). "Interaction of October–1 and automodification domain of poly(ADP-ribose) synthetase". FEBS Lett. (NETHERLANDS) 424 (1–2): 27–32. doi:10.1016/S0014-5793(98)00131-8. ISSN 0014-5793. PMID 9537509. 
  5. ^ 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. 
  6. ^ 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[edit]