Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS gene.[5][6]

EPRS1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesEPRS1, EARS, GLUPRORS, PARS, QARS, QPRS, PIG32, glutamyl-prolyl-tRNA synthetase, HLD15, glutamyl-prolyl-tRNA synthetase 1, EPRS
External IDsOMIM: 138295; MGI: 97838; HomoloGene: 5870; GeneCards: EPRS1; OMA:EPRS1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004446

NM_029735
NM_001357474

RefSeq (protein)

NP_004437

NP_084011
NP_001344403

Location (UCSC)Chr 1: 219.97 – 220.05 MbChr 1: 185.1 – 185.16 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Gene

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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

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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]

Interactions

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EPRS has been shown to interact with POU2F1,[8] Heat shock protein 90kDa alpha (cytosolic), member A1[9] and IARS.[10]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000136628Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026615Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. doi:10.1016/S0021-9258(18)52315-2. PMID 1988429.
  6. ^ a b c "Entrez Gene: EPRS glutamyl-prolyl-tRNA synthetase".
  7. ^ 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.
  8. ^ 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. S2CID 872132.
  9. ^ 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. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. ISSN 0021-9258. PMID 10913161.
  10. ^ Rho SB, 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. 273 (18): 11267–73. doi:10.1074/jbc.273.18.11267. ISSN 0021-9258. PMID 9556618.

Further reading

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