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EPRS

From Wikipedia, the free encyclopedia
Protein-coding gene in humans
EPRS1
Available structures
PDB Ortholog search: PDBe RCSB
List of PDB id codes

1FYJ, 4HVC, 4K86, 4K87, 4K88, 5A34, 5BMU, 5A1N, 5A5H

Identifiers
Aliases EPRS1 , 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
Gene location (Human)
Chromosome 1 (human)
Chr. Chromosome 1 (human) [1]
Band 1q41Start219,968,600 bp [1]
End220,046,530 bp [1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr. Chromosome 1 (mouse)[2]
Band 1|1 H5Start185,095,241 bp [2]
End185,160,557 bp [2]
RNA expression pattern
Bgee
Human Mouse (ortholog)
  • parotid gland

  • optic nerve

  • secondary oocyte

  • Achilles tendon

  • lateral nuclear group of thalamus

  • ventricular zone

  • tibia

  • islet of Langerhans

  • external globus pallidus

  • Brodmann area 23
  • otic placode

  • Rostral migratory stream

  • parotid gland

  • saccule

  • maxillary prominence

  • human fetus

  • mandibular prominence

  • tail of embryo

  • genital tubercle

  • otic vesicle
More reference expression data
BioGPS
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2058

107508

Ensembl

ENSG00000136628

ENSMUSG00000026615

UniProt

P07814

Q8CGC7

RefSeq (mRNA)

NM_004446

NM_029735
NM_001357474

RefSeq (protein)

NP_004437

NP_084011
NP_001344403

Location (UCSC)Chr 1: 219.97 – 220.05 Mb Chr 1: 185.1 – 185.16 Mb
PubMed search[3] [4]
Wikidata

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

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]

EPRS1 acts, in human cells, as a proviral factor in mammarenaviruses infection, including LCMV, JUNV, and LASV, and its inhibition using halofuginon compound, a prolyl domain inhibitor, completely abolishes the viral infection by interrupting viral assembly and budding. [8]

Interactions

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EPRS has been shown to interact with POU2F1,[9] Heat shock protein 90kDa alpha (cytosolic), member A1 [10] and IARS.[11]

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年05月02日8. PMC 2752289 . PMID 19647514.
  8. ^ Witwit H, Ibanez P, Zhou R, Jackson N, Escobedo R, Cubitt B, Khafaji R, Sattler RY, Martinez-Sobrido L, de la Torre JC (2026年02月04日). "Prolyl tRNA Synthetase Is Required for Mammarenavirus Multiplication". Viruses. 18 (2): 202. doi:10.3390/v18020202 . ISSN 1999-4915.
  9. ^ 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. Bibcode:1998FEBSL.424...27N. doi:10.1016/S0014-5793(98)00131-8 . PMID 9537509. S2CID 872132.
  10. ^ 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.
  11. ^ 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

[edit ]
PDB gallery


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