EPRS

EPRS1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1FYJ, 4HVC, 4K86, 4K87, 4K88, 5A34, 5BMU, 5A1N, 5A5H Contents Gene ; Function ; Interactions ; References ; Further reading ;
Identifiers
Aliases	EPRS1 , EARS, GLUPRORS, PARS, QARS, QPRS, PIG32, glutamyl-prolyl-tRNA synthetase, HLD15, glutamyl-prolyl-tRNA synthetase 1, EPRS
External IDs	OMIM: 138295 MGI: 97838 HomoloGene: 5870 GeneCards: EPRS1
Gene location (Human)
Chr.	Chromosome 1 (human)
End	220,046,530 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	185,160,557 bp
RNA expression pattern
	Top expressed in
	parotid gland; ; optic nerve; ; secondary oocyte; ; Achilles tendon; ; tibia; ; islet of Langerhans; ; external globus pallidus; ; Brodmann area 23; ; internal globus pallidus; ; middle temporal gyrus;
	Top expressed in
	otic placode; ; parotid gland; ; saccule; ; maxillary prominence; ; lacrimal gland; ; primitive streak; ; intercostal muscle; ; somite; ; extensor digitorum longus muscle; ; hair follicle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	nucleotide binding ; protein binding ; RNA stem-loop binding ; ATP binding ; catalytic activity ; ligase activity ; aminoacyl-tRNA ligase activity ; GTPase binding ; RNA binding ; glutamate-tRNA ligase activity ; proline-tRNA ligase activity ; zinc ion binding ; protein homodimerization activity ; metal ion binding ; identical protein binding ;
Cellular component	membrane ; GAIT complex ; cytoplasm ; aminoacyl-tRNA synthetase multienzyme complex ; cytosol ; plasma membrane ; ribonucleoprotein complex ;
Biological process	regulation of translation ; tRNA aminoacylation ; metabolism ; protein biosynthesis ; tRNA aminoacylation for protein translation ; negative regulation of translation ; cellular response to interferon-gamma ; glutamyl-tRNA aminoacylation ; prolyl-tRNA aminoacylation ; cellular response to insulin stimulus ; long-chain fatty acid import into cell ; protein-containing complex assembly ; regulation of long-chain fatty acid import into cell ;
	Sources:Amigo / QuickGO
Orthologs
	2058
	107508
	ENSG00000136628
	ENSMUSG00000026615
	P07814
	Q8CGC7
	NM_004446
	NM_029735 ; NM_001357474
	NP_004437
	NP_084011 ; NP_001344403
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 28, 2023

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

Gene

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

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

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

Related Research Articles

Elongation factor 1-delta is a protein that in humans is encoded by the EEF1D gene.

Glycine—tRNA ligase also known as glycyl–tRNA synthetase is an enzyme that in humans is encoded by the GARS1 gene.

Tyrosine—tRNA ligase, also known as tyrosyl-tRNA synthetase is an enzyme that is encoded by the gene YARS. Tyrosine—tRNA ligase catalyzes the chemical reaction

Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 is a protein that in humans is encoded by the AIMP1 gene.

Elongation factor 1-gamma is a protein that in humans is encoded by the EEF1G gene.

Tyrosyl-tRNA synthetase, cytoplasmic, also known as Tyrosine-tRNA ligase, is an enzyme that in humans is encoded by the YARS gene.

Histidyl-tRNA synthetase (HARS) also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene.

Arginyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the RARS gene.

Aspartyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the DARS gene.

<span class="mw-page-title-main">Multisynthetase complex auxiliary component p38</span> Protein-coding gene in the species Homo sapiens

Aminoacyl tRNA synthetase complex-interacting multifunctional protein 2 is an enzyme that in humans is encoded by the AIMP2 gene.

Leucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the LARS gene.

Glutaminyl-tRNA synthetase is an enzyme that in humans is encoded by the QARS gene.

Methionyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the MARS gene.

Threonyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the TARS gene.

Isoleucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the IARS1 gene.

Eukaryotic translation elongation factor 1 epsilon-1 is a protein that in humans is encoded by the EEF1E1 gene.

Probable histidyl-tRNA synthetase, mitochondrial is an enzyme that in humans is encoded by the HARS2 gene.

In molecular biology, the protein domain WHEP-TRS refers to helix-turn-helix domains. They are found in variable numbers in glutamyl-prolyl tRNA synthetase (EPRS). This protein domain has an important function in protein–protein interactions between synthetases. WHEP domains exhibit high-affinity interactions with tRNA, indicating a putative evolutionary relationship to facilitate tRNA binding to fused synthetases, thereby enhancing catalytic efficiency.

Karin Musier-Forsyth, an American biochemist, is an Ohio Eminent Scholar on the faculty of the Department of Chemistry & Biochemistry at Ohio State University. Musier-Forsyth's research involves biochemical, biophysical and cell-based approaches to understand the interactions of proteins and RNAs involved in protein synthesis and viral replication, especially in HIV.

Xiang-Lei Yang (杨湘磊) is a Chinese-born American molecular biologist. She is a professor at The Scripps Research Institute, located in La Jolla, California. Her work has contributed to the establishment of physiological importance of aminoacyl-tRNA synthetases beyond their classical role in supporting mRNA translation and their disordered processes that contribute to disease. She founded the Translation Machinery in Health and Disease Gordon Research Conference, an ongoing biannual international conference since 2015. She helped co-found aTyr Pharma, a Nasdaq-listed biotechnology company.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000136628 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026615 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
1 2 3 "Entrez Gene: EPRS glutamyl-prolyl-tRNA synthetase".
↑ 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.
↑ 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.
↑ 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.
↑ 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.

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. Bibcode:1992JMolE..34...45K. doi:10.1007/BF00163851. PMID 1556743. S2CID 6021527.
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. doi: 10.1016/S0021-9258(18)98629-1 . 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. doi:10.1002/j.1460-2075.1991.tb05005.x. PMC 453179 . PMID 1756734.
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. doi:10.1007/BF00194231. PMID 2227938. S2CID 27487450.
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. doi:10.1093/nar/16.12.5391. PMC 336774 . 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. doi: 10.1101/gr.6.9.807 . 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. doi: 10.1074/jbc.273.18.11267 . 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. doi:10.1021/bi001393h. PMID 11123902. S2CID 25514243.
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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . 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. S2CID 11683986.
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. Bibcode:2004PNAS..10112130B. doi: 10.1073/pnas.0404720101 . PMC 514446 . 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. S2CID 18944876.
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. S2CID 14294292.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948 . PMID 17353931.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000136628 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026615 - Ensembl, 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.

[pmid1988429-5] 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.

[entrez-6] 1 2 3 "Entrez Gene: EPRS glutamyl-prolyl-tRNA synthetase".

[pmid19647514-7] 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.

[pmid9537509-8] 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.

[pmid10913161-9] 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.

[pmid9556618-10] 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.

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