EPRS

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 IDs	OMIM: 138295; MGI: 97838; HomoloGene: 5870; GeneCards: EPRS1; OMA:EPRS1 - orthologs
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; ; lateral nuclear group of thalamus; ; ventricular zone; ; tibia; ; islet of Langerhans; ; external globus pallidus; ; Brodmann area 23;
	Top expressed in
	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
	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

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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000136628 – Ensembl, May 2017
^ ^a ^b ^c 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. PMID 1988429.
^ ^a ^b ^c "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.
^ 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). UNITED STATES: 31682–8. doi:10.1074/jbc.M909965199. ISSN 0021-9258. PMID 10913161. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)CS1 maint: unflagged free DOI (link)
^ 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. 273 (18). UNITED STATES: 11267–73. doi:10.1074/jbc.273.18.11267. ISSN 0021-9258. PMID 9556618. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)CS1 maint: unflagged free DOI (link)

Gene

Function

Interactions

References

Further reading