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Literature summary extracted from

  • Lee, E.Y.; Lee, H.C.; Kim, H.K.; Jang, S.Y.; Park, S.J.; Kim, Y.H.; Kim, J.H.; Hwang, J.; Kim, J.H.; Kim, T.H.; Arif, A.; Kim, S.Y.; Choi, Y.K.; Lee, C.; Lee, C.H.; Jung, J.U.; Fox, P.L.; Kim, S.; Lee, J.S.; Kim, M.H.
    Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity (2016), Nat. Immunol., 17, 1252-1262 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.15 expressed in Escherichia coli BL21-CodonPlus (DE3) cells and HEK-293T cells Mus musculus
6.1.1.15 quantitative real-time PCR enzyme expression analysis, recombinant expression of tagged wild-type and mutant enzymes in Escherichia coli strain Escherichia coli BL21-CodonPlus (DE3)-RIPL Homo sapiens
6.1.1.15 quantitative real-time PCR enzyme expression analysis, recombinant expression of tagged wild-type and mutant enzymes in Escherichia coli strain Escherichia coli BL21-CodonPlus (DE3)-RIPL Mus musculus
6.1.1.17 quantitative real-time PCR enzyme expression analysis, recombinant expression of tagged wild-type and mutant enzymes in Escherichia coli strain Escherichia coli BL21-CodonPlus (DE3)-RIPL Homo sapiens
6.1.1.17 quantitative real-time PCR enzyme expression analysis, recombinant expression of tagged wild-type and mutant enzymes in Escherichia coli strain Escherichia coli BL21-CodonPlus (DE3)-RIPL Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.15 additional information siRNA-mediated enzyme knockout in HEK-293T cells. Cells in which EPRS is knocked down show considerable attenuation of the production of antiviral cytokines (IFN-beta and interleukin-6) following viral infection or treatment with the synthetic double-stranded RNA poly(I:C). Activation of the interferon-related signaling molecules IRF3 and STAT1 is significantly lower in cells in which EPRS is knocked down than in their EPRS-sufficient counterparts Homo sapiens
6.1.1.15 additional information siRNA-mediated enzyme knockout in RAW-264.7 cells. Activation of the interferon-related signaling molecules IRF3 and STAT1 is significantly lower in cells in which EPRS is knocked down than in their EPRS-sufficient counterparts . RAW-264.7 cells stably overexpressing EPRS show significantly less viral replication and more production of IFN-beta and interleukin-6 following infection with PR8 or VSV than those of their counterparts with basal expression of EPRS Mus musculus
6.1.1.15 R1152L catalytically inactive Mus musculus
6.1.1.15 R201L/R395L/S434A/K435L catalytic mutant Mus musculus
6.1.1.15 S886D phosphomimetic mutant Mus musculus
6.1.1.15 S886D/S990D phosphomimetic mutant Mus musculus
6.1.1.15 S886D/S999D phosphomimetic mutant Mus musculus
6.1.1.15 S990A phosphorylation-resistant mutant Mus musculus
6.1.1.15 S990A site-directed mutagenesis, the mutant is unable to rescue virus-infected cells Homo sapiens
6.1.1.15 S990A site-directed mutagenesis, the mutant is unable to rescue virus-infected cells Mus musculus
6.1.1.15 S990D phosphomimetic mutant Mus musculus
6.1.1.15 S990D site-directed mutagenesis, the mutation markedly inhibits viral replication in cells Homo sapiens
6.1.1.15 S990D site-directed mutagenesis, the mutation markedly inhibits viral replication in cells Mus musculus
6.1.1.15 S999D phosphomimetic mutant Mus musculus
6.1.1.17 additional information siRNA-mediated enzyme knockout in HEK-293T cells. Cells in which EPRS is knocked down show considerable attenuation of the production of antiviral cytokines (IFN-beta and interleukin-6) following viral infection or treatment with the synthetic double-stranded RNA poly(I:C). Activation of the interferon-related signaling molecules IRF3 and STAT1 is significantly lower in cells in which EPRS is knocked down than in their EPRS-sufficient counterparts Homo sapiens
6.1.1.17 additional information siRNA-mediated enzyme knockout in RAW-264.7 cells. Activation of the interferon-related signaling molecules IRF3 and STAT1 is significantly lower in cells in which EPRS is knocked down than in their EPRS-sufficient counterparts . RAW-264.7 cells stably overexpressing EPRS show significantly less viral replication and more production of IFN-beta and interleukin-6 following infection with PR8 or VSV than those of their counterparts with basal expression of EPRS Mus musculus
6.1.1.17 S990A site-directed mutagenesis, the mutant is unable to rescue virus-infected cells Homo sapiens
6.1.1.17 S990A site-directed mutagenesis, the mutant is unable to rescue virus-infected cells Mus musculus
6.1.1.17 S990D site-directed mutagenesis, the mutation markedly inhibits viral replication in cells Homo sapiens
6.1.1.17 S990D site-directed mutagenesis, the mutation markedly inhibits viral replication in cells Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.1.1.15 cytoplasm
-
 Homo sapiens 5737
-
6.1.1.15 cytoplasm
-
 Mus musculus 5737
-
6.1.1.17 cytoplasm
-
 Homo sapiens 5737
-
6.1.1.17 cytoplasm
-
 Mus musculus 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.15 Mg2+ required Homo sapiens
6.1.1.15 Mg2+ required Mus musculus
6.1.1.17 Mg2+ required Homo sapiens
6.1.1.17 Mg2+ required Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.15 ATP + L-glutamate + tRNAGlu Mus musculus
-
 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.15 ATP + L-glutamate + tRNAGlu Mus musculus C57BL/6
-
 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.15 ATP + L-proline + tRNAGlu Homo sapiens
-
 AMP + diphosphate + L-prolylyl-tRNAGlu
-
 ?
6.1.1.15 ATP + L-proline + tRNAGlu Mus musculus
-
 AMP + diphosphate + L-prolylyl-tRNAGlu
-
 ?
6.1.1.15 ATP + L-proline + tRNAGlu Mus musculus C57BL/6
-
 AMP + diphosphate + L-prolylyl-tRNAGlu
-
 ?
6.1.1.15 ATP + L-proline + tRNAPro Mus musculus
-
 AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
6.1.1.15 ATP + L-proline + tRNAPro Mus musculus C57BL/6
-
 AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu Homo sapiens
-
 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu Mus musculus
-
 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu Mus musculus C57BL/6
-
 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.15 Homo sapiens P07814
-
-
6.1.1.15 Mus musculus Q8CGC7
-
-
6.1.1.15 Mus musculus C57BL/6 Q8CGC7
-
-
6.1.1.17 Homo sapiens P07814
-
-
6.1.1.17 Mus musculus Q8CGC7
-
-
6.1.1.17 Mus musculus C57BL/6 Q8CGC7
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.1.1.15 phosphoprotein
-
 Mus musculus
6.1.1.15 phosphoprotein infection-specific phosphorylation of EPRS at a Ser induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity Homo sapiens
6.1.1.15 phosphoprotein infection-specific phosphorylation of EPRS at Ser990 induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity Mus musculus
6.1.1.17 phosphoprotein infection-specific phosphorylation of EPRS at a Ser induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity Homo sapiens
6.1.1.17 phosphoprotein infection-specific phosphorylation of EPRS at Ser990 induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity Mus musculus

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.15 glutathione Sepharose column chromatography Mus musculus
6.1.1.15 recombinant tagged wild-type and mutant enzymes from Escherichia coli strain Escherichia coli BL21-CodonPlus (DE3)-RIPL by affinity chromatography and gel filtration Homo sapiens
6.1.1.15 recombinant tagged wild-type and mutant enzymes from Escherichia coli strain Escherichia coli BL21-CodonPlus (DE3)-RIPL by affinity chromatography and gel filtration Mus musculus
6.1.1.17 recombinant tagged wild-type and mutant enzymes from Escherichia coli strain Escherichia coli BL21-CodonPlus (DE3)-RIPL by affinity chromatography and gel filtration Homo sapiens
6.1.1.17 recombinant tagged wild-type and mutant enzymes from Escherichia coli strain Escherichia coli BL21-CodonPlus (DE3)-RIPL by affinity chromatography and gel filtration Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.1.1.15 HEK-293T cell
-
 Homo sapiens
-
6.1.1.15 macrophage
-
 Homo sapiens
-
6.1.1.15 macrophage
-
 Mus musculus
-
6.1.1.15 RAW-264.7 cell
-
 Mus musculus
-
6.1.1.15 RAW264.7 cell
-
 Mus musculus
-
6.1.1.15 U-937 cell
-
 Homo sapiens
-
6.1.1.17 HEK-293T cell
-
 Homo sapiens
-
6.1.1.17 macrophage
-
 Homo sapiens
-
6.1.1.17 macrophage
-
 Mus musculus
-
6.1.1.17 RAW-264.7 cell
-
 Mus musculus
-
6.1.1.17 U-937 cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.15 ATP + L-glutamate + tRNAGlu
-
 Mus musculus AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.15 ATP + L-glutamate + tRNAGlu
-
 Mus musculus C57BL/6 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.15 ATP + L-proline + tRNAGlu
-
 Homo sapiens AMP + diphosphate + L-prolylyl-tRNAGlu
-
 ?
6.1.1.15 ATP + L-proline + tRNAGlu
-
 Mus musculus AMP + diphosphate + L-prolylyl-tRNAGlu
-
 ?
6.1.1.15 ATP + L-proline + tRNAGlu
-
 Mus musculus C57BL/6 AMP + diphosphate + L-prolylyl-tRNAGlu
-
 ?
6.1.1.15 ATP + L-proline + tRNAPro
-
 Mus musculus AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
6.1.1.15 ATP + L-proline + tRNAPro
-
 Mus musculus C57BL/6 AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Homo sapiens AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Mus musculus AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Mus musculus C57BL/6 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.15 More the enzyme is part of a multi-tRNA synthetase complex (MSC) Homo sapiens
6.1.1.15 More the enzyme is part of a multi-tRNA synthetase complex (MSC) Mus musculus
6.1.1.17 More the enzyme is part of a multi-tRNA synthetase complex (MSC) Homo sapiens
6.1.1.17 More the enzyme is part of a multi-tRNA synthetase complex (MSC) Mus musculus

Synonyms

EC Number Synonyms Comment Organism
6.1.1.15 bifunctional aminoacyl-tRNA synthetase UniProt Homo sapiens
6.1.1.15 bifunctional aminoacyl-tRNA synthetase UniProt Mus musculus
6.1.1.15 bifunctional glutamate/proline-tRNA ligase UniProt Homo sapiens
6.1.1.15 bifunctional glutamate/proline-tRNA ligase UniProt Mus musculus
6.1.1.15 EPRS
-
 Homo sapiens
6.1.1.15 EPRS
-
 Mus musculus
6.1.1.15 glutamyl-prolyl tRNA synthetase
-
 Homo sapiens
6.1.1.15 glutamyl-prolyl tRNA synthetase
-
 Mus musculus
6.1.1.17 bifunctional aminoacyl-tRNA synthetase UniProt Homo sapiens
6.1.1.17 bifunctional aminoacyl-tRNA synthetase UniProt Mus musculus
6.1.1.17 bifunctional glutamate/proline-tRNA ligase UniProt Homo sapiens
6.1.1.17 bifunctional glutamate/proline-tRNA ligase UniProt Mus musculus
6.1.1.17 EPRS
-
 Homo sapiens
6.1.1.17 EPRS
-
 Mus musculus
6.1.1.17 glutamyl-prolyl tRNA synthetase
-
 Homo sapiens
6.1.1.17 glutamyl-prolyl tRNA synthetase
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.15 37
-
 assay at Homo sapiens
6.1.1.15 37
-
 assay at Mus musculus
6.1.1.17 37
-
 assay at Homo sapiens
6.1.1.17 37
-
 assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.15 7.5
-
 assay at Homo sapiens
6.1.1.15 7.5
-
 assay at Mus musculus
6.1.1.17 7.5
-
 assay at Homo sapiens
6.1.1.17 7.5
-
 assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.15 ATP
-
 Homo sapiens
6.1.1.15 ATP
-
 Mus musculus
6.1.1.17 ATP
-
 Homo sapiens
6.1.1.17 ATP
-
 Mus musculus

Expression

EC Number Organism Comment Expression
6.1.1.15 Mus musculus both enzyme mRNA and protein are slightly upregulated following viral infection up
6.1.1.15 Homo sapiens requirement for sensing by the immune system in the induction of EPRS expression during infection with an RNA virus up
6.1.1.15 Mus musculus requirement for sensing by the immune system in the induction of EPRS expression during infection with an RNA virus, VSV Indiana strain up
6.1.1.17 Homo sapiens requirement for sensing by the immune system in the induction of EPRS expression during infection with an RNA virus up
6.1.1.17 Mus musculus requirement for sensing by the immune system in the induction of EPRS expression during infection with an RNA virus, VSV Indiana strain up

General Information

EC Number General Information Comment Organism
6.1.1.15 malfunction EPRS-haploid (Eprs+/-) mice show enhanced viremia and inflammation and delayed viral clearance Mus musculus
6.1.1.15 malfunction glutamyl-prolyl-tRNA synthetase-haploid (Eprs+/-) mice show enhanced viremia and inflammation and delayed viral clearance Mus musculus
6.1.1.15 metabolism under conditions of stress, several MSC components, including EPRS, methionyl-tRNA synthetase (MRS), lysyl-tRNA synthetase (KRS), AIMP1 and AIMP2, are released from the complex through post-translational modifications to exert activities during non-translational events such as inflammation, cell metabolism, angiogenesis, and tumorigenesis. Phosphorylation is the critical regulatory mechanism that determines the non-translational function of ARSs in cells, overview Homo sapiens
6.1.1.15 metabolism under conditions of stress, several MSC components, including EPRS, methionyl-tRNA synthetase (MRS), lysyl-tRNA synthetase (KRS), AIMP1 and AIMP2, are released from the complex through post-translational modifications to exert activities during non-translational events such as inflammation, cell metabolism, angiogenesis, and tumorigenesis. Phosphorylation is the critical regulatory mechanism that determines the non-translational function of ARSs in cells, overview Mus musculus
6.1.1.15 additional information the enzyme is part of a multi-tRNA synthetase complex (MSC) Homo sapiens
6.1.1.15 additional information the enzyme is part of a multi-tRNA synthetase complex (MSC) Mus musculus
6.1.1.15 physiological function the enzyme regulates immune responses to viral infection and is critical for antiviral immunity in vivo Mus musculus
6.1.1.15 physiological function the multi-tRNA synthetase complex (MSC) component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function following viral infection and exhibited potent antiviral activity. Infection-specific phosphorylation of EPRS at a Ser induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity. EPRS protects MAVS from PCBP2-mediated ubiquitination. The stimulus-inducible activation of MAVS by enzyme EPRS suggests an unexpected role for the MSC as a regulator of immune responses to viral infection. Phosphorylation of EPRS at a Ser is the driving force that leads to the antiviral roles of EPRS in regulating MAVS Homo sapiens
6.1.1.15 physiological function the multi-tRNA synthetase complex (MSC) component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function following viral infection and exhibited potent antiviral activity. Infection-specific phosphorylation of EPRS at Ser990 induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity. EPRS protects MAVS from PCBP2-mediated ubiquitination. The stimulus-inducible activation of MAVS by enzyme EPRS suggests an unexpected role for the MSC as a regulator of immune responses to viral infection. Phosphorylation of EPRS at Ser990 is the driving force that leads to the antiviral roles of EPRS in regulating MAVS Mus musculus
6.1.1.17 malfunction EPRS-haploid (Eprs+/-) mice show enhanced viremia and inflammation and delayed viral clearance Mus musculus
6.1.1.17 metabolism under conditions of stress, several MSC components, including EPRS, methionyl-tRNA synthetase (MRS), lysyl-tRNA synthetase (KRS), AIMP1 and AIMP2, are released from the complex through post-translational modifications to exert activities during non-translational events such as inflammation, cell metabolism, angiogenesis, and tumorigenesis. Phosphorylation is the critical regulatory mechanism that determines the non-translational function of ARSs in cells, overview Homo sapiens
6.1.1.17 metabolism under conditions of stress, several MSC components, including EPRS, methionyl-tRNA synthetase (MRS), lysyl-tRNA synthetase (KRS), AIMP1 and AIMP2, are released from the complex through post-translational modifications to exert activities during non-translational events such as inflammation, cell metabolism, angiogenesis, and tumorigenesis. Phosphorylation is the critical regulatory mechanism that determines the non-translational function of ARSs in cells, overview Mus musculus
6.1.1.17 additional information the enzyme is part of a multi-tRNA synthetase complex (MSC) Homo sapiens
6.1.1.17 additional information the enzyme is part of a multi-tRNA synthetase complex (MSC) Mus musculus
6.1.1.17 physiological function the multi-tRNA synthetase complex (MSC) component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function following viral infection and exhibited potent antiviral activity. Infection-specific phosphorylation of EPRS at a Ser induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity. EPRS protects MAVS from PCBP2-mediated ubiquitination. The stimulus-inducible activation of MAVS by enzyme EPRS suggests an unexpected role for the MSC as a regulator of immune responses to viral infection. Phosphorylation of EPRS at a Ser is the driving force that leads to the antiviral roles of EPRS in regulating MAVS Homo sapiens
6.1.1.17 physiological function the multi-tRNA synthetase complex (MSC) component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function following viral infection and exhibited potent antiviral activity. Infection-specific phosphorylation of EPRS at Ser990 induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity. EPRS protects MAVS from PCBP2-mediated ubiquitination. The stimulus-inducible activation of MAVS by enzyme EPRS suggests an unexpected role for the MSC as a regulator of immune responses to viral infection. Phosphorylation of EPRS at Ser990 is the driving force that leads to the antiviral roles of EPRS in regulating MAVS Mus musculus