| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AARS | EPRS | ENSP00000261772 | ENSP00000355890 | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | 0.988 |
| AARS | FARS2 | ENSP00000261772 | ENSP00000316335 | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | Phenylalanine--tRNA ligase, mitochondrial; Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.875 |
| AARS | FARSA | ENSP00000261772 | ENSP00000320309 | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | phenylalanyl-tRNA synthetase alpha subunit; Aminoacyl tRNA synthetases, Class II | 0.751 |
| AARS | FARSB | ENSP00000261772 | ENSP00000281828 | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | phenylalanyl-tRNA synthetase beta subunit; Aminoacyl tRNA synthetases, Class II | 0.952 |
| AARS | FDXACB1 | ENSP00000261772 | ENSP00000260257 | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | Ferredoxin-fold anticodon-binding domain-containing protein 1; Ferredoxin-fold anticodon binding domain containing 1 | 0.423 |
| AARS | IARS | ENSP00000261772 | ENSP00000364794 | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | Isoleucine--tRNA ligase, cytoplasmic; Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction- the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA; Aminoacyl tRNA synthetases, Class I | 0.990 |
| AARS | KARS | ENSP00000261772 | ENSP00000325448 | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | Lysine--tRNA ligase; Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction- the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity; Belongs to the class-I [...] | 0.964 |
| AARS | TARS | ENSP00000261772 | ENSP00000387710 | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | Threonine--tRNA ligase, cytoplasmic; Aminoacyl tRNA synthetases, Class II | 0.923 |
| AARS | WARS | ENSP00000261772 | ENSP00000347495 | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | Tryptophan--tRNA ligase, cytoplasmic; Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression; Belongs to the class-I aminoacyl-tRNA synthetase family | 0.796 |
| AARS | YARS | ENSP00000261772 | ENSP00000362576 | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | Tyrosine--tRNA ligase, cytoplasmic; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family | 0.990 |
| EPRS | AARS | ENSP00000355890 | ENSP00000261772 | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | Alanine--tRNA ligase, cytoplasmic; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.988 |
| EPRS | FARS2 | ENSP00000355890 | ENSP00000316335 | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | Phenylalanine--tRNA ligase, mitochondrial; Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.741 |
| EPRS | FARSA | ENSP00000355890 | ENSP00000320309 | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | phenylalanyl-tRNA synthetase alpha subunit; Aminoacyl tRNA synthetases, Class II | 0.950 |
| EPRS | FARSB | ENSP00000355890 | ENSP00000281828 | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | phenylalanyl-tRNA synthetase beta subunit; Aminoacyl tRNA synthetases, Class II | 0.977 |
| EPRS | FDXACB1 | ENSP00000355890 | ENSP00000260257 | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | Ferredoxin-fold anticodon-binding domain-containing protein 1; Ferredoxin-fold anticodon binding domain containing 1 | 0.692 |
| EPRS | IARS | ENSP00000355890 | ENSP00000364794 | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | Isoleucine--tRNA ligase, cytoplasmic; Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction- the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA; Aminoacyl tRNA synthetases, Class I | 0.999 |
| EPRS | KARS | ENSP00000355890 | ENSP00000325448 | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | Lysine--tRNA ligase; Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction- the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity; Belongs to the class-I [...] | 0.999 |
| EPRS | TARS | ENSP00000355890 | ENSP00000387710 | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | Threonine--tRNA ligase, cytoplasmic; Aminoacyl tRNA synthetases, Class II | 0.954 |
| EPRS | WARS | ENSP00000355890 | ENSP00000347495 | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | Tryptophan--tRNA ligase, cytoplasmic; Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression; Belongs to the class-I aminoacyl-tRNA synthetase family | 0.676 |
| EPRS | YARS | ENSP00000355890 | ENSP00000362576 | Bifunctional glutamate/proline--tRNA ligase; Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction- the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript- selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase co [...] | Tyrosine--tRNA ligase, cytoplasmic; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family | 0.998 |
