| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Aars | Dars2 | ENSMUSP00000034441 | ENSMUSP00000041851 | 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. | Aspartate--tRNA ligase, mitochondrial. | 0.913 |
| Aars | Eprs | ENSMUSP00000034441 | ENSMUSP00000045841 | 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. | Bifunctional glutamate/proline--tRNA ligase; Multifunctional protein which is primarily part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that 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 (By similarity). The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex [...] | 0.980 |
| Aars | Gars | ENSMUSP00000034441 | ENSMUSP00000003572 | 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. | Glycine--tRNA ligase; Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis. | 0.955 |
| Aars | Hars | ENSMUSP00000034441 | ENSMUSP00000001416 | 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. | Histidine--tRNA ligase, cytoplasmic; Catalyzes the ATP-dependent ligation of histidine to the 3'- end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). Plays a role in axon guidance. Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.870 |
| Aars | Hars2 | ENSMUSP00000034441 | ENSMUSP00000117231 | 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. | Histidine--tRNA ligase, mitochondrial; Mitochondrial aminoacyl-tRNA synthetase that catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). | 0.840 |
| Aars | Kars | ENSMUSP00000034441 | ENSMUSP00000126268 | 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. | 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 [...] | 0.942 |
| Aars | Mars | ENSMUSP00000034441 | ENSMUSP00000130666 | 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. | Methionine--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. Plays a role in the synthesis of ribosomal RNA in the nucleolus; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.913 |
| Aars | Nars | ENSMUSP00000034441 | ENSMUSP00000157402 | 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. | Asparagine--tRNA ligase, cytoplasmic; Catalyzes the attachment of asparagine to tRNA(Asn) in a two- step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn). In addition to its essential role in protein synthesis, acts as a signaling molecule that induces immune response in a CCR3-dependent manner. | 0.924 |
| Aars | Wars | ENSMUSP00000034441 | ENSMUSP00000124625 | 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. | Tryptophan--tRNA ligase, cytoplasmic; T1-TrpRS has aminoacylation activity while T2-TrpRS lacks it. T1-TrpRS and T2-TrpRS possess angiostatic activity. 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 (By similarity). | 0.891 |
| Aars | Yars | ENSMUSP00000034441 | ENSMUSP00000101669 | 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. | Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed; 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. | 0.983 |
| Dars2 | Aars | ENSMUSP00000041851 | ENSMUSP00000034441 | Aspartate--tRNA ligase, mitochondrial. | 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. | 0.913 |
| Dars2 | Eprs | ENSMUSP00000041851 | ENSMUSP00000045841 | Aspartate--tRNA ligase, mitochondrial. | Bifunctional glutamate/proline--tRNA ligase; Multifunctional protein which is primarily part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that 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 (By similarity). The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex [...] | 0.972 |
| Dars2 | Gars | ENSMUSP00000041851 | ENSMUSP00000003572 | Aspartate--tRNA ligase, mitochondrial. | Glycine--tRNA ligase; Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis. | 0.564 |
| Dars2 | Hars | ENSMUSP00000041851 | ENSMUSP00000001416 | Aspartate--tRNA ligase, mitochondrial. | Histidine--tRNA ligase, cytoplasmic; Catalyzes the ATP-dependent ligation of histidine to the 3'- end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). Plays a role in axon guidance. Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.856 |
| Dars2 | Hars2 | ENSMUSP00000041851 | ENSMUSP00000117231 | Aspartate--tRNA ligase, mitochondrial. | Histidine--tRNA ligase, mitochondrial; Mitochondrial aminoacyl-tRNA synthetase that catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). | 0.858 |
| Dars2 | Kars | ENSMUSP00000041851 | ENSMUSP00000126268 | Aspartate--tRNA ligase, mitochondrial. | 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 [...] | 0.835 |
| Dars2 | Mars | ENSMUSP00000041851 | ENSMUSP00000130666 | Aspartate--tRNA ligase, mitochondrial. | Methionine--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. Plays a role in the synthesis of ribosomal RNA in the nucleolus; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.743 |
| Dars2 | Nars | ENSMUSP00000041851 | ENSMUSP00000157402 | Aspartate--tRNA ligase, mitochondrial. | Asparagine--tRNA ligase, cytoplasmic; Catalyzes the attachment of asparagine to tRNA(Asn) in a two- step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn). In addition to its essential role in protein synthesis, acts as a signaling molecule that induces immune response in a CCR3-dependent manner. | 0.455 |
| Dars2 | Wars | ENSMUSP00000041851 | ENSMUSP00000124625 | Aspartate--tRNA ligase, mitochondrial. | Tryptophan--tRNA ligase, cytoplasmic; T1-TrpRS has aminoacylation activity while T2-TrpRS lacks it. T1-TrpRS and T2-TrpRS possess angiostatic activity. 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 (By similarity). | 0.624 |
| Dars2 | Yars | ENSMUSP00000041851 | ENSMUSP00000101669 | Aspartate--tRNA ligase, mitochondrial. | Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed; 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. | 0.926 |