node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AARS | AIMP1 | ENSP00000261772 | ENSP00000378191 | 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 | Aminoacyl tRNA synthase complex-interacting multifunctional protein 1; Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1 [...] | 0.722 |
AARS | AIMP2 | ENSP00000261772 | ENSP00000223029 | 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 | Aminoacyl tRNA synthase complex-interacting multifunctional protein 2; Required for assembly and stability of the aminoacyl- tRNA synthase complex. Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor | 0.665 |
AARS | DARS | ENSP00000261772 | ENSP00000264161 | 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 | Aspartate--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; Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily | 0.970 |
AARS | EEF1E1 | ENSP00000261772 | ENSP00000369038 | 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 | Eukaryotic translation elongation factor 1 epsilon-1; Positive modulator of ATM response to DNA damage | 0.583 |
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 | GARS | ENSP00000261772 | ENSP00000373918 | 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 | Glycine--tRNA ligase; Catalyzes the ligation of glycine to the 3’-end of its cognate tRNA. Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.994 |
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 | LARS | ENSP00000261772 | ENSP00000377954 | 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 | Leucine--tRNA ligase, cytoplasmic; Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two 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. Exhibits a post-transfer editing activity to hydrolyze mischarged tRNAs; Aminoacyl tRNA synthetases, Class I | 0.989 |
AARS | MARS | ENSP00000261772 | ENSP00000262027 | 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 | 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; Belongs to the class-I aminoacyl-tRNA synthetase family | 0.975 |
AARS | QARS | ENSP00000261772 | ENSP00000307567 | 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 | Glutamine--tRNA ligase; Glutamine--tRNA ligase. Plays a critical role in brain development; Belongs to the class-I aminoacyl-tRNA synthetase family | 0.983 |
AARS | RARS | ENSP00000261772 | ENSP00000231572 | 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 | Arginine--tRNA ligase, cytoplasmic; Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1; Aminoacyl tRNA synthetases, Class I | 0.748 |
AARS | UBA1 | ENSP00000261772 | ENSP00000338413 | 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 | Ubiquitin-like modifier-activating enzyme 1; Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin- proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Essential for the formation of radiation- induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites | 0.832 |
AIMP1 | AARS | ENSP00000378191 | ENSP00000261772 | Aminoacyl tRNA synthase complex-interacting multifunctional protein 1; Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1 [...] | 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 | 0.722 |
AIMP1 | AIMP2 | ENSP00000378191 | ENSP00000223029 | Aminoacyl tRNA synthase complex-interacting multifunctional protein 1; Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1 [...] | Aminoacyl tRNA synthase complex-interacting multifunctional protein 2; Required for assembly and stability of the aminoacyl- tRNA synthase complex. Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor | 0.999 |
AIMP1 | DARS | ENSP00000378191 | ENSP00000264161 | Aminoacyl tRNA synthase complex-interacting multifunctional protein 1; Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1 [...] | Aspartate--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; Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily | 0.996 |
AIMP1 | EEF1E1 | ENSP00000378191 | ENSP00000369038 | Aminoacyl tRNA synthase complex-interacting multifunctional protein 1; Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1 [...] | Eukaryotic translation elongation factor 1 epsilon-1; Positive modulator of ATM response to DNA damage | 0.999 |
AIMP1 | EPRS | ENSP00000378191 | ENSP00000355890 | Aminoacyl tRNA synthase complex-interacting multifunctional protein 1; Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1 [...] | 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 [...] | 0.999 |
AIMP1 | GARS | ENSP00000378191 | ENSP00000373918 | Aminoacyl tRNA synthase complex-interacting multifunctional protein 1; Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1 [...] | Glycine--tRNA ligase; Catalyzes the ligation of glycine to the 3’-end of its cognate tRNA. Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.720 |
AIMP1 | IARS | ENSP00000378191 | ENSP00000364794 | Aminoacyl tRNA synthase complex-interacting multifunctional protein 1; Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1 [...] | 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 | 0.998 |