node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AARS1 | EPRS1 | 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; 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. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it [...] | 0.976 |
AARS1 | IARS1 | 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. | 0.980 |
AARS1 | LARS1 | 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. | 0.968 |
AARS1 | LARS2 | ENSP00000261772 | ENSP00000498867 | 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. | Probable leucine--tRNA ligase, mitochondrial; leucyl-tRNA synthetase 2, mitochondrial. | 0.929 |
AARS1 | NARS1 | ENSP00000261772 | ENSP00000256854 | 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. | 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 induced migration of CCR3-expressing cells. | 0.947 |
AARS1 | SARS1 | ENSP00000261772 | ENSP00000358939 | 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. | Serine--tRNA ligase, cytoplasmic; Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser). Is probably also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). In the nucleus, binds to the VEGFA core promoter and prevents MYC binding and transcriptional activation by MYC. Recruits SIRT2 to the VEGFA promoter, promoting deacetylation of histone H4 at 'Lys-16' (H4K16). [...] | 0.881 |
AARS1 | TARS1 | 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 1, cytoplasmic; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage (By similarity); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.929 |
AARS1 | TARS3 | ENSP00000261772 | ENSP00000338093 | 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 2, cytoplasmic; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post- transfer stage; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.955 |
AARS1 | YARS1 | 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, 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. | 0.996 |
EIF4E2 | TARS1 | ENSP00000258416 | ENSP00000387710 | Eukaryotic translation initiation factor 4E type 2; Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation. In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity). | Threonine--tRNA ligase 1, cytoplasmic; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage (By similarity); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.932 |
EIF4E2 | TARS3 | ENSP00000258416 | ENSP00000338093 | Eukaryotic translation initiation factor 4E type 2; Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation. In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity). | Threonine--tRNA ligase 2, cytoplasmic; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post- transfer stage; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.601 |
EPRS1 | AARS1 | ENSP00000355890 | ENSP00000261772 | 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. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it [...] | 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. | 0.976 |
EPRS1 | IARS1 | ENSP00000355890 | ENSP00000364794 | 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. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it [...] | 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. | 0.999 |
EPRS1 | LARS1 | ENSP00000355890 | ENSP00000377954 | 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. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it [...] | 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. | 0.999 |
EPRS1 | LARS2 | ENSP00000355890 | ENSP00000498867 | 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. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it [...] | Probable leucine--tRNA ligase, mitochondrial; leucyl-tRNA synthetase 2, mitochondrial. | 0.992 |
EPRS1 | NARS1 | ENSP00000355890 | ENSP00000256854 | 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. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it [...] | 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 induced migration of CCR3-expressing cells. | 0.998 |
EPRS1 | SARS1 | ENSP00000355890 | ENSP00000358939 | 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. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it [...] | Serine--tRNA ligase, cytoplasmic; Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser). Is probably also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). In the nucleus, binds to the VEGFA core promoter and prevents MYC binding and transcriptional activation by MYC. Recruits SIRT2 to the VEGFA promoter, promoting deacetylation of histone H4 at 'Lys-16' (H4K16). [...] | 0.860 |
EPRS1 | TARS1 | ENSP00000355890 | ENSP00000387710 | 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. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it [...] | Threonine--tRNA ligase 1, cytoplasmic; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage (By similarity); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.928 |
EPRS1 | TARS3 | ENSP00000355890 | ENSP00000338093 | 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. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it [...] | Threonine--tRNA ligase 2, cytoplasmic; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post- transfer stage; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.924 |
EPRS1 | YARS1 | ENSP00000355890 | ENSP00000362576 | 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. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it [...] | 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. | 0.999 |