| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AGO1 | Iru | FBpp0294043 | FBpp0081445 | Argonaute-1, isoform A; Argonaute-1 (AGO1) encodes an Argonaute/Piwi family protein, which interacts with microRNAs to form miRNA-induced silencing complexes (miRISCs). miRISCs are guided to target and repress mRNAs either by transcript destabilisation, translational inhibition, or both. | E3 ubiquitin-protein ligase Iruka; E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys- 48'- and/or 'Lys-63'-linked polyubiquitination of substrates. Recognizes miRNA-empty Ago1 and triggers its degradation via polyubiquitination independently of the Bag6 complex. By targeting miRNA-empty Ago1, eliminates dysfunctional Ago1 not able to bind miRNA and thereby plays a role in the quality control of miRNA-mediated silencing. | 0.659 |
| CG34401 | Iru | FBpp0423174 | FBpp0081445 | Uncharacterized protein, isoform C; Zinc ion binding. It is involved in the biological process described with: regulation of axon guidance. | E3 ubiquitin-protein ligase Iruka; E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys- 48'- and/or 'Lys-63'-linked polyubiquitination of substrates. Recognizes miRNA-empty Ago1 and triggers its degradation via polyubiquitination independently of the Bag6 complex. By targeting miRNA-empty Ago1, eliminates dysfunctional Ago1 not able to bind miRNA and thereby plays a role in the quality control of miRNA-mediated silencing. | 0.671 |
| CG7546 | CG8209 | FBpp0288465 | FBpp0076470 | Uncharacterized protein, isoform D; Enzyme binding; misfolded protein binding; polyubiquitin modification-dependent protein binding. It is involved in the biological process described with: negative regulation of apoptotic process; ubiquitin-dependent ERAD pathway. | GM09977p; Nucleic acid binding. | 0.943 |
| CG7546 | CG9853 | FBpp0288465 | FBpp0112104 | Uncharacterized protein, isoform D; Enzyme binding; misfolded protein binding; polyubiquitin modification-dependent protein binding. It is involved in the biological process described with: negative regulation of apoptotic process; ubiquitin-dependent ERAD pathway. | Golgi to ER traffic protein 4 homolog; May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane. | 0.984 |
| CG7546 | Iru | FBpp0288465 | FBpp0081445 | Uncharacterized protein, isoform D; Enzyme binding; misfolded protein binding; polyubiquitin modification-dependent protein binding. It is involved in the biological process described with: negative regulation of apoptotic process; ubiquitin-dependent ERAD pathway. | E3 ubiquitin-protein ligase Iruka; E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys- 48'- and/or 'Lys-63'-linked polyubiquitination of substrates. Recognizes miRNA-empty Ago1 and triggers its degradation via polyubiquitination independently of the Bag6 complex. By targeting miRNA-empty Ago1, eliminates dysfunctional Ago1 not able to bind miRNA and thereby plays a role in the quality control of miRNA-mediated silencing. | 0.948 |
| CG7546 | Ubi-p5E | FBpp0288465 | FBpp0311816 | Uncharacterized protein, isoform D; Enzyme binding; misfolded protein binding; polyubiquitin modification-dependent protein binding. It is involved in the biological process described with: negative regulation of apoptotic process; ubiquitin-dependent ERAD pathway. | Ubiquitin-5E, isoform A; Protein tag; ubiquitin protein ligase binding. It is involved in the biological process described with: ubiquitin-dependent protein catabolic process; protein ubiquitination; modification-dependent protein catabolic process; cellular protein modification process. | 0.506 |
| CG7546 | Ubi-p63E | FBpp0288465 | FBpp0073035 | Uncharacterized protein, isoform D; Enzyme binding; misfolded protein binding; polyubiquitin modification-dependent protein binding. It is involved in the biological process described with: negative regulation of apoptotic process; ubiquitin-dependent ERAD pathway. | Polyubiquitin; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradatio [...] | 0.517 |
| CG8209 | CG7546 | FBpp0076470 | FBpp0288465 | GM09977p; Nucleic acid binding. | Uncharacterized protein, isoform D; Enzyme binding; misfolded protein binding; polyubiquitin modification-dependent protein binding. It is involved in the biological process described with: negative regulation of apoptotic process; ubiquitin-dependent ERAD pathway. | 0.943 |
| CG8209 | Iru | FBpp0076470 | FBpp0081445 | GM09977p; Nucleic acid binding. | E3 ubiquitin-protein ligase Iruka; E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys- 48'- and/or 'Lys-63'-linked polyubiquitination of substrates. Recognizes miRNA-empty Ago1 and triggers its degradation via polyubiquitination independently of the Bag6 complex. By targeting miRNA-empty Ago1, eliminates dysfunctional Ago1 not able to bind miRNA and thereby plays a role in the quality control of miRNA-mediated silencing. | 0.576 |
| CG8209 | RpL40 | FBpp0076470 | FBpp0306837 | GM09977p; Nucleic acid binding. | Ubiquitin-60S ribosomal protein L40; [Ubiquitin]: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is invol [...] | 0.476 |
| CG8209 | RpS27A | FBpp0076470 | FBpp0079606 | GM09977p; Nucleic acid binding. | Ubiquitin-40S ribosomal protein S27a; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involve [...] | 0.619 |
| CG8209 | Ubi-p5E | FBpp0076470 | FBpp0311816 | GM09977p; Nucleic acid binding. | Ubiquitin-5E, isoform A; Protein tag; ubiquitin protein ligase binding. It is involved in the biological process described with: ubiquitin-dependent protein catabolic process; protein ubiquitination; modification-dependent protein catabolic process; cellular protein modification process. | 0.555 |
| CG8209 | Ubi-p63E | FBpp0076470 | FBpp0073035 | GM09977p; Nucleic acid binding. | Polyubiquitin; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradatio [...] | 0.572 |
| CG9853 | CG7546 | FBpp0112104 | FBpp0288465 | Golgi to ER traffic protein 4 homolog; May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane. | Uncharacterized protein, isoform D; Enzyme binding; misfolded protein binding; polyubiquitin modification-dependent protein binding. It is involved in the biological process described with: negative regulation of apoptotic process; ubiquitin-dependent ERAD pathway. | 0.984 |
| CG9853 | Iru | FBpp0112104 | FBpp0081445 | Golgi to ER traffic protein 4 homolog; May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane. | E3 ubiquitin-protein ligase Iruka; E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys- 48'- and/or 'Lys-63'-linked polyubiquitination of substrates. Recognizes miRNA-empty Ago1 and triggers its degradation via polyubiquitination independently of the Bag6 complex. By targeting miRNA-empty Ago1, eliminates dysfunctional Ago1 not able to bind miRNA and thereby plays a role in the quality control of miRNA-mediated silencing. | 0.659 |
| CG9853 | RpS27A | FBpp0112104 | FBpp0079606 | Golgi to ER traffic protein 4 homolog; May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane. | Ubiquitin-40S ribosomal protein S27a; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involve [...] | 0.483 |
| CG9853 | Ubi-p5E | FBpp0112104 | FBpp0311816 | Golgi to ER traffic protein 4 homolog; May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane. | Ubiquitin-5E, isoform A; Protein tag; ubiquitin protein ligase binding. It is involved in the biological process described with: ubiquitin-dependent protein catabolic process; protein ubiquitination; modification-dependent protein catabolic process; cellular protein modification process. | 0.483 |
| CG9853 | Ubi-p63E | FBpp0112104 | FBpp0073035 | Golgi to ER traffic protein 4 homolog; May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane. | Polyubiquitin; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradatio [...] | 0.484 |
| Iru | AGO1 | FBpp0081445 | FBpp0294043 | E3 ubiquitin-protein ligase Iruka; E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys- 48'- and/or 'Lys-63'-linked polyubiquitination of substrates. Recognizes miRNA-empty Ago1 and triggers its degradation via polyubiquitination independently of the Bag6 complex. By targeting miRNA-empty Ago1, eliminates dysfunctional Ago1 not able to bind miRNA and thereby plays a role in the quality control of miRNA-mediated silencing. | Argonaute-1, isoform A; Argonaute-1 (AGO1) encodes an Argonaute/Piwi family protein, which interacts with microRNAs to form miRNA-induced silencing complexes (miRISCs). miRISCs are guided to target and repress mRNAs either by transcript destabilisation, translational inhibition, or both. | 0.659 |
| Iru | CG34401 | FBpp0081445 | FBpp0423174 | E3 ubiquitin-protein ligase Iruka; E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys- 48'- and/or 'Lys-63'-linked polyubiquitination of substrates. Recognizes miRNA-empty Ago1 and triggers its degradation via polyubiquitination independently of the Bag6 complex. By targeting miRNA-empty Ago1, eliminates dysfunctional Ago1 not able to bind miRNA and thereby plays a role in the quality control of miRNA-mediated silencing. | Uncharacterized protein, isoform C; Zinc ion binding. It is involved in the biological process described with: regulation of axon guidance. | 0.671 |