node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
C52E12.1 | ubr-4 | C52E12.1.1 | C44E4.1d.1 | RING-type domain-containing protein. | UBR-type domain-containing protein. | 0.676 |
C52E12.1 | ubr-5 | C52E12.1.1 | F36A2.13.1 | RING-type domain-containing protein. | UBR E3 ubiquitin ligase homolog. | 0.489 |
T04C4.1 | ubr-4 | T04C4.1a.1 | C44E4.1d.1 | Uncharacterized protein. | UBR-type domain-containing protein. | 0.640 |
ZK652.6 | ubr-4 | ZK652.6a.1 | C44E4.1d.1 | Uncharacterized protein ZK652.6. | UBR-type domain-containing protein. | 0.928 |
ate-1 | ubr-1 | K07A1.9a.1 | C32E8.11.1 | Arginyl-tRNA--protein transferase 1; Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Belongs to the R-transferase family. | E3 ubiquitin-protein ligase ubr-1; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N- end rule, leading to their ubiquitination and subsequent degradation (By similarity). In complex with ced-3, required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 to regulate seam cell fate patterning during larval development. Negatively regulates glutamate metabolism through the aspartate aminotrans [...] | 0.754 |
ate-1 | ubr-4 | K07A1.9a.1 | C44E4.1d.1 | Arginyl-tRNA--protein transferase 1; Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Belongs to the R-transferase family. | UBR-type domain-containing protein. | 0.836 |
ate-1 | ubr-5 | K07A1.9a.1 | F36A2.13.1 | Arginyl-tRNA--protein transferase 1; Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Belongs to the R-transferase family. | UBR E3 ubiquitin ligase homolog. | 0.784 |
eel-1 | hecd-1 | Y67D8C.5h.1 | C34D4.14f.1 | Enhancer of EfL-1 mutant phenotype. | E3 ubiquitin-protein ligase hecd-1; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Involved in the ubiquitination and proteasomal-mediated degradation of cytoplasmic and mitochondrial proteins. Positively regulates lin-12 activity in the anchor cell (AC)/vulval precursor (VU) cell fate decision. Negatively regulates glp-1 activity in germline proliferation. May play a role in the formation of fibrous organelles, a hemidesmosome-like s [...] | 0.447 |
eel-1 | ubr-1 | Y67D8C.5h.1 | C32E8.11.1 | Enhancer of EfL-1 mutant phenotype. | E3 ubiquitin-protein ligase ubr-1; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N- end rule, leading to their ubiquitination and subsequent degradation (By similarity). In complex with ced-3, required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 to regulate seam cell fate patterning during larval development. Negatively regulates glutamate metabolism through the aspartate aminotrans [...] | 0.485 |
eel-1 | ubr-4 | Y67D8C.5h.1 | C44E4.1d.1 | Enhancer of EfL-1 mutant phenotype. | UBR-type domain-containing protein. | 0.565 |
eel-1 | ubr-5 | Y67D8C.5h.1 | F36A2.13.1 | Enhancer of EfL-1 mutant phenotype. | UBR E3 ubiquitin ligase homolog. | 0.544 |
hecd-1 | eel-1 | C34D4.14f.1 | Y67D8C.5h.1 | E3 ubiquitin-protein ligase hecd-1; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Involved in the ubiquitination and proteasomal-mediated degradation of cytoplasmic and mitochondrial proteins. Positively regulates lin-12 activity in the anchor cell (AC)/vulval precursor (VU) cell fate decision. Negatively regulates glp-1 activity in germline proliferation. May play a role in the formation of fibrous organelles, a hemidesmosome-like s [...] | Enhancer of EfL-1 mutant phenotype. | 0.447 |
hecd-1 | ubr-1 | C34D4.14f.1 | C32E8.11.1 | E3 ubiquitin-protein ligase hecd-1; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Involved in the ubiquitination and proteasomal-mediated degradation of cytoplasmic and mitochondrial proteins. Positively regulates lin-12 activity in the anchor cell (AC)/vulval precursor (VU) cell fate decision. Negatively regulates glp-1 activity in germline proliferation. May play a role in the formation of fibrous organelles, a hemidesmosome-like s [...] | E3 ubiquitin-protein ligase ubr-1; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N- end rule, leading to their ubiquitination and subsequent degradation (By similarity). In complex with ced-3, required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 to regulate seam cell fate patterning during larval development. Negatively regulates glutamate metabolism through the aspartate aminotrans [...] | 0.502 |
hecd-1 | ubr-4 | C34D4.14f.1 | C44E4.1d.1 | E3 ubiquitin-protein ligase hecd-1; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Involved in the ubiquitination and proteasomal-mediated degradation of cytoplasmic and mitochondrial proteins. Positively regulates lin-12 activity in the anchor cell (AC)/vulval precursor (VU) cell fate decision. Negatively regulates glp-1 activity in germline proliferation. May play a role in the formation of fibrous organelles, a hemidesmosome-like s [...] | UBR-type domain-containing protein. | 0.612 |
hecd-1 | ubr-5 | C34D4.14f.1 | F36A2.13.1 | E3 ubiquitin-protein ligase hecd-1; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Involved in the ubiquitination and proteasomal-mediated degradation of cytoplasmic and mitochondrial proteins. Positively regulates lin-12 activity in the anchor cell (AC)/vulval precursor (VU) cell fate decision. Negatively regulates glp-1 activity in germline proliferation. May play a role in the formation of fibrous organelles, a hemidesmosome-like s [...] | UBR E3 ubiquitin ligase homolog. | 0.417 |
set-16 | ubr-4 | T12D8.1.1 | C44E4.1d.1 | Histone-lysine N-methyltransferase. | UBR-type domain-containing protein. | 0.555 |
srb-1 | ubr-4 | C27D6.10.1 | C44E4.1d.1 | Serpentine receptor class beta-1. | UBR-type domain-containing protein. | 0.692 |
ubr-1 | ate-1 | C32E8.11.1 | K07A1.9a.1 | E3 ubiquitin-protein ligase ubr-1; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N- end rule, leading to their ubiquitination and subsequent degradation (By similarity). In complex with ced-3, required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 to regulate seam cell fate patterning during larval development. Negatively regulates glutamate metabolism through the aspartate aminotrans [...] | Arginyl-tRNA--protein transferase 1; Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Belongs to the R-transferase family. | 0.754 |
ubr-1 | eel-1 | C32E8.11.1 | Y67D8C.5h.1 | E3 ubiquitin-protein ligase ubr-1; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N- end rule, leading to their ubiquitination and subsequent degradation (By similarity). In complex with ced-3, required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 to regulate seam cell fate patterning during larval development. Negatively regulates glutamate metabolism through the aspartate aminotrans [...] | Enhancer of EfL-1 mutant phenotype. | 0.485 |
ubr-1 | hecd-1 | C32E8.11.1 | C34D4.14f.1 | E3 ubiquitin-protein ligase ubr-1; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N- end rule, leading to their ubiquitination and subsequent degradation (By similarity). In complex with ced-3, required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 to regulate seam cell fate patterning during larval development. Negatively regulates glutamate metabolism through the aspartate aminotrans [...] | E3 ubiquitin-protein ligase hecd-1; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Involved in the ubiquitination and proteasomal-mediated degradation of cytoplasmic and mitochondrial proteins. Positively regulates lin-12 activity in the anchor cell (AC)/vulval precursor (VU) cell fate decision. Negatively regulates glp-1 activity in germline proliferation. May play a role in the formation of fibrous organelles, a hemidesmosome-like s [...] | 0.502 |