| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CGRRF1 | RNF145 | ENSP00000216420 | ENSP00000430955 | Cell growth regulator with RING finger domain protein 1; Able to inhibit growth in several cell lines; Ring finger proteins | Ring finger protein 145 | 0.573 |
| CGRRF1 | RNF170 | ENSP00000216420 | ENSP00000445725 | Cell growth regulator with RING finger domain protein 1; Able to inhibit growth in several cell lines; Ring finger proteins | E3 ubiquitin-protein ligase RNF170; E3 ubiquitin-protein ligase that plays an essential role in stimulus-induced inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ubiquitination and degradation via the endoplasmic reticulum-associated degradation (ERAD) pathway. Also involved in ITPR1 turnover in resting cells; Ring finger proteins | 0.725 |
| CGRRF1 | RNF19B | ENSP00000216420 | ENSP00000362555 | Cell growth regulator with RING finger domain protein 1; Able to inhibit growth in several cell lines; Ring finger proteins | E3 ubiquitin-protein ligase RNF19B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects against staurosporin-induced cell death | 0.557 |
| CGRRF1 | RNFT1 | ENSP00000216420 | ENSP00000304670 | Cell growth regulator with RING finger domain protein 1; Able to inhibit growth in several cell lines; Ring finger proteins | E3 ubiquitin-protein ligase RNFT1; E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome- mediated degradation. Protects cells from ER stress-induced apoptosis; Ring finger proteins | 0.659 |
| RNF103 | RNF145 | ENSP00000237455 | ENSP00000430955 | E3 ubiquitin-protein ligase RNF103; Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway; Ring finger proteins | Ring finger protein 145 | 0.601 |
| RNF103 | RNF170 | ENSP00000237455 | ENSP00000445725 | E3 ubiquitin-protein ligase RNF103; Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway; Ring finger proteins | E3 ubiquitin-protein ligase RNF170; E3 ubiquitin-protein ligase that plays an essential role in stimulus-induced inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ubiquitination and degradation via the endoplasmic reticulum-associated degradation (ERAD) pathway. Also involved in ITPR1 turnover in resting cells; Ring finger proteins | 0.586 |
| RNF103 | RNFT1 | ENSP00000237455 | ENSP00000304670 | E3 ubiquitin-protein ligase RNF103; Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway; Ring finger proteins | E3 ubiquitin-protein ligase RNFT1; E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome- mediated degradation. Protects cells from ER stress-induced apoptosis; Ring finger proteins | 0.640 |
| RNF103 | UBA52 | ENSP00000237455 | ENSP00000388107 | E3 ubiquitin-protein ligase RNF103; Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway; Ring finger proteins | 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-6-linked may be invo [...] | 0.937 |
| RNF144A | RNF183 | ENSP00000321330 | ENSP00000419454 | E3 ubiquitin-protein ligase RNF144A; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the ubiquitination and degradation of the DNA damage kinase PRKDC | Probable E3 ubiquitin-protein ligase RNF183; May act as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. May collaborate with FATE1 to restrain BIK protein levels thus regulating apoptotic signaling; Ring finger proteins | 0.614 |
| RNF144A | RNF223 | ENSP00000321330 | ENSP00000410533 | E3 ubiquitin-protein ligase RNF144A; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the ubiquitination and degradation of the DNA damage kinase PRKDC | Ring finger protein 223 | 0.655 |
| RNF144A | RNFT1 | ENSP00000321330 | ENSP00000304670 | E3 ubiquitin-protein ligase RNF144A; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the ubiquitination and degradation of the DNA damage kinase PRKDC | E3 ubiquitin-protein ligase RNFT1; E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome- mediated degradation. Protects cells from ER stress-induced apoptosis; Ring finger proteins | 0.672 |
| RNF144A | UBA52 | ENSP00000321330 | ENSP00000388107 | E3 ubiquitin-protein ligase RNF144A; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the ubiquitination and degradation of the DNA damage kinase PRKDC | 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-6-linked may be invo [...] | 0.900 |
| RNF145 | CGRRF1 | ENSP00000430955 | ENSP00000216420 | Ring finger protein 145 | Cell growth regulator with RING finger domain protein 1; Able to inhibit growth in several cell lines; Ring finger proteins | 0.573 |
| RNF145 | RNF103 | ENSP00000430955 | ENSP00000237455 | Ring finger protein 145 | E3 ubiquitin-protein ligase RNF103; Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway; Ring finger proteins | 0.601 |
| RNF145 | RNF170 | ENSP00000430955 | ENSP00000445725 | Ring finger protein 145 | E3 ubiquitin-protein ligase RNF170; E3 ubiquitin-protein ligase that plays an essential role in stimulus-induced inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ubiquitination and degradation via the endoplasmic reticulum-associated degradation (ERAD) pathway. Also involved in ITPR1 turnover in resting cells; Ring finger proteins | 0.605 |
| RNF145 | RNF19B | ENSP00000430955 | ENSP00000362555 | Ring finger protein 145 | E3 ubiquitin-protein ligase RNF19B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects against staurosporin-induced cell death | 0.588 |
| RNF145 | RNFT1 | ENSP00000430955 | ENSP00000304670 | Ring finger protein 145 | E3 ubiquitin-protein ligase RNFT1; E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome- mediated degradation. Protects cells from ER stress-induced apoptosis; Ring finger proteins | 0.658 |
| RNF145 | UBA52 | ENSP00000430955 | ENSP00000388107 | Ring finger protein 145 | 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-6-linked may be invo [...] | 0.720 |
| RNF145 | UBE2G2 | ENSP00000430955 | ENSP00000338348 | Ring finger protein 145 | Ubiquitin-conjugating enzyme E2 G2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-linked polyubiquitination. Involved in endoplasmic reticulum- associated degradation (ERAD); Ubiquitin conjugating enzymes E2 | 0.756 |
| RNF170 | CGRRF1 | ENSP00000445725 | ENSP00000216420 | E3 ubiquitin-protein ligase RNF170; E3 ubiquitin-protein ligase that plays an essential role in stimulus-induced inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ubiquitination and degradation via the endoplasmic reticulum-associated degradation (ERAD) pathway. Also involved in ITPR1 turnover in resting cells; Ring finger proteins | Cell growth regulator with RING finger domain protein 1; Able to inhibit growth in several cell lines; Ring finger proteins | 0.725 |
