| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RNF130 | RNF144B | ENSP00000430237 | ENSP00000259939 | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; Ring finger proteins | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | 0.954 |
| RNF130 | RNF182 | ENSP00000430237 | ENSP00000420465 | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; Ring finger proteins | E3 ubiquitin-protein ligase RNF182; E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway; Ring finger proteins | 0.924 |
| RNF130 | RNF19A | ENSP00000430237 | ENSP00000428968 | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; Ring finger proteins | E3 ubiquitin-protein ligase RNF19A; 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 SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection; Belongs to the RBR family. RNF19 subfamily | 0.935 |
| RNF130 | RNF19B | ENSP00000430237 | ENSP00000362555 | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; 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 | 0.945 |
| RNF130 | RNF217 | ENSP00000430237 | ENSP00000428698 | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; Ring finger proteins | Probable E3 ubiquitin-protein ligase RNF217; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates; Belongs to the RBR family. RNF217 subfamily | 0.915 |
| RNF130 | TRAIP | ENSP00000430237 | ENSP00000328203 | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; Ring finger proteins | E3 ubiquitin-protein ligase TRAIP; E3 ubiquitin ligase acting as a negative regulator of innate immune signaling. Inhibits activation of NF-kappa-B mediated by TNF. Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting ’Lys-48’-linked polyubiquitination of TNK1 leading to its proteasomal degradation (By similarity). Involved in response to genotoxic lesions during genome replication. Promotes H2AX and RPA2 phosphorylation after replication-associated DNA damage and assists fork progression at UV-indu [...] | 0.903 |
| RNF130 | TRIM9 | ENSP00000430237 | ENSP00000298355 | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; Ring finger proteins | E3 ubiquitin-protein ligase TRIM9; E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation; Belongs to the TRIM/RBCC family | 0.902 |
| RNF130 | UBC | ENSP00000430237 | ENSP00000441543 | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; Ring finger proteins | Polyubiquitin-C; 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 involved in DNA repair; [...] | 0.946 |
| RNF130 | UBE2D1 | ENSP00000430237 | ENSP00000363019 | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; Ring finger proteins | Ubiquitin-conjugating enzyme E2 D1; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys-48’-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubi [...] | 0.951 |
| RNF130 | UBE2Q2 | ENSP00000430237 | ENSP00000267938 | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; Ring finger proteins | Ubiquitin-conjugating enzyme E2 Q2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-linked polyubiquitination; Ubiquitin conjugating enzymes E2 | 0.907 |
| RNF144B | RNF130 | ENSP00000259939 | ENSP00000430237 | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | E3 ubiquitin-protein ligase RNF130; May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin- protein ligase; Ring finger proteins | 0.954 |
| RNF144B | RNF182 | ENSP00000259939 | ENSP00000420465 | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | E3 ubiquitin-protein ligase RNF182; E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway; Ring finger proteins | 0.929 |
| RNF144B | RNF19A | ENSP00000259939 | ENSP00000428968 | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | E3 ubiquitin-protein ligase RNF19A; 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 SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection; Belongs to the RBR family. RNF19 subfamily | 0.928 |
| RNF144B | RNF19B | ENSP00000259939 | ENSP00000362555 | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | 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 | 0.927 |
| RNF144B | RNF217 | ENSP00000259939 | ENSP00000428698 | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | Probable E3 ubiquitin-protein ligase RNF217; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates; Belongs to the RBR family. RNF217 subfamily | 0.930 |
| RNF144B | TRAIP | ENSP00000259939 | ENSP00000328203 | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | E3 ubiquitin-protein ligase TRAIP; E3 ubiquitin ligase acting as a negative regulator of innate immune signaling. Inhibits activation of NF-kappa-B mediated by TNF. Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting ’Lys-48’-linked polyubiquitination of TNK1 leading to its proteasomal degradation (By similarity). Involved in response to genotoxic lesions during genome replication. Promotes H2AX and RPA2 phosphorylation after replication-associated DNA damage and assists fork progression at UV-indu [...] | 0.903 |
| RNF144B | TRIM9 | ENSP00000259939 | ENSP00000298355 | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | E3 ubiquitin-protein ligase TRIM9; E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation; Belongs to the TRIM/RBCC family | 0.903 |
| RNF144B | UBC | ENSP00000259939 | ENSP00000441543 | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | Polyubiquitin-C; 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 involved in DNA repair; [...] | 0.937 |
| RNF144B | UBE2D1 | ENSP00000259939 | ENSP00000363019 | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | Ubiquitin-conjugating enzyme E2 D1; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys-48’-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubi [...] | 0.928 |
| RNF144B | UBE2Q2 | ENSP00000259939 | ENSP00000267938 | E3 ubiquitin-protein ligase RNF144B; 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 LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se | Ubiquitin-conjugating enzyme E2 Q2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-linked polyubiquitination; Ubiquitin conjugating enzymes E2 | 0.900 |
