| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FKBP8 | IDE | ENSP00000476767 | ENSP00000265986 | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | 0.904 |
| FKBP8 | MUL1 | ENSP00000476767 | ENSP00000264198 | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | Mitochondrial ubiquitin ligase activator of NFKB 1; Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at ’Lys-284’ involving ’Lys-48’-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the con [...] | 0.909 |
| FKBP8 | RHOT1 | ENSP00000476767 | ENSP00000351132 | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | Mitochondrial Rho GTPase 1; Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution; EF-hand domain containing | 0.928 |
| FKBP8 | TOMM20 | ENSP00000476767 | ENSP00000355566 | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | Mitochondrial import receptor subunit TOM20 homolog; Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity); Belongs to the Tom20 family | 0.917 |
| FKBP8 | TOMM70A | ENSP00000476767 | ENSP00000284320 | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | Mitochondrial import receptor subunit TOM70; Receptor that accelerates the import of all mitochondrial precursor proteins | 0.925 |
| FKBP8 | USP30 | ENSP00000476767 | ENSP00000257548 | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | Ubiquitin carboxyl-terminal hydrolase 30; Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN)- hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin’s ability to drive mitophagy. Preferentially cleaves ’Lys-6’- and ’Lys-11’- linked polyubiquitin chains, 2 types of linkage that participate to mitophagic signaling. Does not cleave efficiently polyubiquitin phosphorylated at ’Ser-65’. Acts as negative regulator of mitochondri [...] | 0.902 |
| FKBP8 | VDAC1 | ENSP00000476767 | ENSP00000265333 | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | Voltage-dependent anion-selective channel protein 1; Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition p [...] | 0.927 |
| FKBP8 | VDAC2 | ENSP00000476767 | ENSP00000361635 | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | Voltage-dependent anion-selective channel protein 2; Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation- selective; Belongs to the eukaryotic mitochondrial porin family | 0.912 |
| FKBP8 | VDAC3 | ENSP00000476767 | ENSP00000428845 | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | Voltage-dependent anion-selective channel protein 3; Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules; Belongs to the eukaryotic mitochondrial porin family | 0.910 |
| IDE | FKBP8 | ENSP00000265986 | ENSP00000476767 | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | 0.904 |
| IDE | MUL1 | ENSP00000265986 | ENSP00000264198 | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | Mitochondrial ubiquitin ligase activator of NFKB 1; Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at ’Lys-284’ involving ’Lys-48’-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the con [...] | 0.905 |
| IDE | RHOT1 | ENSP00000265986 | ENSP00000351132 | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | Mitochondrial Rho GTPase 1; Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution; EF-hand domain containing | 0.905 |
| IDE | TOMM20 | ENSP00000265986 | ENSP00000355566 | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | Mitochondrial import receptor subunit TOM20 homolog; Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity); Belongs to the Tom20 family | 0.903 |
| IDE | TOMM70A | ENSP00000265986 | ENSP00000284320 | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | Mitochondrial import receptor subunit TOM70; Receptor that accelerates the import of all mitochondrial precursor proteins | 0.920 |
| IDE | USP30 | ENSP00000265986 | ENSP00000257548 | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | Ubiquitin carboxyl-terminal hydrolase 30; Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN)- hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin’s ability to drive mitophagy. Preferentially cleaves ’Lys-6’- and ’Lys-11’- linked polyubiquitin chains, 2 types of linkage that participate to mitophagic signaling. Does not cleave efficiently polyubiquitin phosphorylated at ’Ser-65’. Acts as negative regulator of mitochondri [...] | 0.901 |
| IDE | VDAC1 | ENSP00000265986 | ENSP00000265333 | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | Voltage-dependent anion-selective channel protein 1; Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition p [...] | 0.910 |
| IDE | VDAC2 | ENSP00000265986 | ENSP00000361635 | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | Voltage-dependent anion-selective channel protein 2; Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation- selective; Belongs to the eukaryotic mitochondrial porin family | 0.902 |
| IDE | VDAC3 | ENSP00000265986 | ENSP00000428845 | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | Voltage-dependent anion-selective channel protein 3; Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules; Belongs to the eukaryotic mitochondrial porin family | 0.900 |
| MUL1 | FKBP8 | ENSP00000264198 | ENSP00000476767 | Mitochondrial ubiquitin ligase activator of NFKB 1; Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at ’Lys-284’ involving ’Lys-48’-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the con [...] | Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases | 0.909 |
| MUL1 | IDE | ENSP00000264198 | ENSP00000265986 | Mitochondrial ubiquitin ligase activator of NFKB 1; Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at ’Lys-284’ involving ’Lys-48’-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the con [...] | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases | 0.905 |
