| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FKBP8 | PPIF | ENSP00000476767 | ENSP00000225174 | 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 | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | 0.442 |
| 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 | 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 |
| PPIF | FKBP8 | ENSP00000225174 | ENSP00000476767 | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | 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 | 0.442 |
| PPIF | SLC25A4 | ENSP00000225174 | ENSP00000281456 | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | ADP/ATP translocase 1; Involved in mitochondrial ADP/ATP transport. Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane; Belongs to the mitochondrial carrier (TC 2.A.29) family | 0.969 |
| PPIF | SLC25A6 | ENSP00000225174 | ENSP00000370808 | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | ADP/ATP translocase 3; Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis; Belongs to the mitochondrial carrier (TC 2.A.29) family | 0.966 |
| PPIF | TOMM20 | ENSP00000225174 | ENSP00000355566 | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | 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 | 0.479 |
| PPIF | TSPO | ENSP00000225174 | ENSP00000379563 | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | Translocator protein; Can bind protoporphyrin IX and may play a role in the transport of porphyrins and heme (By similarity). Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism, but its precise physiological role is controversial. It is apparently not required for steroid hormone biosynthesis. Was initially identified as peripheral-type benzodiazepine receptor; can also bind isoquinoline carboxamides; Belongs to the TspO/BZRP family | 0.574 |
| PPIF | VDAC1 | ENSP00000225174 | ENSP00000265333 | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | 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 [...] | 0.989 |
| PPIF | VDAC2 | ENSP00000225174 | ENSP00000361635 | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | 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 | 0.935 |
| PPIF | VDAC3 | ENSP00000225174 | ENSP00000428845 | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | 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 | 0.972 |
| RHOT1 | FKBP8 | ENSP00000351132 | ENSP00000476767 | 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 | 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 | 0.928 |
| RHOT1 | TOMM20 | ENSP00000351132 | ENSP00000355566 | 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 | 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 | 0.961 |
| RHOT1 | TOMM70A | ENSP00000351132 | ENSP00000284320 | 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 | Mitochondrial import receptor subunit TOM70; Receptor that accelerates the import of all mitochondrial precursor proteins | 0.958 |
| RHOT1 | VDAC1 | ENSP00000351132 | ENSP00000265333 | 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 | 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 [...] | 0.963 |
| RHOT1 | VDAC2 | ENSP00000351132 | ENSP00000361635 | 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 | 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 | 0.946 |
