| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| C5 | C8B | ENSP00000223642 | ENSP00000360281 | Complement C5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled; C3 and PZP like, alpha-2-macroglobulin domain containing | Complement component C8 beta chain; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells; Belongs to the complement C6/C7/C8/C9 family | 0.978 |
| C5 | PPIF | ENSP00000223642 | ENSP00000225174 | Complement C5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled; C3 and PZP like, alpha-2-macroglobulin domain containing | 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 [...] | 0.901 |
| C5 | SPG7 | ENSP00000223642 | ENSP00000268704 | Complement C5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled; C3 and PZP like, alpha-2-macroglobulin domain containing | Paraplegin; ATP-dependent zinc metalloprotease. Plays a role in the formation and regulation of the mitochondrial permeability transition pore (mPTP) and its proteolytic activity is dispensable for this function; In the N-terminal section; belongs to the AAA ATPase family | 0.900 |
| C5 | VDAC1 | ENSP00000223642 | ENSP00000265333 | Complement C5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled; C3 and PZP like, alpha-2-macroglobulin 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 [...] | 0.900 |
| C5 | VDAC2 | ENSP00000223642 | ENSP00000361635 | Complement C5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled; C3 and PZP like, alpha-2-macroglobulin 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 | 0.540 |
| C5 | VDAC3 | ENSP00000223642 | ENSP00000428845 | Complement C5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled; C3 and PZP like, alpha-2-macroglobulin domain containing | 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 | 0.540 |
| C8B | C5 | ENSP00000360281 | ENSP00000223642 | Complement component C8 beta chain; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells; Belongs to the complement C6/C7/C8/C9 family | Complement C5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled; C3 and PZP like, alpha-2-macroglobulin domain containing | 0.978 |
| C8B | PPIF | ENSP00000360281 | ENSP00000225174 | Complement component C8 beta chain; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells; Belongs to the complement C6/C7/C8/C9 family | 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 [...] | 0.900 |
| C8B | SPG7 | ENSP00000360281 | ENSP00000268704 | Complement component C8 beta chain; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells; Belongs to the complement C6/C7/C8/C9 family | Paraplegin; ATP-dependent zinc metalloprotease. Plays a role in the formation and regulation of the mitochondrial permeability transition pore (mPTP) and its proteolytic activity is dispensable for this function; In the N-terminal section; belongs to the AAA ATPase family | 0.900 |
| C8B | VDAC1 | ENSP00000360281 | ENSP00000265333 | Complement component C8 beta chain; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells; Belongs to the complement C6/C7/C8/C9 family | 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 [...] | 0.900 |
| C8B | VDAC2 | ENSP00000360281 | ENSP00000361635 | Complement component C8 beta chain; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells; Belongs to the complement C6/C7/C8/C9 family | 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 | 0.540 |
| C8B | VDAC3 | ENSP00000360281 | ENSP00000428845 | Complement component C8 beta chain; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells; Belongs to the complement C6/C7/C8/C9 family | 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 | 0.540 |
| FKBP1A | PPIF | ENSP00000383003 | ENSP00000225174 | Peptidyl-prolyl cis-trans isomerase FKBP1A; Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the FKBP-type PPIase family. FKBP1 subfamily | 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 [...] | 0.909 |
| PPIF | C5 | ENSP00000225174 | ENSP00000223642 | 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 [...] | Complement C5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled; C3 and PZP like, alpha-2-macroglobulin domain containing | 0.901 |
| PPIF | C8B | ENSP00000225174 | ENSP00000360281 | 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 [...] | Complement component C8 beta chain; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells; Belongs to the complement C6/C7/C8/C9 family | 0.900 |
| PPIF | FKBP1A | ENSP00000225174 | ENSP00000383003 | 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 FKBP1A; Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the FKBP-type PPIase family. FKBP1 subfamily | 0.909 |
| 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 | SLC25A5 | ENSP00000225174 | ENSP00000360671 | 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 2; Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation; Solute carriers | 0.960 |
| 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 | SPG7 | ENSP00000225174 | ENSP00000268704 | 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 [...] | Paraplegin; ATP-dependent zinc metalloprotease. Plays a role in the formation and regulation of the mitochondrial permeability transition pore (mPTP) and its proteolytic activity is dispensable for this function; In the N-terminal section; belongs to the AAA ATPase family | 0.954 |
