| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Bak1 | Bax | ENSRNOP00000000576 | ENSRNOP00000028328 | BCL2-antagonist/killer 1, isoform CRA_b. | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | 0.977 |
| Bak1 | Bcl2 | ENSRNOP00000000576 | ENSRNOP00000003768 | BCL2-antagonist/killer 1, isoform CRA_b. | Apoptosis regulator Bcl-2; Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity). Belongs to the Bcl-2 family. | 0.991 |
| Bak1 | Bcl2l1 | ENSRNOP00000000576 | ENSRNOP00000069758 | BCL2-antagonist/killer 1, isoform CRA_b. | Bcl-2-like protein 1; Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage- dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Isoform Bcl-X(S) promotes apoptosis. | 0.966 |
| Bak1 | Bcl2l11 | ENSRNOP00000000576 | ENSRNOP00000039006 | BCL2-antagonist/killer 1, isoform CRA_b. | Bcl-2-like protein 11; Induces apoptosis and anoikis. | 0.987 |
| Bak1 | Bcl2l2 | ENSRNOP00000000576 | ENSRNOP00000020409 | BCL2-antagonist/killer 1, isoform CRA_b. | RCG23437, isoform CRA_b. | 0.914 |
| Bak1 | Bid | ENSRNOP00000000576 | ENSRNOP00000016776 | BCL2-antagonist/killer 1, isoform CRA_b. | BH3-interacting domain death agonist p11; Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). | 0.999 |
| Bak1 | Casp2 | ENSRNOP00000000576 | ENSRNOP00000022672 | BCL2-antagonist/killer 1, isoform CRA_b. | Caspase-2 subunit p12; Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival (By similarity). Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress (By similarity). Belongs to the peptidase C14A family. | 0.478 |
| Bak1 | Casp8 | ENSRNOP00000000576 | ENSRNOP00000016613 | BCL2-antagonist/killer 1, isoform CRA_b. | Caspase-8 subunit p10; Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CA [...] | 0.652 |
| Bak1 | E9PU78_RAT | ENSRNOP00000000576 | ENSRNOP00000024954 | BCL2-antagonist/killer 1, isoform CRA_b. | BH4_2 domain-containing protein. | 0.958 |
| Bak1 | Pmaip1 | ENSRNOP00000000576 | ENSRNOP00000025361 | BCL2-antagonist/killer 1, isoform CRA_b. | Phorbol-12-myristate-13-acetate-induced protein 1; Promotes activation of caspases and apoptosis. Promotes mitochondrial membrane changes and efflux of apoptogenic proteins from the mitochondria. Contributes to p53/TP53-dependent apoptosis after radiation exposure. Promotes proteasomal degradation of MCL1. Competes with BAK1 and with BIM/BCL2L11 for binding to MCL1; can displace BAK1 and BIM/BCL2L11 from their binding sites (By similarity). Belongs to the PMAIP1 family. | 0.783 |
| Bax | Bak1 | ENSRNOP00000028328 | ENSRNOP00000000576 | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | BCL2-antagonist/killer 1, isoform CRA_b. | 0.977 |
| Bax | Bcl2 | ENSRNOP00000028328 | ENSRNOP00000003768 | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | Apoptosis regulator Bcl-2; Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity). Belongs to the Bcl-2 family. | 0.999 |
| Bax | Bcl2l1 | ENSRNOP00000028328 | ENSRNOP00000069758 | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | Bcl-2-like protein 1; Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage- dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Isoform Bcl-X(S) promotes apoptosis. | 0.996 |
| Bax | Bcl2l11 | ENSRNOP00000028328 | ENSRNOP00000039006 | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | Bcl-2-like protein 11; Induces apoptosis and anoikis. | 0.996 |
| Bax | Bcl2l2 | ENSRNOP00000028328 | ENSRNOP00000020409 | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | RCG23437, isoform CRA_b. | 0.974 |
| Bax | Bid | ENSRNOP00000028328 | ENSRNOP00000016776 | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | BH3-interacting domain death agonist p11; Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). | 0.995 |
| Bax | Casp2 | ENSRNOP00000028328 | ENSRNOP00000022672 | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | Caspase-2 subunit p12; Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival (By similarity). Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress (By similarity). Belongs to the peptidase C14A family. | 0.570 |
| Bax | Casp8 | ENSRNOP00000028328 | ENSRNOP00000016613 | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | Caspase-8 subunit p10; Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CA [...] | 0.829 |
| Bax | E9PU78_RAT | ENSRNOP00000028328 | ENSRNOP00000024954 | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | BH4_2 domain-containing protein. | 0.932 |
| Bax | Pmaip1 | ENSRNOP00000028328 | ENSRNOP00000025361 | Apoptosis regulator BAX; Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. | Phorbol-12-myristate-13-acetate-induced protein 1; Promotes activation of caspases and apoptosis. Promotes mitochondrial membrane changes and efflux of apoptogenic proteins from the mitochondria. Contributes to p53/TP53-dependent apoptosis after radiation exposure. Promotes proteasomal degradation of MCL1. Competes with BAK1 and with BIM/BCL2L11 for binding to MCL1; can displace BAK1 and BIM/BCL2L11 from their binding sites (By similarity). Belongs to the PMAIP1 family. | 0.977 |
