node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Birc2 | Birc3 | ENSRNOP00000014560 | ENSRNOP00000007702 | Baculoviral IAP repeat-containing 2. | Baculoviral IAP repeat-containing 3. | 0.983 |
Birc2 | Casp8 | ENSRNOP00000014560 | ENSRNOP00000016613 | Baculoviral IAP repeat-containing 2. | 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 [...] | 0.849 |
Birc2 | Fadd | ENSRNOP00000014560 | ENSRNOP00000066289 | Baculoviral IAP repeat-containing 2. | FAS-associated death domain protein; Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling. | 0.978 |
Birc2 | Ripk1 | ENSRNOP00000014560 | ENSRNOP00000023962 | Baculoviral IAP repeat-containing 2. | Receptor (TNFRSF)-interacting serine-threonine kinase 1 (Predicted). | 0.994 |
Birc2 | Ripk3 | ENSRNOP00000014560 | ENSRNOP00000027759 | Baculoviral IAP repeat-containing 2. | Receptor-interacting serine/threonine-protein kinase 3; Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production (By similarity). | 0.963 |
Birc2 | Tradd | ENSRNOP00000014560 | ENSRNOP00000020405 | Baculoviral IAP repeat-containing 2. | TNFRSF1A-associated via death domain. | 0.994 |
Birc2 | Traf2 | ENSRNOP00000014560 | ENSRNOP00000008253 | Baculoviral IAP repeat-containing 2. | TNF receptor-associated factor. | 0.997 |
Birc3 | Birc2 | ENSRNOP00000007702 | ENSRNOP00000014560 | Baculoviral IAP repeat-containing 3. | Baculoviral IAP repeat-containing 2. | 0.983 |
Birc3 | Casp8 | ENSRNOP00000007702 | ENSRNOP00000016613 | Baculoviral IAP repeat-containing 3. | 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 [...] | 0.868 |
Birc3 | Fadd | ENSRNOP00000007702 | ENSRNOP00000066289 | Baculoviral IAP repeat-containing 3. | FAS-associated death domain protein; Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling. | 0.980 |
Birc3 | Ripk1 | ENSRNOP00000007702 | ENSRNOP00000023962 | Baculoviral IAP repeat-containing 3. | Receptor (TNFRSF)-interacting serine-threonine kinase 1 (Predicted). | 0.994 |
Birc3 | Ripk3 | ENSRNOP00000007702 | ENSRNOP00000027759 | Baculoviral IAP repeat-containing 3. | Receptor-interacting serine/threonine-protein kinase 3; Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production (By similarity). | 0.968 |
Birc3 | Tradd | ENSRNOP00000007702 | ENSRNOP00000020405 | Baculoviral IAP repeat-containing 3. | TNFRSF1A-associated via death domain. | 0.994 |
Birc3 | Traf2 | ENSRNOP00000007702 | ENSRNOP00000008253 | Baculoviral IAP repeat-containing 3. | TNF receptor-associated factor. | 0.998 |
Casp8 | Birc2 | ENSRNOP00000016613 | ENSRNOP00000014560 | 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 [...] | Baculoviral IAP repeat-containing 2. | 0.849 |
Casp8 | Birc3 | ENSRNOP00000016613 | ENSRNOP00000007702 | 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 [...] | Baculoviral IAP repeat-containing 3. | 0.868 |
Casp8 | Fadd | ENSRNOP00000016613 | ENSRNOP00000066289 | 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 [...] | FAS-associated death domain protein; Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling. | 0.999 |
Casp8 | Mlkl | ENSRNOP00000016613 | ENSRNOP00000034575 | 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 [...] | Mixed lineage kinase domain-like pseudokinase. | 0.877 |
Casp8 | Ripk1 | ENSRNOP00000016613 | ENSRNOP00000023962 | 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 [...] | Receptor (TNFRSF)-interacting serine-threonine kinase 1 (Predicted). | 0.999 |
Casp8 | Ripk3 | ENSRNOP00000016613 | ENSRNOP00000027759 | 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 [...] | Receptor-interacting serine/threonine-protein kinase 3; Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production (By similarity). | 0.999 |