node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
GCLC | GCLM | ENSPPYP00000018706 | ENSPPYP00000001323 | Glutamate-cysteine ligase catalytic subunit. | Glutamate-cysteine ligase modifier subunit. | 0.999 |
GCLC | HMOX1 | ENSPPYP00000018706 | ENSPPYP00000013121 | Glutamate-cysteine ligase catalytic subunit. | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | 0.747 |
GCLC | KEAP1 | ENSPPYP00000018706 | ENSPPYP00000010716 | Glutamate-cysteine ligase catalytic subunit. | Kelch-like ECH-associated protein 1; Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting NFE2L2/NRF2 for ubiquitination. KEAP1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes. In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine [...] | 0.774 |
GCLC | NFE2L2 | ENSPPYP00000018706 | ENSPPYP00000014484 | Glutamate-cysteine ligase catalytic subunit. | NFE2L2 isoform 2. | 0.769 |
GCLC | NQO1 | ENSPPYP00000018706 | ENSPPYP00000008478 | Glutamate-cysteine ligase catalytic subunit. | NAD(P)H dehydrogenase [quinone] 1; The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis; Belongs to the NAD(P)H dehydrogenase (quinone) family. | 0.761 |
GCLC | TP53 | ENSPPYP00000018706 | ENSPPYP00000008923 | Glutamate-cysteine ligase catalytic subunit. | Cellular tumor antigen p53; Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression; Belongs to the p53 family. | 0.459 |
GCLM | GCLC | ENSPPYP00000001323 | ENSPPYP00000018706 | Glutamate-cysteine ligase modifier subunit. | Glutamate-cysteine ligase catalytic subunit. | 0.999 |
GCLM | HMOX1 | ENSPPYP00000001323 | ENSPPYP00000013121 | Glutamate-cysteine ligase modifier subunit. | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | 0.783 |
GCLM | KEAP1 | ENSPPYP00000001323 | ENSPPYP00000010716 | Glutamate-cysteine ligase modifier subunit. | Kelch-like ECH-associated protein 1; Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting NFE2L2/NRF2 for ubiquitination. KEAP1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes. In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine [...] | 0.793 |
GCLM | NFE2L2 | ENSPPYP00000001323 | ENSPPYP00000014484 | Glutamate-cysteine ligase modifier subunit. | NFE2L2 isoform 2. | 0.757 |
GCLM | NQO1 | ENSPPYP00000001323 | ENSPPYP00000008478 | Glutamate-cysteine ligase modifier subunit. | NAD(P)H dehydrogenase [quinone] 1; The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis; Belongs to the NAD(P)H dehydrogenase (quinone) family. | 0.819 |
GCLM | TP53 | ENSPPYP00000001323 | ENSPPYP00000008923 | Glutamate-cysteine ligase modifier subunit. | Cellular tumor antigen p53; Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression; Belongs to the p53 family. | 0.456 |
GGCX | NQO1 | ENSPPYP00000013637 | ENSPPYP00000008478 | Vitamin K-dependent gamma-carboxylase; Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. | NAD(P)H dehydrogenase [quinone] 1; The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis; Belongs to the NAD(P)H dehydrogenase (quinone) family. | 0.927 |
GGCX | VKORC1 | ENSPPYP00000013637 | ENSPPYP00000008254 | Vitamin K-dependent gamma-carboxylase; Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. | T0121409 isoform 1. | 0.981 |
GGCX | VKORC1L1 | ENSPPYP00000013637 | ENSPPYP00000019647 | Vitamin K-dependent gamma-carboxylase; Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. | VKORC1L1 isoform 1. | 0.930 |
HMOX1 | GCLC | ENSPPYP00000013121 | ENSPPYP00000018706 | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | Glutamate-cysteine ligase catalytic subunit. | 0.747 |
HMOX1 | GCLM | ENSPPYP00000013121 | ENSPPYP00000001323 | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | Glutamate-cysteine ligase modifier subunit. | 0.783 |
HMOX1 | KEAP1 | ENSPPYP00000013121 | ENSPPYP00000010716 | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | Kelch-like ECH-associated protein 1; Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting NFE2L2/NRF2 for ubiquitination. KEAP1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes. In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine [...] | 0.755 |
HMOX1 | NFE2L2 | ENSPPYP00000013121 | ENSPPYP00000014484 | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | NFE2L2 isoform 2. | 0.903 |
HMOX1 | NQO1 | ENSPPYP00000013121 | ENSPPYP00000008478 | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | NAD(P)H dehydrogenase [quinone] 1; The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis; Belongs to the NAD(P)H dehydrogenase (quinone) family. | 0.785 |