| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AHP1 | GLR1 | YLR109W | YPL091W | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | 0.946 |
| AHP1 | GRX1 | YLR109W | YCL035C | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | Glutaredoxin-1; Glutathione-dependent disulfide oxidoreductase; hydroperoxide and superoxide-radical responsive, heat-stable, with active site cysteine pair; protects cells from oxidative damage; GRX1 has a paralog, GRX2, that arose from the whole genome duplication; protein abundance increases in response to DNA replication stress. | 0.734 |
| AHP1 | GRX2 | YLR109W | YDR513W | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | Glutaredoxin-2; Cytoplasmic glutaredoxin; thioltransferase, glutathione-dependent disulfide oxidoreductase involved in maintaining redox state of target proteins, also exhibits glutathione peroxidase activity, expression induced in response to stress; GRX2 has two in-frame start codons resulting in a shorter isoform that is retained in the cytosol and a longer form translocated to the mitochondrial matrix; GRX2 has a paralog, GRX1, that arose from the whole genome duplication. | 0.698 |
| AHP1 | TRR1 | YLR109W | YDR353W | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | Cytoplasmic thioredoxin reductase; key regulatory enzyme that determines the redox state of the thioredoxin system, which acts as a disulfide reductase system and protects cells against both oxidative and reductive stress; protein abundance increases in response to DNA replication stress; TRR1 has a paralog, TRR2, that arose from the whole genome duplication; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.805 |
| AHP1 | TRX1 | YLR109W | YLR043C | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | Thioredoxin-1; Cytoplasmic thioredoxin isoenzyme; part of thioredoxin system which protects cells against oxidative and reductive stress; forms LMA1 complex with Pbi2p; acts as a cofactor for Tsa1p; required for ER-Golgi transport and vacuole inheritance; with Trx2p, facilitates mitochondrial import of small Tims Tim9p, Tim10p, Tim13p by maintaining them in reduced form; abundance increases iunder DNA replication stress; TRX1 has a paralog, TRX2, that arose from the whole genome duplication. | 0.947 |
| AHP1 | TRX2 | YLR109W | YGR209C | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | Thioredoxin-2; Cytoplasmic thioredoxin isoenzyme; part of thioredoxin system which protects cells against oxidative and reductive stress; forms LMA1 complex with Pbi2p; acts as a cofactor for Tsa1p; required for ER-Golgi transport and vacuole inheritance; with Trx1p, facilitates mitochondrial import of small Tims Tim9p, Tim10p, Tim13p by maintaining them in reduced form; abundance increases under DNA replication stress; TRX2 has a paralog, TRX1, that arose from the whole genome duplication. | 0.991 |
| AHP1 | TSA1 | YLR109W | YML028W | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | Peroxiredoxin TSA1; Thioredoxin peroxidase; acts as both ribosome-associated and free cytoplasmic antioxidant; self-associates to form high-molecular weight chaperone complex under oxidative stress; chaperone activity essential for growth in zinc deficiency; required for telomere length maintenance; binds and modulates Cdc19p activity; protein abundance increases, forms cytoplasmic foci during DNA replication stress; TSA1 has a paralog, TSA2, that arose from the whole genome duplication; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | 0.999 |
| AHP1 | TSA2 | YLR109W | YDR453C | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | Peroxiredoxin TSA2; Stress inducible cytoplasmic thioredoxin peroxidase; cooperates with Tsa1p in the removal of reactive oxygen, nitrogen and sulfur species using thioredoxin as hydrogen donor; deletion enhances the mutator phenotype of tsa1 mutants; protein abundance increases in response to DNA replication stress; TSA2 has a paralog, TSA1, that arose from the whole genome duplication; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | 0.977 |
| AHP1 | YAP1 | YLR109W | YML007W | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | Basic leucine zipper (bZIP) transcription factor; required for oxidative stress tolerance; activated by H2O2 through the multistep formation of disulfide bonds and transit from the cytoplasm to the nucleus; Yap1p is degraded in the nucleus after the oxidative stress has passed; mediates resistance to cadmium; relative distribution to the nucleus increases upon DNA replication stress; YAP1 has a paralog, CAD1, that arose from the whole genome duplication. | 0.731 |
| GLR1 | AHP1 | YPL091W | YLR109W | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | 0.946 |
| GLR1 | GRX1 | YPL091W | YCL035C | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | Glutaredoxin-1; Glutathione-dependent disulfide oxidoreductase; hydroperoxide and superoxide-radical responsive, heat-stable, with active site cysteine pair; protects cells from oxidative damage; GRX1 has a paralog, GRX2, that arose from the whole genome duplication; protein abundance increases in response to DNA replication stress. | 0.910 |
| GLR1 | GRX2 | YPL091W | YDR513W | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | Glutaredoxin-2; Cytoplasmic glutaredoxin; thioltransferase, glutathione-dependent disulfide oxidoreductase involved in maintaining redox state of target proteins, also exhibits glutathione peroxidase activity, expression induced in response to stress; GRX2 has two in-frame start codons resulting in a shorter isoform that is retained in the cytosol and a longer form translocated to the mitochondrial matrix; GRX2 has a paralog, GRX1, that arose from the whole genome duplication. | 0.917 |
| GLR1 | TRR1 | YPL091W | YDR353W | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | Cytoplasmic thioredoxin reductase; key regulatory enzyme that determines the redox state of the thioredoxin system, which acts as a disulfide reductase system and protects cells against both oxidative and reductive stress; protein abundance increases in response to DNA replication stress; TRR1 has a paralog, TRR2, that arose from the whole genome duplication; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.968 |
| GLR1 | TRX1 | YPL091W | YLR043C | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | Thioredoxin-1; Cytoplasmic thioredoxin isoenzyme; part of thioredoxin system which protects cells against oxidative and reductive stress; forms LMA1 complex with Pbi2p; acts as a cofactor for Tsa1p; required for ER-Golgi transport and vacuole inheritance; with Trx2p, facilitates mitochondrial import of small Tims Tim9p, Tim10p, Tim13p by maintaining them in reduced form; abundance increases iunder DNA replication stress; TRX1 has a paralog, TRX2, that arose from the whole genome duplication. | 0.952 |
| GLR1 | TRX2 | YPL091W | YGR209C | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | Thioredoxin-2; Cytoplasmic thioredoxin isoenzyme; part of thioredoxin system which protects cells against oxidative and reductive stress; forms LMA1 complex with Pbi2p; acts as a cofactor for Tsa1p; required for ER-Golgi transport and vacuole inheritance; with Trx1p, facilitates mitochondrial import of small Tims Tim9p, Tim10p, Tim13p by maintaining them in reduced form; abundance increases under DNA replication stress; TRX2 has a paralog, TRX1, that arose from the whole genome duplication. | 0.954 |
| GLR1 | TSA1 | YPL091W | YML028W | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | Peroxiredoxin TSA1; Thioredoxin peroxidase; acts as both ribosome-associated and free cytoplasmic antioxidant; self-associates to form high-molecular weight chaperone complex under oxidative stress; chaperone activity essential for growth in zinc deficiency; required for telomere length maintenance; binds and modulates Cdc19p activity; protein abundance increases, forms cytoplasmic foci during DNA replication stress; TSA1 has a paralog, TSA2, that arose from the whole genome duplication; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | 0.912 |
| GLR1 | TSA2 | YPL091W | YDR453C | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | Peroxiredoxin TSA2; Stress inducible cytoplasmic thioredoxin peroxidase; cooperates with Tsa1p in the removal of reactive oxygen, nitrogen and sulfur species using thioredoxin as hydrogen donor; deletion enhances the mutator phenotype of tsa1 mutants; protein abundance increases in response to DNA replication stress; TSA2 has a paralog, TSA1, that arose from the whole genome duplication; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | 0.805 |
| GLR1 | YAP1 | YPL091W | YML007W | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | Basic leucine zipper (bZIP) transcription factor; required for oxidative stress tolerance; activated by H2O2 through the multistep formation of disulfide bonds and transit from the cytoplasm to the nucleus; Yap1p is degraded in the nucleus after the oxidative stress has passed; mediates resistance to cadmium; relative distribution to the nucleus increases upon DNA replication stress; YAP1 has a paralog, CAD1, that arose from the whole genome duplication. | 0.908 |
| GRX1 | AHP1 | YCL035C | YLR109W | Glutaredoxin-1; Glutathione-dependent disulfide oxidoreductase; hydroperoxide and superoxide-radical responsive, heat-stable, with active site cysteine pair; protects cells from oxidative damage; GRX1 has a paralog, GRX2, that arose from the whole genome duplication; protein abundance increases in response to DNA replication stress. | Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily. | 0.734 |
| GRX1 | GLR1 | YCL035C | YPL091W | Glutaredoxin-1; Glutathione-dependent disulfide oxidoreductase; hydroperoxide and superoxide-radical responsive, heat-stable, with active site cysteine pair; protects cells from oxidative damage; GRX1 has a paralog, GRX2, that arose from the whole genome duplication; protein abundance increases in response to DNA replication stress. | Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress. | 0.910 |