| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | GRX3 | YPL091W | YDR098C | 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. | Monothiol glutaredoxin-3; Glutathione-dependent oxidoreductase; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; with Grx4p, binds to Aft1p in iron-replete conditions, promoting its dissociation from promoters; evidence exists indicating that the translation start site is not Met1 as currently annotated, but rather Met36; GRX3 has a paralog, GRX4, that arose from the whole genome duplication. | 0.632 |
| GLR1 | GRX5 | YPL091W | YPL059W | 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. | Monothiol glutaredoxin-5, mitochondrial; Glutathione-dependent oxidoreductase; mitochondrial matrix protein involved at an early step in the biogenesis of iron-sulfur centers along with Bol1p; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p. | 0.663 |
| GLR1 | GRX7 | YPL091W | YBR014C | 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. | Cis-golgi localized monothiol glutaredoxin; more similar in activity to dithiol than other monothiol glutaredoxins; involved in the oxidative stress response; does not bind metal ions; GRX7 has a paralog, GRX6, that arose from the whole genome duplication. | 0.636 |
| GLR1 | GRX8 | YPL091W | YLR364W | 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-8; Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic. | 0.676 |
| GRX2 | GLR1 | YDR513W | YPL091W | 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. | 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. | 0.917 |
| GRX2 | GRX3 | YDR513W | YDR098C | 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. | Monothiol glutaredoxin-3; Glutathione-dependent oxidoreductase; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; with Grx4p, binds to Aft1p in iron-replete conditions, promoting its dissociation from promoters; evidence exists indicating that the translation start site is not Met1 as currently annotated, but rather Met36; GRX3 has a paralog, GRX4, that arose from the whole genome duplication. | 0.860 |
| GRX2 | GRX5 | YDR513W | YPL059W | 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. | Monothiol glutaredoxin-5, mitochondrial; Glutathione-dependent oxidoreductase; mitochondrial matrix protein involved at an early step in the biogenesis of iron-sulfur centers along with Bol1p; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p. | 0.855 |
| GRX2 | GRX7 | YDR513W | YBR014C | 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. | Cis-golgi localized monothiol glutaredoxin; more similar in activity to dithiol than other monothiol glutaredoxins; involved in the oxidative stress response; does not bind metal ions; GRX7 has a paralog, GRX6, that arose from the whole genome duplication. | 0.543 |
| GRX2 | GRX8 | YDR513W | YLR364W | 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. | Glutaredoxin-8; Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic. | 0.755 |
| GRX3 | GLR1 | YDR098C | YPL091W | Monothiol glutaredoxin-3; Glutathione-dependent oxidoreductase; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; with Grx4p, binds to Aft1p in iron-replete conditions, promoting its dissociation from promoters; evidence exists indicating that the translation start site is not Met1 as currently annotated, but rather Met36; GRX3 has a paralog, GRX4, that arose from the whole genome duplication. | 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. | 0.632 |
| GRX3 | GRX2 | YDR098C | YDR513W | Monothiol glutaredoxin-3; Glutathione-dependent oxidoreductase; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; with Grx4p, binds to Aft1p in iron-replete conditions, promoting its dissociation from promoters; evidence exists indicating that the translation start site is not Met1 as currently annotated, but rather Met36; GRX3 has a paralog, GRX4, that arose from the whole genome duplication. | 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. | 0.860 |
| GRX3 | GRX5 | YDR098C | YPL059W | Monothiol glutaredoxin-3; Glutathione-dependent oxidoreductase; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; with Grx4p, binds to Aft1p in iron-replete conditions, promoting its dissociation from promoters; evidence exists indicating that the translation start site is not Met1 as currently annotated, but rather Met36; GRX3 has a paralog, GRX4, that arose from the whole genome duplication. | Monothiol glutaredoxin-5, mitochondrial; Glutathione-dependent oxidoreductase; mitochondrial matrix protein involved at an early step in the biogenesis of iron-sulfur centers along with Bol1p; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p. | 0.947 |
| GRX3 | GRX7 | YDR098C | YBR014C | Monothiol glutaredoxin-3; Glutathione-dependent oxidoreductase; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; with Grx4p, binds to Aft1p in iron-replete conditions, promoting its dissociation from promoters; evidence exists indicating that the translation start site is not Met1 as currently annotated, but rather Met36; GRX3 has a paralog, GRX4, that arose from the whole genome duplication. | Cis-golgi localized monothiol glutaredoxin; more similar in activity to dithiol than other monothiol glutaredoxins; involved in the oxidative stress response; does not bind metal ions; GRX7 has a paralog, GRX6, that arose from the whole genome duplication. | 0.979 |
| GRX3 | GRX8 | YDR098C | YLR364W | Monothiol glutaredoxin-3; Glutathione-dependent oxidoreductase; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; with Grx4p, binds to Aft1p in iron-replete conditions, promoting its dissociation from promoters; evidence exists indicating that the translation start site is not Met1 as currently annotated, but rather Met36; GRX3 has a paralog, GRX4, that arose from the whole genome duplication. | Glutaredoxin-8; Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic. | 0.732 |
| GRX5 | GLR1 | YPL059W | YPL091W | Monothiol glutaredoxin-5, mitochondrial; Glutathione-dependent oxidoreductase; mitochondrial matrix protein involved at an early step in the biogenesis of iron-sulfur centers along with Bol1p; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p. | 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. | 0.663 |
| GRX5 | GRX2 | YPL059W | YDR513W | Monothiol glutaredoxin-5, mitochondrial; Glutathione-dependent oxidoreductase; mitochondrial matrix protein involved at an early step in the biogenesis of iron-sulfur centers along with Bol1p; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p. | 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. | 0.855 |
| GRX5 | GRX3 | YPL059W | YDR098C | Monothiol glutaredoxin-5, mitochondrial; Glutathione-dependent oxidoreductase; mitochondrial matrix protein involved at an early step in the biogenesis of iron-sulfur centers along with Bol1p; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p. | Monothiol glutaredoxin-3; Glutathione-dependent oxidoreductase; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; with Grx4p, binds to Aft1p in iron-replete conditions, promoting its dissociation from promoters; evidence exists indicating that the translation start site is not Met1 as currently annotated, but rather Met36; GRX3 has a paralog, GRX4, that arose from the whole genome duplication. | 0.947 |
| GRX5 | GRX7 | YPL059W | YBR014C | Monothiol glutaredoxin-5, mitochondrial; Glutathione-dependent oxidoreductase; mitochondrial matrix protein involved at an early step in the biogenesis of iron-sulfur centers along with Bol1p; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p. | Cis-golgi localized monothiol glutaredoxin; more similar in activity to dithiol than other monothiol glutaredoxins; involved in the oxidative stress response; does not bind metal ions; GRX7 has a paralog, GRX6, that arose from the whole genome duplication. | 0.983 |
| GRX5 | GRX8 | YPL059W | YLR364W | Monothiol glutaredoxin-5, mitochondrial; Glutathione-dependent oxidoreductase; mitochondrial matrix protein involved at an early step in the biogenesis of iron-sulfur centers along with Bol1p; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p. | Glutaredoxin-8; Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic. | 0.813 |