| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | 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 |
| 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 |
| GRX1 | GRX2 | YCL035C | YDR513W | 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. | 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. | 0.895 |
| GRX1 | TRX1 | YCL035C | YLR043C | 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. | 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. | 0.900 |
| GRX1 | TRX2 | YCL035C | YGR209C | 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. | 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. | 0.910 |
| 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 | GRX1 | YDR513W | YCL035C | 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-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. | 0.895 |
| GRX2 | POP4 | YDR513W | YBR257W | 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. | RNases MRP/P 32.9 kDa subunit; Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5' ends and facilitates turnover of nuclear RNAs; binds to the RPR1 RNA subunit in RNase P. | 0.961 |
| GRX2 | POP5 | YDR513W | YAL033W | 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. | Ribonuclease P/MRP protein subunit POP5; Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5' ends and facilitates turnover of nuclear RNAs. | 0.930 |
| GRX2 | POP6 | YDR513W | YGR030C | 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. | Ribonucleases P/MRP protein subunit POP6; Subunit of RNase MRP, nuclear RNase P and telomerase; forms a soluble heterodimer with Pop7p that binds P3 domain of RNase MRP and RNase P RNAs; RNase MRP cleaves pre-rRNA, nuclear RNase P cleaves tRNA precursors to generate mature 5' ends and facilitates turnover of nuclear RNAs, while telomerase replenishes telomeric DNA; relocalizes to the cytosol in response to hypoxia. | 0.963 |
| GRX2 | POP7 | YDR513W | YBR167C | 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. | Ribonucleases P/MRP protein subunit POP7; Subunit of RNase MRP, nuclear RNase P and telomerase; forms a soluble heterodimer with Pop6p that binds P3 domain of RNase MRP and RNase P RNAs; RNase MRP cleaves pre-rRNA, nuclear RNase P cleaves tRNA precursors to generate mature 5' ends and facilitates turnover of nuclear RNAs, while telomerase replenishes telomeric DNA. | 0.880 |
| GRX2 | POP8 | YDR513W | YBL018C | 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. | Ribonucleases P/MRP protein subunit POP8; Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5' ends and facilitates turnover of nuclear RNAs; relocalizes to the cytosol in response to hypoxia. | 0.961 |
| GRX2 | RPP1 | YDR513W | YHR062C | 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. | Ribonuclease P/MRP protein subunit RPP1; Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5' ends and facilitates turnover of nuclear RNAs; relocalizes to the cytosol in response to hypoxia; Belongs to the eukaryotic/archaeal RNase P protein component 3 family. | 0.876 |
| GRX2 | TRX1 | YDR513W | YLR043C | 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. | 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. | 0.912 |
| GRX2 | TRX2 | YDR513W | YGR209C | 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. | 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. | 0.928 |
| POP4 | GRX2 | YBR257W | YDR513W | RNases MRP/P 32.9 kDa subunit; Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5' ends and facilitates turnover of nuclear RNAs; binds to the RPR1 RNA subunit in RNase P. | 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. | 0.961 |
| POP4 | POP5 | YBR257W | YAL033W | RNases MRP/P 32.9 kDa subunit; Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5' ends and facilitates turnover of nuclear RNAs; binds to the RPR1 RNA subunit in RNase P. | Ribonuclease P/MRP protein subunit POP5; Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5' ends and facilitates turnover of nuclear RNAs. | 0.999 |