| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AAP1 | APE3 | YHR047C | YBR286W | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | Vacuolar aminopeptidase Y; processed to mature form by Prb1p. | 0.773 |
| AAP1 | DUG1 | YHR047C | YFR044C | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | Cys-Gly metallodipeptidase DUG1; Cys-Gly metallo-di-peptidase; forms a complex with Dug2p and Dug3p to degrade glutathione (GSH) and other peptides containing a gamma-glu-X bond in an alternative pathway to GSH degradation by gamma-glutamyl transpeptidase (Ecm38p); human homolog CNDP2 can complement yeast dug1 mutant. | 0.766 |
| AAP1 | ILV2 | YHR047C | YMR108W | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | Acetolactate synthase catalytic subunit, mitochondrial; Acetolactate synthase; catalyses the first common step in isoleucine and valine biosynthesis and is the target of several classes of inhibitors, localizes to the mitochondria; expression of the gene is under general amino acid control; Belongs to the TPP enzyme family. | 0.773 |
| AAP1 | LPD1 | YHR047C | YFL018C | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; the lipoamide dehydrogenase component (E3) of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multi-enzyme complexes; PDH complex is concentrated in spots within the mitochondrial matrix, often near the ERMES complex and near peroxisomes; LPD1 has a paralog, IRC15, that arose from the whole genome duplication; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | 0.827 |
| AAP1 | PEP3 | YHR047C | YLR148W | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | Component of CORVET membrane tethering complex; vacuolar peripheral membrane protein that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins, required for vacuolar biogenesis. | 0.848 |
| AAP1 | PGK1 | YHR047C | YCR012W | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | 3-phosphoglycerate kinase; catalyzes transfer of high-energy phosphoryl groups from the acyl phosphate of 1,3-bisphosphoglycerate to ADP to produce ATP; key enzyme in glycolysis and gluconeogenesis. | 0.805 |
| AAP1 | PUF3 | YHR047C | YLL013C | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | mRNA-binding protein PUF3; Protein of the mitochondrial outer surface; links the Arp2/3 complex with the mitochore during anterograde mitochondrial movement; also binds to and promotes degradation of mRNAs for select nuclear-encoded mitochondrial proteins. | 0.803 |
| AAP1 | RSM27 | YHR047C | YGR215W | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | Mitochondrial ribosomal protein of the small subunit. | 0.772 |
| AAP1 | SSA2 | YHR047C | YLL024C | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | Heat shock protein SSA2; HSP70 family ATP-binding protein; involved in protein folding, vacuolar import of proteins; required for ubiquitin-dependent degradation of short-lived proteins; associated with chaperonin-containing T-complex; 98% identical to paralog Ssa1p with distinct functional specificity in propagation of yeast [URE3] prions and vacuolar-mediated degradation of gluconeogenesis enzymes; binds tRNA, has role in tRNA nuclear import during starvation. | 0.778 |
| AAP1 | TPI1 | YHR047C | YDR050C | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5' non-coding region; inhibition of Tpi1p activity by PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human homolog TPI1 causes a rare autosomal disease; human TPI1 can complement yeast null mutant. | 0.778 |
| APE3 | AAP1 | YBR286W | YHR047C | Vacuolar aminopeptidase Y; processed to mature form by Prb1p. | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | 0.773 |
| DUG1 | AAP1 | YFR044C | YHR047C | Cys-Gly metallodipeptidase DUG1; Cys-Gly metallo-di-peptidase; forms a complex with Dug2p and Dug3p to degrade glutathione (GSH) and other peptides containing a gamma-glu-X bond in an alternative pathway to GSH degradation by gamma-glutamyl transpeptidase (Ecm38p); human homolog CNDP2 can complement yeast dug1 mutant. | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | 0.766 |
| DUG1 | TPI1 | YFR044C | YDR050C | Cys-Gly metallodipeptidase DUG1; Cys-Gly metallo-di-peptidase; forms a complex with Dug2p and Dug3p to degrade glutathione (GSH) and other peptides containing a gamma-glu-X bond in an alternative pathway to GSH degradation by gamma-glutamyl transpeptidase (Ecm38p); human homolog CNDP2 can complement yeast dug1 mutant. | Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5' non-coding region; inhibition of Tpi1p activity by PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human homolog TPI1 causes a rare autosomal disease; human TPI1 can complement yeast null mutant. | 0.640 |
| ILV2 | AAP1 | YMR108W | YHR047C | Acetolactate synthase catalytic subunit, mitochondrial; Acetolactate synthase; catalyses the first common step in isoleucine and valine biosynthesis and is the target of several classes of inhibitors, localizes to the mitochondria; expression of the gene is under general amino acid control; Belongs to the TPP enzyme family. | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | 0.773 |
| ILV2 | LPD1 | YMR108W | YFL018C | Acetolactate synthase catalytic subunit, mitochondrial; Acetolactate synthase; catalyses the first common step in isoleucine and valine biosynthesis and is the target of several classes of inhibitors, localizes to the mitochondria; expression of the gene is under general amino acid control; Belongs to the TPP enzyme family. | Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; the lipoamide dehydrogenase component (E3) of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multi-enzyme complexes; PDH complex is concentrated in spots within the mitochondrial matrix, often near the ERMES complex and near peroxisomes; LPD1 has a paralog, IRC15, that arose from the whole genome duplication; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | 0.680 |
| ILV2 | PGK1 | YMR108W | YCR012W | Acetolactate synthase catalytic subunit, mitochondrial; Acetolactate synthase; catalyses the first common step in isoleucine and valine biosynthesis and is the target of several classes of inhibitors, localizes to the mitochondria; expression of the gene is under general amino acid control; Belongs to the TPP enzyme family. | 3-phosphoglycerate kinase; catalyzes transfer of high-energy phosphoryl groups from the acyl phosphate of 1,3-bisphosphoglycerate to ADP to produce ATP; key enzyme in glycolysis and gluconeogenesis. | 0.576 |
| ILV2 | PUF3 | YMR108W | YLL013C | Acetolactate synthase catalytic subunit, mitochondrial; Acetolactate synthase; catalyses the first common step in isoleucine and valine biosynthesis and is the target of several classes of inhibitors, localizes to the mitochondria; expression of the gene is under general amino acid control; Belongs to the TPP enzyme family. | mRNA-binding protein PUF3; Protein of the mitochondrial outer surface; links the Arp2/3 complex with the mitochore during anterograde mitochondrial movement; also binds to and promotes degradation of mRNAs for select nuclear-encoded mitochondrial proteins. | 0.475 |
| ILV2 | TPI1 | YMR108W | YDR050C | Acetolactate synthase catalytic subunit, mitochondrial; Acetolactate synthase; catalyses the first common step in isoleucine and valine biosynthesis and is the target of several classes of inhibitors, localizes to the mitochondria; expression of the gene is under general amino acid control; Belongs to the TPP enzyme family. | Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5' non-coding region; inhibition of Tpi1p activity by PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human homolog TPI1 causes a rare autosomal disease; human TPI1 can complement yeast null mutant. | 0.451 |
| LPD1 | AAP1 | YFL018C | YHR047C | Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; the lipoamide dehydrogenase component (E3) of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multi-enzyme complexes; PDH complex is concentrated in spots within the mitochondrial matrix, often near the ERMES complex and near peroxisomes; LPD1 has a paralog, IRC15, that arose from the whole genome duplication; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication. | 0.827 |
| LPD1 | ILV2 | YFL018C | YMR108W | Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; the lipoamide dehydrogenase component (E3) of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multi-enzyme complexes; PDH complex is concentrated in spots within the mitochondrial matrix, often near the ERMES complex and near peroxisomes; LPD1 has a paralog, IRC15, that arose from the whole genome duplication; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | Acetolactate synthase catalytic subunit, mitochondrial; Acetolactate synthase; catalyses the first common step in isoleucine and valine biosynthesis and is the target of several classes of inhibitors, localizes to the mitochondria; expression of the gene is under general amino acid control; Belongs to the TPP enzyme family. | 0.680 |
