node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ATP5 | CPR5 | YDR298C | YDR304C | Subunit 5 of the stator stalk of mitochondrial F1F0 ATP synthase; F1F0 ATP synthase is a large, evolutionarily conserved enzyme complex required for ATP synthesis; homologous to bovine subunit OSCP (oligomycin sensitivity-conferring protein); phosphorylated; Belongs to the ATPase delta chain family | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | 0.809 |
ATP5 | HSP82 | YDR298C | YPL240C | Subunit 5 of the stator stalk of mitochondrial F1F0 ATP synthase; F1F0 ATP synthase is a large, evolutionarily conserved enzyme complex required for ATP synthesis; homologous to bovine subunit OSCP (oligomycin sensitivity-conferring protein); phosphorylated; Belongs to the ATPase delta chain family | ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication | 0.463 |
ATP5 | POR1 | YDR298C | YNL055C | Subunit 5 of the stator stalk of mitochondrial F1F0 ATP synthase; F1F0 ATP synthase is a large, evolutionarily conserved enzyme complex required for ATP synthesis; homologous to bovine subunit OSCP (oligomycin sensitivity-conferring protein); phosphorylated; Belongs to the ATPase delta chain family | Mitochondrial porin (voltage-dependent anion channel); outer membrane protein required for maintenance of mitochondrial osmotic stability and mitochondrial membrane permeability; couples the glutathione pools of the intermembrane space (IMS) and the cytosol; interacts with Om45 and Om14 in the outer membrane; phosphorylated; protein abundance increases in response to DNA replication stress | 0.616 |
CPR5 | ATP5 | YDR304C | YDR298C | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | Subunit 5 of the stator stalk of mitochondrial F1F0 ATP synthase; F1F0 ATP synthase is a large, evolutionarily conserved enzyme complex required for ATP synthesis; homologous to bovine subunit OSCP (oligomycin sensitivity-conferring protein); phosphorylated; Belongs to the ATPase delta chain family | 0.809 |
CPR5 | DUG1 | YDR304C | YFR044C | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, 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 | 0.731 |
CPR5 | FPR1 | YDR304C | YNL135C | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A | 0.716 |
CPR5 | FPR2 | YDR304C | YDR519W | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | Membrane-bound peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; expression pattern suggests possible involvement in ER protein trafficking; relocalizes from nucleus to vacuole upon DNA replication stress; mutation is functionally complemented by human FKBP2 | 0.907 |
CPR5 | GUK1 | YDR304C | YDR454C | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | Guanylate kinase; converts GMP to GDP; required for growth and mannose outer chain elongation of cell wall N-linked glycoproteins | 0.765 |
CPR5 | HAM1 | YDR304C | YJR069C | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | Inosine triphosphate pyrophosphatase; Nucleoside triphosphate pyrophosphohydrolase; active against various substrates including ITP, dITP and XTP; mediates exclusion of non canonical purines, pyrimidines from dNTP pools; functions with YJL055W to mediate resistance to 5-FU; specifically reduces the incorporation of 5-FU into RNA without affecting uptake or incorporation of uracil into RNA; protein abundance increases in response to DNA replication stress; yeast HAM1 can complement knockdown of human homolog ITPA | 0.741 |
CPR5 | HSP82 | YDR304C | YPL240C | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication | 0.758 |
CPR5 | KAR2 | YDR304C | YJL034W | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | 78 kDa glucose-regulated protein homolog; ATPase involved in protein import into the ER; also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p | 0.896 |
CPR5 | PDI1 | YDR304C | YCL043C | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | Protein disulfide isomerase; multifunctional oxidoreductase of the ER lumen, essential for disulfide bond formation in secretory and cell-surface proteins, processing of non-native disulfide bonds; Ero1p activator; complexes with exomannosidase, Mnl1p to facilitate the recognition of misfolded glycoproteins and the trimming of glycan Man8GlcNAc2 to Man7GlcNAc2 on substrates, thereby accelerating ERAD; PDI1 has a paralog, EUG1, that arose from the whole genome duplication | 0.981 |
CPR5 | POR1 | YDR304C | YNL055C | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | Mitochondrial porin (voltage-dependent anion channel); outer membrane protein required for maintenance of mitochondrial osmotic stability and mitochondrial membrane permeability; couples the glutathione pools of the intermembrane space (IMS) and the cytosol; interacts with Om45 and Om14 in the outer membrane; phosphorylated; protein abundance increases in response to DNA replication stress | 0.945 |
DUG1 | CPR5 | YFR044C | YDR304C | 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 | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | 0.731 |
DUG1 | GUK1 | YFR044C | YDR454C | 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 | Guanylate kinase; converts GMP to GDP; required for growth and mannose outer chain elongation of cell wall N-linked glycoproteins | 0.803 |
DUG1 | HAM1 | YFR044C | YJR069C | 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 | Inosine triphosphate pyrophosphatase; Nucleoside triphosphate pyrophosphohydrolase; active against various substrates including ITP, dITP and XTP; mediates exclusion of non canonical purines, pyrimidines from dNTP pools; functions with YJL055W to mediate resistance to 5-FU; specifically reduces the incorporation of 5-FU into RNA without affecting uptake or incorporation of uracil into RNA; protein abundance increases in response to DNA replication stress; yeast HAM1 can complement knockdown of human homolog ITPA | 0.848 |
FPR1 | CPR5 | YNL135C | YDR304C | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | 0.716 |
FPR1 | FPR2 | YNL135C | YDR519W | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A | Membrane-bound peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; expression pattern suggests possible involvement in ER protein trafficking; relocalizes from nucleus to vacuole upon DNA replication stress; mutation is functionally complemented by human FKBP2 | 0.976 |
FPR1 | HSP82 | YNL135C | YPL240C | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A | ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication | 0.837 |
FPR2 | CPR5 | YDR519W | YDR304C | Membrane-bound peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; expression pattern suggests possible involvement in ER protein trafficking; relocalizes from nucleus to vacuole upon DNA replication stress; mutation is functionally complemented by human FKBP2 | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication | 0.907 |