node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
HMS2 | HSC82 | YJR147W | YMR186W | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, that arose from the whole genome duplication. | ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. | 0.682 |
HMS2 | HSP82 | YJR147W | YPL240C | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, 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. | 0.683 |
HMS2 | SKN7 | YJR147W | YHR206W | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, that arose from the whole genome duplication. | Transcription factor SKN7; Nuclear response regulator and transcription factor; physically interacts with the Tup1-Cyc8 complex and recruits Tup1p to its targets; part of a branched two-component signaling system; required for optimal induction of heat-shock genes in response to oxidative stress; involved in osmoregulation; relocalizes to the cytosol in response to hypoxia; SKN7 has a paralog, HMS2, that arose from the whole genome duplication. | 0.625 |
HMS2 | SSA1 | YJR147W | YAL005C | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, that arose from the whole genome duplication. | Heat shock protein SSA1; ATPase involved in protein folding and NLS-directed nuclear transport; member of HSP70 family; required for ubiquitin-dependent degradation of short-lived proteins; forms chaperone complex with Ydj1p; localized to nucleus, cytoplasm, cell wall; 98% identical to paralog Ssa2p with different functional specificity in propagation of yeast [URE3] prions, vacuolar-mediated degradations of gluconeogenesis enzymes; general targeting factor of Hsp104p to prion fibrils. | 0.639 |
HMS2 | SSA2 | YJR147W | YLL024C | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, 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. | 0.644 |
HMS2 | SSA3 | YJR147W | YBL075C | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, that arose from the whole genome duplication. | Heat shock protein SSA3; ATPase involved in protein folding and the response to stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; SSA3 has a paralog, SSA4, that arose from the whole genome duplication. | 0.627 |
HMS2 | SSA4 | YJR147W | YER103W | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, that arose from the whole genome duplication. | Heat shock protein that is highly induced upon stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the HSP70 family; cytoplasmic protein that concentrates in nuclei upon starvation; SSA4 has a paralog, SSA3, that arose from the whole genome duplication. | 0.627 |
HMS2 | SSB1 | YJR147W | YDL229W | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, that arose from the whole genome duplication. | Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p; SSB1 has a paralog, SSB2, that arose from the whole genome duplication; Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily. | 0.637 |
HMS2 | SSB2 | YJR147W | YNL209W | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, that arose from the whole genome duplication. | Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in the folding of newly-synthesized polypeptide chains; member of the HSP70 family; SSB2 has a paralog, SSB1, that arose from the whole genome duplication; Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily. | 0.639 |
HMS2 | YJR149W | YJR147W | YJR149W | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, that arose from the whole genome duplication. | Putative nitronate monooxygenase; Putative protein of unknown function; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm. | 0.631 |
HSC82 | HMS2 | YMR186W | YJR147W | ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, that arose from the whole genome duplication. | 0.682 |
HSC82 | HSP82 | YMR186W | YPL240C | ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, 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. | 0.999 |
HSC82 | SKN7 | YMR186W | YHR206W | ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. | Transcription factor SKN7; Nuclear response regulator and transcription factor; physically interacts with the Tup1-Cyc8 complex and recruits Tup1p to its targets; part of a branched two-component signaling system; required for optimal induction of heat-shock genes in response to oxidative stress; involved in osmoregulation; relocalizes to the cytosol in response to hypoxia; SKN7 has a paralog, HMS2, that arose from the whole genome duplication. | 0.851 |
HSC82 | SSA1 | YMR186W | YAL005C | ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. | Heat shock protein SSA1; ATPase involved in protein folding and NLS-directed nuclear transport; member of HSP70 family; required for ubiquitin-dependent degradation of short-lived proteins; forms chaperone complex with Ydj1p; localized to nucleus, cytoplasm, cell wall; 98% identical to paralog Ssa2p with different functional specificity in propagation of yeast [URE3] prions, vacuolar-mediated degradations of gluconeogenesis enzymes; general targeting factor of Hsp104p to prion fibrils. | 0.999 |
HSC82 | SSA2 | YMR186W | YLL024C | ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, 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. | 0.991 |
HSC82 | SSA3 | YMR186W | YBL075C | ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. | Heat shock protein SSA3; ATPase involved in protein folding and the response to stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; SSA3 has a paralog, SSA4, that arose from the whole genome duplication. | 0.955 |
HSC82 | SSA4 | YMR186W | YER103W | ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. | Heat shock protein that is highly induced upon stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the HSP70 family; cytoplasmic protein that concentrates in nuclei upon starvation; SSA4 has a paralog, SSA3, that arose from the whole genome duplication. | 0.968 |
HSC82 | SSB1 | YMR186W | YDL229W | ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. | Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p; SSB1 has a paralog, SSB2, that arose from the whole genome duplication; Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily. | 0.893 |
HSC82 | SSB2 | YMR186W | YNL209W | ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. | Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in the folding of newly-synthesized polypeptide chains; member of the HSP70 family; SSB2 has a paralog, SSB1, that arose from the whole genome duplication; Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily. | 0.934 |
HSP82 | HMS2 | YPL240C | YJR147W | 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. | Protein with similarity to heat shock transcription factors; overexpression suppresses the pseudohyphal filamentation defect of a diploid mep1 mep2 homozygous null mutant; HMS2 has a paralog, SKN7, that arose from the whole genome duplication. | 0.683 |