| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | NOP56 | YMR186W | YLR197W | 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. | Nucleolar protein 56; Essential evolutionarily-conserved nucleolar protein; component of the box C/D snoRNP complexes that direct 2'-O-methylation of pre-rRNA during its maturation; overexpression causes spindle orientation defects. | 0.505 |
| HSC82 | NOP58 | YMR186W | YOR310C | 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. | Nucleolar protein 58; Protein involved in producing mature rRNAs and snoRNAs; involved in pre-rRNA processing, 18S rRNA synthesis, and snoRNA synthesis; component of the small subunit processome complex, which is required for processing of pre-18S rRNA. | 0.561 |
| HSC82 | PIH1 | YMR186W | YHR034C | 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 interacting with Hsp90 1; Component of the conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); R2TP complex interacts with Hsp90 (Hsp82p and Hsc82p) to mediate assembly large protein complexes such as box C/D snoRNPs and RNA polymerase II. | 0.920 |
| HSC82 | RSA1 | YMR186W | YPL193W | 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 involved in the assembly of 60S ribosomal subunits; functionally interacts with Dbp6p; functions in a late nucleoplasmic step of the assembly. | 0.471 |
| HSC82 | RVB1 | YMR186W | YDR190C | 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. | RuvB-like protein 1; ATP-dependent DNA helicase, also known as pontin; member of the AAA+ and RuvB-like protein families; similar to Rvb2p; conserved component of multiple complexes including the INO80 complex, the Swr1 complex, and the R2TP complex (Rvb1-Rvb2-Tah1-Pih1); involved in multiple processes such as chromatin remodeling, box C/D snoRNP assembly, and RNA polymerase II assembly. | 0.958 |
| HSC82 | RVB2 | YMR186W | YPL235W | 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. | RuvB-like protein 2; ATP-dependent DNA helicase, also known as reptin; member of the AAA+ and RuvB protein families, similar to Rvb1p; conserved component of multiple complexes including the INO80 complex, the Swr1 complex, and the R2TP complex (Rvb1-Rvb2-Tah1-Pih1); involved in multiple processes such as chromatin remodeling, box C/D snoRNP assembly, and RNA polymerase II assembly. | 0.955 |
| HSC82 | SNU13 | YMR186W | YEL026W | 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. | 13 kDa ribonucleoprotein-associated protein; RNA binding protein; part of U3 snoRNP involved in rRNA processing, part of U4/U6-U5 tri-snRNP involved in mRNA splicing, similar to human 15.5K protein; Belongs to the eukaryotic ribosomal protein eL8 family. | 0.556 |
| HSC82 | TAH1 | YMR186W | YCR060W | 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. | TPR repeat-containing protein associated with Hsp90; Component of conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); R2TP complex interacts with Hsp90 (Hsp82p and Hsc82p) to mediate assembly of large protein complexes such as box C/D snoRNPs and RNA polymerase II; contains a single TPR domain with at least two TPR motifs; plays a role in determining prion variants. | 0.839 |
| HSC82 | TTI1 | YMR186W | YKL033W | 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. | TEL2-interacting protein 1; Subunit of the ASTRA complex, involved in chromatin remodeling; telomere length regulator involved in the stability or biogenesis of PIKKs such as TORC1; similar to S. pombe Tti1p; detected in highly purified mitochondria in high-throughput studies. | 0.921 |
| HSP82 | HSC82 | YPL240C | YMR186W | 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. | 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. | 0.999 |
| HSP82 | NOP56 | YPL240C | YLR197W | 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. | Nucleolar protein 56; Essential evolutionarily-conserved nucleolar protein; component of the box C/D snoRNP complexes that direct 2'-O-methylation of pre-rRNA during its maturation; overexpression causes spindle orientation defects. | 0.614 |
| HSP82 | NOP58 | YPL240C | YOR310C | 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. | Nucleolar protein 58; Protein involved in producing mature rRNAs and snoRNAs; involved in pre-rRNA processing, 18S rRNA synthesis, and snoRNA synthesis; component of the small subunit processome complex, which is required for processing of pre-18S rRNA. | 0.558 |
| HSP82 | PIH1 | YPL240C | YHR034C | 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 interacting with Hsp90 1; Component of the conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); R2TP complex interacts with Hsp90 (Hsp82p and Hsc82p) to mediate assembly large protein complexes such as box C/D snoRNPs and RNA polymerase II. | 0.967 |
| HSP82 | RSA1 | YPL240C | YPL193W | 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 involved in the assembly of 60S ribosomal subunits; functionally interacts with Dbp6p; functions in a late nucleoplasmic step of the assembly. | 0.496 |
| HSP82 | RVB1 | YPL240C | YDR190C | 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. | RuvB-like protein 1; ATP-dependent DNA helicase, also known as pontin; member of the AAA+ and RuvB-like protein families; similar to Rvb2p; conserved component of multiple complexes including the INO80 complex, the Swr1 complex, and the R2TP complex (Rvb1-Rvb2-Tah1-Pih1); involved in multiple processes such as chromatin remodeling, box C/D snoRNP assembly, and RNA polymerase II assembly. | 0.939 |
| HSP82 | RVB2 | YPL240C | YPL235W | 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. | RuvB-like protein 2; ATP-dependent DNA helicase, also known as reptin; member of the AAA+ and RuvB protein families, similar to Rvb1p; conserved component of multiple complexes including the INO80 complex, the Swr1 complex, and the R2TP complex (Rvb1-Rvb2-Tah1-Pih1); involved in multiple processes such as chromatin remodeling, box C/D snoRNP assembly, and RNA polymerase II assembly. | 0.939 |
| HSP82 | SNU13 | YPL240C | YEL026W | 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. | 13 kDa ribonucleoprotein-associated protein; RNA binding protein; part of U3 snoRNP involved in rRNA processing, part of U4/U6-U5 tri-snRNP involved in mRNA splicing, similar to human 15.5K protein; Belongs to the eukaryotic ribosomal protein eL8 family. | 0.529 |
| HSP82 | TAH1 | YPL240C | YCR060W | 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. | TPR repeat-containing protein associated with Hsp90; Component of conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); R2TP complex interacts with Hsp90 (Hsp82p and Hsc82p) to mediate assembly of large protein complexes such as box C/D snoRNPs and RNA polymerase II; contains a single TPR domain with at least two TPR motifs; plays a role in determining prion variants. | 0.957 |
| HSP82 | TTI1 | YPL240C | YKL033W | 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. | TEL2-interacting protein 1; Subunit of the ASTRA complex, involved in chromatin remodeling; telomere length regulator involved in the stability or biogenesis of PIKKs such as TORC1; similar to S. pombe Tti1p; detected in highly purified mitochondria in high-throughput studies. | 0.902 |