node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
FZO1 | VPS30 | YBR179C | YPL120W | Mitofusin; integral membrane protein involved in mitochondrial outer membrane tethering and fusion; role in mitochondrial genome maintenance; efficient tethering and degradation of Fzo1p requires an intact N-terminal GTPase domain; targeted for destruction by the ubiquitin ligase SCF-Mdm30p and the cytosolic ubiquitin-proteasome system; Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily. | Vacuolar protein sorting-associated protein 30; Subunit of phosphatidylinositol (PtdIns) 3-kinase complexes I and II; Complex I is essential in autophagy, Complex II is required for vacuolar protein sorting; required for overflow degradation of misfolded proteins when ERAD is saturated; C-terminus has novel globular fold essential for autophagy through the targeting of the PI3-kinase complex I to the pre-autophagosomal structure; ortholog of higher eukaryote gene Beclin 1; human BECN1 can complement yeast null mutant. | 0.620 |
GCN2 | HSC82 | YDR283C | YMR186W | eIF-2-alpha kinase GCN2; Protein kinase; phosphorylates the alpha-subunit of translation initiation factor eIF2 (Sui2p) in response to starvation; activated by uncharged tRNAs and the Gcn1p-Gcn20p complex; contributes to DNA damage checkpoint control. | 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. | 0.601 |
GCN2 | HSP82 | YDR283C | YPL240C | eIF-2-alpha kinase GCN2; Protein kinase; phosphorylates the alpha-subunit of translation initiation factor eIF2 (Sui2p) in response to starvation; activated by uncharged tRNAs and the Gcn1p-Gcn20p complex; contributes to DNA damage checkpoint control. | 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. | 0.724 |
HSC82 | GCN2 | YMR186W | YDR283C | 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. | eIF-2-alpha kinase GCN2; Protein kinase; phosphorylates the alpha-subunit of translation initiation factor eIF2 (Sui2p) in response to starvation; activated by uncharged tRNAs and the Gcn1p-Gcn20p complex; contributes to DNA damage checkpoint control. | 0.601 |
HSC82 | HSF1 | YMR186W | YGL073W | 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. | Trimeric heat shock transcription factor; activates multiple genes in response to highly diverse stresses; recognizes variable heat shock elements (HSEs) consisting of inverted NGAAN repeats; monitors translational status of cell through an RQC (Ribosomal Quality Control)-mediated translation-stress signal; involved in diauxic shift; posttranslationally regulated; human homolog HSF1 with linker region mutations can complement yeast hsf1 mutant; Belongs to the HSF family. | 0.991 |
HSC82 | HSP104 | YMR186W | YLL026W | 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. | Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation; Belongs to the ClpA/ClpB family. | 0.980 |
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 | VPS30 | YMR186W | YPL120W | 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. | Vacuolar protein sorting-associated protein 30; Subunit of phosphatidylinositol (PtdIns) 3-kinase complexes I and II; Complex I is essential in autophagy, Complex II is required for vacuolar protein sorting; required for overflow degradation of misfolded proteins when ERAD is saturated; C-terminus has novel globular fold essential for autophagy through the targeting of the PI3-kinase complex I to the pre-autophagosomal structure; ortholog of higher eukaryote gene Beclin 1; human BECN1 can complement yeast null mutant. | 0.740 |
HSC82 | YDJ1 | YMR186W | YNL064C | 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. | Mitochondrial protein import protein MAS5; Type I HSP40 co-chaperone; involved in regulation of HSP90 and HSP70 functions; acts as an adaptor that helps Rsp5p recognize cytosolic misfolded proteins for ubiquitination after heat shock; critical for determining cell size at Start as a function of growth rate; involved in protein translocation across membranes; member of the DnaJ family; chimeric protein in which human p58IPK J domain replaces yeast Ydj1p J domain can complement yeast ydj1 mutant. | 0.999 |
HSF1 | HSC82 | YGL073W | YMR186W | Trimeric heat shock transcription factor; activates multiple genes in response to highly diverse stresses; recognizes variable heat shock elements (HSEs) consisting of inverted NGAAN repeats; monitors translational status of cell through an RQC (Ribosomal Quality Control)-mediated translation-stress signal; involved in diauxic shift; posttranslationally regulated; human homolog HSF1 with linker region mutations can complement yeast hsf1 mutant; Belongs to the HSF family. | 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. | 0.991 |
HSF1 | HSP104 | YGL073W | YLL026W | Trimeric heat shock transcription factor; activates multiple genes in response to highly diverse stresses; recognizes variable heat shock elements (HSEs) consisting of inverted NGAAN repeats; monitors translational status of cell through an RQC (Ribosomal Quality Control)-mediated translation-stress signal; involved in diauxic shift; posttranslationally regulated; human homolog HSF1 with linker region mutations can complement yeast hsf1 mutant; Belongs to the HSF family. | Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation; Belongs to the ClpA/ClpB family. | 0.885 |
HSF1 | HSP82 | YGL073W | YPL240C | Trimeric heat shock transcription factor; activates multiple genes in response to highly diverse stresses; recognizes variable heat shock elements (HSEs) consisting of inverted NGAAN repeats; monitors translational status of cell through an RQC (Ribosomal Quality Control)-mediated translation-stress signal; involved in diauxic shift; posttranslationally regulated; human homolog HSF1 with linker region mutations can complement yeast hsf1 mutant; Belongs to the HSF 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. | 0.982 |
HSF1 | YDJ1 | YGL073W | YNL064C | Trimeric heat shock transcription factor; activates multiple genes in response to highly diverse stresses; recognizes variable heat shock elements (HSEs) consisting of inverted NGAAN repeats; monitors translational status of cell through an RQC (Ribosomal Quality Control)-mediated translation-stress signal; involved in diauxic shift; posttranslationally regulated; human homolog HSF1 with linker region mutations can complement yeast hsf1 mutant; Belongs to the HSF family. | Mitochondrial protein import protein MAS5; Type I HSP40 co-chaperone; involved in regulation of HSP90 and HSP70 functions; acts as an adaptor that helps Rsp5p recognize cytosolic misfolded proteins for ubiquitination after heat shock; critical for determining cell size at Start as a function of growth rate; involved in protein translocation across membranes; member of the DnaJ family; chimeric protein in which human p58IPK J domain replaces yeast Ydj1p J domain can complement yeast ydj1 mutant. | 0.794 |
HSP104 | HSC82 | YLL026W | YMR186W | Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation; Belongs to the ClpA/ClpB family. | 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. | 0.980 |
HSP104 | HSF1 | YLL026W | YGL073W | Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation; Belongs to the ClpA/ClpB family. | Trimeric heat shock transcription factor; activates multiple genes in response to highly diverse stresses; recognizes variable heat shock elements (HSEs) consisting of inverted NGAAN repeats; monitors translational status of cell through an RQC (Ribosomal Quality Control)-mediated translation-stress signal; involved in diauxic shift; posttranslationally regulated; human homolog HSF1 with linker region mutations can complement yeast hsf1 mutant; Belongs to the HSF family. | 0.885 |
HSP104 | HSP82 | YLL026W | YPL240C | Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation; Belongs to the ClpA/ClpB 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. | 0.995 |
HSP104 | YDJ1 | YLL026W | YNL064C | Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation; Belongs to the ClpA/ClpB family. | Mitochondrial protein import protein MAS5; Type I HSP40 co-chaperone; involved in regulation of HSP90 and HSP70 functions; acts as an adaptor that helps Rsp5p recognize cytosolic misfolded proteins for ubiquitination after heat shock; critical for determining cell size at Start as a function of growth rate; involved in protein translocation across membranes; member of the DnaJ family; chimeric protein in which human p58IPK J domain replaces yeast Ydj1p J domain can complement yeast ydj1 mutant. | 0.999 |
HSP82 | GCN2 | YPL240C | YDR283C | 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. | eIF-2-alpha kinase GCN2; Protein kinase; phosphorylates the alpha-subunit of translation initiation factor eIF2 (Sui2p) in response to starvation; activated by uncharged tRNAs and the Gcn1p-Gcn20p complex; contributes to DNA damage checkpoint control. | 0.724 |
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 | HSF1 | YPL240C | YGL073W | 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. | Trimeric heat shock transcription factor; activates multiple genes in response to highly diverse stresses; recognizes variable heat shock elements (HSEs) consisting of inverted NGAAN repeats; monitors translational status of cell through an RQC (Ribosomal Quality Control)-mediated translation-stress signal; involved in diauxic shift; posttranslationally regulated; human homolog HSF1 with linker region mutations can complement yeast hsf1 mutant; Belongs to the HSF family. | 0.982 |