Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AHA1 | CDC37 | YDR214W | YDR168W | Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family. | Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family. | 0.996 |
| AHA1 | CNS1 | YDR214W | YBR155W | Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family. | Hsp70/Hsp90 co-chaperone CNS1; TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70); stimulates ATPase activity of Ssa1p; ts mutants reduce Hsp82p function, overexpression suppresses phenotypes of HSP82 ts allele and cpr7 deletion; human homolog TTC4 complements yeast cns1 mutant; Belongs to the TTC4 family. | 0.572 |
| AHA1 | HCH1 | YDR214W | YNL281W | Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family. | Hsp90 co-chaperone HCH1; Heat shock protein regulator; binds to Hsp90p and may stimulate ATPase activity; originally identified as a high-copy number suppressor of a HSP90 loss-of-function mutation; role in regulating Hsp90 inhibitor drug sensitivity; GFP-fusion protein localizes to the cytoplasm and nucleus; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family. | 0.997 |
| AHA1 | HSC82 | YDR214W | YMR186W | Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 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. | 0.999 |
| AHA1 | HSP82 | YDR214W | YPL240C | Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 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. | 0.999 |
| AHA1 | PPT1 | YDR214W | YGR123C | Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family. | Protein serine/threonine phosphatase; regulates Hsp90 chaperone by affecting its ATPase and cochaperone binding activities; has similarity to human phosphatase PP5; present in both the nucleus and cytoplasm; expressed during logarithmic growth; Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily. | 0.735 |
| AHA1 | SBA1 | YDR214W | YKL117W | Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family. | Co-chaperone protein SBA1; Co-chaperone that binds and regulates Hsp90 family chaperones; plays a role in determining prion variants; important for pp60v-src activity in yeast; homologous to the mammalian p23 proteins, and like p23 can regulate telomerase activity; protein abundance increases in response to DNA replication stress; Belongs to the p23/wos2 family. | 0.997 |
| CDC37 | AHA1 | YDR168W | YDR214W | Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family. | Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family. | 0.996 |
| CDC37 | CNS1 | YDR168W | YBR155W | Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family. | Hsp70/Hsp90 co-chaperone CNS1; TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70); stimulates ATPase activity of Ssa1p; ts mutants reduce Hsp82p function, overexpression suppresses phenotypes of HSP82 ts allele and cpr7 deletion; human homolog TTC4 complements yeast cns1 mutant; Belongs to the TTC4 family. | 0.774 |
| CDC37 | HCH1 | YDR168W | YNL281W | Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family. | Hsp90 co-chaperone HCH1; Heat shock protein regulator; binds to Hsp90p and may stimulate ATPase activity; originally identified as a high-copy number suppressor of a HSP90 loss-of-function mutation; role in regulating Hsp90 inhibitor drug sensitivity; GFP-fusion protein localizes to the cytoplasm and nucleus; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family. | 0.921 |
| CDC37 | HSC82 | YDR168W | YMR186W | Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 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. | 0.999 |
| CDC37 | HSP82 | YDR168W | YPL240C | Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 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. | 0.999 |
| CDC37 | PPT1 | YDR168W | YGR123C | Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family. | Protein serine/threonine phosphatase; regulates Hsp90 chaperone by affecting its ATPase and cochaperone binding activities; has similarity to human phosphatase PP5; present in both the nucleus and cytoplasm; expressed during logarithmic growth; Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily. | 0.955 |
| CDC37 | SBA1 | YDR168W | YKL117W | Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family. | Co-chaperone protein SBA1; Co-chaperone that binds and regulates Hsp90 family chaperones; plays a role in determining prion variants; important for pp60v-src activity in yeast; homologous to the mammalian p23 proteins, and like p23 can regulate telomerase activity; protein abundance increases in response to DNA replication stress; Belongs to the p23/wos2 family. | 0.994 |
| CNS1 | AHA1 | YBR155W | YDR214W | Hsp70/Hsp90 co-chaperone CNS1; TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70); stimulates ATPase activity of Ssa1p; ts mutants reduce Hsp82p function, overexpression suppresses phenotypes of HSP82 ts allele and cpr7 deletion; human homolog TTC4 complements yeast cns1 mutant; Belongs to the TTC4 family. | Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family. | 0.572 |
| CNS1 | CDC37 | YBR155W | YDR168W | Hsp70/Hsp90 co-chaperone CNS1; TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70); stimulates ATPase activity of Ssa1p; ts mutants reduce Hsp82p function, overexpression suppresses phenotypes of HSP82 ts allele and cpr7 deletion; human homolog TTC4 complements yeast cns1 mutant; Belongs to the TTC4 family. | Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family. | 0.774 |
| CNS1 | HCH1 | YBR155W | YNL281W | Hsp70/Hsp90 co-chaperone CNS1; TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70); stimulates ATPase activity of Ssa1p; ts mutants reduce Hsp82p function, overexpression suppresses phenotypes of HSP82 ts allele and cpr7 deletion; human homolog TTC4 complements yeast cns1 mutant; Belongs to the TTC4 family. | Hsp90 co-chaperone HCH1; Heat shock protein regulator; binds to Hsp90p and may stimulate ATPase activity; originally identified as a high-copy number suppressor of a HSP90 loss-of-function mutation; role in regulating Hsp90 inhibitor drug sensitivity; GFP-fusion protein localizes to the cytoplasm and nucleus; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family. | 0.648 |
| CNS1 | HSC82 | YBR155W | YMR186W | Hsp70/Hsp90 co-chaperone CNS1; TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70); stimulates ATPase activity of Ssa1p; ts mutants reduce Hsp82p function, overexpression suppresses phenotypes of HSP82 ts allele and cpr7 deletion; human homolog TTC4 complements yeast cns1 mutant; Belongs to the TTC4 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. | 0.949 |
| CNS1 | HSP82 | YBR155W | YPL240C | Hsp70/Hsp90 co-chaperone CNS1; TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70); stimulates ATPase activity of Ssa1p; ts mutants reduce Hsp82p function, overexpression suppresses phenotypes of HSP82 ts allele and cpr7 deletion; human homolog TTC4 complements yeast cns1 mutant; Belongs to the TTC4 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. | 0.984 |
| CNS1 | PPT1 | YBR155W | YGR123C | Hsp70/Hsp90 co-chaperone CNS1; TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70); stimulates ATPase activity of Ssa1p; ts mutants reduce Hsp82p function, overexpression suppresses phenotypes of HSP82 ts allele and cpr7 deletion; human homolog TTC4 complements yeast cns1 mutant; Belongs to the TTC4 family. | Protein serine/threonine phosphatase; regulates Hsp90 chaperone by affecting its ATPase and cochaperone binding activities; has similarity to human phosphatase PP5; present in both the nucleus and cytoplasm; expressed during logarithmic growth; Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily. | 0.620 |
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