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 |
| BTN2 | HSC82 | YGR142W | YMR186W | v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress. | 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. | 0.550 |
| BTN2 | HSP30 | YGR142W | YCR021C | v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress. | 30 kDa heat shock protein; Negative regulator of the H(+)-ATPase Pma1p; stress-responsive protein; hydrophobic plasma membrane localized; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase; Belongs to the archaeal/bacterial/fungal opsin family. | 0.921 |
| BTN2 | HSP82 | YGR142W | YPL240C | v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress. | 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. | 0.809 |
| BTN2 | RHB1 | YGR142W | YCR027C | v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress. | Rheb-like protein RHB1; Putative Rheb-related GTPase; involved in regulating canavanine resistance and arginine uptake; member of the Ras superfamily of G-proteins. | 0.950 |
| BTN2 | YHC3 | YGR142W | YJL059W | v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress. | Protein required for the ATP-dependent transport of arginine; vacuolar membrane protein; involved in the ATP-dependent transport of arginine into the vacuole and possibly in balancing ion homeostasis; human homolog CLN3 involved in Batten disease (juvenile onset neuronal ceroid lipofuscinosis) can complement yeast null mutant; Belongs to the battenin family. | 0.964 |
| HSC82 | BTN2 | YMR186W | YGR142W | 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. | v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress. | 0.550 |
| HSC82 | HSP30 | YMR186W | YCR021C | 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. | 30 kDa heat shock protein; Negative regulator of the H(+)-ATPase Pma1p; stress-responsive protein; hydrophobic plasma membrane localized; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase; Belongs to the archaeal/bacterial/fungal opsin family. | 0.717 |
| 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 | RHB1 | YMR186W | YCR027C | 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. | Rheb-like protein RHB1; Putative Rheb-related GTPase; involved in regulating canavanine resistance and arginine uptake; member of the Ras superfamily of G-proteins. | 0.928 |
| HSC82 | TOR1 | YMR186W | YJR066W | 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. | Serine/threonine-protein kinase TOR1; PIK-related protein kinase and rapamycin target; subunit of TORC1, a complex that controls growth in response to nutrients by regulating translation, transcription, ribosome biogenesis, nutrient transport and autophagy; involved in meiosis; TOR1 has a paralog, TOR2, that arose from the whole genome duplication; Belongs to the PI3/PI4-kinase family. | 0.854 |
| HSC82 | TOR2 | YMR186W | YKL203C | 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. | Serine/threonine-protein kinase TOR2; PIK-related protein kinase and rapamycin target; subunit of TORC1, a complex that regulates growth in response to nutrients and TORC2, a complex that regulates cell-cycle dependent polarization of the actin cytoskeleton; involved in meiosis; TOR2 has a paralog, TOR1, that arose from the whole genome duplication. | 0.794 |
| HSP30 | BTN2 | YCR021C | YGR142W | 30 kDa heat shock protein; Negative regulator of the H(+)-ATPase Pma1p; stress-responsive protein; hydrophobic plasma membrane localized; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase; Belongs to the archaeal/bacterial/fungal opsin family. | v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress. | 0.921 |
| HSP30 | HSC82 | YCR021C | YMR186W | 30 kDa heat shock protein; Negative regulator of the H(+)-ATPase Pma1p; stress-responsive protein; hydrophobic plasma membrane localized; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase; Belongs to the archaeal/bacterial/fungal opsin 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. | 0.717 |
| HSP30 | HSP82 | YCR021C | YPL240C | 30 kDa heat shock protein; Negative regulator of the H(+)-ATPase Pma1p; stress-responsive protein; hydrophobic plasma membrane localized; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase; Belongs to the archaeal/bacterial/fungal opsin 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. | 0.825 |
| HSP30 | RHB1 | YCR021C | YCR027C | 30 kDa heat shock protein; Negative regulator of the H(+)-ATPase Pma1p; stress-responsive protein; hydrophobic plasma membrane localized; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase; Belongs to the archaeal/bacterial/fungal opsin family. | Rheb-like protein RHB1; Putative Rheb-related GTPase; involved in regulating canavanine resistance and arginine uptake; member of the Ras superfamily of G-proteins. | 0.898 |
| HSP30 | YHC3 | YCR021C | YJL059W | 30 kDa heat shock protein; Negative regulator of the H(+)-ATPase Pma1p; stress-responsive protein; hydrophobic plasma membrane localized; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase; Belongs to the archaeal/bacterial/fungal opsin family. | Protein required for the ATP-dependent transport of arginine; vacuolar membrane protein; involved in the ATP-dependent transport of arginine into the vacuole and possibly in balancing ion homeostasis; human homolog CLN3 involved in Batten disease (juvenile onset neuronal ceroid lipofuscinosis) can complement yeast null mutant; Belongs to the battenin family. | 0.932 |
| HSP82 | BTN2 | YPL240C | YGR142W | 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. | v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress. | 0.809 |
| 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 | HSP30 | YPL240C | YCR021C | 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. | 30 kDa heat shock protein; Negative regulator of the H(+)-ATPase Pma1p; stress-responsive protein; hydrophobic plasma membrane localized; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase; Belongs to the archaeal/bacterial/fungal opsin family. | 0.825 |
| HSP82 | RHB1 | YPL240C | YCR027C | 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. | Rheb-like protein RHB1; Putative Rheb-related GTPase; involved in regulating canavanine resistance and arginine uptake; member of the Ras superfamily of G-proteins. | 0.928 |
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