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 | 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 |
| HSC82 | AHA1 | YMR186W | YDR214W | 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. | 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. | 0.999 |
| 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 |
| HSP82 | AHA1 | YPL240C | YDR214W | 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. | 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. | 0.999 |
| 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 |
| LAM4 | SIP3 | YHR080C | YNL257C | Membrane-anchored lipid-binding protein LAM4; Sterol-binding protein that localizes to puncta in the cortical ER; sterol binding occurs via two StART-like domains; one of six StART-like domain-containing proteins in yeast that may be involved in intracellular sterol transfer between membranes; conserved across eukaryotes; has both GRAM and StART-like (VASt) domains; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies. | Membrane-anchored lipid-binding protein SIP3; Putative sterol transfer protein; has a probable role in retrograde transport of sterols from the plasma membrane to the ER; co-localizes to puncta in the cortical ER with Ysp2p; contains GRAM, StART-like (VASt) and two PH-like domains; one of 6 StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes; previously identified as a transcription cofactor that interacts with DNA-bound Snf1p. | 0.920 |
| LAM4 | YSP2 | YHR080C | YDR326C | Membrane-anchored lipid-binding protein LAM4; Sterol-binding protein that localizes to puncta in the cortical ER; sterol binding occurs via two StART-like domains; one of six StART-like domain-containing proteins in yeast that may be involved in intracellular sterol transfer between membranes; conserved across eukaryotes; has both GRAM and StART-like (VASt) domains; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies. | Membrane-anchored lipid-binding protein YSP2; Sterol-binding protein; has a probable role in retrograde transport of sterols from the plasma membrane to the ER; contains two StART-like domains that bind sterols and a GRAM domain; co-localizes to puncta in the cortical ER with Sip3p; one of six StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes. | 0.552 |
| SIP3 | LAM4 | YNL257C | YHR080C | Membrane-anchored lipid-binding protein SIP3; Putative sterol transfer protein; has a probable role in retrograde transport of sterols from the plasma membrane to the ER; co-localizes to puncta in the cortical ER with Ysp2p; contains GRAM, StART-like (VASt) and two PH-like domains; one of 6 StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes; previously identified as a transcription cofactor that interacts with DNA-bound Snf1p. | Membrane-anchored lipid-binding protein LAM4; Sterol-binding protein that localizes to puncta in the cortical ER; sterol binding occurs via two StART-like domains; one of six StART-like domain-containing proteins in yeast that may be involved in intracellular sterol transfer between membranes; conserved across eukaryotes; has both GRAM and StART-like (VASt) domains; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies. | 0.920 |
| SIP3 | YSP2 | YNL257C | YDR326C | Membrane-anchored lipid-binding protein SIP3; Putative sterol transfer protein; has a probable role in retrograde transport of sterols from the plasma membrane to the ER; co-localizes to puncta in the cortical ER with Ysp2p; contains GRAM, StART-like (VASt) and two PH-like domains; one of 6 StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes; previously identified as a transcription cofactor that interacts with DNA-bound Snf1p. | Membrane-anchored lipid-binding protein YSP2; Sterol-binding protein; has a probable role in retrograde transport of sterols from the plasma membrane to the ER; contains two StART-like domains that bind sterols and a GRAM domain; co-localizes to puncta in the cortical ER with Sip3p; one of six StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes. | 0.912 |
| YSP2 | LAM4 | YDR326C | YHR080C | Membrane-anchored lipid-binding protein YSP2; Sterol-binding protein; has a probable role in retrograde transport of sterols from the plasma membrane to the ER; contains two StART-like domains that bind sterols and a GRAM domain; co-localizes to puncta in the cortical ER with Sip3p; one of six StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes. | Membrane-anchored lipid-binding protein LAM4; Sterol-binding protein that localizes to puncta in the cortical ER; sterol binding occurs via two StART-like domains; one of six StART-like domain-containing proteins in yeast that may be involved in intracellular sterol transfer between membranes; conserved across eukaryotes; has both GRAM and StART-like (VASt) domains; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies. | 0.552 |
| YSP2 | SIP3 | YDR326C | YNL257C | Membrane-anchored lipid-binding protein YSP2; Sterol-binding protein; has a probable role in retrograde transport of sterols from the plasma membrane to the ER; contains two StART-like domains that bind sterols and a GRAM domain; co-localizes to puncta in the cortical ER with Sip3p; one of six StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes. | Membrane-anchored lipid-binding protein SIP3; Putative sterol transfer protein; has a probable role in retrograde transport of sterols from the plasma membrane to the ER; co-localizes to puncta in the cortical ER with Ysp2p; contains GRAM, StART-like (VASt) and two PH-like domains; one of 6 StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes; previously identified as a transcription cofactor that interacts with DNA-bound Snf1p. | 0.912 |