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 |
| Ahsa1 | Cct3 | ENSRNOP00000065600 | ENSRNOP00000025824 | Activator of Hsp90 ATPase activity 1. | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | 0.505 |
| Ahsa1 | Cdc37 | ENSRNOP00000065600 | ENSRNOP00000051248 | Activator of Hsp90 ATPase activity 1. | Hsp90 co-chaperone Cdc37, N-terminally processed; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity. Belongs to the CDC37 family. | 0.827 |
| Ahsa1 | Dnajb1 | ENSRNOP00000065600 | ENSRNOP00000032313 | Activator of Hsp90 ATPase activity 1. | DnaJ (Hsp40) homolog, subfamily B, member 1 (Predicted), isoform CRA_a. | 0.757 |
| Ahsa1 | Hsp90aa1 | ENSRNOP00000065600 | ENSRNOP00000075715 | Activator of Hsp90 ATPase activity 1. | Heat shock protein 90 alpha family class A member 1. | 0.890 |
| Ahsa1 | Hsp90ab1 | ENSRNOP00000065600 | ENSRNOP00000026920 | Activator of Hsp90 ATPase activity 1. | Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interact [...] | 0.909 |
| Ahsa1 | Hspa4 | ENSRNOP00000065600 | ENSRNOP00000023628 | Activator of Hsp90 ATPase activity 1. | Heat shock 70 kDa protein 4; Belongs to the heat shock protein 70 family. | 0.754 |
| Ahsa1 | LOC103692716 | ENSRNOP00000065600 | ENSRNOP00000009556 | Activator of Hsp90 ATPase activity 1. | Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...] | 0.843 |
| Ahsa1 | Ptges3 | ENSRNOP00000065600 | ENSRNOP00000003787 | Activator of Hsp90 ATPase activity 1. | Prostaglandin E synthase 3; Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (By similarity). | 0.878 |
| Ahsa1 | Stip1 | ENSRNOP00000065600 | ENSRNOP00000028743 | Activator of Hsp90 ATPase activity 1. | Stress-induced-phosphoprotein 1; Acts as a co-chaperone for HSP90AA1 (By similarity). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90. | 0.969 |
| Cct3 | Ahsa1 | ENSRNOP00000025824 | ENSRNOP00000065600 | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | Activator of Hsp90 ATPase activity 1. | 0.505 |
| Cct3 | Cdc37 | ENSRNOP00000025824 | ENSRNOP00000051248 | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | Hsp90 co-chaperone Cdc37, N-terminally processed; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity. Belongs to the CDC37 family. | 0.758 |
| Cct3 | Dnajb1 | ENSRNOP00000025824 | ENSRNOP00000032313 | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | DnaJ (Hsp40) homolog, subfamily B, member 1 (Predicted), isoform CRA_a. | 0.452 |
| Cct3 | Hsp90aa1 | ENSRNOP00000025824 | ENSRNOP00000075715 | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | Heat shock protein 90 alpha family class A member 1. | 0.677 |
| Cct3 | Hsp90ab1 | ENSRNOP00000025824 | ENSRNOP00000026920 | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interact [...] | 0.918 |
| Cct3 | Hspa4 | ENSRNOP00000025824 | ENSRNOP00000023628 | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | Heat shock 70 kDa protein 4; Belongs to the heat shock protein 70 family. | 0.658 |
| Cct3 | LOC103692716 | ENSRNOP00000025824 | ENSRNOP00000009556 | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...] | 0.693 |
| Cct3 | Ptges3 | ENSRNOP00000025824 | ENSRNOP00000003787 | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | Prostaglandin E synthase 3; Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (By similarity). | 0.785 |
| Cct3 | Stip1 | ENSRNOP00000025824 | ENSRNOP00000028743 | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | Stress-induced-phosphoprotein 1; Acts as a co-chaperone for HSP90AA1 (By similarity). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90. | 0.959 |
| Cdc37 | Ahsa1 | ENSRNOP00000051248 | ENSRNOP00000065600 | Hsp90 co-chaperone Cdc37, N-terminally processed; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity. Belongs to the CDC37 family. | Activator of Hsp90 ATPase activity 1. | 0.827 |
| Cdc37 | Cct3 | ENSRNOP00000051248 | ENSRNOP00000025824 | Hsp90 co-chaperone Cdc37, N-terminally processed; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity. Belongs to the CDC37 family. | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | 0.758 |
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