| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CDC37L1 | G1SWK6_RABIT | ENSOCUP00000003006 | ENSOCUP00000007873 | Cell division cycle 37 like 1. | HATPase_c domain-containing protein. | 0.854 |
| CDC37L1 | G1T464_RABIT | ENSOCUP00000003006 | ENSOCUP00000011046 | Cell division cycle 37 like 1. | HATPase_c domain-containing protein. | 0.854 |
| CDC37L1 | HSP90AA1 | ENSOCUP00000003006 | ENSOCUP00000036544 | Cell division cycle 37 like 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 [...] | 0.854 |
| CDC37L1 | HSP90AB1 | ENSOCUP00000003006 | ENSOCUP00000012976 | Cell division cycle 37 like 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 [...] | 0.854 |
| CDC37L1 | HSPA4 | ENSOCUP00000003006 | ENSOCUP00000007228 | Cell division cycle 37 like 1. | Heat shock protein family A (Hsp70) member 4. | 0.575 |
| CDC37L1 | LOC103348580 | ENSOCUP00000003006 | ENSOCUP00000045003 | Cell division cycle 37 like 1. | Uncharacterized protein. | 0.854 |
| CDC37L1 | PTGES3 | ENSOCUP00000003006 | ENSOCUP00000029851 | Cell division cycle 37 like 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. | 0.709 |
| CDC37L1 | STIP1 | ENSOCUP00000003006 | ENSOCUP00000029749 | Cell division cycle 37 like 1. | Stress induced phosphoprotein 1. | 0.917 |
| G1SWK6_RABIT | CDC37L1 | ENSOCUP00000007873 | ENSOCUP00000003006 | HATPase_c domain-containing protein. | Cell division cycle 37 like 1. | 0.854 |
| G1SWK6_RABIT | HSPA4 | ENSOCUP00000007873 | ENSOCUP00000007228 | HATPase_c domain-containing protein. | Heat shock protein family A (Hsp70) member 4. | 0.655 |
| G1SWK6_RABIT | NR3C1 | ENSOCUP00000007873 | ENSOCUP00000046838 | HATPase_c domain-containing protein. | Glucocorticoid receptor; Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP [...] | 0.776 |
| G1SWK6_RABIT | PTGES3 | ENSOCUP00000007873 | ENSOCUP00000029851 | HATPase_c domain-containing protein. | 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. | 0.886 |
| G1SWK6_RABIT | STIP1 | ENSOCUP00000007873 | ENSOCUP00000029749 | HATPase_c domain-containing protein. | Stress induced phosphoprotein 1. | 0.916 |
| G1T464_RABIT | CDC37L1 | ENSOCUP00000011046 | ENSOCUP00000003006 | HATPase_c domain-containing protein. | Cell division cycle 37 like 1. | 0.854 |
| G1T464_RABIT | HSPA4 | ENSOCUP00000011046 | ENSOCUP00000007228 | HATPase_c domain-containing protein. | Heat shock protein family A (Hsp70) member 4. | 0.672 |
| G1T464_RABIT | NR3C1 | ENSOCUP00000011046 | ENSOCUP00000046838 | HATPase_c domain-containing protein. | Glucocorticoid receptor; Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP [...] | 0.809 |
| G1T464_RABIT | PTGES3 | ENSOCUP00000011046 | ENSOCUP00000029851 | HATPase_c domain-containing protein. | 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. | 0.886 |
| G1T464_RABIT | STIP1 | ENSOCUP00000011046 | ENSOCUP00000029749 | HATPase_c domain-containing protein. | Stress induced phosphoprotein 1. | 0.916 |
| HSP90AA1 | CDC37L1 | ENSOCUP00000036544 | ENSOCUP00000003006 | 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 [...] | Cell division cycle 37 like 1. | 0.854 |
| HSP90AA1 | HSP90AB1 | ENSOCUP00000036544 | ENSOCUP00000012976 | 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 [...] | 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 [...] | 0.573 |