| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EDRF1 | HSP90AB1 | ENSPTRP00000070789 | ENSPTRP00000031135 | Erythroid differentiation regulatory factor 1. | HSP90AB1 isoform 1. | 0.538 |
| EDRF1 | LOC461365 | ENSPTRP00000070789 | ENSPTRP00000093883 | Erythroid differentiation regulatory factor 1. | Heat shock protein HSP 90-beta pseudogene. | 0.459 |
| EDRF1 | TTC4 | ENSPTRP00000070789 | ENSPTRP00000001344 | Erythroid differentiation regulatory factor 1. | Tetratricopeptide repeat domain 4. | 0.750 |
| HGH1 | HSP90AB1 | ENSPTRP00000089528 | ENSPTRP00000031135 | Family with sequence similarity 203, member A. | HSP90AB1 isoform 1. | 0.640 |
| HGH1 | LOC461365 | ENSPTRP00000089528 | ENSPTRP00000093883 | Family with sequence similarity 203, member A. | Heat shock protein HSP 90-beta pseudogene. | 0.533 |
| HGH1 | TTC4 | ENSPTRP00000089528 | ENSPTRP00000001344 | Family with sequence similarity 203, member A. | Tetratricopeptide repeat domain 4. | 0.852 |
| HSP90AA1 | HSP90AB1 | ENSPTRP00000070946 | ENSPTRP00000031135 | 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 [...] | HSP90AB1 isoform 1. | 0.999 |
| HSP90AA1 | LOC461365 | ENSPTRP00000070946 | ENSPTRP00000093883 | 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 pseudogene. | 0.983 |
| HSP90AA1 | TTC4 | ENSPTRP00000070946 | ENSPTRP00000001344 | 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 [...] | Tetratricopeptide repeat domain 4. | 0.753 |
| HSP90AB1 | EDRF1 | ENSPTRP00000031135 | ENSPTRP00000070789 | HSP90AB1 isoform 1. | Erythroid differentiation regulatory factor 1. | 0.538 |
| HSP90AB1 | HGH1 | ENSPTRP00000031135 | ENSPTRP00000089528 | HSP90AB1 isoform 1. | Family with sequence similarity 203, member A. | 0.640 |
| HSP90AB1 | HSP90AA1 | ENSPTRP00000031135 | ENSPTRP00000070946 | HSP90AB1 isoform 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 [...] | 0.999 |
| HSP90AB1 | TTC4 | ENSPTRP00000031135 | ENSPTRP00000001344 | HSP90AB1 isoform 1. | Tetratricopeptide repeat domain 4. | 0.771 |
| LOC461365 | EDRF1 | ENSPTRP00000093883 | ENSPTRP00000070789 | Heat shock protein HSP 90-beta pseudogene. | Erythroid differentiation regulatory factor 1. | 0.459 |
| LOC461365 | HGH1 | ENSPTRP00000093883 | ENSPTRP00000089528 | Heat shock protein HSP 90-beta pseudogene. | Family with sequence similarity 203, member A. | 0.533 |
| LOC461365 | HSP90AA1 | ENSPTRP00000093883 | ENSPTRP00000070946 | Heat shock protein HSP 90-beta pseudogene. | 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 [...] | 0.983 |
| LOC461365 | TTC4 | ENSPTRP00000093883 | ENSPTRP00000001344 | Heat shock protein HSP 90-beta pseudogene. | Tetratricopeptide repeat domain 4. | 0.717 |
| TTC4 | EDRF1 | ENSPTRP00000001344 | ENSPTRP00000070789 | Tetratricopeptide repeat domain 4. | Erythroid differentiation regulatory factor 1. | 0.750 |
| TTC4 | HGH1 | ENSPTRP00000001344 | ENSPTRP00000089528 | Tetratricopeptide repeat domain 4. | Family with sequence similarity 203, member A. | 0.852 |
| TTC4 | HSP90AA1 | ENSPTRP00000001344 | ENSPTRP00000070946 | Tetratricopeptide repeat domain 4. | 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 [...] | 0.753 |
