node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
FKBP4 | FKBP5 | ENSGALP00000070868 | ENSGALP00000067232 | Peptidylprolyl isomerase. | Peptidylprolyl isomerase. | 0.578 |
FKBP4 | HSP90AA1 | ENSGALP00000070868 | ENSGALP00000060285 | Peptidylprolyl isomerase. | 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 [...] | 0.863 |
FKBP4 | HSP90AB1 | ENSGALP00000070868 | ENSGALP00000016523 | Peptidylprolyl isomerase. | Heat shock cognate 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 [...] | 0.871 |
FKBP4 | HSPA8 | ENSGALP00000070868 | ENSGALP00000051563 | Peptidylprolyl isomerase. | Heat shock cognate 71 kDa protein; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis a [...] | 0.741 |
FKBP4 | NR3C1 | ENSGALP00000070868 | ENSGALP00000052544 | Peptidylprolyl isomerase. | Uncharacterized protein. | 0.943 |
FKBP4 | NR3C2 | ENSGALP00000070868 | ENSGALP00000058137 | Peptidylprolyl isomerase. | Mineralocorticoid receptor; Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels (By similarity). | 0.860 |
FKBP4 | PTGES3 | ENSGALP00000070868 | ENSGALP00000069892 | Peptidylprolyl isomerase. | Prostaglandin E synthase 3; Molecular chaperone. | 0.947 |
FKBP4 | STIP1 | ENSGALP00000070868 | ENSGALP00000066776 | Peptidylprolyl isomerase. | Stress induced phosphoprotein 1. | 0.836 |
FKBP5 | FKBP4 | ENSGALP00000067232 | ENSGALP00000070868 | Peptidylprolyl isomerase. | Peptidylprolyl isomerase. | 0.578 |
FKBP5 | HSP90AA1 | ENSGALP00000067232 | ENSGALP00000060285 | Peptidylprolyl isomerase. | 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 [...] | 0.869 |
FKBP5 | HSP90AB1 | ENSGALP00000067232 | ENSGALP00000016523 | Peptidylprolyl isomerase. | Heat shock cognate 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 [...] | 0.920 |
FKBP5 | HSPA8 | ENSGALP00000067232 | ENSGALP00000051563 | Peptidylprolyl isomerase. | Heat shock cognate 71 kDa protein; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis a [...] | 0.770 |
FKBP5 | NR3C1 | ENSGALP00000067232 | ENSGALP00000052544 | Peptidylprolyl isomerase. | Uncharacterized protein. | 0.966 |
FKBP5 | NR3C2 | ENSGALP00000067232 | ENSGALP00000058137 | Peptidylprolyl isomerase. | Mineralocorticoid receptor; Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels (By similarity). | 0.778 |
FKBP5 | PTGES3 | ENSGALP00000067232 | ENSGALP00000069892 | Peptidylprolyl isomerase. | Prostaglandin E synthase 3; Molecular chaperone. | 0.949 |
FKBP5 | STIP1 | ENSGALP00000067232 | ENSGALP00000066776 | Peptidylprolyl isomerase. | Stress induced phosphoprotein 1. | 0.794 |
HSP90AA1 | FKBP4 | ENSGALP00000060285 | ENSGALP00000070868 | 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 [...] | Peptidylprolyl isomerase. | 0.863 |
HSP90AA1 | FKBP5 | ENSGALP00000060285 | ENSGALP00000067232 | 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 [...] | Peptidylprolyl isomerase. | 0.869 |
HSP90AA1 | HSP90AB1 | ENSGALP00000060285 | ENSGALP00000016523 | 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 cognate 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 [...] | 0.907 |
HSP90AA1 | HSPA8 | ENSGALP00000060285 | ENSGALP00000051563 | 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 cognate 71 kDa protein; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis a [...] | 0.977 |