Table-3.
HSP70 interacting proteins during cell cycle regulation and signal transduction.
| Interacting protein | Protein details | Combined score |
|---|---|---|
| HSF1 | Heat shock factor protein 1; DNA-binding protein that specifically binds HSEs and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked | 0.990 |
| DNAJB1 | DnaJ homolog subfamily B member 1; interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP | 0.996 |
| DNAJB6 | DnaJ homolog subfamily B member 6; plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a cochaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity | 0.994 |
| HSP90AA1 | HSP90-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. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various cochaperones that modulate its substrate recognition, ATPase cycle, and chaperone function | 0.990 |
| BAG3 | BAG family molecular chaperone regulator 3 | 0.987 |
| HSP90AB1 | HSP90-beta | 0.986 |
| LOC783577 | HSP90-beta | 0.985 |
| DNAJC7 | Uncharacterized protein | 0.982 |
| BAG1 | BAG family molecular chaperone regulator 1 | 0.979 |
| DNAJC2 | DnaJ homolog subfamily C member 2; acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: Component of the RAC, a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of HSP70-type chaperones HSPA14 that bind to the nascent polypeptide chain | 0.972 |
HSP=Heat shock protein, HSE=Heat shock promoter elements, RAC=Ribosome-associated complex