Heat Shock Protein 90 Alpha (HSP90AA1) Recombinant Protein

Function: 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

By similarity.

Subunit structure: Homodimer. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Interacts with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity

By similarity.

Subcellular location: Cytoplasm

By similarity. Melanosome

By similarity.

Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1

By similarity.

Post-translational modification: S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1

By similarity.ISGylated

By similarity.

Sequence similarities: Belongs to the heat shock protein 90 family.