HSPB1 (human, P04792) review notes

Deep research: not run. In this environment falcon times out and perplexity-lite is not installed. This review uses the UniProt record and cached GOA-cited publications.

Key points

• ATP-independent sHSP chaperone (holdase) [file:human/HSPB1/HSPB1-uniprot.txt "functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state"]. GO:0044183 is used as the core MF; unfolded protein binding is obsolete.
• Oligomer dynamics are controlled by MAPKAPK2/3 phosphorylation PMID:15581903.
• CMT2F/dHMN mutants alter chaperone activity PMID:20178975.
• Anti-apoptotic via DAXX PMID:11003656.
• Translation inhibition via eIF4G during heat shock is kept as non-core PMID:10859165.
• The VEGF/endothelial migration IMP terms from a single study PMID:18440775 are kept as non-core. Intracellular signal transduction is marked over-annotated, because HSPB1 is a phospho-target there.
• Marked over-annotated: proteasome complex (ISS), RNA binding (HDA), response to virus (IEP), platelet aggregation (HMP), PKC inhibitor activity / negative regulation of PKC signalling (ISS), and Pol II TF binding (single Y2H).
• 231 protein binding IPI rows are removed as uninformative.