Protein-Folding Chaperones Predict Structure-Function Relationships and Cancer Risk in BRCA1 Mutation Carriers

We used a high-throughput LUMIER assay to test whether the binding patterns of protein-folding chaperones can be used to predict structure-function relationships of BRCA1 variants and the clinical manifestations of BRCA1 mutations in carriers. Our findings are presented in the following tables.
Table S1. Chaperone binding detects BRCA1-BRCT pathogenic ClinVar variants and rationally designed variants that disrupt domain structure
Table S2. Computational analysis of thermodynamic stability for pathogenic BRCA1-BRCT missense mutations in ClinVar
Table S3. Diverse functional outcomes of BRCA1-BRCT variants detected by chaperone binding
Table S4. Features of human hypomorphic BRCA1 variants characterized by chaperones
Table S5. Human BRCA1 carriers exhibiting early disease onset identified by chaperone binding