MYPBPC3 is the gene most commonly mutated in hypertrophic cardiomyopathy (HCM) located within the A-band of the sarcomere. It has been previously demonstrated that N-terminally flag-tagged MyBP-C, the protein encoded by MYBPC3, normally localizes to the sarcomere within neonatal rat cardiomyocytes. Proximity labeling is a technique that involves using a mutated form of biotin ligase (TurboID) to rapidly label proteins with biotin in proximity to the protein of interest. The proximity proteins of MyBP-C within cardiomyocytes have not previously been identified. We hypothesized that TurboID could be attached to the N-terminus of our Flag-MyBP-C construct while still maintaining its ability to localize to the sarcomere. If our hypothesis is correct, this would enable us to label proximity proteins within the sarcomere with biotin. This hypothesis was tested by transfecting TurboID-Flag-MYBPC3 into induced pluripotent stem cell derived cardiomyocytes that have been genetically modified not to express MyBP-C. This study answered questions about the localization of TurboID-Flag-MyBP-C using immunofluorescence staining with antibodies for MyBP-C and Flag. To evaluate the localization of biotin-labeled proximity proteins, fluorescently labeled streptavidin protein was used that tightly binds to biotin. This study reveals that TurboID-Flag-MyBP-C localizes to the sarcomere and labels proteins in the A-band for both wild-type MyBP-C and mutant forms of MyBP-C that carry pathogenic missense variants causing hypertrophic cardiomyopathy (R495Q, R502W, W792R, R810H). This work validated essential protein constructs which will enable proximity labeling mass spectroscopy to be performed. We hope this future work will identify changes in proximity proteins caused by pathogenic missense variants.