Despite recent improvements in tag size, proximity labelling tools characterizing protein-protein interaction in cells still have drawbacks by requiring the fusion of a relatively large protein to the protein of interest (POI). The fusion tag may interfere with the POI function and cannot be used to target events close to translation such as in-cell protein folding (since the fusion tag needs to fold first to be functional). We are developing strategies to overcome both limitations by combing proximity labeling methods TurboID and APEX with an epitope targeting approach called SunTag, which only has nineteen amino acids in length and does not require folding. In our method, biotin ligase (TurboID) or ascorbate peroxidase (APEX) is recombinantly fused to an anti-SunTag antibody and co-expressed with a POI fused SunTag epitope in mammalian cells. The anti-SunTag antibody can target the TurboID or APEX to the POI, promoting POI biotinylation, and subsequent biotinylated protein capture, and mass spectrometry. We have applied this new strategy to human lamin A (lamin) protein, which is a component of the nuclear envelope and found that TurboID and APEX can specifically label it with biotin in human cells. Using this new method, we also identified numbers of known lamin interactors, many of which have been previously identified by direct tagging of lamin with proximity labeling enzymes, suggests that the antibody can target the biotin ligase or ascorbate peroxidase to the epitope tag fused lamin and identify neighboring proteins with good efficacy.