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Mutations in lamin A (LMNA) have been reported to cause laminopathies. However, the proteins associated with the LMNA mutation have mostly remained unexplored. Herein, a new chemical tool for proximal proteomics is reported, developed by a combination of proximity chemical tagging and a bio\u2010orthogonal supramolecular latching based on cucurbit[7]uril (CB[7])\u2010based host\u2013guest interactions. As this host\u2013guest interaction acts as a noncovalent clickable motif that can be unclicked on\u2010demand, this new chemical tool is exploited for reliable detection of the proximal proteins of LMNA and its mutant that causes laminopathic dilated cardiomyopathy (DCM). Most importantly, a comparison study reveals, for the first time, mutant\u2010dependent alteration in LMNA proteomic environments, which allows to identify putative laminopathic DCM\u2010linked proteins including FOXJ3\u00a0and CELF2. 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