LAMTOR1 interactome upon mutation of USP32

Ubiquitination is among the most prevalent post-translational modifications regulating a great number of cellular functions, and defects in such processes contribute to many diseases. Deubiquitinating enzymes (DUBs) are essential to control the precise outcome of ubiquitin signals. The ubiquitin-specific protease 32 (USP32) differs from all other DUBs as it comprises in addition to its catalytic USP domain and the DUSP domain also multiple EF hands and a C-terminal prenylation site. This dataset represents an interactome analysis of GFP-tagged LAMTOR1 in human RPE-1 cells upon knock-out and inactivation (C743S) of USP32.