BPM proteins participate in targeted protein degradation via the 26S proteasome. During growth, development and stress in the cell, targeted degradation of the protein occurs continuously. The degradation of transcription factors, which are important regulators of growth and development, plays a key role in this. BPM proteins are adapters of the E3 ligase CUL3 (cullin 3) and by their binding to transcription factors participate in their ubiquitination and regulation of degradation. Studies to date have shown that the Arabidopsis thaliana BPM1 protein localizes to the nucleus and cytoplasm of transformed BY2 tobacco cells, and the C-terminal bipartite nuclear localization signal (NLS) of BPM1 protein was detected. Its role in the Arabidopsis was investigated in this paper. For this purpose, transgenic plants with enhanced expression of truncated BPM1 protein (to which the C-terminal NLS region was deleted) fused with green fluorescent protein (GFP) and plants with enhanced expression of the nuclear localization signal of BPM1 protein fused with GFP were regenerated. In transgenic plants, the presence of transgenes and their expression was checked, and the presence of recombinant proteins was checked by immunodetection. Fluorescence microscopy has determined that the nuclear localization signal of BPM1 fused with GFP (NLSbpm1-GFP) localizes to the nucleus and is thus responsible for the placement of BPM1 in the nucleus, which is a prerequisite for the involvement of BPM1 in various cellular processes in the nucleus place. Sub-cellular localization of truncated BPM1 protein fused with GFP protein (delta-3-BPM1-GFP) has not been established.