Abstract: StSN2 belongs to the Snakin/GASA（gibberellic acid-stimulated arabidopsis） family of potato（Solanum tuberosum L.）. Its N-terminal has a signal peptide, and its C-terminal has 12 conserved cysteine residues, mainly playing an important regulatory role in plant growth and development and stress response to stress. In order to understand how the N-terminal signal peptide region of StSN2 affects its subcellular localization and interactions, we conducted several experiments. First, we predicted the location of the signal peptide using computational methods and then amplified the corresponding DNA fragments. We obtained fragments of 315 bp（containing the signal peptide） and 243 bp（deleted signal peptide）. Next, we cloned the deleted signal peptide fragment into a subcellular localization vector and expressed it as a fusion protein(YFP-StSN2△_SP). Transient expression analysis revealed that the localization of the StSN2△_SP protein without the signal peptide was altered and restricted to the nucleus. Finally, we created yeast bait carriers for both the full-length and deleted signal peptide versions of StSN2 and performed yeast two-hybrid experiments with StSnRK1α. The results demonstrated that full-length StSN2 could not grow in a four-deficiency medium when transformed with StSnRK1α. However, the StSN2△_SP variant without the signal peptide and StSnRK1α grew normally under these conditions. These findings suggest that deleting the signal peptide from StSN2 impacts its subcellular localization and protein-protein interactions. This study provides a theoretical basis for studying the biological functions of StSN2 proteins. It also lays an experimental foundation for further improving the functional studies of this gene in potato tuber dormancy.