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Ubiquitin-conjugating enzymes (E2s/UBC) are components of the ubiquitin proteasome system (UPS), and the ubiquitin-conjugating enzyme variant (UEV) is one of E2s (ubiquitin-conjugating enzymes, UBC) subfamily. The UEVs and UBC13 play an auxiliary role in mediating Lys63-linked polyUb chain assembly, which is correlated with target protein non-proteolytic functions, such as DNA repair or response to stress. However, the collaborative mechanism of <i>StUBC13</i> (homologue of AtUBC13) and <i>StUEVs</i> (the UEVs in potato) involved in potato are not fully understood understood. Here, we identified two <i>StUBC13</i> and seven <i>StUEVs</i> from potato genome. We analyzed protein motif and conserved domain, gene structure, phylogenetic features, <i>cis</i>-acting elements of <i>StUBC13</i> and <i>StUEVs</i>. Subsequently, we screened <i>StUBC13</i> partners protein and verified interaction between <i>StUBC13</i> and <i>StUEVs</i> using yeast two-hybrid, split luciferase complementation (SLC) and bimolecular fluorescence complementation (BiFC) approach. The expression profile and qRT-PCR analysis suggested that <i>StUBC13</i> and <i>StUEVs</i> gene exhibited a tissue-specific expression and were induced by different stress. Overall, this investigative study provides a comprehensive reference and view for further functional research on <i>StUBC13</i> and <i>StUEV1s</i> in potato.