Abstract:The ubiquitin-conjugating enzyme, named TaE2, was obtained as the candidate interaction protein of TaMAPK2 by yeast-two-hybrid system. Bioinformatic analysis showed that TaE2 was a member of ubiquitin-conjugating enzyme E2 family. Semi-quantitative RT-PCR showed that TaE2 was expressed in root, stem, leaves and seeds. TaE2 was up-regulated under drought, high-salt and ABA treatments. The fusion protein GST-TaE2 was expressed in Escherichia.coli and purified by GST-Trap HP. TaE2 gene reported in this study lay a foundation for further studying the function and mechanisms of the ubiquitin proteasome pathway response to stresses.