Abstract: The ubiquitin proteasome pathway (UPP) is the crucial regulatory mechanism for selective protein degradation. Ubquitin-conjugating enzyme (UBC/E2) is a key enzyme involved in UPP. In this study, the HbUBC22 was cloned in Hevea brasiliensis by assembly the Hevea homologous EST and RT-PCR amplification. The ORF of HbUBC22 contained 807 bp in length and encoded 268 amino acid residues. The putative protein of HbUBC22 had a conserved UBC domain and a conserved active-site cysteine in the UBC domain. Phylogenetic analysis showed that HbUBC22 shared the highest similarity with the UBC protein from Ricinus communis, Populus trichocarpa, Camellia oleifera, and Vitis vinifera, with 89%, 85%, 85% and 81% sequence identities, respectively. In the genome of Arabidopsis thaliana, HbUBC22 shared the highest similarity with AtUBC22 with 73% identical residues. Transcription pattern analysis revealed that HbUBC22 expression was markedly induced by ethephon (ET) and methyl jasmonate (MeJA). Prokaryotic expression in E. coli indicated that HbUBC22 recombinant protein was expressed in the IPTG induced cells. These results provide a good basis for further characterization of the biological function of HbUBC22 in Hevea brasiliensis.