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Mareks disease (MD) is a highly contagious lymphoproliferative diseases of chickens caused by Mareks disease virus (MDV) infection.The mechanisms of MDV oncogenesis,genomic integration and immunosuppression are not fully understood.The appropriate ubiquitination of protein is an important regulatory strategy for maintaining intracellular homeostasis,and involves in almost all intracellular processes.We hypothesize that MDV may hijack ubiquitination pathway to promote viral life cycle in host cells.In current study,using mass spectrometry,we identified ubiquitinated peptides from MDV transformed or na(i)ve T lymphocytes that were enriched by treatment of antibody against K-ε-GG standard peptides.We identified 10,024 lysine ubiquitination sites in 2,880 proteins.We further quantified 7,097 ubiquitination sites in 2,350 proteins identified above.The ubiquitinated proteins with quantitative ratios (MDV transformed/naive T cells) above 2 or below 0.5 were deemed significant.Among these proteins,865 were up-regulated and 936 were down-regulated.The altered ubiquitylome covered some important cell processes,such as cellular proliferation,apoptosis,cell cycle,DNA damage repair and chromosome stability,immune regulatory pathway etc.The modified lysine residues of some proteins (such as PKC,TPK,Uch48,CDK1 and IAP-3) were confirmed with site-directed mutation.Further investigations into the functional and structural changes of these identified proteins may reveal the regulatory mechanisms of oncogenesis,transformation,immunosuppression ofT lymphocytes induced by MDV infection.