The ubiquitin(UB) gene of Bombyx mori nuclear polyhedrosis virus Zhenjiang strain (BmNPV-ZJ) was cloned and sequenced. Sequencing analysis shows that the BmVUB gene, which contains 234 nucleotides encoding 77 amino acids, contains a conservative HTH, a conservative LRLRGG and four conservative functional sites: Lys-29,Cys-48,Cys-63,Gly-76 which play important roles in ubiquitin-proteasome complex formation .It also shows that the C-terminal amino acid was redundant which locate at the downstream of conservative Gly-Gly proteinase cleavage signal sequence which characterizes as Gly-Gly-X（X was hydrophobic amino acid）. The BmVUB gene was induced and highly expressed in E.coli BL21. The results of gel scanning and Bradford protein assay show that the BmVUB protein was about 9 ku and the yield consists of 50 percent of total bacterial protein. The concentration of purified BmVUB protein was 1.03～2.46 g/L. The high titer antibody was obtained from rabbits immunized with the (His)₆- BmVUB fusion protein and ELISA shows that the titer of antibody was over 3.2×10^-5. Peptides binding ubiquitin were obtained from phage displayed peptide library using BmNPV-ZJ ubiquitin purified with His-affinity chromatography as a ligand. Five short peptides were identified which displayed obvious biological activity. Peptide VAPHHAYAPMRT could regulate the cell proliferation and further more this function which depends on the concentration variation, namely low concentration could promote the cell proliferation, whereas high concentration will inhibit the proliferation.