Members of ULP family contain a catalytic domain about 220 amino acids which usually locate in C terminus. The N-terminal regions are always involved in determining the substrate specificity or localization of these enzymes. Seven members have been found in human and they contain eight blocks of highly conserved sequence in the catalytic domain. Two ULPs exist in yeast and both can hydrolyze SUMO-1 and SUMO-2/3 derivatives, although with different apparent specificity and nuclear localization (1).

1. Gan-Erdene, T., Nagamalleswari, K., Yin, L., Wu, K., Pan, Z.Q. and Wilkinson, K.D. (2003). Identification and characterization of DEN1, a deneddylase of the ULP family. J. Biol. Chem., 278, 28892-28900. PMID: 12759362