Sentrin Specific Protease 5 (SENP5)

SENP5 contains a C-terminal catalytic domain. SENP5 shares highest similarity with SENP3, including 62% amino acid identity in the catalytic domain and 40% identity in the region preceding the catalytic domain.SENP5 also showed isopeptidase activity and desumoylated SUMO-modified RANGAP1, with highest activity toward SUMO2 and SUMO3. In cotransfection assays, SENP5 preferentially reduced high molecular mass conjugates of SUMO2 compared with SUMO1. Deletion of the noncatalytic N-terminal domain of SENP5 led to loss of nucleolar localization and increased desumoylation activity. Knockdown of SENP5 in HeLa cells increased the number of multinucleated cells and the number of cells with aberrant nuclear structure, consistent with defects in mitosis and cytokinesis.