In budding yeast, the Cdc14a phosphatase activates mitotic exit by dephosphorylation of specific cyclin-dependent kinase (Cdk) substrates and seems to be regulated by sequestration in the nucleolus until its release during mitosis. Human Cdc14a phosphatase is highly similar to Saccharomyces cerevisiae Cdc14 and is a member of the dual specificity protein Tyrosine phosphatase family. It interacts with and dephosphorylates tumor suppressor protein p53 and may regulate the function of p53. In addition, Cdc14a dephosphorylates hCdh1 and activates APCCdh1. Cdc14a phosphatase plays a role in the regulation of the centrosome cycle, mitosis and cytokinesis, thereby influencing chromosome partitioning and genomic stability in human cells. Deregulated human Cdc14a phosphatase disrupts centrosome separation and chromosome segregation.