Cell division cycle associated 2 (CDCA2, Repo-Man) is a cell-cycle protein that recruits protein phosphatase 1 (PP1) to mitotic chromatin at anaphase onset, which is essential for cell proliferation. Carboxy-terminal phosphorylation of CDCA2 at Ser893 by Aurora B inhibits the protein and leads to diffuse localization during prometaphase and metaphase. Dephosphorylation of CDCA2 by PP2A is necessary for CDCA2/PP1 complex reformation. The CDCA2/PP1 complex is required for chromatin binding and dephosphorylation of histone H3 at Thr3, Ser10, and Ser28. The CDCA2/PP1 complex is also involved in nuclear envelope reformation during mitotic exit for proper progression through the M/G1 transition. The interaction of CDCA2 with importin beta and Nup153, which is required for nuclear envelope formation, is negatively regulated by CDK phosphorylation of the amino-terminal domain of CDCA2. CDCA2 may play a role in DNA repair as the release of CDCA2 from chromatin at sites of DNA damage promotes the activation of DNA damage response. These results imply that the CDCA2/PP1 complex may play a part in cancer progression. Research studies indicate that CDCA2 may serve as a prognostic marker, as increased CDCA2 expression is seen in a number of cancers, including melanoma, neuroblastoma tumors, squamous cell carcinoma, and synovial sarcomas.
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Protein Aliases: Cell division cycle-associated protein 2; FLJ25804; MGC129906; MGC129907; protein phosphatase 1, regulatory subunit 81; Recruits PP1 onto mitotic chromatin at anaphase protein; Repo-Man
Gene Aliases: 2610311M19Rik; AI586158; CDCA2; PPP1R81; Repo-Man