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Background: Chk1 is an evolutionarily conserved protein kinase that has been implicated in cell cycle checkpoint control in lower eukaryotes. Chk1 plays an essential role in the mammalian DNA damage checkpoint, embryonic development, and tumor suppression (1). It is activated in response to replication blocks and genotoxic stress, via phosphorylation of Serine 317 and Serine 345 (2). Activated Chk1 can bind to, phosphorylate (at Serine 216) and inactivate cdc25c (3, 4). Chk1 is phosphorylated by ATR in response to ultraviolet irradiation and inhibition of DNA replication, and by ATM in response to ionizing irradiation, resulting in enhanced kinase activity. Chk1 is phosphorylated at Serine 280 by AKT1/PKB, which is thought to promote mono and/or diubiquitination (5).