Catalytic activity:Protein tyrosine phosphate + H (2) O = protein tyrosine + phosphate. ,Domain:The phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-79 and Ser-82 appear to be essential for this interaction. ,enzyme regulation:Stimulated by B-type cyclins. ,Function:Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDC2 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E , in vitro. ,PTM:Phosphorylated by CHEK1 on Ser-76 , Ser-124 , Ser-178 , Ser-279 , Ser-293 and Thr-507 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124 , Ser-279 , and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-507 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76 , Ser-124 , Ser-178 , Ser-279 and Ser-293 may also promote ubiquitin-dependent proteolysis of CDC25A. ,PTM:Ubiquitinated. Association with the F-box proteins BTRC and FBXW11 targets the protein for ubiquitination by CUL1 and proteolysis by the ubiquitin-dependent proteasome pathway. ,similarity:Belongs to the MPI phosphatase family. ,similarity:Contains 1 rhodanese domain. ,subunit:Interacts with CCNB1/cyclin B1. Interacts with YWHAE/14-3-3 epsilon when phosphorylated. Interacts with CUL1 specifically when CUL1 is neddylated and active. Interacts with BTRC/BTRCP1 and FBXW11/BTRCP2. Interactions with CUL1 , BTRC and FBXW11 are enhanced upon DNA damage. ,
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