M-phase inducer phosphatase-1 (dual-specificity phosphatase Cdc25A, CDC25A)
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Function
- tyrosine protein phosphatase
- dosage-dependent inducer of mitotic progression
- directly dephosphorylates CDC2 & stimulates its kinase activity
- dephosphorylates CDK2 in complex with cyclin E, in vitro
- stimulated by B-type cyclins
- interacts with CCNB1/cyclin B
- interacts with YWHAE/14-3-3 epsilon when phosphorylated
- interacts with CUL1 specifically when CUL1 is neddylated & active
- interacts with BTRC/BTRCP1 & FBXW11/BTRCP2
- interactions with CUL1, BTRC & FBXW11 are enhanced upon DNA damage
- phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-279, Ser-293 & Thr-507 during checkpoint mediated cell cycle arrest
- phosphorylated by CHEK2 on Ser-124, Ser-279, & Ser-293 during checkpoint mediated cell cycle arrest
- phosphorylation on Ser-178 & Thr-507 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A
- phosphorylation on Ser-76, Ser-124, Ser-178, Ser-279 & Ser-293 may also promote ubiquitin-dependent proteolysis of CDC25A
- ubiquitinated
- association with the F-box proteins BTRC & FBXW11 targets the protein for ubiquitination by CUL1 & proteolysis by the ubiquitin-dependent proteasome pathway
protein tyrosine phosphate + H2O <--> protein tyrosine + phosphate
Structure
- phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated; phosphorylation sites at Ser-79 & Ser-82 appear to be essential for this interaction
- belongs to the MPI phosphatase family
- contains 1 rhodanese domain
Alternative splicing
named isoforms=2