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Physicochemical compatibility

Phosphorylation of S321 in the 14-3-3-binding motif of M-phase inducer phosphatase 2 (CDC25B) by Cyclin-dependent kinase 1 (CDK1) during mitosis abolishes binding of the motif, phosphorylated at S323, to 14-3-3 protein beta/alpha (YWHAB), thereby maintaining active Cdc25B.

(1) M-phase inducer phosphatase 2 (CDC25B)
(2) 14-3-3 protein beta/alpha (YWHAB)

Interaction #1 CDC25B - YWHAB

(1) LIG_14-3-3_3 motif (320RSPSMP325) in M-phase inducer phosphatase 2 (CDC25B)
(2) 14-3-3 protein (5-238) in 14-3-3 protein beta/alpha (YWHAB)

Interaction Regulation
PTM-dependent Abrogation (Phosphorylation of S321 on M-phase inducer phosphatase 2 (CDC25B)) of the M-phase inducer phosphatase 2 (CDC25B) LIG_14-3-3_3 motif - 14-3-3 protein beta/alpha (YWHAB) 14-3-3 protein interaction

Regulatory Enzymes for switch
Modifying enzymes for residue: S321: Cyclin-dependent kinase 1 (CDK1)

Inferred Regulatory Enzymes for switch
Putative modifying enzymes for residue: S321 : Cyclin-dependent kinase 1 (CDK1).


(1) Mitotic phosphorylation of Cdc25B Ser321 disrupts 14-3-3 binding to the high affinity Ser323 site.
Astuti et al. J. Biol. Chem. (2010)

See also

Other switches involving participants
M-phase inducer phosphatase 2 (CDC25B) - 2 more (view)
14-3-3 protein beta/alpha (YWHAB) - 8 more (view)

Other switches involving interfaces
LIG_14-3-3_3 - 16 more (view)
14-3-3 protein - 38 more (view)

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