Fructose 2,6-bisphosphate binds to its allosteric site on PFK-1, it increases the enzyme’s affinity for its substrate fructose 6-phosphate and reduces its affinity for the allosteric inhibitors ATP and citrate

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cyclin-CDK complexes preferentially phosphorylate

serine and threonine residues when they are found within the consensus sequence:

[S/T]PX[R/K]K 

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G1 Cyclin–CDKs

In human - cyclin D-CDK 4 

cyclin D-CDK 6

In budding yeast - CIn 3-Cdc 28 

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G1/S Cyclin–CDKs

In human - cyclin E-CDK 2 

In budding yeast - CIn 1/2-Cdc 28

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S phase Cyclin–CDKs

In human - cyclin A-CDK 2 

In budding yeast - CIb 5/6-Cdc 28

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M phase Cyclin–CDKs

In human - cyclin A-CDK 1

cyclin B-CDK 1

In budding yeast - CIb 1/2/3/4-Cdc 28

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Cdk1 

=Cdc2 (vertebrates and fission yeast)

= Cdc28  (budding yeast)