EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.1.105 | phosphoprotein |
- |
640288, 640310, 640315, 673017, 761491, 94948, 94952 |
| 2.7.1.105 | phosphoprotein |
at acid pH-values |
640314 |
| 2.7.1.105 | phosphoprotein |
brain enzyme is phosphorylated, but not activated |
640304 |
| 2.7.1.105 | phosphoprotein |
forskolin induces a 40% increase in phosphorylation at residue Ser32. The enzyme dimer favors binding of monomers in the same Ser32 phosphorylation state in living cells. Phosphorylation at Ser32 may tighten the liver enzyme dimer complex |
722278 |
| 2.7.1.105 | phosphoprotein |
in response to glucagon, cyclic AMP-dependent protein kinase phosphorylates Ser32 in the liver isoform variant of PFKFB1, leading to inactivation of its PFK-2 activity while activating its FBPase-2 function. Two serine residues, Ser466 and Ser483, within the C-terminal regulatory domain of PFKFB2 can be phosphorylated by protein kinase B (Akt/PKB) in response to insulin |
737973 |
| 2.7.1.105 | phosphoprotein |
kinetic of phosphorylation by cAMP-dependent protein kinase |
640344 |
| 2.7.1.105 | phosphoprotein |
loss of phosphorylation-dependent reduction of enzyme by deletion of the N-terminal residues of enzyme, The deletion of 7 N-terminal amino acids causes a 75% decrease in activity |
640325 |
| 2.7.1.105 | phosphoprotein |
MW 58000 enzyme form |
640303 |
| 2.7.1.105 | phosphoprotein |
phophorylation by cAMP-dependent protein kinase causes activation |
640281, 640299, 640302, 640303, 640314, 640321, 94928, 94949, 94951 |
| 2.7.1.105 | phosphoprotein |
phosphorylation at lower pH-values |
640288 |
