Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase, but no inhibition
phosphoprotein
-
phosphorylation site
phosphoprotein
-
MW 58000 enzyme form
phosphoprotein
-
brain enzyme is phosphorylated, but not activated
phosphoprotein
-
phophorylation by cAMP-dependent protein kinase causes activation
phosphoprotein
-
rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
phosphoprotein
-
phosphorylation by protein kinase C causes activation
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
phosphoprotein
-
rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
phosphoprotein
-
phophorylation by cAMP-dependent protein kinase causes activation
phosphoprotein
phosphorylation site: Ser-32
phosphoprotein
-
phosphorylation by protein kinase C causes activation
phosphoprotein
recombinant His-tagged HBP2, and nontagged wild-type and mutant S460D HBP1 are phosphorylated by several protein kinases, i.e. protein kinases A, B, and C, and by AMP activated kinase, HBP1 mutants are phosphorylated by protein kinase C, overview
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
phosphoprotein
specific phosphorylation of heart 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase isoenzyme PFKFB2 at Ser483. This activation is mediated by the phosphatidylinositol-4,5-bisphosphate 3-kinase and p38 signaling pathways. Amino acid-activated Akt phosphorylates PFKFB2 at Ser483. Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
phosphoprotein
phosphorylation of Ser461 by AMPK and Thr463 and Ser467 by CDK6 activates 6-phosphofructo-2-kinase activity and promotes glycolysis
phosphoprotein
-
phophorylation by cAMP-dependent protein kinase causes activation
phosphoprotein
-
at acid pH-values
phosphoprotein
-
the islet enzyme lacks protein kinase A and C phosphorylation sites
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes 35% inactivation of isozyme L of adipose tissue, not isozyme M
phosphoprotein
-
phophorylation by cAMP-dependent protein kinase causes activation
phosphoprotein
-
phosphorylation site: Ser-32
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not of kidney, testis and heart enzyme
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase of liver enzyme, not of skeletal muscle enzyme, since the phosphorylation site target Ser-32 of the liver isozyme is replaced by Ala in the muscle isozyme
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes 80% decrease in activity of the liver cells but not of hepatoma cells
phosphoprotein
-
phosphorylation at pH 6.6, not at pH 8
phosphoprotein
-
rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
phosphoprotein
-
phosphorylation at lower pH-values
phosphoprotein
-
phosphorylation of foetal liver enzyme by protein kinase C, but no effect on adult liver cells
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
phosphoprotein
-
kinetic of phosphorylation by cAMP-dependent protein kinase
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not of heart and skeletal muscle enzyme
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
94932, 94935, 640283, 640285, 640288, 640292, 640294, 640295, 640298, 640306, 640324, 640339
phosphoprotein
-
rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
phosphoprotein
-
the native and the recombinant wild-type and mutant enzymes are phosphorylated after incubation with glucagon inactivating the enzyme
phosphoprotein
Ser-32 is the phophorylation site
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
phosphoprotein
phosphorylation of PFK2/FBPase2 on Ser32 by protein kinase A
phosphoprotein
specific phosphorylation of heart 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase isoenzyme PFKFB2 at Ser483. This activation is mediated by the phosphatidylinositol-4,5-bisphosphate 3-kinase and p38 signaling pathways. Amino acid-activated Akt phosphorylates PFKFB2 at Ser483. Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
phosphoprotein
-
specific phosphorylation of heart 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase isoenzyme PFKFB2 at Ser483. This activation is mediated by the phosphatidylinositol-4,5-bisphosphate 3-kinase and p38 signaling pathways. Amino acid-activated Akt phosphorylates PFKFB2 at Ser483. Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
-
phosphoprotein
-
phosphorylation of PFK2/FBPase2 on Ser32 by protein kinase A
-
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase, but no inhibition
phosphoprotein
-
phophorylation by cAMP-dependent protein kinase causes activation
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not skeletal muscle enzyme
side-chain modification
-
specific modification by N-(1-pyrenyl)maleimide, the results demonstrate the presence of SH residue in the interface of enzyme subunits critical for interactions between them and that conformational changes occurring through dimers are essential for catalytic activity
side-chain modification
PCAF- and GCN5-mediated acetylation of Lys472/473 disrupts the NLS and sequesters PFKFB3 in the cytoplasm, facilitating its phosphorylation on Ser461 by AMPK. Polyubiquitination on Lys142 of PFKFB3 leads to proteasomal degradation of PFKFB3, shunting glucose metabolism from glycolysis to the PPP. Asymmetrical dimethylation on Arg131 and Arg134 stabilizes PFKFB3. Reduced methylation of PFKFB3 reroutes flux into the oxidative arm of PPP