EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.4.53 | phosphoprotein |
aryl-hydrocarbon receptor-interacting protein XAP2 attenuates the ability of cAMP-dependent protein kinase to phosphorylate PDE4A5 |
687496 |
| 3.1.4.53 | phosphoprotein |
PDE4 activation is regulated via phosphorylation by PKA in the UCR or phosphorylation by ERK in the C-terminus, depending on the individual isoform |
716435 |
| 3.1.4.53 | phosphoprotein |
phosphorylation by cAMP-dependent protein kinase |
678086 |
| 3.1.4.53 | phosphoprotein |
phosphorylation of cAMP-specific PDE4A5 by MAPK-activated protein kinase 2, also called MAPKAPK2. PDE4A5 is phosphorylated at Ser147, within the regulatory UCR1, ultraconserved region 1, domain conserved among PDE4 long isoforms. Phosphorylation by MK2, although not altering PDE4A5 activity, markedly attenuates PDE4A5 activation through phosphorylation by protein kinase A. Phosphorylation by MK2 also triggers a conformational change in PDE4A5 that attenuates PDE4A5 interaction with proteins whose binding involves UCR2, such as DISC1 and AIP, but not the UCR2-independent interacting scaffold protein beta-arrestin |
714097 |
| 3.1.4.53 | phosphoprotein |
phosphorylation of enzyme by cAMP-dependent protein kinase at S123 |
678086 |
| 3.1.4.53 | phosphoprotein |
phosphorylation of PDE-4D3 by protein kinase A produces a monophasic Mg2+ response curve. Phosphorylation of PDE-4D3 increased the sensitivity of the enzyme to inhibition by RS-25344 (about 100fold) and RS-33793 (about 330fold). Phosphorylation of PDE-4D3 induces an apparent conformation change that increases maximum velocity and sensitivity to inhibition by some analogues of nitraquazone |
689067 |
| 3.1.4.53 | phosphoprotein |
protein kinase A catalyzes phosphorylation (at Ser-54) and activation of isoform PDE4D3. Protein phosphatase 2A associated with muscle A kinase-anchoring protein complexes promotes PDE4D3 dephosphorylation at Ser-54 |
712415 |
| 3.1.4.53 | phosphoprotein |
the enzyme is phosphorylated and activated by protein kinase A within upstream conserved region 1 and inhibited by phosphorylation at serine 42 within the N-terminal region |
750540 |
| 3.1.4.53 | phosphoprotein |
treatment of COS7 cells with forskolin, to elevate cAMP levels, produced activation of PDE4B4, which is associated with the phosphorylation of PDE4B4 on Ser-56 within UCR1 |
684954 |
| 3.1.4.53 | proteolytic modification |
protein sequence predicts a leader sequence, two transmembrane segments, and an extracellular catalytic domain |
669475 |
