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| Domain hiding | Altered binding specificity | Motif hiding | Composite binding site formation |
| Uncategorised | Rheostatic | Allostery | Avidity-sensing |
| Physicochemical compatibility | Pre-translational | Competition |
| Protein | Motif | Start | End | Switch description | Information |
Type: Binary Subtype: Pre‑translational | |||||||
| Pre-translational mechanisms such as alternative splicing, alternative promoter-usage and/or RNA editing result in inclusion or removal of exons that contain an entire or partial motif. | |||||||
| PDE2A_HUMAN | MOD_NMyristoyl | 1 | 7 | Alternative splicing removes the myristoylation motif of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A). The soluble Isoform PDE2A1 of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A) is expressed in a variety of peripheral tissues, whereas the membrane-associated Isoform PDE2A3 of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A) is found exclusively in the brain. Isoform PDE2A3 of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A) requires N-myristoylation together with palmitoylation to be targeted to synapses, allowing control and crosstalk of cyclic nucleotides. | |||
Type: Binary Subtype: Allostery | |||||||
| The binding properties of a motif or a motif-binding domain are modulated indirectly by allosteric effects resulting from PTM or effector binding at a site that is distinct from the actual interaction interface. | |||||||
| RECO_BOVIN | MOD_NMyristoyl | 1 | 7 | Binding of calcium(2+) to Recoverin (RCVRN) results in a conformational change in Recoverin that makes the myristoyl moiety available for binding to the membrane. | |||
| KAPCA_HUMAN | MOD_NMyristoyl | 1 | 7 | Phosphorylation of cAMP-dependent protein kinase catalytic subunit alpha (PRKACA) at S11 shifts the conformational equilibrium to the myristoyl-out conformation, making the myristoyl moiety available for interaction with the membrane. | |||