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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: Physicochemical compatibility | |||||||
| PTM of a residue in a motif or in its flanking regions alters the physicochemical and/or structural compatibility of the motif with its binding partner. This can either induce or enhance an interaction, or result in inhibition or even abrogation of an interaction. | |||||||
| SOC1_ARATH | DOC_WW_Pin1_4 | 192 | 197 | Phosphorylation of S195 in the Pin1-binding motif of MADS-box protein SOC1 (SOC1) induces binding to the Peptidyl-prolyl cis-trans isomerase Pin1 (PIN1) protein. | |||
| SOC1_ARATH | DOC_WW_Pin1_4 | 46 | 51 | Phosphorylation of S49 in the Pin1-binding motif of MADS-box protein SOC1 (SOC1) induces binding to the Peptidyl-prolyl cis-trans isomerase Pin1 (PIN1) protein. | |||
| AGL24_ARATH | DOC_WW_Pin1_4 | 199 | 204 | Phosphorylation of T202 in the Pin1-binding motif of MADS-box protein AGL24 (AGL24) induces binding to the Peptidyl-prolyl cis-trans isomerase Pin1 (PIN1) protein. | |||