|   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. | |||||||
| NANOG_MOUSE | DOC_WW_Pin1_4 | 49 | 54 | Phosphorylation of S52 in the Pin1-binding motif of Homeobox protein NANOG (Nanog) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | |||
| NANOG_MOUSE | DOC_WW_Pin1_4 | 62 | 67 | Phosphorylation of S65 in the Pin1-binding motif of Homeobox protein NANOG (Nanog) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | |||