|   Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
|   Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
|   Physicochemical compatibility |   Pre-translational |   Competition |
| Protein | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
DOC_WW_Pin1_4 - The Class IV WW domain interaction motif is recognised primarily by the Pin1 phosphorylation-dependent prolyl isomerase. | |||||||
| GEPH_MOUSE | 185 | 190 | Binary | Physicochemical compatibility | Phosphorylation of S188 in the Pin1-binding motif of Gephyrin (Gphn) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||
| GEPH_MOUSE | 191 | 196 | Binary | Physicochemical compatibility | Phosphorylation of S194 in the Pin1-binding motif of Gephyrin (Gphn) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||
| GEPH_MOUSE | 197 | 202 | Binary | Physicochemical compatibility | Phosphorylation of S200 in the Pin1-binding motif of Gephyrin (Gphn) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||