|   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. | |||||||
| MEF2C_MOUSE | 107 | 112 | Binary | Physicochemical compatibility | Phosphorylation of S110 in the Pin1-binding motif of Myocyte-specific enhancer factor 2C (Mef2c) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||
| MEF2C_MOUSE | 95 | 100 | Binary | Physicochemical compatibility | Phosphorylation of S98 in the Pin1-binding motif of Myocyte-specific enhancer factor 2C (Mef2c) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||