|   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.  | |||||||
| NONO_MOUSE | 409 | 414 | Binary | Physicochemical compatibility | Phosphorylation of T412 in the Pin1-binding motif of Non-POU domain-containing octamer-binding protein (Nono) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||
| NONO_MOUSE | 427 | 432 | Binary | Physicochemical compatibility | Phosphorylation of T430 in the Pin1-binding motif of Non-POU domain-containing octamer-binding protein (Nono) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||
| NONO_MOUSE | 449 | 454 | Binary | Physicochemical compatibility | Phosphorylation of T452 in the Pin1-binding motif of Non-POU domain-containing octamer-binding protein (Nono) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||