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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 |
| Motif | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
Proto-oncogene c-Fos - Fos - Mus musculus | |||||||
| DOC_WW_Pin1_4 | 229 | 234 | Binary | Physicochemical compatibility | Phosphorylation of T232 in the Pin1-binding motif of Proto-oncogene c-Fos (Fos) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||
| DOC_WW_Pin1_4 | 322 | 327 | Binary | Physicochemical compatibility | Phosphorylation of T325 in the Pin1-binding motif of Proto-oncogene c-Fos (Fos) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||
| DOC_WW_Pin1_4 | 328 | 333 | Binary | Physicochemical compatibility | Phosphorylation of T331 in the Pin1-binding motif of Proto-oncogene c-Fos (Fos) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||
| DOC_WW_Pin1_4 | 371 | 376 | Binary | Physicochemical compatibility | Phosphorylation of S374 in the Pin1-binding motif of Proto-oncogene c-Fos (Fos) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | ||