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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 |
| Protein | Motif | Start | End | Switch description | Information |
Type: Specificity Subtype: Motif hiding | |||||||
| Motif hiding occurs when there is a large difference in intrinsic affinity of overlapping or adjacent motifs for their respective binding partners, or a large difference in the local abundance of these partners. Binding of an effector to one motif sterically masks the overlapping or adjacent motif, thereby precluding it from binding. Binding of the masking molecule can be PTM-dependent or -independent. | |||||||
| MKL1_MOUSE | LIG_Actin_RPEL_3 | 17 61 105 | 36 80 124 | Hiding of the NLS of MKL/myocardin-like protein 1 (Mkl1) by binding of G-actin to the RPEL motifs of MKL/myocardin-like protein 1 (Mkl1) prevents translocation of this transcription factor to the nucleus. | |||
Type: Binary Subtype: Pre‑translational | |||||||
| Pre-translational mechanisms such as alternative splicing, alternative promoter-usage and/or RNA editing result in inclusion or removal of exons that contain an entire or partial motif. | |||||||
| MYCD_MOUSE | LIG_Actin_RPEL_3 | 20 | 39 | Alternative promoter usage removes the RPEL-binding motif of Myocardin (Myocd), abrogating binding to Actin, alpha skeletal muscle (Acta1). 3 RPEL motifs are found in Myocd. The shortened form lacks 2 RPEL motifs but no definitive comparison of binding to actin has been undertaken between isoforms. | |||
| MYCD_MOUSE | LIG_Actin_RPEL_3 | 64 | 83 | Alternative promoter usage removes the RPEL-binding motif of Myocardin (Myocd), abrogating binding to Actin, alpha skeletal muscle (Acta1). 3 RPEL motifs are found in Myocd. The shortened form lacks 2 RPEL motifs but no definitive comparison of binding to actin has been undertaken between isoforms. | |||
| DMD_HUMAN | LIG_Actin_DMD | 5 | 10 | Alternative splicing removes the actin-binding motif of Isoform Dp71 of Dystrophin (DMD), abrogating binding to Actin, alpha skeletal muscle (ACTA1). The presence of the actin-binding motif in Isoform Dp71 of Dystrophin (DMD) may allow it to participate in the clustering of sodium channels by anchoring the syntrophin/channel complex to the actin cytoskeleton. | |||