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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: Binary Subtype: Physicochemical compatibility | |||||||
| PTM of a residue in a motif or in its flanking regions alters the physicochemical and/or structural compatibility of the motif with its binding partner. This can either induce or enhance an interaction, or result in inhibition or even abrogation of an interaction. | |||||||
| MPIP3_HUMAN | TRG_NES_CRM1_1 | 189 | 203 | Phosphorylation of S198 in the NES of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase PLK1 (PLK1) inhibits binding to Exportin-1 (XPO1), thus promoting nuclear localization of M-phase inducer phosphatase 3 (CDC25C). | |||
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. | |||||||
| P53_HUMAN | TRG_NES_CRM1_1 | 339 | 352 | Alternative splicing removes the nuclear export signal (NES) of Cellular tumor antigen p53 (TP53), abrogating binding to Exportin-1 (XPO1) and export from the nucleus. | |||
| PML_HUMAN | TRG_NES_CRM1_1 | 702 | 716 | Alternative splicing removes the nuclear export signal (NES) of Protein PML (PML), abrogating binding to Exportin-1 (XPO1) and export from the nucleus. | |||
| CTND1_HUMAN | TRG_NES_CRM1_1 | 942 | 956 | Alternative splicing removes the nuclear export signal (NES) of Catenin delta-1 (CTNND1), abrogating binding to Exportin-1 (XPO1). Despite demonstration of the importance of the NES for removing Catenin delta-1 (CTNND1) from the nucleus, those isoforms without NES are rarely found in the nucleus. | |||