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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 |
| Type: Binary Subtype: Pre‑translational | Type: Specificity Subtype: Altered binding specificity |
| Protein | Motif | Start | End | Switch description | Information |
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. | |||||||
| PEX5R_MOUSE | TRG_ENDOCYTIC_2 | 38 | 41 | Alternative splicing removes the endocytosis motif of Isoform 3 of PEX5-related protein (Pex5l), abrogating binding to AP-2 complex subunit mu (Ap2m1). The motif is present in exon 2, and its absence causes a significant increase in channel density of members from the potassium channel HCN family. | |||
| PI51C_MOUSE | TRG_ENDOCYTIC_2 | 644 | 647 | Alternative splicing removes the endocytosis motif of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c), abrogating binding to AP-2 complex subunit mu (Ap2m1). The direct interaction between the AP-2 complex and Isoform PIPKIgamma661 of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c) (PIPKIgamma661) targets this isoform to sites of endocytosis at the plasma membrane. Consequently, this results in the generation of a highly concentrated pool of PI(4,5)P2 at these sites. | |||
Type: Specificity Subtype: Altered binding specificity | |||||||
| The balance of the competition for overlapping or adjacent, mutually exclusive interaction interfaces is tipped in favor of one of the interactors by PTM-dependent modulation of the intrinsic affinity of a binding region. Multiple, successive PTMs allow sequential switching of different binding partners in an ordered manner by step-wise alteration of binding specificity. | |||||||
| CTLA4_MOUSE | TRG_ENDOCYTIC_2 | 201 | 204 | Dephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4. | |||