|   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 | 
Cytotoxic T-lymphocyte protein 4 - Ctla4 -  Mus musculus  | |||||||
| LIG_SH2_STAT5 | 201 | 204 | Specificity | Altered binding specificity | 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. | ||
Sialic acid-binding Ig-like lectin 12 - Siglec12 -  Mus musculus  | |||||||
| LIG_TYR_ITIM | 430 | 435 | Binary | Pre‑translational | Alternative splicing removes the ITIM (immunoreceptor tyrosine-based inhibitory motif) of Sialic acid-binding Ig-like lectin 12 (Siglec12), abrogating binding to Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11). | ||
| LIG_TYR_ITIM | 430 | 435 | Binary | Pre‑translational | Alternative splicing removes the ITIM (immunoreceptor tyrosine-based inhibitory motif) of Sialic acid-binding Ig-like lectin 12 (Siglec12), abrogating binding to Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11). | ||