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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 | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
LIG_SH3_2 - This is the motif recognized by class II SH3 domains | |||||||
| PAK1_HUMAN | 13 | 18 | Binary | Physicochemical compatibility | Phosphorylation of S21 adjacent to the SH3-binding motif of Serine/threonine-protein kinase PAK 1 (PAK1) by RAC subfamily inhibits binding to Cytoplasmic protein NCK1 (NCK1), which regulates its localization to focal contacts. | ||
| ADA15_HUMAN | 767 | 772 | Binary | Pre‑translational | Alternative splicing removes the SH3-binding motif of Disintegrin and metalloproteinase domain-containing protein 15 (ADAM15), abrogating binding to Proto-oncogene tyrosine-protein kinase Src (SRC). The overexpression of this splice variant has been linked to clinical aggressiveness of breast cancer. | ||
LIG_SH3_3 - This is the motif recognized by those SH3 domains with a non-canonical class I recognition specificity | |||||||
| TAU_HUMAN | 213 | 219 | Binary | Physicochemical compatibility | Phosphorylation of S210 adjacent to the SH3-binding motif of Isoform Tau-F of Microtubule-associated protein tau (MAPT) inhibits binding to Tyrosine-protein kinase Fyn (Fyn). | ||
| CD2_HUMAN | 294 | 300 | Specificity | Competition | T-cell surface antigen CD2 (CD2) uses overlapping motifs to bind to CD2 antigen cytoplasmic tail-binding protein 2 (CD2BP2) and Fyn, which makes their interactions mutually exclusive. Since CD2BP2 and Tyrosine-protein kinase Fyn (FYN) reside in different subcellular locations, the specificity of CD2 for the two competitors is switched by changing its cellular localization, from non-raft membranes to lipid raft membranes. | ||
| DAG1_HUMAN | 888 | 894 | Specificity | Competition | The WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive. | ||
| DAG1_HUMAN | 888 | 894 | Specificity | Competition | The WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive. | ||
LIG_SH3_5 - PXXDY motif recognized by some SH3 domains | |||||||
| CD3E_HUMAN | 184 | 188 | Binary | Allostery | Ligand binding to the T cell receptor complex TCR-CD3 results in a conformational change that exposes an SH3-binding motif in T-cell surface glycoprotein CD3 epsilon chain (CD3E), resulting in recruitment of Cytoplasmic protein NCK2 (NCK2), involved in T cell activation. | ||
| CD3E_HUMAN | 184 | 188 | Specificity | Altered binding specificity | Phosphorylation of T-cell surface glycoprotein CD3 epsilon chain (CD3E) by Lck (Tyrosine-protein kinase Lck (LCK)) during T cell activation switches the specificity of CD3E from SH3 domain containing proteins like Epidermal growth factor receptor kinase substrate 8-like protein 1 (EPS8L1) to SH2 domain containing proteins like Tyrosine-protein kinase ZAP-70 (ZAP70). | ||