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 |
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 - PLCB1 -  Homo sapiens | |||||||
LIG_SH3_3 | 1162 | 1168 | Binary | Pre‑translational | Alternative splicing removes the SH3-binding motif of Isoform B of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (PLCB1), abrogating binding to SH3 and multiple ankyrin repeat domains protein 3 (SHANK3). PLCB1 associates with a SHANK3 complex in cardiomyocytes via its splice variant-specific C-terminal tail. Studies show that Isoform B of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (PLCB1) selectively mediates downstream responses initiated by Gq-coupled receptors, in particular hypertrophy and apoptosis. | ||
Dynamin-2 - DNM2 -  Homo sapiens | |||||||
LIG_SH3_2 | 829 | 834 | Specificity | Domain hiding | An intramolecular interaction of a Bin1 SH3 binding motif, encoded by exon 10, with the Dynamin-2 (DNM2) SH3 domain prevents binding of dynamin2 to the Bin1 SH3 domain. Binding of PI(4,5)P2 to the overlapping PI(4,5)P2 binding motif encoded by exon 10 relieves the intramolecular auto-inhibitory interaction and allows the Bin1 SH3 domain to interact with the dynamin2 PxxP motif | ||
Myc box-dependent-interacting protein 1 - BIN1 -  Homo sapiens | |||||||
LIG_SH3_3 | 305 | 311 | Specificity | Domain hiding | An intramolecular interaction of an SH3 binding motif, encoded by exon 12A, in Isoform II2 of Myc box-dependent-interacting protein 1 (BIN1) with the SH3 domain of Bin1 prevents interaction of the Bin1 SH3 domain with the SH3 binding motif of Isoform II2 of Myc box-dependent-interacting protein 1 (BIN1). | ||
Myc box-dependent-interacting protein 1 - BIN1 -  Homo sapiens | |||||||
LIG_SH3_8 | 265 | 268 | Specificity | Domain hiding | An intramolecular interaction of a Bin1 SH3 binding motif, encoded by exon 10, with the Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1) SH3 domain prevents binding of dynamin2 to the Bin1 SH3 domain. Binding of PI(4,5)P2 to the overlapping PI(4,5)P2-binding motif encoded by exon 10 relieves the intramolecular auto-inhibitory interaction and allows the Bin1 SH3 domain to interact with the dynamin2 PxxP motif. | ||
LIG_SH3_8 | 265 | 268 | Binary | Pre‑translational | Alternative splicing removes the SH3-binding motif of Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1), abrogating binding to the SH3 domain of Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1). Splice-specific motifs in Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1) engage in an intra-molecular interaction with its own SH3 domain. Auto-inhibition is relieved at the plasma membrane when an overlapping lipid-binding motif outcompetes the SH3-binding motif. This means that the SH3 domain is only available for inter-molecular interactions at the plasma membrane. | ||
Myc proto-oncogene protein - MYC -  Homo sapiens | |||||||
LIG_SH3_2 | 60 | 65 | Binary | Physicochemical compatibility | Phosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1). | ||
LIG_SH3_2 | 60 | 65 | Specificity | Domain hiding | An intramolecular interaction of an SH3 binding motif, encoded by exon 12A, in Isoform II2 of Myc box-dependent-interacting protein 1 (BIN1) with the SH3 domain of Bin1 prevents interaction of the Bin1 SH3 domain with the SH3 binding motif of Myc proto-oncogene protein (MYC). | ||
Synaptojanin-2 - Synj2 -  Rattus norvegicus | |||||||
LIG_SH3_2 | 1120 | 1125 | Binary | Pre‑translational | Alternative splicing removes the SH3-binding motif of Synaptojanin-2 (Synj2), abrogating binding to Endophilin-A2 (Sh3gl1). Endophilin-A1 (Sh3gl2) and Endophilin-A3 (Sh3gl3) were also shown to bind in this study. |