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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_Dynein_DLC8_1 - The [KR]xTQT motif interacts with the common target-accepting grooves of 8kDa Dynein Light Chain dimer. | |||||||
| B2L11_HUMAN | 50 | 56 | Binary | Physicochemical compatibility | Phosphorylation of T56 by Mitogen-activated protein kinase 8 (MAPK8) in the Dynein-binding motif of Isoform Bim(L) of Bcl-2-like protein 11 (BCL2L11) inhibits binding to Dynein light chain 1, cytoplasmic (DYNLL1). Most Bim in healthy cells is sequestered away bound to light chain dynein molecules. Cells exposed to environmental stress up-regulate c-Jun NH(2)-terminal kinase (JNK) that phosphorylates both Bim and Bmf, releasing them from motor complexes and promoting apoptosis. | ||
| B2L11_HUMAN | 110 | 116 | Binary | Pre‑translational | Alternative splicing removes the Dynein-binding motif of Bcl-2-like protein 11 (BCL2L11), abrogating binding to Dynein light chain 1, cytoplasmic (DYNLL1). Most BCL2L11 in healthy cells is sequestered away bound to DYNLL1 (the exception is Bim-S Isoform BCL2-like 11 transcript variant 9 of Bcl-2-like protein 11 (BCL2L11)). Cells exposed to environmental stress up-regulate c-Jun NH(2)-terminal kinases (JNK) that phosphorylate both BCL2L11 and BMF, releasing them from motor complexes and promoting apoptosis. | ||
LIG_Dynein_DLC8_2 - | |||||||
| MYO5A_HUMAN | 1286 | 1290 | Binary | Pre‑translational | Alternative splicing removes the dynein-binding motif of Unconventional myosin-Va (MYO5A), abrogating binding to Dynein light chain 2, cytoplasmic (DYNLL2). DYNLL2 (also known as DLC2) globally protects the tail domains of MYO5A against limited proteolysis. | ||