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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 |
| Motif | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
Retinoblastoma-associated protein - RB1 - Homo sapiens | |||||||
| DOC_CYCLIN_1 | 873 | 877 | Specificity | Competition | The docking sites for PP1 (e.g. Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA)) and Cdk-Cyclins (e.g. Cyclin-A2 (CCNA2)) on Retinoblastoma-associated protein (RB1) overlap, which makes their binding to RB1 mutually exclusive. Hypophosphorylated RB1 blocks E2F-dependent transcription, while hyperphosphorylation inactivates RB1 as a repressor, thereby promoting cell cycle progression. | ||
| DOC_PP1 | 872 | 878 | Specificity | Competition | The docking sites for PP1 (e.g. Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA)) and Cdk-Cyclins (e.g. Cyclin-A2 (CCNA2)) on Retinoblastoma-associated protein (RB1) overlap, which makes their binding to RB1 mutually exclusive. Hypophosphorylated RB1 blocks E2F-dependent transcription, while hyperphosphorylation inactivates RB1 as a repressor, thereby promoting cell cycle progression. | ||
Serine/threonine-protein kinase Nek2 - NEK2 - Homo sapiens | |||||||
| DOC_PP1 | 380 | 387 | Binary | Pre‑translational | Alternative splicing removes the PP1-docking motif of Serine/threonine-protein kinase Nek2 (NEK2), abrogating binding to Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA). Isoform Nek2A of Serine/threonine-protein kinase Nek2 (NEK2) is localised at centrosomes and causes centrosome splitting. Isoform Nek2B of Serine/threonine-protein kinase Nek2 (NEK2) is expressed at a different point in the cell cycle and required for assembly/maintenance of centrosomes. | ||