Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
  Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
  Physicochemical compatibility |   Pre-translational |   Competition |
Cell division control protein 6 homolog | Cyclin-dependent kinase inhibitor 1B | Retinoblastoma-associated protein |
Motif | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
Cell division control protein 6 homolog - CDC6 -  Homo sapiens | |||||||
DOC_CYCLIN_1 | 94 | 98 | Specificity | Domain hiding | Binding of the CDK-cyclin inhibitor p27 (Cyclin-dependent kinase inhibitor 1B (CDKN1B)) blocks the substrate recruitment site on Cyclin-A2 (CCNA2). | ||
Cyclin-dependent kinase inhibitor 1B - CDKN1B -  Homo sapiens | |||||||
DOC_CYCLIN_1 | 30 | 33 | Specificity | Domain hiding | Binding of the CDK-cyclin inhibitor p27 (Cyclin-dependent kinase inhibitor 1B (CDKN1B)) blocks the substrate recruitment site on Cyclin-A2 (CCNA2). | ||
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. |