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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:P62136 (3 hits) x


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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

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Retinoblastoma-associated proteinSerine/threonine-protein kinase Nek2


MotifStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

Retinoblastoma-associated protein - RB1 -  Homo sapiens
DOC_CYCLIN_1873877SpecificityCompetitionThe 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.
details
DOC_PP1872878SpecificityCompetitionThe 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.
details

Serine/threonine-protein kinase Nek2 - NEK2 -  Homo sapiens
DOC_PP1380387BinaryPre‑translationalAlternative 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.
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