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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: ELM:DOC_PP1 (5 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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Type: Binary Subtype: Physicochemical compatibilityType: Binary Subtype: Pre‑translationalType: Specificity Subtype: Competition


ProteinMotifStartEndSwitch descriptionInformation

Type: Specificity Subtype: Competition
Competitive binding of multiple binding partners to overlapping or adjacent, mutually exclusive interaction interfaces depends on local target protein abundance, which can be regulated by changing the expression level or subcellular localisation of the competitors, or by scaffolding.
RB_HUMANDOC_PP1872878The 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.
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Type: Binary Subtype: Physicochemical compatibility
PTM of a residue in a motif or in its flanking regions alters the physicochemical and/or structural compatibility of the motif with its binding partner. This can either induce or enhance an interaction, or result in inhibition or even abrogation of an interaction.
NEB1_RATDOC_PP1455461Phosphorylation of S461 in the PP1-binding motif of Neurabin-1 (Ppp1r9a) by cAMP subfamily inhibits binding to the Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Ppp1ca). Binding of Neurabin-1 (Ppp1r9a) inhibits activity of the phosphatase.
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Type: Binary Subtype: Pre‑translational
Pre-translational mechanisms such as alternative splicing, alternative promoter-usage and/or RNA editing result in inclusion or removal of exons that contain an entire or partial motif.
NEK2_HUMANDOC_PP1380387Alternative splicing removes the PP1-docking motif of Serine/threonine-protein kinase Nek2 (NEK2), abrogating binding to Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PPP1CC). 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 is required for assembly/maintenance of centrosomes.
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NEK2_HUMANDOC_PP1380387Alternative 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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AKAP1_HUMANDOC_PP1151158Alternative splicing removes the PP1-binding motif of A-kinase anchor protein 1, mitochondrial (AKAP1), abrogating binding to PP-1 subfamily. Isoform AKAP149 of A-kinase anchor protein 1, mitochondrial (AKAP1) may conceivably position PKA and PP1 in close proximity where they can reversibly modulate the phosphorylation of nuclear substrates such as NPP1, DNA-binding cAMP response elements, B-type lamins and inner nuclear membrane proteins LBR and lamina-associated polypeptides, which all harbor PKA phosphorylation sites.
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