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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:Q01968 (2 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 compatibility


ProteinMotifStartEndSwitch descriptionInformation

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.
DP13A_HUMANLIG_RhoGAP_OCRL_1403415Phosphorylation of S403 in the RhoGAP-binding motif of DCC-interacting protein 13-alpha (APPL1), possibly by PKA, inhibits its interaction with Inositol polyphosphate 5-phosphatase OCRL-1 (OCRL).
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DP13A_HUMANLIG_RhoGAP_OCRL_1403415Phosphorylation of S410 in the RhoGAP-binding motif of DCC-interacting protein 13-alpha (APPL1) inhibits its interaction with Inositol polyphosphate 5-phosphatase OCRL-1 (OCRL).
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