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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:Q9ULV5 (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 compatibilityType: Binary Subtype: Pre‑translational


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.
HSF4_HUMANMOD_SUMO292295The phosphorylation-dependent sumoylation of the PDSM (phosphorylation-dependent sumoylation motif) strongly represses Isoform HSF4B of Heat shock factor protein 4 (HSF4) activity.
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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.
HSF4_HUMANMOD_SUMO292295Alternative splicing removes the sumoylation motif of Heat shock factor protein 4 (HSF4), abrogating binding to SUMO-conjugating enzyme UBC9 (UBE2I). The phosphorylation-dependent sumoylation of the PDSM (phosphorylation-dependent sumoylation motif) strongly represses Isoform HSF4B of Heat shock factor protein 4 (HSF4) activity.
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