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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: ELM:MOD_SUMO_PHOS (2 hits) x

x  Coloured by switch type.
  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

x  Index
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.
ESR2_HUMANMOD_SUMO_PHOS47The GSK3-beta binding site at S12 in Estrogen receptor beta (ESR2) is primed by (most likely) RAC-alpha serine/threonine-protein kinase (AKT1). This enhances the binding of SUMO-conjugating enzyme UBC9 (UBE2I) at the adjacent Sumoylation site. This site is also primed at S6 (most likely) by AKT1. The addition of SUMO at K4 stabilises ESR2 as it prevents the ubiquitination at K4 (see switch details)
ESR2_HUMANMOD_SUMO_PHOS47Sumoylation of K4 in Estrogen receptor beta (ESR2) is inhibited by ubiquitination K4. This destabilises ESR2 increasing its turnover (see also switch details)
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