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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:Q9Y618 (4 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: AllosteryType: 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.
NCOR2_HUMANDOC_WW_Pin1_412381243Phosphorylation of T1241 in the Pin1-binding motif of Nuclear receptor corepressor 2 (NCOR2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
NCOR2_HUMANDOC_WW_Pin1_414411446Phosphorylation of T1444 in the Pin1-binding motif of Nuclear receptor corepressor 2 (NCOR2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Type: Binary Subtype: Allostery
The binding properties of a motif or a motif-binding domain are modulated indirectly by allosteric effects resulting from PTM or effector binding at a site that is distinct from the actual interaction interface.
NCOR2_HUMANLIG_CORNRBOX21432151Binding of the leukotriene D4 ligand to the nuclear Peroxisome proliferator-activated receptor alpha (PPARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 2 (NCOR2) inaccessible.
details
NCOR2_HUMANLIG_CORNRBOX23502358Binding of the leukotriene D4 ligand to the nuclear Peroxisome proliferator-activated receptor alpha (PPARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 2 (NCOR2) inaccessible.
details
           
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