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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: ELM:MOD_NMyristoyl (3 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: Pre‑translational

ProteinMotifStartEndSwitch descriptionInformation

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.
PDE2A_HUMANMOD_NMyristoyl17Alternative splicing removes the myristoylation motif of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A). The soluble Isoform PDE2A1 of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A) is expressed in a variety of peripheral tissues, whereas the membrane-associated Isoform PDE2A3 of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A) is found exclusively in the brain. Isoform PDE2A3 of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A) requires N-myristoylation together with palmitoylation to be targeted to synapses, allowing control and crosstalk of cyclic nucleotides.

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.
RECO_BOVINMOD_NMyristoyl17Binding of calcium(2+) to Recoverin (RCVRN) results in a conformational change in Recoverin that makes the myristoyl moiety available for binding to the membrane.
KAPCA_HUMANMOD_NMyristoyl17Phosphorylation of cAMP-dependent protein kinase catalytic subunit alpha (PRKACA) at S11 shifts the conformational equilibrium to the myristoyl-out conformation, making the myristoyl moiety available for interaction with the membrane.
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