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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:P78352 (9 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‑translationalType: Specificity Subtype: Motif hiding


ProteinMotifStartEndSwitch descriptionInformation

Type: Specificity Subtype: Motif hiding
Motif hiding occurs when there is a large difference in intrinsic affinity of overlapping or adjacent motifs for their respective binding partners, or a large difference in the local abundance of these partners. Binding of an effector to one motif sterically masks the overlapping or adjacent motif, thereby precluding it from binding. Binding of the masking molecule can be PTM-dependent or -independent.
NMDZ1_HUMANLIG_PDZ_Class_1917922Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
details
NMDZ1_HUMANTRG_ER_diArg_1893895Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
details
NMDZ1_HUMANLIG_PDZ_Class_1917922Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
details
NMDZ1_HUMANLIG_PDZ_Class_1917922Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
details

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.
IRK4_HUMANLIG_PDZ_Class_1440445Phosphorylation of S443 in the PDZ-binding motif of Inward rectifier potassium channel 4 (KCNJ4) by inhibits its interaction with the Disks large homolog 4 (DLG4) protein.
details

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.
ADA22_HUMANLIG_PDZ_Class_1901906Alternative splicing removes the PDZ-binding motif of Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22), abrogating binding to Disks large homolog 4 (DLG4). The motif-containing Isoform Epsilon of Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22) forms part of a complex containing Leucine-rich glioma-inactivated protein 1 (LGI1), AMPA-R (e.g. Glutamate receptor 1 (GRIA1)) and AMPA-R regulatory proteins (e.g. Voltage-dependent calcium channel gamma-2 subunit (CACNG2)), and is closely associated with epilepsy.
details
NMDZ1_HUMANLIG_PDZ_Class_1917922Alternative splicing removes the PDZ-binding motif of Isoform 4 of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1), abrogating binding to Disks large homolog 4 (DLG4). Binding of the PDZ domain of DLG4 suppresses an ER-retention motif in GRIN1, promoting its cell surface expression in a splice variant-specific manner.
details
NMDZ1_HUMANLIG_PDZ_Class_1917922Alternative splicing removes the PDZ-binding motif of Isoform 4 of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1), abrogating binding to Disks large homolog 4 (DLG4). Binding of the PDZ domain of DLG4 suppresses an ER-retention motif in GRIN1, promoting its cell surface expression in a splice variant-specific manner.
details
NMDZ1_HUMANLIG_PDZ_Class_1917922Alternative splicing removes the PDZ-binding motif of Isoform 4 of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1), abrogating binding to Disks large homolog 4 (DLG4). Binding of the PDZ domain of DLG4 suppresses an ER-retention motif in GRIN1, promoting its cell surface expression in a splice variant-specific manner.
details
           
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