LIG_PDZ_Class_1 - The C-terminal class 1 PDZ-binding motif is classically represented by a pattern like (ST)X(VIL)* |
IRK4_HUMAN | 440 | 445 | Binary | Physicochemical compatibility | Phosphorylation 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 |
ADA22_HUMAN | 901 | 906 | Binary | Pre‑translational | Alternative 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_HUMAN | 917 | 922 | Binary | Pre‑translational | Alternative 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_HUMAN | 917 | 922 | Specificity | Motif hiding | Binding 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_HUMAN | 917 | 922 | Binary | Pre‑translational | Alternative 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_HUMAN | 917 | 922 | Specificity | Motif hiding | Binding 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_HUMAN | 917 | 922 | Binary | Pre‑translational | Alternative 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_HUMAN | 917 | 922 | Specificity | Motif hiding | Binding 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 |
TRG_ER_diArg_1 - The di-Arg ER retention motif is defined by two consecutive arginine residues (RR) or with a single residue insertion (RXR). The motif is completed by an adjacent hydrophobic/arginine residue which may be on either side of the Arg pair. |
NMDZ1_HUMAN | 893 | 895 | Specificity | Motif hiding | Binding 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 |