switches.ELM

Group by :Switch type Motif class Protein Enzyme Pathway Hide inferred Group Index Colouring Info Filtered: UNIPROT:Q05586-4 (9 hits) x

x Coloured by: Pathway evidence source
Curated inferred

x Index

Glutamatergic synapse

Motif

Protein

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Information

Evidence

Glutamatergic synapse (KEGG - hsa04724)
LIG_PDZ_Class_1	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	Inferred
LIG_PDZ_Class_1	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	Inferred
TRG_ER_diArg_1	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	Inferred
LIG_PDZ_Class_1	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	Inferred
LIG_PDZ_Class_1	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	Inferred
TRG_ER_diArg_1	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	Inferred
LIG_PDZ_Class_1	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	Inferred
LIG_PDZ_Class_1	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	Inferred
TRG_ER_diArg_1	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	Inferred