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Group by :Switch typeMotif classProteinEnzymePathway         Hide inferred   Group Index    Colouring Info              Filtered: UNIPROT:Q05586-4 (9 hits) x


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Glutamatergic synapse


MotifProteinStartEndSwitch TypeSwitch SubtypeSwitch descriptionInformationEvidence

Glutamatergic synapse (KEGG - hsa04724)
LIG_PDZ_Class_1 NMDZ1_HUMAN917922BinaryPre‑translationalAlternative 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_HUMAN917922SpecificityMotif hidingBinding 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_HUMAN893895SpecificityMotif hidingBinding 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_HUMAN917922BinaryPre‑translationalAlternative 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_HUMAN917922SpecificityMotif hidingBinding 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_HUMAN893895SpecificityMotif hidingBinding 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_HUMAN917922BinaryPre‑translationalAlternative 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_HUMAN917922SpecificityMotif hidingBinding 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_HUMAN893895SpecificityMotif hidingBinding 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
           
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