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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 |
| Protein | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
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 | Binary | Physicochemical compatibility | Phosphorylation of S896 adjacent to the ER retention motif of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1) by PKC subfamily (and possibly S897 by PKA) inactivates the motif and promotes delivery of the receptor to the plasma membrane. Optimal trafficking upon dual phosphorylation of S896 and S897 allows regulation of receptor trafficking by coordinated PKA and PKC signaling. | ||
| ADA22_HUMAN | 829 851 | 831 854 | Specificity | Motif hiding | Phosphorylation-induced binding of dimeric 14-3-3 protein beta/alpha (YWHAB) to Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22) blocks ER retention motifs in Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22) and regulates transport of this protein to the membrane. | ||
| GPR15_HUMAN | 352 | 354 | Specificity | Motif hiding | Phosphorylation-induced binding of 14-3-3 protein beta/alpha (YWHAB) promotes cell surface expression of G-protein coupled receptor 15 (GPR15) by releasing the receptor from the ER retrieval/retention pathway that is mediated by the interaction of its ER retention motif with Coatomer subunit beta (COPB1). | ||
| HG2A_HUMAN | 3 | 5 | Specificity | Motif hiding | The basic ER retention motif of HLA class II histocompatibility antigen gamma chain (CD74) is blocked from binding to Coatomer subunit beta (COPB1) by phosphorylation-induced binding of 14-3-3 protein beta/alpha (YWHAB), regulating its release from the ER and trafficking to the plasma membrane. | ||
| GABR1_HUMAN | 923 | 926 | Specificity | Motif hiding | Interaction of the GABA receptor R2 subunit (Gamma-aminobutyric acid type B receptor subunit 2 (GABBR2)) with the R1 subunit (Gamma-aminobutyric acid type B receptor subunit 1 (GABBR1)) via coiled-coil forming domains masks the ER retention motif in the R1 subunit (Gamma-aminobutyric acid type B receptor subunit 1 (GABBR1)), thereby promoting surface expression of fully assembled GABA receptors. | ||
| 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. | ||
| 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. | ||
| 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. | ||
TRG_ER_diArg_2 - | |||||||
| GRIK1_RAT | 937 | 941 | Binary | Pre‑translational | Alternative splicing removes the di-arginine ER-retention motif of Glutamate receptor, ionotropic kainate 1 (Grik1), abrogating binding to Coatomer subunit beta (COPB1). | ||