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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 |
DEG_SCF_TRCP1_1 - The DSGxxS phospho-dependent degron binds the F box protein of the SCF-betaTrCP1 complex. The degron is found in various proteins that function in regulation of cell state. | |||||||
| DLG1_HUMAN | 597 | 602 | Binary | Physicochemical compatibility | Dual phosphorylation of S598 and S602 in the TrCP1-binding motif of Disks large homolog 1 (DLG1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation. | ||
LIG_PDZ_Class_1 - The C-terminal class 1 PDZ-binding motif is classically represented by a pattern like (ST)X(VIL)* | |||||||
| AT2B4_HUMAN | 1236 | 1241 | Binary | Pre‑translational | Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Disks large homolog 1 (DLG1). A much lower affinity was recorded for the third PDZ domain of DLG1 (in in the micromolar range (KD = 1.2 microM) compared to nanomolar affinity (KD = 1.6 nM)). PMCA4b and DLG1 are co-expressed in kidney and intestinal epithelial cells as well as in several areas of the brain. Should be noted that the 'b' isoforms of Plasma membrane calcium-transporting ATPase 2 (ATP2B2) bind much more weakly to all PDZ domains of DLG1 | ||
| AT2B4_HUMAN | 1236 | 1241 | Binary | Pre‑translational | Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Disks large homolog 1 (DLG1). A much lower affinity was recorded for the third PDZ domain of DLG1 (in in the micromolar range (KD = 1.2 microM) compared to nanomolar affinity (KD = 1.6 nM)). PMCA4b and DLG1 are co-expressed in kidney and intestinal epithelial cells as well as in several areas of the brain. | ||