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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 |
DOC_WW_Pin1_4 - The Class IV WW domain interaction motif is recognised primarily by the Pin1 phosphorylation-dependent prolyl isomerase. | |||||||
| PML_HUMAN | 400 | 405 | Binary | Physicochemical compatibility | Phosphorylation of S403 in the Pin1-binding motif of Protein PML (PML) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein. | ||
| PML_HUMAN | 502 | 507 | Binary | Physicochemical compatibility | Phosphorylation of S505 in the Pin1-binding motif of Protein PML (PML) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein. | ||
| PML_HUMAN | 515 | 520 | Binary | Physicochemical compatibility | Phosphorylation of S518 in the Pin1-binding motif of Protein PML (PML) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein. | ||
| PML_HUMAN | 524 | 529 | Binary | Physicochemical compatibility | Phosphorylation of S527 in the Pin1-binding motif of Protein PML (PML) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein. | ||
LIG_SUMO_SBM_1 - Motif that mediates binding to SUMO proteins non-covalently. | |||||||
| PML_HUMAN | 556 | 566 | Binary | Pre‑translational | Alternative splicing removes the Sumoylation interacting motif (SIM) of Protein PML (PML), abrogating binding to Small ubiquitin-related modifier 1 (SUMO1) in Isoform TRIM19epsilon of Protein PML (PML). Isoforms lacking the SIM were resistant to As2O3-induced PML degradation. | ||
MOD_SUMO - Motif recognised for modification by SUMO-1 | |||||||
| PML_HUMAN | 489 | 492 | Binary | Pre‑translational | Alternative splicing removes the SUMO motif of Protein PML (PML), abrogating binding to SUMO-conjugating enzyme UBC9 (UBE2I). The study identified a major sumoylation site within the nuclear localisation signal (NLS) of PML. Although they did not determine whether the lysine residue regulates the NLS, they found that sumoylation was not necessary for nuclear localisation and that SUMO-modification only occurs in the nucleus. | ||
| PML_HUMAN | 159 | 162 | Uncategorised | Uncategorised | Sumoylation of K160 induces binding to the Protein PML (PML) protein. SUMO-modified forms of PML are essential for the recruitment of Protein PML (PML) to PML nuclear bodies. | ||
| PML_HUMAN | 159 | 162 | Uncategorised | Uncategorised | Sumoylation of K160 induces binding to the Protein PML (PML) protein. SUMO-modified forms of PML are essential for the recruitment of Death domain-associated protein 6 (DAXX) to PML nuclear bodies. | ||
TRG_NES_CRM1_1 - Some proteins re-exported from the nucleus contain a Leucine-rich nuclear export signal (NES) binding to the CRM1 exportin protein. | |||||||
| PML_HUMAN | 702 | 716 | Binary | Pre‑translational | Alternative splicing removes the nuclear export signal (NES) of Protein PML (PML), abrogating binding to Exportin-1 (XPO1) and export from the nucleus. | ||
TRG_NLS - | |||||||
| PML_HUMAN | 476 | 490 | Binary | Pre‑translational | Alternative splicing removes the nuclear localisation signal (NLS) of Protein PML (PML), abrogating binding to Importin subunit alpha-1 (KPNA1) and import into the nucleus. | ||