Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
  Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
  Physicochemical compatibility |   Pre-translational |   Competition |
Type: Binary Subtype: Physicochemical compatibility | Type: Binary Subtype: Pre‑translational |
Protein | Motif | Start | End | Switch description | Information |
Type: Binary Subtype: Physicochemical compatibility | |||||||
PTM of a residue in a motif or in its flanking regions alters the physicochemical and/or structural compatibility of the motif with its binding partner. This can either induce or enhance an interaction, or result in inhibition or even abrogation of an interaction. | |||||||
LMP1_EBVB9 | DEG_SCF_TRCP1_1 | 210 | 215 | Dual phosphorylation of S211 and S215 in the TrCP1-binding motif of Latent membrane protein 1 (LMP1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation. | |||
PRLR_HUMAN | DEG_SCF_TRCP1_1 | 348 | 353 | Dual phosphorylation of S349 and S353 in the TrCP1-binding motif of Prolactin receptor (PRLR) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation. | |||
Type: Binary Subtype: Pre‑translational | |||||||
Pre-translational mechanisms such as alternative splicing, alternative promoter-usage and/or RNA editing result in inclusion or removal of exons that contain an entire or partial motif. | |||||||
PRLR_HUMAN | DEG_SCF_TRCP1_1 | 348 | 353 | Alternative Splicing removes the degron motif of Prolactin receptor (PRLR) abrogating binding to F-box/WD repeat-containing protein 11 (FBXW11). SCF-beta-TrCP2 negatively regulates the long isoform of PRLR (Isoform 1 of Prolactin receptor (PRLR)). Should be noted that TrCP2 has a predominately cytoplasmic localisation compared to TrCP1 that is located in the nucleus. The mechanism for the down-regulation of the intermediate (Isoform Intermediate of Prolactin receptor (PRLR)) and short (Isoform Short form 1a of Prolactin receptor (PRLR) and Isoform Short form 1b of Prolactin receptor (PRLR)) that lack the TrCP degron is still not known. However it should be noted that the short and intermediate are either partially deficient or entirely deficient in mediating the signal transduction pathways induced by PRL (see Kine et al. (1999) (here) and Ross et al. (1997) (here)). This though is likely due to the missing STAT5-SH2-binding motif. |