Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
  Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
  Physicochemical compatibility |   Pre-translational |   Competition |
PEX5-related protein (Mus) | T-cell surface glycoprotein CD3 delta chain (Mus) | T-cell surface glycoprotein CD3 gamma chain (Mus) |
Motif | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
PEX5-related protein - Pex5l -  Mus musculus | |||||||
TRG_LysEnd_APsAcLL_1 | 14 | 19 | Binary | Pre‑translational | Alternative splicing removes the di-leucine endocytosis motif of PEX5-related protein (Pex5l), abrogating binding to AP-2 complex subunit sigma (Ap2s1). The motif is present in exon 5. | ||
T-cell surface glycoprotein CD3 delta chain - Cd3d -  Mus musculus | |||||||
TRG_LysEnd_APsAcLL_1 | 138 | 143 | Binary | Allostery | Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (Ap2s1) subunit for recruitment of T-cell surface glycoprotein CD3 delta chain (Cd3d) via an endocytosis motif. | ||
T-cell surface glycoprotein CD3 gamma chain - Cd3g -  Mus musculus | |||||||
TRG_LysEnd_APsAcLL_1 | 149 | 154 | Binary | Allostery | Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (Ap2s1) subunit for recruitment of T-cell surface glycoprotein CD3 gamma chain (Cd3g) via an endocytosis motif. |