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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: PFAM:PF01217 (16 hits) x


x  Coloured by switch type.
  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

x  Index
Type: Binary Subtype: AllosteryType: Binary Subtype: Pre‑translational


ProteinMotifStartEndSwitch descriptionInformation

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.
PEX5R_MOUSETRG_LysEnd_APsAcLL_11419Alternative 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.
details
SORC1_HUMANTRG_LysEnd_APsAcLL_211361140Alternative splicing removes the di-leucine motif of Isoform 4 of VPS10 domain-containing receptor SorCS1 (SORCS1), abrogating binding to AP-2 complex subunit sigma (AP2S1). Human and mouse have completely different C-termini for SorCS1a (also known as Isoform 4 of VPS10 domain-containing receptor SorCS1 (SORCS1)), with only the human splice variant containing the motif.
details
PRLR_RATTRG_LysEnd_APsAcLL_1301306Alternative splicing removes the di-leucine endocytosis motif of Prolactin receptor (Prlr), partially inhibiting binding to AP-2 complex subunit sigma (AP2S1) and the rate of endocytosis. Isoform Long of Prolactin receptor (Prlr) (also known as PRLR-long) has a longer C-terminal tail than the Isoform Short of Prolactin receptor (Prlr) (also known as PRLR-short) splice variant. PRLR-long internalises faster than PRLR-short due to two additional di-leucine motifs in the C-terminus (where the adjacent phenylalanine also plays a role). PRLR-short has two di-leucine motifs whereas PRLR-long has four.
details

Type: Binary Subtype: Allostery
The binding properties of a motif or a motif-binding domain are modulated indirectly by allosteric effects resulting from PTM or effector binding at a site that is distinct from the actual interaction interface.
CD4_HUMANTRG_LysEnd_APsAcLL_1434439Binding 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 CD4 (CD4) via an endocytosis motif.
details
NPC1_HUMANTRG_LysEnd_APsAcLL_112711276Binding 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 Niemann-Pick C1 protein (NPC1) via an endocytosis motif.
details
HG2A_HUMANTRG_LysEnd_APsAcLL_11924Binding 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 HLA class II histocompatibility antigen gamma chain (CD74) via an endocytosis motif.
details
CD3D_MOUSETRG_LysEnd_APsAcLL_1138143Binding 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.
details
NEF_HV1H2TRG_LysEnd_APsAcLL_1160165Binding 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 Nef protein (nef) via an endocytosis motif.
details
NEF_HV1B8TRG_LysEnd_APsAcLL_1159164Binding 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 Protein Nef (nef) via an endocytosis motif.
details
CD3G_MOUSETRG_LysEnd_APsAcLL_1149154Binding 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.
details
CD44_HUMANTRG_LysEnd_APsAcLL_1708713Binding 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 CD44 antigen (CD44) via an endocytosis motif.
details
OPRD_HUMANTRG_LysEnd_APsAcLL_1241246Binding 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 Delta-type opioid receptor (OPRD1) via an endocytosis motif.
details
BCAM_HUMANTRG_LysEnd_APsAcLL_1604609Binding 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 Basal cell adhesion molecule (BCAM) via an endocytosis motif.
details
ENV_BLVTRG_LysEnd_APsAcLL_1463468Binding 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 Envelope glycoprotein (env) via an endocytosis motif.
details
BACE1_HUMANTRG_LysEnd_APsAcLL_1495500Binding 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 Beta-secretase 1 (BACE1) via an endocytosis motif.
details
ATP7A_HUMANTRG_LysEnd_APsAcLL_114831488Binding 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 Copper-transporting ATPase 1 (ATP7A) via an endocytosis motif.
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