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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: PFAM:PF00928 (22 hits) x
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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

x  Index
Type: Binary Subtype: AllosteryType: Binary Subtype: Physicochemical compatibilityType: Binary Subtype: Pre‑translational
Type: Specificity Subtype: Altered binding specificityType: Uncategorised Subtype: Uncategorised


ProteinMotifStartEndSwitch descriptionInformation

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.
L1CAM_HUMANTRG_ENDOCYTIC_211761179Phosphorylation of Y1176 by Proto-oncogene tyrosine-protein kinase Src (SRC) in the endocytosis motif of Neural cell adhesion molecule L1 (L1CAM) inhibits binding to AP-2 complex subunit mu (AP2M1).
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PI51C_HUMANTRG_ENDOCYTIC_2649652Phosphorylation of S645 near the AP2-binding motif of Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma (PIP5K1C) by Cyclin-dependent kinase 5 (Cdk5) inhibits its interaction with AP-2 complex subunit mu (AP2M1).
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L1CAM_HUMANTRG_ENDOCYTIC_211761179Phosphorylation of Y1176 in the endocytotic motif of Neural cell adhesion molecule L1 (L1CAM) by Proto-oncogene tyrosine-protein kinase Src (SRC) abolishes binding to the AP-2 complex subunit mu (AP2M1) and thereby inhibits internalisation of Neural cell adhesion molecule L1 (L1CAM).
details

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.
L1CAM_HUMANTRG_ENDOCYTIC_211761179Alternative splicing removes the endocytosis motif of Neural cell adhesion molecule L1 (L1CAM), abrogating binding to AP-2 complex subunit mu (AP2M1). This motif is required for sorting of L1CAM to the axonal growth cone of neurons and its clathrin-mediated internalisation. Non-neuronal cells, such as Schwann cells, do not require these motifs, probably because these cells are not highly polarised.
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PEX5R_MOUSETRG_ENDOCYTIC_23841Alternative splicing removes the endocytosis motif of Isoform 3 of PEX5-related protein (Pex5l), abrogating binding to AP-2 complex subunit mu (Ap2m1). The motif is present in exon 2, and its absence causes a significant increase in channel density of members from the potassium channel HCN family.
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SORC1_HUMANTRG_ENDOCYTIC_211321135Alternative splicing removes the endocytosis motif of Isoform 2 of VPS10 domain-containing receptor SorCS1 (SORCS1), abrogating binding to AP-2 complex subunit mu (AP2M1). The sequence is conserved in both human and mouse. Different splice variants have different endocytosis motifs.
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PI51C_MOUSETRG_ENDOCYTIC_2644647Alternative splicing removes the endocytosis motif of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c), abrogating binding to AP-2 complex subunit mu (Ap2m1). The direct interaction between the AP-2 complex and Isoform PIPKIgamma661 of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c) (PIPKIgamma661) targets this isoform to sites of endocytosis at the plasma membrane. Consequently, this results in the generation of a highly concentrated pool of PI(4,5)P2 at these sites.
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Type: Uncategorised Subtype: Uncategorised
Switches that have unique regulatory mechanisms. As more instances accumulate these switches may be worthy of a novel switch type
PPAL_HUMANTRG_ENDOCYTIC_2413416Phosphorylation of T156 in AP-2 complex subunit mu (AP2M1) by AP2-associated protein kinase 1 (AAK1) upon clathrin recruitment strengthens the interaction between AP-2 complex subunit mu (AP2M1) and cargo proteins.
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Type: Specificity Subtype: Altered binding specificity
The balance of the competition for overlapping or adjacent, mutually exclusive interaction interfaces is tipped in favor of one of the interactors by PTM-dependent modulation of the intrinsic affinity of a binding region. Multiple, successive PTMs allow sequential switching of different binding partners in an ordered manner by step-wise alteration of binding specificity.
CTLA4_MOUSETRG_ENDOCYTIC_2201204Dephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
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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.
TGON3_RATTRG_ENDOCYTIC_2350353Binding 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 mu (Ap2m1) subunit for recruitment of Trans-Golgi network integral membrane protein TGN38 (Ttgn1) via an endocytosis motif.
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EGFR_HUMANTRG_ENDOCYTIC_29981001Binding 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 mu (AP2M1) subunit for recruitment of Epidermal growth factor receptor (EGFR) via an endocytosis motif.
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TFR1_HUMANTRG_ENDOCYTIC_22023Binding 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 mu (AP2M1) subunit for recruitment of Transferrin receptor protein 1 (TFRC) via an endocytosis motif.
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ENV_HTLV2TRG_ENDOCYTIC_2477480Binding 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 mu (AP2M1) subunit for recruitment of Envelope glycoprotein gp63 (env) via an endocytosis motif.
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VGLG_VSIVATRG_ENDOCYTIC_2501504Binding 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 mu (AP2M1) subunit for recruitment of Glycoprotein G (G) via an endocytosis motif.
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ENV_HV1H2TRG_ENDOCYTIC_2712715Binding 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 mu (AP2M1) subunit for recruitment of Envelope glycoprotein gp160 (env) via an endocytosis motif.
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ENV_SIVMKTRG_ENDOCYTIC_2723726Binding 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 mu (AP2M1) subunit for recruitment of Envelope glycoprotein gp160 (env) via an endocytosis motif.
details
ASGR1_HUMANTRG_ENDOCYTIC_258Binding 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 mu (AP2M1) subunit for recruitment of Asialoglycoprotein receptor 1 (ASGR1) via an endocytosis motif.
details
LAMP1_HUMANTRG_ENDOCYTIC_2414417Binding 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 mu (AP2M1) subunit for recruitment of Lysosome-associated membrane glycoprotein 1 (LAMP1) via an endocytosis motif.
details
CTLA4_HUMANTRG_ENDOCYTIC_2201204Binding 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 mu (AP2M1) subunit for recruitment of Cytotoxic T-lymphocyte protein 4 (CTLA4) via an endocytosis motif.
details
L1CAM_HUMANTRG_ENDOCYTIC_211761179Binding 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 mu (AP2M1) subunit for recruitment of Neural cell adhesion molecule L1 (L1CAM) via an endocytosis motif.
details
ENV_BLVTRG_ENDOCYTIC_2487490Binding 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 mu (AP2M1) subunit for recruitment of Envelope glycoprotein (env) via an endocytosis motif.
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GE_VZVOTRG_ENDOCYTIC_2582585Binding 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 mu (AP2M1) subunit for recruitment of Envelope glycoprotein E (gE) via an endocytosis motif.
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