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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:P84091 (3 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

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Cytotoxic T-lymphocyte protein 4 (Mus)PEX5-related protein (Mus)Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Mus)


MotifStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

Cytotoxic T-lymphocyte protein 4 - Ctla4 -  Mus musculus
TRG_ENDOCYTIC_2201204SpecificityAltered binding specificityDephosphorylation 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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PEX5-related protein - Pex5l -  Mus musculus
TRG_ENDOCYTIC_23841BinaryPre‑translationalAlternative 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.
details

Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma - Pip5k1c -  Mus musculus
TRG_ENDOCYTIC_2644647BinaryPre‑translationalAlternative 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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