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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:O00499 (9 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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Type: Binary Subtype: Physicochemical compatibilityType: Binary Subtype: Pre‑translationalType: Specificity Subtype: Domain hiding


ProteinMotifStartEndSwitch descriptionInformation

Type: Specificity Subtype: Domain hiding
A domain can be sterically masked by binding of an effector when there is a large difference in intrinsic affinity of the domain for different binding partners, or a large difference in the local abundance of these partners, thereby precluding further interactions of the domain. Binding of the masking molecule can be PTM-dependent or -independent.
BIN1_HUMANLIG_SH3_3305311An intramolecular interaction of an SH3 binding motif, encoded by exon 12A, in Isoform II2 of Myc box-dependent-interacting protein 1 (BIN1) with the SH3 domain of Bin1 prevents interaction of the Bin1 SH3 domain with the SH3 binding motif of Isoform II2 of Myc box-dependent-interacting protein 1 (BIN1).
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MYC_HUMANLIG_SH3_26065An intramolecular interaction of an SH3 binding motif, encoded by exon 12A, in Isoform II2 of Myc box-dependent-interacting protein 1 (BIN1) with the SH3 domain of Bin1 prevents interaction of the Bin1 SH3 domain with the SH3 binding motif of Myc proto-oncogene protein (MYC).
details
BIN1_HUMANLIG_SH3_8265268An intramolecular interaction of a Bin1 SH3 binding motif, encoded by exon 10, with the Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1) SH3 domain prevents binding of dynamin2 to the Bin1 SH3 domain. Binding of PI(4,5)P2 to the overlapping PI(4,5)P2-binding motif encoded by exon 10 relieves the intramolecular auto-inhibitory interaction and allows the Bin1 SH3 domain to interact with the dynamin2 PxxP motif.
details
DYN2_HUMANLIG_SH3_2829834An intramolecular interaction of a Bin1 SH3 binding motif, encoded by exon 10, with the Dynamin-2 (DNM2) SH3 domain prevents binding of dynamin2 to the Bin1 SH3 domain. Binding of PI(4,5)P2 to the overlapping PI(4,5)P2 binding motif encoded by exon 10 relieves the intramolecular auto-inhibitory interaction and allows the Bin1 SH3 domain to interact with the dynamin2 PxxP motif
details

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.
MYC_HUMANLIG_SH3_26065Phosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
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.
BIN1_HUMANLIG_Clathr_ClatBox_1390394Alternative splicing removes the Clathrin I-binding motif of Myc box-dependent-interacting protein 1 (BIN1), abrogating binding to Clathrin heavy chain 1 (CLTC).
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BIN1_HUMANLIG_Clathr_ClatBox_2415420Alternative splicing removes the Clathrin II-binding motif of Myc box-dependent-interacting protein 1 (BIN1), abrogating binding to Clathrin heavy chain 1 (CLTC).
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BIN1_HUMANLIG_SH3_8265268Alternative splicing removes the SH3-binding motif of Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1), abrogating binding to the SH3 domain of Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1). Splice-specific motifs in Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1) engage in an intra-molecular interaction with its own SH3 domain. Auto-inhibition is relieved at the plasma membrane when an overlapping lipid-binding motif outcompetes the SH3-binding motif. This means that the SH3 domain is only available for inter-molecular interactions at the plasma membrane.
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BIN1_HUMANLIG_PI(4,5)P2258266Alternative splicing removes the PI(4,5)P2-binding motif of Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1), abrogating binding to 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate. Splice-specific motifs in Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1) engage in an intra-molecular interaction with its own SH3 domain. Auto-inhibition is relieved at the plasma membrane when an overlapping lipid-binding motif outcompetes the SH3-binding motif. This means that the SH3 domain is only available for inter-molecular interactions at the plasma membrane.
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