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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 |
| Type: Specificity Subtype: Altered binding specificity | Type: Specificity Subtype: Competition | Type: Uncategorised Subtype: Uncategorised |
| Protein | Motif | Start | End | Switch description | Information |
Type: Specificity Subtype: Competition | |||||||
| Competitive binding of multiple binding partners to overlapping or adjacent, mutually exclusive interaction interfaces depends on local target protein abundance, which can be regulated by changing the expression level or subcellular localisation of the competitors, or by scaffolding. | |||||||
| CD2_HUMAN | LIG_GYF | 295 | 303 | T-cell surface antigen CD2 (CD2) uses overlapping motifs to bind to CD2 antigen cytoplasmic tail-binding protein 2 (CD2BP2) and Fyn, which makes their interactions mutually exclusive. Since CD2BP2 and Tyrosine-protein kinase Fyn (FYN) reside in different subcellular locations, the specificity of CD2 for the two competitors is switched by changing its cellular localization, from non-raft membranes to lipid raft membranes. | |||
| CD2_HUMAN | LIG_SH3_3 | 294 | 300 | T-cell surface antigen CD2 (CD2) uses overlapping motifs to bind to CD2 antigen cytoplasmic tail-binding protein 2 (CD2BP2) and Fyn, which makes their interactions mutually exclusive. Since CD2BP2 and Tyrosine-protein kinase Fyn (FYN) reside in different subcellular locations, the specificity of CD2 for the two competitors is switched by changing its cellular localization, from non-raft membranes to lipid raft membranes. | |||
Type: Uncategorised Subtype: Uncategorised | |||||||
| Switches that have unique regulatory mechanisms. As more instances accumulate these switches may be worthy of a novel switch type | |||||||
| WASP_HUMAN | LIG_GBD_WASP_1 | 466 | 476 | Phosphorylation of Wiskott-Aldrich syndrome protein (WAS) at Y291 by Src kinases, e.g. , destabilises the auto-inhibitory intramolecular interaction of Wiskott-Aldrich syndrome protein (WAS). | |||
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. | |||||||
| DAG1_HUMAN | LIG_SH2_SRC | 892 | 895 | Adhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by Src kinase (Proto-oncogene tyrosine-protein kinase Src (SRC)) switches the specificity of DAG1 from the WW domain containing cytoskeletal linker Dystrophin (DMD) to the SH2 domain containing Tyrosine-protein kinase Fyn (FYN). | |||