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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:P06241 (4 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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DystroglycanT-cell surface antigen CD2Wiskott-Aldrich syndrome protein


MotifStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

Dystroglycan - DAG1 -  Homo sapiens
LIG_SH2_SRC892895SpecificityAltered binding specificityAdhesion-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).
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T-cell surface antigen CD2 - CD2 -  Homo sapiens
LIG_GYF295303SpecificityCompetitionT-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.
details
LIG_SH3_3294300SpecificityCompetitionT-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.
details

Wiskott-Aldrich syndrome protein - WAS -  Homo sapiens
LIG_GBD_WASP_1466476UncategorisedUncategorisedPhosphorylation 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).
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