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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:P62993 (15 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
LIG_SH2_GRB2LIG_SH2_ICLIG_SH3_3
LIG_WW_1


ProteinStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

LIG_SH2_GRB2 - GRB2-like Src Homology 2 (SH2) domains binding motif.
A4_HUMAN757760CumulativeRheostaticWhile phosphorylation of Y757 in the SH2-binding motif of Amyloid beta A4 protein (APP) induces binding to Growth factor receptor-bound protein 2 (GRB2), additional phosphorylation of T743 further increases the strength of the interaction.
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A4_HUMAN757760SpecificityAltered binding specificityPhosphorylation of Y757 in APP (Amyloid beta A4 protein (APP)) switches its specificity from PTB domain containing proteins, like Amyloid beta A4 precursor protein-binding family B member 1 (APBB1), which is involved in trafficking and processing of APP, to SH2 domain containing proteins, such as Growth factor receptor-bound protein 2 (GRB2).
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ERBB3_HUMAN12621265BinaryPhysicochemical compatibilityPhosphorylation of Y1262 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to Growth factor receptor-bound protein 2 (GRB2).
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LIG_SH2_IC -
A9UF02_HUMAN174180BinaryPhysicochemical compatibilityPhosphorylation of Y177 in the SH2-binding motif of BCR/ABL fusion induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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EGFR_HUMAN10921100BinaryPhysicochemical compatibilityPhosphorylation of Y1092 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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MET_HUMAN13511360BinaryPhysicochemical compatibilityPhosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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SHC1_HUMAN423435BinaryPhysicochemical compatibilityPhosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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FRS2_HUMAN191200BinaryPhysicochemical compatibilityPhosphorylation of Y196 in the SH2-binding motif of Fibroblast growth factor receptor substrate 2 (FRS2) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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FRS2_HUMAN301310BinaryPhysicochemical compatibilityPhosphorylation of Y306 in the SH2-binding motif of Fibroblast growth factor receptor substrate 2 (FRS2) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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FRS2_HUMAN345355BinaryPhysicochemical compatibilityPhosphorylation of Y349 in the SH2-binding motif of Fibroblast growth factor receptor substrate 2 (FRS2) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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FRS2_HUMAN385395BinaryPhysicochemical compatibilityPhosphorylation of Y392 in the SH2-binding motif of Fibroblast growth factor receptor substrate 2 (FRS2) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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LIG_SH3_3 - This is the motif recognized by those SH3 domains with a non-canonical class I recognition specificity
DAG1_HUMAN888894SpecificityCompetitionThe WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive.
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DAG1_HUMAN888894SpecificityCompetitionThe WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive.
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LIG_WW_1 - PPXY is the motif recognized by WW domains of Group I
DAG1_HUMAN889892SpecificityCompetitionThe WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive.
details
DAG1_HUMAN889892SpecificityCompetitionThe WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive.
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