About Help Definitions Submit Search Analyse Browse Home


Group by :Switch typeMotif classProteinEnzymePathway         Hide inferred   Group Index    Colouring Info              Filtered: UNIPROT:Q9Y490 (5 hits) x


x  Coloured by: Pathway evidence source
          Curated          inferred


x  Index
Focal adhesion


MotifProteinStartEndSwitch TypeSwitch SubtypeSwitch descriptionInformationEvidence

Focal adhesion (KEGG - hsa04510)
LIG_PTB_Talin PI51C_HUMAN650653BinaryPhysicochemical compatibilityPhosphorylation of S650 in the PTB-binding motif of Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma (PIP5K1C) blocks its interaction with Talin-1 (TLN1). Phosphorylation of Y649 by Src kinase enhances the interaction, possibly indirectly by inhibiting S650 phosphorylation.
details
Inferred
LIG_PTB_Apo_2 ITB3_HUMAN767774SpecificityAltered binding specificityPhosphorylation of Y773 in Integrin beta-3 (ITGB3) switches the specificity of ITGB3 from Talin-1 (TLN1) to Docking protein 1 (DOK1), with a 2-fold decrease of the affinity for TLN1 and close to a 400-fold increase of the affinity for DOK1. This switch results in negative regulation of integrin activation.
details
Inferred
LIG_Talin ITB7_HUMAN770779SpecificityCompetitionThe integrin regulator Talin-1 (TLN1) and the actin-crosslinking Filamins Filamin-A (FLNA) use overlapping binding sites on the cytoplasmic tails of beta integrin subunits Integrin beta-7 (ITGB7), which makes their interaction with beta integrin mutually exclusive.
details
Inferred
LIG_Filamin ITB7_HUMAN776787SpecificityCompetitionThe integrin regulator Talin-1 (TLN1) and the actin-crosslinking Filamins Filamin-A (FLNA) use overlapping binding sites on the cytoplasmic tails of beta integrin subunits Integrin beta-7 (ITGB7), which makes their interaction with beta integrin mutually exclusive.
details
Inferred
LIG_Talin ITB1_HUMAN775785BinaryPre‑translationalAlternative splicing alters the flanking regions of the PTB-binding motif of Isoform Beta-1D of Integrin beta-1 (ITGB1), inducing higher affinity binding to Talin-1 (TLN1). Alteration of residue 788 from G to Q and alteration of residue 786 from A to P increases the binding affinity from 491 micromolar in the canonical Isoform Beta-1A of Integrin beta-1 (ITGB1) to 95 micromolar in Isoform Beta-1D of Integrin beta-1 (ITGB1).
details
Inferred
           
Please send any suggestions/comments to: switches@elm.eu.org