Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Molecular cloning of a novel gene encoding a membrane-associated adaptor protein (LAX) in lymphocyte signaling.
Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region.
Towards a proteome-scale map of the human protein-protein interaction network.
A quantitative protein interaction network for the ErbB receptors using protein microarrays.
A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex.
Crystal structure of the C-terminal SH3 domain of the adaptor protein GADS in complex with SLP-76 motif peptide reveals a unique SH3-SH3 interaction.
A noncanonical SH3 domain binding motif links BK channels to the actin cytoskeleton via the SH3 adapter cortactin.
Efficient T-cell receptor signaling requires a high-affinity interaction between the Gads C-SH3 domain and the SLP-76 RxxK motif.
SH2 domain containing leukocyte phosphoprotein of 76-kDa (SLP-76) feedback regulation of ZAP-70 microclustering.
Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL.
Next-generation sequencing to generate interactome datasets.
The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells.
Enhanced prediction of Src homology 2 (SH2) domain binding potentials using a fluorescence polarization-derived c-Met, c-Kit, ErbB, and androgen receptor interactome.
Identification of SH3 domain proteins interacting with the cytoplasmic tail of the a disintegrin and metalloprotease 10 (ADAM10).
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
A proteome-scale map of the human interactome network.
Phospho-tyrosine dependent protein-protein interaction network.
Pooled-matrix protein interaction screens using Barcode Fusion Genetics.
Architecture of the human interactome defines protein communities and disease networks.
LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells.
Maximizing binary interactome mapping with a minimal number of assays.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
AI-guided pipeline for protein-protein interaction drug discovery identifies a SARS-CoV-2 inhibitor.
Molecular cloning and expression of human grap-2, a novel leukocyte-specific SH2- and SH3-containing adaptor-like protein that binds to gab-1.
Interaction of other adapter proteins with p-KIT
Phosphorylation of SLP-76
Recruitment of SLP-76 to Gads
Phosphorylation of PLC-gamma1
Recruitment of Gads to LAT
Recruitment of PLC-gamma1 to SLP-76
Recruitment of ITK to SLP-76
Disassociation of PLC-gamma1 from SLP-76
Recruitment of GADS:SLP-76 to p-5Y-LAT
Phosphorylation of SLP-76 by p-SYK
Recruitment of PLC-gamma to SLP-76 and p-5Y-LAT
Activation of RAC1 by VAV2/3
Recruitment of VAV and BTK to p-SLP-76
Phosphorylation of BTK by p-SYK
Phosphorylation and activation of VAV2/VAV3 by SYK
Phosphorylation of PLC-gamma by p-BTK/p-SYK
Phosphorylation of TEC kinases by p-SYK
Activation of RAC1 by VAV
Phosphorylation and activation of VAV
Hydrolysis of PIP2 by PLCG
Phosphorylation of SLP-76 by p-SYK
Autophosphorylation of PAK
Autophosphorylation of BTK/ITK
Recruitment of PAK to the membrane by binding active RAC1
Recruitment of VAV to p-SLP-76
Active FLT3 binds to GRAP2
The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors.
GrpL, a Grb2-related adaptor protein, interacts with SLP-76 to regulate nuclear factor of activated T cell activation.
Requirement for the SLP-76 adaptor GADS in T cell development.
Leukocyte-specific adaptor protein Grap2 interacts with hematopoietic progenitor kinase 1 (HPK1) to activate JNK signaling pathway in T lymphocytes.
Structural basis for differential recognition of tyrosine-phosphorylated sites in the linker for activation of T cells (LAT) by the adaptor Gads.
Disruption of SLP-76 interaction with Gads inhibits dynamic clustering of SLP-76 and FcepsilonRI signaling in mast cells.
Selective impairment of FcepsilonRI-mediated allergic reaction in Gads-deficient mice.
Modulation of TCR responsiveness by the Grb2-family adaptor, Gads.
Bridging the Gap: Modulatory Roles of the Grb2-Family Adaptor, Gads, in Cellular and Allergic Immune Responses.
Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc.
Mona, a novel hematopoietic-specific adaptor interacting with the macrophage colony-stimulating factor receptor, is implicated in monocyte/macrophage development.
Expression of Mona (monocytic adapter) in myeloid progenitor cells results in increased and prolonged MAP kinase activation upon macrophage colony-stimulating factor stimulation.
Differential roles for the adapters Gads and LAT in platelet activation by GPVI and CLEC-2.
Critical redundant functions of the adapters Grb2 and Gads in platelet (hem)ITAM signaling in mice.
T Cell Costimulation by CD6 Is Dependent on Bivalent Binding of a GADS/SLP-76 Complex.
Itk Promotes the Integration of TCR and CD28 Costimulation through Its Direct Substrates SLP-76 and Gads.
A high-affinity Arg-X-X-Lys SH3 binding motif confers specificity for the interaction between Gads and SLP-76 in T cell signaling.
Grf40, A novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT.
GADS is required for TCR-mediated calcium influx and cytokine release, but not cellular adhesion, in human T cells.
Cooperative assembly of a four-molecule signaling complex formed upon T cell antigen receptor activation.
Mapping the SLP76 interactome in T cells lacking each of the GRB2-family adaptors reveals molecular plasticity of the TCR signaling pathway.
Expression of GADS enhances FLT3-induced mitogenic signaling.
Falcon deep research report for human GRAP2