Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Association of Grb2, Gads, and phospholipase C-gamma 1 with phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations on T cell angigen receptor-mediated signaling.
Characterization of the tyrosine kinase Tnk1 and its binding with phospholipase C-gamma1.
Real time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor.
PLC-gamma1 enzyme activity is required for insulin-induced DNA synthesis.
Use of signal specific receptor tyrosine kinase oncoproteins reveals that pathways downstream from Grb2 or Shc are sufficient for cell transformation and metastasis.
Identification of two C-terminal autophosphorylation sites in the PDGF beta-receptor: involvement in the interaction with phospholipase C-gamma.
Role of the pleckstrin homology domain of PLCgamma1 in its interaction with the insulin receptor.
Human scavenger receptor class B type II (SR-BII) and cellular cholesterol efflux.
The importance of three membrane-distal tyrosines in the adaptor protein NTAL/LAB.
TrkA alternative splicing: a regulated tumor-promoting switch in human neuroblastoma.
NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain.
Molecular cloning and characterization of a novel phospholipase C, PLC-eta.
Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region.
A quantitative protein interaction network for the ErbB receptors using protein microarrays.
Akt binds to and phosphorylates phospholipase C-gamma1 in response to epidermal growth factor.
A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1.
Interaction of phospholipase C-gamma1 with villin regulates epithelial cell migration.
Evidence of LAT as a dual substrate for Lck and Syk in T lymphocytes.
Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration.
Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening.
A2 isoform of mammalian translation factor eEF1A displays increased tyrosine phosphorylation and ability to interact with different signalling molecules.
PLC-gamma1 and Rac1 coregulate EGF-induced cytoskeleton remodeling and cell migration.
A phosphoinositide 3-kinase/phospholipase Cgamma1 pathway regulates fibroblast growth factor-induced capillary tube formation.
Phospholipase C-gamma1 is required for the epidermal growth factor receptor-induced squamous cell carcinoma cell mitogenesis.
Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake by inducing Vav2-RhoA-mediated cytoskeletal rearrangements.
Grb14 inhibits FGF receptor signaling through the regulation of PLCγ recruitment and activation.
Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor.
Sequential phosphorylation of SLP-76 at tyrosine 173 is required for activation of T and mast cells.
A novel regulatory mechanism links PLCγ1 to PDK1.
Tespa1 is involved in late thymocyte development through the regulation of TCR-mediated signaling.
Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation.
Analysis of protein-protein interactions in cross-talk pathways reveals CRKL protein as a novel prognostic marker in hepatocellular carcinoma.
GRB2-mediated recruitment of THEMIS to LAT is essential for thymocyte development.
Competition between Grb2 and Plcγ1 for FGFR2 regulates basal phospholipase activity and invasion.
Fine specificity and molecular competition in SLAM family receptor signalling.
Enhanced prediction of Src homology 2 (SH2) domain binding potentials using a fluorescence polarization-derived c-Met, c-Kit, ErbB, and androgen receptor interactome.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
Isolation and characterization of one soluble and two membrane-associated forms of phosphoinositide-specific phospholipase C from human platelets.
MiR-30s Family Inhibit the Proliferation and Apoptosis in Human Coronary Artery Endothelial Cells Through Targeting the 3'UTR Region of ITGA4 and PLCG1.
Tespa1 regulates T cell receptor-induced calcium signals by recruiting inositol 1,4,5-trisphosphate receptors.
HENA, heterogeneous network-based data set for Alzheimer's disease.
Physical and functional interactome atlas of human receptor tyrosine kinases.
A gain-of-function variation in PLCG1 causes a new immune dysregulation disease.
Formation of signal transfer complexes between stem cell and platelet-derived growth factor receptors and SH2 domain proteins in vitro.
Functional interaction between c-Src and its mitotic target, Sam 68.
Sequence specificity in recognition of the epidermal growth factor receptor by protein tyrosine phosphatase 1B.
Identification of amino acids in the N-terminal SH2 domain of phospholipase C gamma 1 important in the interaction with epidermal growth factor receptor.
Control of fibroblast growth factor receptor kinase signal transduction by heterodimerization of combinatorial splice variants.
Tyrosine 785 is a major determinant of Trk--substrate interaction.
CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-gamma(1) upon B cell activation.
Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk.
Evidence that the Wiskott-Aldrich syndrome protein may be involved in lymphoid cell signaling pathways.
Subsets of epidermal growth factor receptors during activation and endocytosis.
Interaction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signaling.
LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation.
Association of the insulin receptor with phospholipase C-gamma (PLCgamma) in 3T3-L1 adipocytes suggests a role for PLCgamma in metabolic signaling by insulin.
BLNK: a central linker protein in B cell activation.
BLNK (SLP-65) Signalosome hydrolyzes phosphatidyinositol bisphosphate forming diacylglycerol and inositol-1,4,5-trisphosphate
ISGylation of host proteins
PLCG1 binds to ligand-responsive p-6Y-EGFR mutants
Dissociation of phosphorylated PLCG1 from ligand-responsive p-6Y-EGFR mutants
Phosphorylation of PLCG1 by ligand-responsive p-6Y-EGFR mutants
Activated PLC gamma dissociates from the PDGF receptor
Phosphorylation of PLCgamma by PDGFR
Regulation of protein ISGylation by ISG15 deconjugating enzyme USP18
Activated FGFR1 mutants and fusions bind PLCG1
Activated FGFR1 mutants and fusions phosphorylate PLCG1
p-4Y- PLCG1 dissociates from activated FGFR1 mutants and fusions
PI(4,5)P2 is hydrolysed to I(1,4,5)P3 and DAG by tethered PLC[1] at the plasma membrane
PLC-gamma binds to the active receptor
Recruitment of PLC-gamma1 to LAT
Phosphorylation of PLC-gamma1
Recruitment of PLC-gamma1 to SLP-76
Translocation of PLC-gamma1 to PIP2
PLC-gamma1 hydrolyses PIP2
Phosphorylation and activation of PLCG
Recruitment of PLCgamma to membrane
Release of PLCG from FCGR
Interaction of PECAM-1 and PLC gamma1
Phospholipase C-gamma1 binds to the activated EGF receptor
EGFR activates PLC-gamma1 by phosphorylation
Active PLC-gamma1 dissociates from EGFR
Disassociation of PLC-gamma1 from LAT
Disassociation of PLC-gamma1 from SLP-76
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
Fc epsilon receptor (FCERI) signaling
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
PLCG1 disassociates from VEGFR2 and translocate to PM
PLC-gamma 1 binds to p-EGFRvIII mutant
Phosphorylation of PLC-gamma 1 by p-EGFRvIII mutant
Dissociation of phosphorylated PLC-gamma 1 from p-EGFRvIII mutant
Activated FGFR2 phosphorylates PLCG1
p-4Y-PLCG1 dissociates from activated FGFR3
Activated FGFR1 phosphorylates PLCG1
Activated FGFR4 phosphorylates PLCG1
p-4Y-PLCG1 dissociates from activated FGFR2
Activated FGFR2 binds PLCG1
Activated FGFR4 binds PLCG1
p-4Y-PLCG1 dissociates from activated FGFR1
Activated FGFR1 binds PLCG1
p-4Y-PLCG1 dissociates from activated FGFR4
Activated FGFR3 phosphorylates PLCG1
Activated FGFR3 binds PLCG1
p-4Y-PLCG1 dissociates from activated FGFR2 mutants
Activated FGFR3 point and translocation mutants phosphorylate PLCG1
Activated FGFR3 point and translocation mutants bind PLCG1
p-4Y-PLCG1 dissociates from activated FGFR3 point and translocation mutants
Activated FGFR2 mutants phosphorylate PLCG1
Activated FGFR4 mutants bind PLCG1
p-4Y-PLCG1 dissociates from activated FGFR4 mutants
Activated FGFR4 mutants phosphorylate PLCG1
Activated FGFR2 mutants bind PLCG1
2x p-5Y-RET:GDNF:GFRA complexes bind PLCgamma1
Activated PCLG1 dissociates from NTRK2
Activated PCLG1 dissociates from NTRK3
Recruitment of PLCgamma to membrane due to FCGR3A effect
Release of PLCG from FCGR3A
Phosphorylation and activation of PLCG due to FCGR3A effect
FCGR3A-mediated IL10 synthesis
Phosphorylated heterodimers of ERBB2 KD mutants and EGFR phosphorylate PLCG1
Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind PLCG1
Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind PLCG1
Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate PLCG1
Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR phosphorylate PLCG1
Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind PLCG1
Active ALK phosphorylates PLCG1
ALK fusion proteins bind PLCG1
ALK fusions phosphorylate PLCG1
Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis.
Deep research report on PLCG1 (Falcon)
A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells.
Structural basis for the activation of PLC-γ isozymes by phosphorylation and cancer-associated mutations.
PLCγ1 promotes phase separation of T cell signaling components.
Falcon deep research report for human PLCG1 (second run, T cell receptor context)