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 transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Solution structure of the SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide.
Shc and CEACAM1 interact to regulate the mitogenic action of insulin.
Crystal structures of the SH2 domain of Grb2: highlight on the binding of a new high-affinity inhibitor.
Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc.
Novel peptide inhibitors for Grb2 SH2 domain and their detection by surface plasmon resonance.
A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling.
EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis.
Tetraspanin CD81 is linked to ERK/MAPKinase signaling by Shc in liver tumor cells.
TrkA alternative splicing: a regulated tumor-promoting switch in human neuroblastoma.
Comparative analysis of the signaling capabilities of the insulin receptor-related receptor.
Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells.
Towards a proteome-scale map of the human protein-protein interaction network.
A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction.
A quantitative protein interaction network for the ErbB receptors using protein microarrays.
HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors.
Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein.
Charting the molecular network of the drug target Bcr-Abl.
Copine-III interacts with ErbB2 and promotes tumor cell migration.
Tarp regulates early Chlamydia-induced host cell survival through interactions with the human adaptor protein SHC1.
A positive feedback loop of ER-α36/EGFR promotes malignant growth of ER-negative breast cancer cells.
Translationally controlled tumor protein induces human breast epithelial cell transformation through the activation of Src.
Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor.
The SRC-associated protein CUB Domain-Containing Protein-1 regulates adhesion and motility.
A directed protein interaction network for investigating intracellular signal transduction.
Phosphotyrosine mediated protein interactions of the discoidin domain receptor 1.
SnoN/SkiL expression is modulated via arsenic trioxide-induced activation of the PI3K/AKT pathway in ovarian cancer cells.
Threshold-controlled ubiquitination of the EGFR directs receptor fate.
Temporal regulation of EGF signalling networks by the scaffold protein Shc1.
Structure homology and interaction redundancy for discovering virus-host protein interactions.
Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms.
Charting the molecular links between driver and susceptibility genes in colorectal cancer.
Enhanced prediction of Src homology 2 (SH2) domain binding potentials using a fluorescence polarization-derived c-Met, c-Kit, ErbB, and androgen receptor interactome.
A proteome-scale map of the human interactome network.
EGF-receptor specificity for phosphotyrosine-primed substrates provides signal integration with Src.
Phenotypic and Interaction Profiling of the Human Phosphatases Identifies Diverse Mitotic Regulators.
A Global Analysis of the Receptor Tyrosine Kinase-Protein Phosphatase Interactome.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites.
Elucidation of protein interactions necessary for the maintenance of the BCR-ABL signaling complex.
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Mapping the Phospho-dependent ALK Interactome to Identify Novel Components in ALK Signaling.
CFTR interactome mapping using the mammalian membrane two-hybrid high-throughput screening system.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Physical and functional interactome atlas of human receptor tyrosine kinases.
Systematic discovery of mutation-directed neo-protein-protein interactions in cancer.
Differential CFTR-Interactome Proximity Labeling Procedures Identify Enrichment in Multiple SLC Transporters.
Multimodal cell maps as a foundation for structural and functional genomics.
Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor.
Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2.
Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain.
Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor.
The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor.
Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via non-SH2 domains.
Tyrosines 1148 and 1173 of activated human epidermal growth factor receptors are binding sites of Shc in intact cells.
The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling.
Rapid identification of phosphopeptide ligands for SH2 domains. Screening of peptide libraries by fluorescence-activated bead sorting.
The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions.
The Grb2-mSos1 complex binds phosphopeptides with higher affinity than Grb2.
The role of a lymphoid-restricted, Grb2-like SH3-SH2-SH3 protein in T cell receptor signaling.
An alternative to phosphotyrosine-containing motifs for binding to an SH2 domain.
Thermodynamic and structural analysis of phosphotyrosine polypeptide binding to Grb2-SH2.
Shc phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells.
Association of the insulin receptor with phospholipase C-gamma (PLCgamma) in 3T3-L1 adipocytes suggests a role for PLCgamma in metabolic signaling by insulin.
MAPK3,(MAPK1) phosphorylates GRB2-1:SOS1:p-Y427-SHC1
Binding of SHC1 to p-6Y-EGFR mutants
Phosphorylation of SHC1 by ligand-responsive p-6Y-EGFR mutants
SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with phosphorylated SHC1 and ligand-responsive p-6Y-EGFR mutants)
Phosphorylated SHC1 in complex with ligand-responsive p-6Y-EGFR mutants recruits GRB2:SOS1 complex
SHC1 phosphorylation by ERBB2 heterodimers
Phosphorylation of SHC1 by ERBB4 homodimers
SHC1 binds P-ERBB4 isoform dimers
Recruitment of GRB2:SOS1 to phosphorylated SHC1 in complex with phosphorylated ERBB4 homodimers
RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and p-Y349,350-SHC1:p-ERBB4
SHC1 binds to the phosphorylated EGF receptor:ligand complex
SHC1 phosphorylation by phosphorylated EGFR
GRB2:SOS1 binds to phosphorylated SHC1 in complex with EGFR
SOS1-mediated nucleotide exchange of RAS (EGF:EGFR:SHC1:GRB2:SOS1)
Interaction of Tie2 and Shc1
Recruitment of GADS:SLP-76 to p-5Y-LAT
Phosphorylation of SLP-76 by p-SYK
Recruitment of GRB2:SOS to p-5Y-LAT
Recruitment of PLC-gamma to SLP-76 and p-5Y-LAT
IGF1R phosphorylates SHC1
IGF1,2:p-Y1161,1165,1166-IGF1R binds SHC1
Activation of RAC1 by VAV2/3
SOS mediated nucleotide exchange of RAS (SHC)
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
Recruitment of GRB2:SOS to p-10Y-NTAL
Activation of RAC1 by VAV
Phosphorylation and activation of VAV
PI3K associates with phosphorylated GAB2
Interaction of GRB2:SOS complex with p-SHC1
Hydrolysis of PIP2 by PLCG
Phosphorylation of SLP-76 by p-SYK
Autophosphorylation of PAK
Autophosphorylation of BTK/ITK
Phosphorylation of PIP2 to PIP3 by PI3K
Phosphorylation of SHC by SYK kinase
Recruitment of PAK to the membrane by binding active RAC1
Recruitment of VAV to p-SLP-76
Activated integrin alphaIIb beta3 binds SHC1
SHC1 bound to integrin alphaIIb beta3 is phosphorylated somehow
SHC1 dissociates from integrin alphaIIb beta3
Phosphorylation of IL2RB Y338 enables SHC recruitment
SHC1 bound to IL2 receptor is phosphorylated
Phosphorylated SHC1 recruits GRB2:GAB2
Phosphorylated SHC recruits GRB2:SOS1
Gab2 binds the p85 subunit of Class 1A PI3 kinases
Binding of SHC1 to p-5Y-EGFRvIII
Phosphorylation of SHC1 by p-5Y-EGFRvIII
Phosphorylated SHC1 in complex with p-5Y-EGFRvIII recruits GRB2:SOS1 complex
SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with phosphorylated SHC1 and p-EGFRvIII)
Activated FGFR2:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR2 binds SHC1
Activated FGFR2:p-SHC1 binds GRB2:SOS1
Activated FGFR2 phosphorylates SHC1
Activated FGFR4:p-SHC1 binds GRB2:SOS1
Activated FGFR4 binds SHC1
Activated FGFR4:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR4 phosphorylates SHC1
Activated FGFR1 binds SHC1
Activated FGFR1 phosphorylates SHC1
Activated FGFR1:p-SHC1 binds GRB2:SOS1
Activated FGFR1:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR3 binds SHC1
Activated FGFR3 phosphorylates SHC1
Activated FGFR3:p-SHC1 binds GRB2:SOS1
Activated FGFR3:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange
RAS GEFs promote RAS nucleotide exchange
GRB2-1:SOS1 binds p-Y-SHC
p-3Y-SHC1 dissociates from IGF1R
GRB2-1:SOS1 binds p-3Y-SHC1
GRB2-1:p-4S-SOS1:p-Y427-SHC1 dissociates
Binding of SHC1 to insulin receptor
Dissociation of p-Y427-SHC1 from insulin receptor
GRB2-1:SOS1 binds p-Y427-SHC1
De-phosphorylation of p-Y427-SHC1
SHC1 bound to the common beta chain becomes tyrosine phosphorylated
Recruitment of SHC1 is mediated by Y593 of the common beta chain
MET phosphorylates SHC1-2
RAS guanyl nucleotide exchange by SOS1 bound to GRB2, SCH1-2 and MET
SHC1-2 bound to MET recruits GRB2:SOS1
2x p-5Y-RET:GDNF:GFRA complexes:p-Y349,Y350,Y427-SHC1 binds GRB2-1:SOS1
2x p-5Y-RET:GDNF:GFRA complexes bind SHC1
GAB in p-5Y-RET:GDNF:GFRA complexes is phosphorylated
p-5Y-RET complexes bind GRB2
p-5Y-RET-GRB2-containing complexes bind GAB1,GAB2
p-5Y-GAB in the RET-GRB2-GAB complexes binds p85-PI3K
SHC1 in the RET complex is phosphorylated
p-5Y-GAB in RET-GRB2-GAB complexes binds PTPN11
Activated PKC phosphorylates SHC1
IL15:IL15RA:p-Y-IL2RB:p-Y-JAK1:p-Y-IL2RG:p-Y-JAK3:p-Y-SHC1:GRB2 binds SOS1,SOS2
EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-CRKL:RAPGEF1:phospho-SHC1 binds GRB2:VAV1
SHC1 mediates cytokine-induced phosphorylation of GAB2
Phosphorylated SHC1 recruits SHIP
The SHC1:SHIP1 complex is stabilized by GRB2
SHC1 is phosphorylated downstream of estrogen stimulation of GPER1
p-SHC1 binds integrin alpha5beta1:fibronectin
ERBB2 homodimer phosphorylates SHC1
SHC1 binds phosphorylated ERBB2 homodimer
Recruitment of GRB2:SOS1 to p-SHC1 in complex with phosphorylated ERBB2 homodimer
RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and ERBB2 homodimer:p-SHC1
Estrogen receptor binds IGF1R and SHC1 in response to estrogen
Phosphorylated heterodimers of ERBB2 KD mutants bind SHC1
Phosphorylated heterodimers of ERBB2 KD mutants phosphorylate SHC1
Phosphorylated heterodimers of ERBB2 KD mutants recruit GRB2:SOS1 through SHC1
RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants
RAS guanyl nucleotide exchange mediated by the p-6Y- ERBB2 ECD mutants:EGF:p-6Y-EGFR:p-SHC1:GRB2:SOS1
Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate SHC1
Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR recruit GRB2:SOS1 through SHC1
Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind SHC1
Phosphorylated heterodimers of ERBB2 TMD/JMD mutants recruit GRB2:SOS1 through SHC1
RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants
Phosphorylated ERBB2 TMD/JMD heterodimers bind SHC1
Phosphorylated heterodimers of ERBB2 TMD/JMD mutants phosphorylate SHC1
p-Y546,Y584-PTPN11 (in CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2:SHC:GRB2:PTPN11) dephosphorylates KRAS
Active ALK phosphorylates SHC1
ALK mutants phosphorylate SHC1
ALK mutants:p-3Y SHC binds GRB2
The p66shc adaptor protein controls oxidative stress response and life span in mammals.
Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis.
A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria.
UniProtKB entry P29353 (SHC1_HUMAN)
Deep research report on human SHC1 (Falcon)