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ProteomicsGST-SH2 domain of 3BP2, pull down, curdlan-stimulated BMDC
Interacting molecules with GST-fusion protein of the wild-type SH2 domain of 3BP2 (WT) or the mutant form (R486K) were precipitated usng GSH beads and identified by DIA proteome analysis.
ORGANISM(S): Mus Musculus (mouse) 
2024-11-15 | PXD054171 | JPOST Repository
ProteomicsEngineering human SH2 domains for targeted phospho-proteomics
A comprehensive analysis of the phosphoproteome is essential for understanding molecular mechanisms of human diseases. However, current tools to enrich phosphotyrosine are limited in their applicability and scope. Here, we engineered new superbinder SH2 domains that enrich diverse sets of phosphotyr...
ORGANISM(S): Homo sapiens (Human) 
2023-01-13 | PXD030038 | Pride
Phosphoproteomics Synthetic biology K562 Src homology 2 domains Sh2 superbinders Mass spectrometry Human Structural biology Protein engineering Phosphotyrosine 
TranscriptomicsA Dictyostelium SH2 domain adaptor protein required for correct DIF-1 signaling and pattern formation
When developing in the light slug formation in LrrB null (lrrB-) mutants is delayed, relative to the parental strain, and the slugs are highly defective in phototaxis and thermotaxis. In the dark the mutant arrests development as an elongated mound, in a novel process we term dark stalling. The deve...
ORGANISM(S): Dictyostelium discoideum 
2011-05-31 | E-TABM-1090 | biostudies-arrayexpress
ProteomicsDevelopment of a Peptide Inhibitor Targeting the C-SH2 Domain of the SHP2 Phosphatase
Src homology 2 (SH2) domain-containing phosphatase 2 (SHP2) has important cellular functions in mediating signal transduction downstream of receptor tyrosine kinases and immune cell receptors. In T cells, SHP2 is a key regulator of signalling pathways downstream of the checkpoint receptor programmed...
ORGANISM(S): Homo sapiens (Human) 
2025-05-09 | PXD054302 | Pride
Pulldown Shp2 Inhibitor Chemical biology C-sh2 domain 
TranscriptomicsTranscription profiling of Arabidopsis SH2 domain-containing gene PASTA mutant vs. wild type
The protein modules known as SH2 (Src-homology-2) domains are key players in the signal transduction of animals. Two questions arise: Do such modules exist in plants, and when did SH2 domains evolve? Here I show that the Arabidopsis genome contains three strong candidates for plant SH2 proteins (ref...
ORGANISM(S): Arabidopsis thaliana 
2008-06-13 | E-GEOD-5619 | biostudies-arrayexpress
GenomicsSTAT3 SH2 Domain Aspartic Acid 661 Mutations Activate Immune Gene Programs
STAT3 SH2 Domain Aspartic Acid 661 Mutations Activate Immune Gene Programs
PRJNA1495349 | ENA
TranscriptomicsFunctional studies of a new Arabidopsis SH2 domain-containing gene
The protein modules known as SH2 (Src-homology-2) domains are key players in the signal transduction of animals. Two questions arise: Do such modules exist in plants, and when did SH2 domains evolve? Here I show that the Arabidopsis genome contains three strong candidates for plant SH2 proteins (ref...
ORGANISM(S): Arabidopsis thaliana 
2007-01-08 | GSE5619 | GEO
TranscriptomicsThe ShcA PTB Domain Functions as a Biological Sensor of Phospho-tyrosine Signaling During Breast Cancer Progression
The ShcA adaptor possesses two phosphotyrosine binding motifs, which include an SH2 and a PTB domain. In the majority of cases, ShcA utilizes its PTB domain to engage activated receptor tyrosine kinases (RTKs). To establish the mportance of this domain during mammary tumorigenesis, we employed a Sh...
ORGANISM(S): Mus musculus 
2013-08-07 | E-GEOD-41718 | biostudies-arrayexpress
ProteomicsA sensitive and cost-effective approach for tyrosine phosphoproteome analysis based on SH2 superbinder
Albeit much less abundant than Ser/Thr phosphorylation (pSer/pThr), Tyr phosphorylation (pTyr) is considered a hallmark in cellular signal transduction. However, its analysis remains a challenge. The conventional immunopurification (IP) approach using antibodies pan-specific to pTyr sites is known t...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2017-08-29 | PXD005838 | Pride
Lc ms/ms Sh2 superbinder Ptyr phosphoproteome 
UnknownDecoding C‑SH2 Domain/Peptide Interactions in SH2 Domain-Containing Tyrosine Phosphatase 2: A Molecular Framework for Rational Inhibitor Design.
Not available
S-EPMC12878756 | biostudies-literature
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