• Grb2 is phosphorylated on a tyrosine residue (Y209) by the fully active FGFR2, which results in dissociation from the complex with the receptor. (rupress.org)
  • The addition of this single alanine residue did not alter the tertiary structure of the protein but resulted in essentially complete loss of matrix metalloproteinase inhibitory activity. (cancer.gov)
  • The free cysteine nucleophile forms a bond with the phosphorus atom of the phosphate moiety, and the P-O bond linking the phosphate group to the tyrosine is protonated, either by a suitably positioned acidic amino acid residue (Asp in the diagram below) or a water molecule. (wikipedia.org)
  • The LD motifs are predicted to form amphipathic alpha helices, with each leucine residue positioned on one face of the alpha helix to form a hydrophobic protein-binding interface. (wikipedia.org)
  • Sequences of ARF-GAP domains show no recognizable similarity to those of other GAPs, and contain a characteristic Cys-X(2)-Cys-X(16-17)-Cys-X(2)-Cys motif. (embl-heidelberg.de)
  • The ARF-GAP domain comprises a central three-stranded beta-sheet flanked by five alpha-helices, with a Zn(2+) ion coordinated by the four cysteines of the cysteine-rich motif. (embl-heidelberg.de)
  • these serve as binding sites for the protein tyrosine phosphatase-PEST, tubulin and serves as the targeting motif for focal adhesions. (wikipedia.org)
  • The PTP domain is unlikely to be active in tensin 1, owing to mutation of the essential nucleophilic cysteine in the signature motif to asparagine. (wikipedia.org)
  • SH3 domains bind to proline-rich motif containing proteins. (wikipedia.org)
  • All CAS proteins except CASS4 contain a YDYVHL motif within this domain, which is an important binding site for the Src SH2 domain. (wikipedia.org)
  • HER1 in humans) is a transmembrane protein that is a receptor for members of the epidermal growth factor family (EGF family) of extracellular protein ligands. (wikipedia.org)
  • Epidermal growth factor receptor (EGFR) is a transmembrane protein that is activated by binding of its specific ligands, including epidermal growth factor and transforming growth factor α (TGFα) ErbB2 has no known direct activating ligand, and may be in an activated state constitutively or become active upon heterodimerization with other family members such as EGFR. (wikipedia.org)
  • Specifically, STAT3 becomes activated after phosphorylation of tyrosine 705 in response to such ligands as interferons, epidermal growth factor (EGF), Interleukin (IL-)5 and IL-6. (wikipedia.org)
  • The SHP-1 protein tyrosine phosphatase negatively modulates glucose homeostasis. (springer.com)
  • STATs are also negatively regulated by protein inhibitors of activated STAT (PIAS), which act in the nucleus through several mechanisms. (wikipedia.org)
  • In addition to activating Ras/AKT and ERK/MAP kinase, phosphatidylinositol 3-kinase/AKT pathway and STAT transcription factors, phosphotyrosines also serve as docking sites for phosphatases that negatively affect EpoR signaling in order to prevent overactivation that may lead to such disorders as erythrocytosis. (wikipedia.org)
  • They share significantly conserved amino acid sequences within the extracellular domains, but have both activating and inhibitory members. (frontiersin.org)
  • Tyrosine phosphorylation is the addition of a phosphate (PO43−) group to the amino acid tyrosine on a protein. (wikipedia.org)
  • The human and murine cDNAs both encode 533 amino acid proteins that are 72% identical and composed of three modular domains. (wikipedia.org)
  • In humans, the 561 amino acid EFS protein acts as a scaffolding protein for cell signaling based on interactions with SRC, FAK, and other proteins, and has been linked to roles in the function of the immune system, and the development of cancer. (wikipedia.org)
  • The amino acid sequences of the SH3 domains are 70% identical among human EFS, BCAR1, and NEDD9, making this the most highly conserved domain for the whole protein family. (wikipedia.org)
  • Notably, the murine and human EFS SH3 domains are 100% identical, while the rest of the amino acid sequences of mouse and human EFS are only 78% identical. (wikipedia.org)
  • A C-terminal domain (489-561 amino acids in human EFS) is highly conserved between family members at both primary amino acid sequence and predicted fold. (wikipedia.org)
  • In order to confirm the mRNA data at the protein level, we developed a FACS-based protocol designed to phenotype live GI eosinophils isolated from the murine lamina propria. (pubmedcentralcanada.ca)
  • Based on models of the murine phosphatase, structural identification, and human genetics the phosphatase forms complexes with C-src tyrosine kinase (Csk), associated with the control of Src family members. (wikipedia.org)
  • SHP-1 is also known as hematopoietic cell phosphatase (HCP) because of its expression in these cells. (springer.com)
  • Cleavage occurs at the SALD site, resulting in a loss of DNA-binding activity and a concomitant detachment of this protein from nuclear structural sites. (wikipedia.org)
  • As the member of CAS protein family, EFS shares common structural characteristics with other members of the family. (wikipedia.org)
  • Protein tyrosine phosphatase inhibition induces anti-tumor activity: evidence of Cdk2/p27 kip1 and Cdk2/SHP-1 complex formation in human ovarian cancer cells. (springer.com)
  • EpoR induced Jak2-Stat5 signaling, together with transcriptional factor GATA-1, induces the transcription of pro-survival protein Bcl-xL. (wikipedia.org)
  • Upon binding to target phospho-tyrosyl residues, the N-terminal SH2 domain is released from the PTP domain, catalytically activating the enzyme by relieving this auto-inhibition. (wikipedia.org)
  • Recruitment of SHP phosphatases to the membrane leads to the inhibition of myosin accumulation at the cell surface and results in the inhibition of phagocytosis. (wikipedia.org)
  • examined the effect of inhibition of myosin contractility on the integrin adhesome composition and found LIM domain proteins and beta-PIX to be tension sensitive. (wikipedia.org)
  • This renewed glucose tolerance and insulin signaling is caused by the inhibition of the unfolded protein response pathway, particularly the protein IRE1alpha, and its subsequent phosphorylation of IRS-1 that causes insulin signaling to be blocked. (wikipedia.org)