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Human PTPN11 Protein expressed in Wheat germ - ABIN1316822
Jo, Park, Lee, Ahn, Kim, Park, Choi: SHP-2 binds to caveolin-1 and regulates Src activity via competitive inhibition of CSK in response to H2O2 in astrocytes. in PLoS ONE 2014
Studies indicate that multiple classes of PTPN11 mutations with a distinct perturbing effect on SHP2's function.
Mutational status of NRAS (show NRAS Proteins), KRAS, and PTPN11 genes is associated with genetic/cytogenetic features in children with B-precursor acute lymphoblastic leukemia.
Studied mutations of PTPN11 in a cohort of Noonan Syndrome patients. Mutational analysis was performed and PTPN11 mutations were detected in 11 out of 17 (64.7%) patients with Noonan syndrome; 72% had mutation in exon 3 and 27 % had mutation in exon 13.
NO controls the calcium signal propagation through Cx37-containing gap junctions. The tyrosine phosphatase SHP-2 is the essential mediator and NO target.
SHP2 and PTEN deficiencies were detected in liver cancer patients with poor prognosis. These data depict a mechanism of hepato-oncogenesis and suggest a potential therapeutic strategy.
we describe patients with craniosynostosis and Noonan syndrome due to de novo mutations in PTPN11 and patients with craniosynostosis and CFC syndrome due to de novo mutations in BRAF (show BRAF Proteins) or KRAS. All of these patients had cranial deformities in addition to the typical phenotypes of CFC syndrome and Noonan syndrome.
These results suggest that SHP-2-via association with ICAM-1-mediates ICAM-1-induced Src activation and modulates VE-cadherin switching association with ICAM-1 or actin, thereby negatively regulating neutrophil adhesion to endothelial cells and enhancing their transendothelial migration.
High PTPN11 expression is associated with suppression of T lymphocyte function in Melanoma.
PTPN11 mutations are the most common cause of the Noonan syndrome, along with frequent neuroepithelial brain tumors. (Review)
A novel PTPN11 mutation defined in two separate fetuses with Cystic hygroma and associated with Noonan syndrome phenotype is being reported.
SHP2 supports basal pulmonary endothelial barrier function by coordinating the tyrosine phosphorylation profile of VE-cadherin (show CDH5 Proteins), beta-catenin (show CTNNB1 Proteins), and p190RhoGAP (show GRLF1 Proteins) and the activity of RhoA (show RHOA Proteins).
S-nitrosylation of endogenous SHP2 Phosphatase and PTP1B (show PTPN1 Proteins) in endothelial insulin (show INS Proteins) signaling has been demonstrated.
a method that allows the localized visualization of oxidized intermediates of SHP-2 protein-tyrosine phosphatase (show ACP1 Proteins) inside cells during signaling.
Inactivation of ALX4/Alx4 (show ALX4 Proteins) causes lacrimal gland aplasia in both human and mouse. These results reveal a key role of Alx4 (show ALX4 Proteins) in mediating FGF-Shp2-FGF signaling in the neural crest for lacrimal gland development.
findings define a novel physiological function of Shp2 in TGF-beta1 (show TGFB1 Proteins)/MMP12 (show MMP12 Proteins)-dependent emphysema, adding insights into potential etiologies for this chronic lung disorder.
Ptpn11 gain-of-function mutations are associated with myeloproliferative neoplasm.
aberrant SHP2 signaling during cardiac development leads to congenital heart disease and adult-onset heart hypertrophy
Data suggest that phosphorylation of Shp2/Ptpn11 at Tyr542 and its translocation to postsynaptic compartment are integral processes in synaptic scaling/homeostasis; Shp2 phosphatase activity is critical to regulation of Ser (show SIGLEC1 Proteins)(P)845 GluA1 (show GRIA1 Proteins) and surface expression of GluA1 (show GRIA1 Proteins) during synaptic scaling. (Shp2/Ptpn11 = protein tyrosine phosphatase non-receptor type 11; GluA1 (show GRIA1 Proteins) = glutamate receptor ionotropic Ampa1 (show GRIA1 Proteins) [alpha 1])
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains two tandem Src homology-2 domains, which function as phospho-tyrosine binding domains and mediate the interaction of this PTP with its substrates. This PTP is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Mutations in this gene are a cause of Noonan syndrome as well as acute myeloid leukemia. Two transcript variants encoding different isoforms have been found for this gene.
, protein-tyrosine phosphatase 1D
, protein-tyrosine phosphatase 2C
, tyrosine-protein phosphatase non-receptor type 11
, SH2 domain-containing protein tyrosine phosphatase-2
, protein-tyrosine phosphatase SYP
, SH-PTP2 protein tyrosine phosphatase non-receptor type 11
, SH-PTP2 protein tyrosine phosphatase, non-receptor type 11
, encodes catalytic domain
, protein tyrosine phosphatase SH-PTP2
, protein tyrosine phosphatase, non-receptor type 11 (Noonan syndrome 1)
, non-receptor type protein tyrosine phosphatase SHP2