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Validated All-in-One™ qPCR Primer for PTPN11(NM_002834.4) Search again
Product ID:
HQP108233
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
BPTP3, CFC, JMML, METCDS, NS1, PTP-1D, PTP2C, SH-PTP2, SH-PTP3, SHP2
Gene Description:
protein tyrosine phosphatase non-receptor type 11
Target Gene Accession:
NM_002834.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
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. [provided by RefSeq].
Gene References into function
- upon translocation, CagA perturbs cellular functions by deregulating SHP-2
- SHP-2 modulates phosphorylation of PDGF receptors, thereby controls RasGTP recruitment and Ras/MAP kinase signaling in the heterodimeric configuration of the PDGF receptors
- Specific SHP-2 partitioning in raft domains triggers integrin-mediated signaling via Rho activation
- interacts with siglec-11
- PTPN11 mutations in Noonan syndrome: molecular spectrum, genotype-phenotype correlation, and phenotypic heterogeneity.
- Band 3 is an anchor protein for and a target for SHP-2 tyrosine phosphatase in human erythrocytes.
- PTPN11 mutations are responsible for Noonan syndrome in a substantial fraction of patients and that relatively infrequent features of Noonan syndrome, such as sensory deafness and bleeding diathesis, can also result from mutations of PTPN11.
- Some PTPN11 mutations (e.g., Y279C) are associated with both the Noonan syndrome phenotype and with skin pigmentation anomalies, such as multiple lentigines or cafe au lait spots (LEOPARD syndrome).
- SHP-2 is a dual-specificity protein phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues and plays an important role in modulating STAT function in gene regulation
- Mutations in PTPN11/SHP2 underlie a common form of Noonan syndrome and confirm that the disease exhibits both allelic and locus heterogeneity.
- Results indicate that Gab1 and SHP-2 promote the undifferentiated epidermal cell state by facilitating Ras/MAPK signaling.
- absence of mutation in cases of cardiofaciocutaneous syndrome
- activation state of alphaVbeta3 integrin is an important regulator of the duration of insulin-like growth factor I receptor phosphorylation and this regulation is mediated through changes in the subcellular localization of SHP-2
- These data suggest, that there are two, largely distinct modes of negative regulation of gp130 activity, despite the fact that both SOCS3 and SHP2 are recruited to the same site within gp130.
- We sequenced the entire coding region of the PTPN11 gene in ten well-characterised CFC patients and found no base changes. We also studied PTPN11 cDNA in our patients and demonstrated that there are no interstitial deletions either.
- SHP-2 may function as an adaptor molecule downstream of the the prolactin receptor and highlight a new recruitment mechanism of SHP-2 substrates.
- SHP2 positively regulates IL-2 induced MAPK activation in malignant T cells. SHP2 may not be involved in the activation of Stat3 or Stat5 in cutaneous T-cell lymphoma cells.
- The CagA protein of Helicobacter pylori is translocated into epithelial cells and binds to SHP-2 in human gastric mucosa
- During platelet activation, a functionally active complex between SHIP-2, filamin, actin, and GPIb-IX-V may orchestrate the localized hydrolysis of PtdIns(3,4,5)P3 and thereby regulate cortical and submembraneous actin.
- SHP-2 catalytic activity plays a direct role in the inhibitory function of killer cell Ig-like receptors, and SHP-2 inhibits NK cell activation in concert with SHP-1.
- Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia.
- PTPN11 mutations do not cause Costello syndrome
- Required for RetM918T-induced Akt activation. Downstream mediator of mutated receptors RetC634Y and RetM918T. Acts as limiting factor in Ret-associated endocrine tumors, in neoplastic syndromes multiple endocrine neoplasia types 2A and 2B.
- SHP-2 has a role as a positive regulator of cytokine receptor signaling by regulating ubiquitination/degradation pathways
- SHP-2 is an important cellular PTPase that is mutated in myeloid malignancies
- results reveal that Gab1 protein recruits SHP2 protein tyrosine phosphatase to dephosphorylate paxillin
- SHP-2/Gab1 association is critical for linking EGFR to NF-kappaB transcriptional activity via the PI3-kinase/Akt signaling axis in glioblastoma cells
- wider role of PTPN11 lesions in leukemogenesis, but also a lineage-related and differentiation stage-related contribution of these lesions to clonal expansion.
- A missense mutation (836A-->G; Tyr279Cys) in exon 7 of PTPN11 gene was identified in the patient with LEOPARD syndrome, whereas no mutation in PTPN11 gene was detected in the father or in additional family members
- inhibition of NK cell cytotoxicity by KIR2DL5 was blocked by dominant-negative SHP-2, but not dominant-negative SHP-1, whereas both dominant-negative phosphatases can block inhibition by KIR3DL1.
- PTPN11 mutations account for approximately 40% of Noonan syndrome patients. Type of cardiovascular lesions and occurrence of hematological abnormalities are different in mutation-positive and mutation-negative patients.
- In contrast to childood MDS and AML, mutations in PTPN11 make little or no contribution to the pathogenesis of adult MDS and AML.
- PTPN11 missense mutations are associated with acute myeloid leukemia
- Aspartate 61 plays a major role for proper down-regulation of the protein tyrosine phosphatase activity of SHP-2; the D61Del variant is predicted to have lower stability of the D'EF loop of the N-terminal SH2 domain compared to the wild-type
- Most common mutation was A922G in exon 8. In exon 4 a mutation encoded C-SH2 domain of PTPN11 gene in two patients. A 218C-->T mutation was found in exon 3 in a patient with Noonan syndrome and mild juvenile myelomonocytic leukaemia.
- SHP2 binds CAT and acquires a hydrogen peroxide-resistant phosphatase activity via integrin-signaling.
- SHP-2 has a role in regulating IL-1-induced Ca2+ flux and ERK activation via phosphorylation of PLCgamma1
- data support the hypothesis that PTPN11 mutations induce hematopoietic progenitor hypersensitivity to GM-CSF due to hyperactivation of the Ras signaling axis
- Tyr-992 and Tyr-1173 are required for phosphorylation of the epidermal growth factor receptor by ionizing radiation and modulation by SHP2
- Mutations are rare in adult myelodysplastic syndromes and chronic myelomonocytic leukemia.
- 10 genes were down-regulated following treatment of the T-ALL cells with 0.15 and 1.5 microg/mL of metal ores at 72 h
- Pathogenesis of Noonan syndrome and leukemia is associated with enhanced phosphatase activity of mutant SHP-2
- SHPS-1 functions as an anchor protein that recruits both Shc and SHP-2, whose recruitment is necessary for IGF-I-dependent Shc phosphorylation
- data suggest a genotype/phenotype correlation in the spectrum of PTPN11 mutations found in patients with juvenile myelomonocytic leukemia, Noonan syndrome/myeloproliferative disease, and Noonan syndrome
- Results show that PTPN11 mutations are rarely found in two isolated forms of congenital heart disease.
- PTPN11 mutations are rare in adult myeloid malignancies [review]
- Presence of PTPN11 mutations in patients with Noonan syndrome indicates a reduced growth response to long-term human growth hormone treatment.
- an important role for a PECAM1-SHP2-Tie2 pathway in flow-mediated signal transduction.
- SHP-2 mutations in Noonan syndrome cause mild GH resistance by postreceptor signaling defect, partially compensated for by elevated GH secretion. May contribute to short stature phenotype in children with SHP-2 mutations and poor response to rhGH.
- Modeling analyses show that different SHP2 mutants can affect basal activation, SH2 domain-phosphopeptide affinity, and/or substrate specificity to varying degrees.
- aberrantly increased expression of Shp2 may contribute, collaboratively with other factors, to leukemogenesis
- Missense mutations and the role of SHP-2 in signal transduction, development and hematopoiesis, as well as on the consequences of SHP-2 gain-of-function. Review.
- cardiovascular anomalies and hematologic abnormalities are predominant in mutation positive patients
- SHP-2 tyrosine phosphorylation on residue Y542 promoted IL-1beta mediated focal adhesion maturation.
- SHP-2 recruitment to p85 is required for IGF-I-stimulated association of the p85/p110 complex with insulin receptor substrate-1 and for the subsequent activation of the PI-3 kinase pathway leading to increased cell migration
- Type I collagen limits VEGFR-2 signaling by a SHP2 protein-tyrosine phosphatase-dependent mechanism 1.
- Inhibition of focal adhesion kinase by SHP-2 plays a crucial role in the morphogenetic activity of Helicobacter pylori CagA.
- Diversity of germline and somatic PTPN11 mutations were studied in Noonan syndrome, LEOPARD syndrome and leukemia.
- The phosphorylation of SHP-2 by GM-CSF promotes the binding of SHP-2 to the GM-CSF receptor to the disadvantage of CLECSF6.
- data suggests that mutations in the PTPN11 gene are not a cause of hypertrophic cardiomyopathy in the absence of Noonan/LEOPARD syndromes
- A PTPN11 gene mutation (Y63C) causing Noonan syndrome is not associated with short stature in the general population.
- Our data suggest that mutations of PTPN11 as well as RAS play a role in the pathogenesis of not only myeloid hematological malignancies but also a subset of RMS malignancies
- The clinical suspicion of LEOPARD syndrome may be confirmed by molecular screening for PTPN11 mutations.
- The PTPN11 protein mutation can be acquired during progression of myelodysplastic syndrome JMML.
- Recruitment of SHP2 to speicific sites of autophosphorylation contributes to FLT3-mediated Erk activation and proliferation.
- both SHP-1 and SHP-2 have a positive role in epidermal growth factor-induced ERK1/2 activation and they act cooperatively rather than antagonistically.
- Upon IGF-I stimulation, a complex assembles on SHPS-1 that contains SHP-2, c-Src, and Shc wherein Src phosphorylates Shc, a signaling step that is necessary for an optimal mitogenic response
- Tyr-542 of SHP-2 modulates IL-1-induced Ca2+ signals and association of the ER with focal adhesions
- ICSBP tyrosine phosphorylation is necessary for the activation of NF1 transcription. ICSBP is a substrate for SHP2 protein tyrosine phosphatase (SHP2-PTP).
- Our results suggest that DCA differentially regulates focal adhesion complexes and that tyrosine phosphatase ShP2 has a role in DCA signaling.
- Mutation of the PTPN11 gene is the main causal factor in LEOPARD syndrome, and it also plays a role in neurofibromatosis-Noonan syndrome.
- uPAR expression of lung airway epithelial cells is regulated at the level of mRNA stability by inhibition of protein tyrosine phosphatase-mediated dephosphorylation of uPAR mRNA binding proteins and demonstrate that the process involves SHP2.
- 1226 G-->C causes amino acid substitution G409A and results in Noonan Syndrome. Mutations in this particular region of SHP-2 may have effects on the protein that differ from those of the classical mutations.
- PTPN11 as the first proto-oncogene that encodes a cytoplasmic tyrosine phosphatase with Shp2 domain; diseases caused by mutations; role in hematopoiesis
- support the view that an increase in the affinity of SHP-2 for its binding partners, caused by destabilization of the closed, inactive conformation
- The significance of exercise-induced alterations in cytosolic SHP2 and insulin-stimulated Akt pSer(473) on the improvement in insulin sensitivity requires further elucidation.
- This short review discusses the physiological role of Shp2 in the molecular switch governing embryonic stem cell self-renewal versus differentiation.
- Association of single tSNPs with both apoB and LDL cholesterol as well as interactions between the two genes suggest that variants influencing SHP-2 activity may modulate the acute pathway by which insulin regulates these lipids
- novel mechanism regulating GH signaling in which estrogen receptor modulators enhance GH activation of the JAK2/STAT5 pathway in a cell-type-dependent manner by attenuating protein tyrosine phosphatase activities
- An unselected series of 140 patients with therapy-related MDS or AML were investigated for mutations of PTPN11 in Exons 3, 4, 8, and 13. Four cases had mutations of the gene; three of these had deletions or loss of chromosome arm 7q.
- PTPN11 mutations are responsible for Noonan syndrome in Taiwanese patients
- association of the PDGFRbeta with lipid raft microdomains renders it susceptible to LXA(4)-mediated dephosphorylation by possible reactivation of oxidatively inactivated SHP-2.
- understanding of Noonan syndrome and the LEOPARD syndrome pathogenesis will require solving the paradox that mutations oppositely influencing the biochemical activity of SHP-2 result in similar syndromes
- Compund heterozygosity for Noonan syndrome-causing mutations in the PTPN11 gene, documenting association with early fetal death, is reported.
- The most prevalent links to PTPN11 gene dysfunction in cardiac development in patients with a PTPN11 mutation are pulmonary valve stenosis, atrial septal defect, ostium secundum type, and stenosis of the peripheral pulmonary arteries.
- Missense mutations were identified in 48.5% of the NS patients. There was a positive correlation between the presence of PTPN11 mutations and pulmonary stenosis frequency in NS patients.
- SHP-1 and SHP-2, two structurally related cytoplasmic protein-tyrosine phosphatases with different cellular functions and cell-specific expression patterns, were compared for their intrinsic susceptibility to oxidation by H(2)O(2).
- Results describe the neurite outgrowth multiadaptor RhoGAP, NOMA-GAP, and show that it regulates neurite extension through SHP2 and Cdc42.
- occurrence of an unusual TG 3' splice site in intron 10
- Virus attachment induced tyrosine phosphorylation of PVR; this permitted the association of PVR with SHP-2, a protein tyrosine phosphatase whose activation was required for entry and infection
- FIRST CASE TO OUR KNOWLEDGE OF LS SYNDROME FEATURING A NEW PTPN11 GENE MUTATION
- Frequently mutated in high hyperdiploid childhood acute lymphoblastic leukemia.
- Shp2E76K induces cytokine-independent survival of TF-1 cells by a novel mechanism involving up-regulation of Bcl-XL through the Erk1/2 pathway.
- SHP-2 regulates endothelial cell survival through PI3-K-Akt and mitogen-activated protein kinase pathways thereby strongly affecting new vessel formation.
- correlation of PTPN11 mutations with NPM1 mutations and FLT3/ITD among adult AML patients
- The finding that defective Shp2 signaling induced cell movement defects as early as gastrulation may have implications for the monitoring and diagnosis of Noonan and LEOPARD syndrome.
- There is little phenotype-genotype correlation with electrocardiographic findings in Noonan syndrome patients.
- analysis of the gain-of-function SHP-2 mutants with oncogenic RAS-like transforming activity from solid tumors
- activation of SHP2 protein tyrosine phosphatase synergized with ICSBP haploinsufficiency to facilitate cytokine-induced myeloproliferation, apoptosis resistance, and rapid progression to AML in a murine bone marrow transplantation model.
- L282V substitution perturbs the stability of SHP2's closed conformation and T42A substitution promotes phosphopeptide-binding affinity.
- Shp2 binds most strongly when both of the NPXY motifs in LRP1 are phosphorylated
- Shp2 mediates dephosphorylation of ROCKII and, therefore, regulates RhoA-induced cell rounding, indicating that Shp2 couples with RhoA signaling to control ROCKII activation during deadhesion.
- In 22 children with a mutation in PTPN11 mean gain in H-SDS for National standards was +1.3, not different from the mean gain in the five children without a mutation in PTPN11+1.3.
- the Gab1-SHP2-ERK1/2 signaling pathway comprises an inhibitory axis for IGF-I-dependent myogenic differentiation.
- Cdk2-associated complexes, by targeting SHP-1 for proteolysis, counteract the ability of SHP-1 to block cell cycle progression of intestinal epithelial cells
- Mutations in PTPN11, which encodes the protein tyrosine phosphatase Shp2, are commonly found in juvenile myelomonocytic leukemia.
- SHP2 is a widely overexpressed signalling protein in infiltrating ductal carcinoma breast tumours.
- Data show that Shp2 activation promotes the dispersal of pre-patterned acetylcholine receptors (AChRs)clusters to facilitate the selective accumulation of AChRs at developing neuromuscular junction.
- Single nucleotide polymorphism at intron 3 of PTPN11 gene is associated with a lower risk of gastric atrophy.
- higher nuclear SHP2 expression in B-cell lymphoma cases
- SHP-2 is a novel target of Abl kinases during cell proliferation
- Shp-2 retains TERT in the nucleus by regulating tyrosine 707 phosphorylation.
- SHP2 activation induced by HCMV infection is responsible for the down-regulation of IFN-gamma-induced STAT1 tyrosine phosphorylation.
- Mutations in the PTPN11 are associated with Noonan syndrome.
- Protein Tyrosine Phosphatase, Non-Receptor Type 11 modulates Cyclin-Dependent Kinase Inhibitor p27 stability and contributes to Cyclin-Dependent Kinase Inhibitor p27 -mediated cell cycle progression.
- Downregulation of platelet responsiveness upon contact with LDL by the protein-tyrosine phosphatases SHP-1 and SHP-2.
- In more than half the patients with Noonan Syndrome a mutation in the PTPN11 gene was identified.