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Protein tyrosine phosphatase, non-receptor type 3

PTPH1, PTPN3, protein tyrosine phosphatase H1
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 protein contains a C-terminal PTP domain and an N-terminal domain homologous to the band 4.1 superfamily of cytoskeletal-associated proteins. P97, a cell cycle regulator involved in a variety of membrane related functions, has been shown to be a substrate of this PTP. This PTP was also found to interact with, and be regulated by adaptor protein 14-3-3 beta. Several alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2009] (from NCBI)
Top mentioned proteins: Pts, H1, CAN, ACID, HAD
Papers on PTPH1
Protein tyrosine phosphatase PTPN3 inhibits lung cancer cell proliferation and migration by promoting EGFR endocytic degradation.
New
Chen et al., Taipei, Taiwan. In Oncogene, Jul 2015
Using a genetic approach, we found that Drosophila FERM and PDZ domain-containing protein tyrosine phosphatase, dPtpmeg, negatively regulates border cell migration and inhibits the EGFR/Ras/mitogen-activated protein kinase signaling pathway during wing morphogenesis.
Multiple Changes of Gene Expression and Function Reveal Genomic and Phenotypic Complexity in SLE-like Disease.
New
Lindblad-Toh et al., Uppsala, Sweden. In Plos Genet, Jun 2015
In addition to association to certain MHC alleles and haplotypes, we identified 11 genes (WFDC3, HOMER2, VRK1, PTPN3, WHAMM, BANK1, AP3B2, DAPP1, LAMTOR3, DDIT4L and PPP3CA) located on five chromosomes that contain multiple risk haplotypes correlated with gene expression and disease sub-phenotypes in an intricate manner.
Tyrosine dephosphorylation enhances the therapeutic target activity of epidermal growth factor receptor (EGFR) by disrupting its interaction with estrogen receptor (ER).
New
Chen et al., Milwaukee, United States. In Oncotarget, Jun 2015
Protein tyrosine phosphatase H1 (PTPH1) dephosphorylates the tyrosine kinase EGFR, disrupts its interaction with the nuclear receptor ER, and increases breast cancer sensitivity to small molecule tyrosine kinase inhibitors (TKIs).
Substrate specificity and plasticity of FERM-containing protein tyrosine phosphatases.
New
Wang et al., Taipei, Taiwan. In Structure, May 2015
Epidermal growth factor receptor (EGFR) pathway substrate 15 (Eps15) is a newly identified substrate for protein tyrosine phosphatase N3 (PTPN3), which belongs to the FERM-containing PTP subfamily comprising five members including PTPN3, N4, N13, N14, and N21.
The molecular basis for the substrate specificity of protein tyrosine phosphatase PTPN3.
New
Parker, Christchurch, New Zealand. In Structure, May 2015
In this issue of Structure, Chen et al. present structures of the FERM-containing protein tyrosine phosphatase PTPN3 in complex with a phosphopeptide fragment of substrate epidermal growth factor receptor pathway substrate, providing detailed information on substrate specificity.
Reorganization of metastamiRs in the evolution of metastatic aggressive neuroblastoma cells.
Aravindan et al., Oklahoma City, United States. In Bmc Genomics, 2014
Immunoblotting and TMA-IHC analyses revealed alterations in the expression/phosphorylation of metastamiRs' targets, including ADAMTS-1, AKT1/2/3, ASK1, AURKβ, Birc1, Birc2, Bric5, β-CATENIN, CASP8, CD54, CDK4, CREB, CTGF, CXCR4, CYCLIN-D1, EGFR, ELK1, ESR1, CFOS, FOSB, FRA, GRB10, GSK3β, IL1α, JUND, kRAS, KRTAP1, MCP1, MEGF10, MMP2, MMP3, MMP9, MMP10, MTA2, MYB, cMYC, NF2, NOS3, P21, pP38, PTPN3, CLEAVED PARP, PKC, SDF-1β, SEMA3D, SELE, STAT3, TLR3, TNFα, TNFR1, and VEGF in aggressive cells ex vivo and in a manifold of metastatic tumors in vivo.
Gene Expression Signature in Adipose Tissue of Acromegaly Patients.
Bridges et al., Haifa, Israel. In Plos One, 2014
We also identified several novel transcriptional changes, some of which may be important for GH/IGF responses (PTPN3 and PTPN4) and the effects of acromegaly on growth and proliferation.
Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation.
Wang et al., Taipei, Taiwan. In Sci Signal, 2014
The mitogen-activated protein kinase p38γ (also known as MAPK12) and its specific phosphatase PTPN3 (also known as PTPH1) cooperate to promote Ras-induced oncogenesis.
Activating mutations in PTPN3 promote cholangiocarcinoma cell proliferation and migration and are associated with tumor recurrence in patients.
Fan et al., Shanghai, China. In Gastroenterology, 2014
We compared mutations in PTPN3 with tumor recurrence in 124 patients and PTPN3 expression levels with recurrence in 322 patients (the combination of both in 86 patients).
Diverse levels of sequence selectivity and catalytic efficiency of protein-tyrosine phosphatases.
Pei et al., Columbus, United States. In Biochemistry, 2014
The sequence selectivity of 14 classical protein-tyrosine phosphatases (PTPs) (PTPRA, PTPRB, PTPRC, PTPRD, PTPRO, PTP1B, SHP-1, SHP-2, HePTP, PTP-PEST, TCPTP, PTPH1, PTPD1, and PTPD2) was systematically profiled by screening their catalytic domains against combinatorial peptide libraries.
Protein-tyrosine phosphatase H1 increases breast cancer sensitivity to antiestrogens by dephosphorylating estrogen receptor at Tyr537.
Chen et al., Milwaukee, United States. In Mol Cancer Ther, 2014
Here, we tested the hypothesis that the protein-tyrosine phosphatase H1 (PTPH1) may regulate ER tyrosine phosphorylation and thereby impact breast cancer antihormone sensitivity.
Genome-wide association study for wool production traits in a Chinese Merino sheep population.
Wang et al., Harbin, China. In Plos One, 2013
About 43% of the significant SNP markers were located within known or predicted genes, including YWHAZ, KRTCAP3, TSPEAR, PIK3R4, KIF16B, PTPN3, GPRC5A, DDX47, TCF9, TPTE2, EPHA5 and NBEA genes.
A genome-wide SNP scan reveals two loci associated with the chicken resistance to Marek's disease.
Yang et al., Beijing, China. In Anim Genet, 2013
The other one, GGaluGA156129, reaching genome-wide significance (P < 0.05), was located in the protein tyrosine phosphatase, non-receptor type 3 (PTPN3) gene on GGA2.
p38γ Mitogen-activated protein kinase signals through phosphorylating its phosphatase PTPH1 in regulating ras protein oncogenesis and stress response.
GeneRIF
Chen et al., Milwaukee, United States. In J Biol Chem, 2012
p38gamma Mitogen-activated protein kinase signals through phosphorylating its phosphatase PTPH1 in regulating ras protein oncogenesis and stress response.
Discovery of ALK-PTPN3 gene fusion from human non-small cell lung carcinoma cell line using next generation RNA sequencing.
GeneRIF
Kim et al., Seoul, South Korea. In Genes Chromosomes Cancer, 2012
The fusion transcript of ALK and PTPN3 identified resulted from translocation of a part of ALK gene into the third intron of PTPN3. Analysis of the transcript sequence indicates that no protein with any enzymatic activity is produced.
PTPH1 cooperates with vitamin D receptor to stimulate breast cancer growth through their mutual stabilization.
GeneRIF
Chen et al., Milwaukee, United States. In Oncogene, 2011
PTPH1 stimulated breast cancer growth through regulating vitamin D receptor expression. PTPH1 was overexpressed in primary breast cancer and levels of its protein expression positively correlated with clinical metastasis.
Tyrosine phosphatases as a superfamily of tumor suppressors in colorectal cancer.
Review
Sasiadek et al., Wrocław, Poland. In Acta Biochim Pol, 2010
Mutational analysis of the tyrosine phosphatome in CRCs has identified somatic mutations in PTPRG, PTPRT, PTPN3, PTPN13 and PTPN14.
PTPH1 dephosphorylates and cooperates with p38gamma MAPK to increase ras oncogenesis through PDZ-mediated interaction.
GeneRIF
Chen et al., Milwaukee, United States. In Cancer Res, 2010
PTPH1 plays a role in Ras-dependent malignant growth by a mechanism depending on its p38gamma-binding activity. Ras increases p38gamma and PTPH1 expression and there is a coupling of increased p38gamma and PTPH1 protein expression in colon cancer.
The FERM and PDZ domain-containing protein tyrosine phosphatases, PTPN4 and PTPN3, are both dispensable for T cell receptor signal transduction.
GeneRIF
King et al., Ann Arbor, United States. In Plos One, 2007
PTPN3 and PTPN4 are dispensable for TCR signal transduction.
Mutational analysis of the tyrosine phosphatome in colorectal cancers.
Impact
Velculescu et al., Baltimore, United States. In Science, 2004
A mutational analysis of the tyrosine phosphatase gene superfamily in human cancers identified 83 somatic mutations in six PTPs (PTPRF, PTPRG, PTPRT, PTPN3, PTPN13, PTPN14), affecting 26% of colorectal cancers and a smaller fraction of lung, breast, and gastric cancers.
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