gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Protein tyrosine phosphatase, non-receptor type 7

LC-PTP, PTPN7, hematopoietic protein tyrosine phosphatase
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 gene is preferentially expressed in a variety of hematopoietic cells, and is an early response gene in lymphokine stimulated cells. The non-catalytic N-terminus of this PTP can interact with MAP kinases and suppress the MAP kinase activities. This PTP was shown to be involved in the regulation of T cell antigen receptor (TCR) signaling, which was thought to function through dephosphorylating the molecules related to MAP kinase pathway. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Dec 2010] (from NCBI)
Top mentioned proteins: MAPK, p38, Pts, STEP, ERK1
Papers on LC-PTP
Study on inflammation-related genes and microRNAs, with special emphasis on the vascular repair factor HGF and miR-574-3p, in monocytes and serum of patients with T2D.
Leenen et al., Rotterdam, Netherlands. In Diabetol Metab Syndr, Dec 2015
Notably, genes and a microRNA involved in adhesion, cell differentiation and morphology (CD9, DHRS3, PTPN7 and miR-34c-5p) were up-regulated in the T2D monocytes, suggesting a role of the anti-inflammatory cells in adhesion, vascular repair and invasion.
Type 2 Diabetes Monocyte MicroRNA and mRNA Expression: Dyslipidemia Associates with Increased Differentiation-Related Genes but Not Inflammatory Activation.
Leenen et al., Rotterdam, Netherlands. In Plos One, 2014
In addition, we found over expression of 3 mRNAs (CD9, DHRS3 and PTPN7) in the validation cohort.
The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study.
Peti et al., Providence, United States. In Structure, 2013
Although the interaction of PTPSL with p38α is similar to that of the previously described p38α:HePTP (PTPN7) complex, STEP binds and regulates p38α in an unexpected manner.
Role of protein tyrosine phosphatase non-receptor type 7 in the regulation of TNF-α production in RAW 264.7 macrophages.
Cho et al., Seoul, South Korea. In Plos One, 2012
Protein tyrosine phosphatase non-receptor type 7 (PTPN7), a member of the phosphatase family, specifically inactivates mitogen-activated protein kinases (MAPKs).
Inhibition of hematopoietic protein tyrosine phosphatase augments and prolongs ERK1/2 and p38 activation.
Tautz et al., Los Angeles, United States. In Acs Chem Biol, 2012
The hematopoietic protein tyrosine phosphatase (HePTP) is implicated in the development of blood cancers through its ability to negatively regulate the mitogen-activated protein kinases (MAPKs) ERK1/2 and p38.
Fatty acids as natural specific inhibitors of the proto-oncogenic protein Shp2.
Chen et al., Xiamen, China. In Bioorg Med Chem Lett, 2011
The inhibitory effects of these compounds on the enzyme activities of Shp2, VH1-related human protein (VHR), and hematopoietic protein tyrosine phosphatase (HePTP) were investigated.
Inhibition of the Hematopoietic Protein Tyrosine Phosphatase by Phenoxyacetic Acids.
Tautz et al., Los Angeles, United States. In Acs Med Chem Lett, 2011
The hematopoietic protein tyrosine phosphatase (HePTP) is often found dysregulated in preleukemic myelodysplastic syndrome (MDS), as well as in acute myelogenous leukemia (AML).
Inflammatory gene expression in monocytes of patients with schizophrenia: overlap and difference with bipolar disorder. A study in naturalistically treated patients.
Drexhage et al., Rotterdam, Netherlands. In Int J Neuropsychopharmacol, 2010
Subset 2, characterized by PTPN7 and NAB2 was up-regulated in the monocytes of 62% BD, but down-regulated in the monocytes of 48% of SZ patients.
Genetic variants that affect length/height in infancy/early childhood in Vietnamese-Korean families.
Kim et al., Seoul, South Korea. In J Hum Genet, 2010
In a single-SNP-based analysis, the six SNPs in or near genes MAF, MAGI2, BMP4 and PTPN7 showed consistent suggestive associations at all height standard deviation scores using Korean, World Health Organization and Vietnamese growth references.
Identification of protein tyrosine phosphatases and dual-specificity phosphatases in mammalian spermatozoa and their role in sperm motility and protein tyrosine phosphorylation.
Tapia et al., Cáceres, Spain. In Biol Reprod, 2009
In all these species, we did not detect the specific signal with anti-PTPRC (CD45), CDKN3, DUSP1, DUSP2, DUSP6, DUSP9, PTPN1, PTPN3, PTPN6, PTPN7, PTPN13, PTPRA, PTPRG, PTPRJ, PTPRK, or PTPRZ antibodies.
Hematopoietic protein tyrosine phosphatase mediates beta2-adrenergic receptor-induced regulation of p38 mitogen-activated protein kinase in B lymphocytes.
Sanders et al., Columbus, United States. In Mol Cell Biol, 2009
beta(2)AR stimulation on a B cell phosphorylates and inactivates HePTP in a Gs/cAMP/PKA-dependent manner to release bound p38 MAPK, making more available for phosphorylation and subsequent IgE regulation.
Structural basis of substrate recognition by hematopoietic tyrosine phosphatase.
Page et al., Providence, United States. In Biochemistry, 2009
Interactions at the active site between KIM (kinase interaction motif)-phosphatases and their substrates are predominantly nonspecific, with the majority of the KIM-phosphatase residues coordinating the peptide backbone rather than residue side chains.
Sequence-specific 1H, 13C and 15N backbone resonance assignments of the 34 kDa catalytic domain of human PTPN7.
Overduin et al., Birmingham, United Kingdom. In Biomol Nmr Assign, 2008
PTPN7 is a protein tyrosine phosphatase responsible for inactivation of MAPK in leukocytes.
MAPK-specific tyrosine phosphatases: new targets for drug discovery?
Knapp et al., Oxford, United Kingdom. In Trends Pharmacol Sci, 2006
In this article, we focus on the family of mitogen-activated protein kinase (MAPK)-specific tyrosine phosphatases--PTPN5 [also called striatal-enriched phosphatase (STEP)], PTPN7 (also called hematopoietic PTP) and PTPRR (also called PC12 PTP or STEP-like PTP)--and discuss approaches for achieving selectivity for the MAPK-PTPs at the molecular level using recently determined high-resolution X-ray crystal structures.
Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases.
Barr et al., Oxford, United Kingdom. In Biochem J, 2006
determined high-resolution structures of all of the human family members of Mitogen-Activated Protein Kinase-specific protein tyrosine phosphatases
Lipid raft targeting of hematopoietic protein tyrosine phosphatase by protein kinase C theta-mediated phosphorylation.
Mustelin et al., Los Angeles, United States. In Mol Cell Biol, 2006
Here we show that the hematopoietic protein tyrosine phosphatase (HePTP) also accumulates in the immune synapse in a PKC theta-dependent manner upon antigen recognition by T cells and is phosphorylated by PKC theta at Ser-225, which is required for lipid raft translocation.
Structure of the hematopoietic tyrosine phosphatase (HePTP) catalytic domain: structure of a KIM phosphatase with phosphate bound at the active site.
Page et al., Los Angeles, United States. In J Mol Biol, 2005
structure of the protein tyrosine phosphatase catalytic domain of HePTP, residues 44-339
Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals.
Lodish et al., Cambridge, United States. In Cell, 1995
We show that the hematopoietic protein tyrosine phosphatase SH-PTP1 (also called HCP and PTP1C) associates via its SH2 domains with the tyrosine-phosphorylated EPO-R.
share on facebooktweetadd +1mail to friends