Negatively protein tyrosine phosphatase. Medical search. Frequent questions

Protein tyrosine phosphatases (EC 3.1.3.48, systematic name protein-tyrosine-phosphate phosphohydrolase) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins: [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate Protein tyrosine (pTyr) phosphorylation is a common post-translational modification that can create novel recognition motifs for protein interactions and cellular localization, affect protein stability, and regulate enzyme activity. (wikipedia.org)
As a consequence, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. (wikipedia.org)
Together with tyrosine kinases, PTPs regulate the phosphorylation state of many important signalling molecules, such as the MAP kinase family. (wikipedia.org)
Concomitant activation of the insulin-like growth factor-1 receptor, Akt, and extracellular signal-regulated protein kinase 1 and 2 as well as increased phosphorylation of Bad also were unique to the hippocampus of APP Sw mice. (jneurosci.org)
Protein tyrosine phosphatase receptor delta (PTPRD) is a member of a large family of protein tyrosine phosphatases which negatively regulate tyrosine phosphorylation. (biomedcentral.com)
Subcellular localization of IRS-1 and phosphorylation levels of mitogen-activated protein kinase and Akt1 were also analyzed.IGF-IR was differentially expressed across histologic subtypes (P = 0.04), with highest levels observed in squamous cell tumors. (omicsdi.org)
Tyrosine phosphorylation is a central mechanism in the control of key signaling proteins involved in innate immunity. (biomedcentral.com)
Sulfhydration coordinates with other post-translational protein modifications such as phosphorylation and nitrosylation to regulate cellular functions (Altaany et al. (pharmaceuticalintelligence.com)
Current research has demonstrated that the extracellular portions of some receptors act as bait receptors for activating ligands, while in most cases, the phosphorylation of tyrosine residues in their cytoplasmic tails drives critical inhibitory signals. (medicaltrend.org)
CD28 enhances TCR-driven tyrosine phosphorylation and interacts with phosphatidylinositol 3-kinase (PI3K) and Grb2, initiating the Akt-mTOR and Ras-MAPK pathways. (medicaltrend.org)
As a mechanism to control EGFR phosphorylation at the plasma membrane, receptor endocytosis and vesicular trafficking relocalizes activated, phosphorylated EGFR to perinuclear compartments rich in Protein Tyrosine Phosphatases (PTPs), such as PTPN1, which dephosphorylate and inactivate the receptor. (tu-dortmund.de)
Using single cell measurements of phosphorylation of the EGFR downstream signaling tyrosine residue Y1068, we generated a spatial-temporal reactivity map to identify local phosphatase activity. (tu-dortmund.de)
By negatively regulating EGFR phosphorylation, we deduced the role of PTPN2/PTPRJ in determining signal duration: a function that is coupled to vesicular trafficking. (tu-dortmund.de)
Glutamate inputs activate Cdk5, which inhibits postsynaptic dopamine D1 receptor (D1R)-mediated signaling by phosphorylating DARPP-32 at Thr75 (Thr75-DARPP-32) in the striatum, since DARPP-32 with Thr75 phosphorylation (DARPP-32-pThr75) functions as an inhibitor of cAMP-dependent protein kinase A (PKA). (frontiersin.org)
Here, we show that in the mouse striatum, dopamine receptor stimulation negatively regulates phosphorylation of Tyr15-Cdk5 most likely through a D2R-mediated mechanism. (frontiersin.org)
DUSP3 regulated OCLN ubiquitination and degradation through decreasing OCLN tyrosine phosphorylation directly or through suppressing focal adhesion kinase, the OCLN kinase. (biomedcentral.com)
HGF c Met signaling can induce paxillin phosphorylation at its tyrosine residue, which in turn promotes tumor progression by enhancing tumor cell migration and spread.ten Activating c Met mutations are already proven to increase paxillin phosphorylation in SCLC.5 Furthermore, paxillin has become proven to be very expressed, and its gene from time to time amplified or mutated in NSCLC 11. (hormonespathway.com)

PTPs are increasingly viewed as integral components of signal transduction cascades, despite less study and understanding compared to tyrosine kinases. (wikipedia.org)
The insulin receptor (IR) and JAK1 tyrosine kinases and STAT3 can serve as direct substrates for the T-cell protein tyrosine phosphatase (TCPTP). (diabetesjournals.org)
This motif is found in Cdc42/Rac-associated proteins such as the protein kinases Pak, MRCK and Ack, the adaptor proteins Spec and WASP, and, in degenerate form, in the kinases MLK, Mekk4, adaptor Par6, scaffold protein IRSp53, and the Borg proteins. (biomedcentral.com)
The role of protein tyrosine kinases (PTKs) has been widely studied but less is known on the protein tyrosine phosphatases (PTPs) responsible for immunoregulation [ 3 ]. (biomedcentral.com)
These negative signals are mediated by key signaling transducers, such as tyrosine kinases, inositol phosphatases, and diacylglycerol kinases, allowing them to counteract T-cell receptor (TCR)-mediated activation. (medicaltrend.org)
Activated TCR triggers the assembly of a signalosome, with key components including tyrosine kinases like Lck and Zap70, scaffold proteins such as Lat, SLP76, and Themis, and phospholipase Cγ1 (PLC γ1), as well as tyrosine phosphatases and E3 ubiquitin ligases like SHP1 and Cbl, among others. (medicaltrend.org)
Deregulation of receptor tyrosine kinases in human cancers can occur through positive activation of the receptor or through the loss of negative regulatory controls. (mcgill.ca)
Dual specificity phosphatase 3 (DUSP3), a suppressor of multiple protein tyrosine (Tyr) kinases, is decreased in lung cancer tissues. (biomedcentral.com)
DUSP3/VHR, related to the vaccinia virus phosphatase VH1, is initially found to be a phosphatase that dephosphorylates multiple protein tyrosine kinases (PTKs) in vitro [ 21 ]. (biomedcentral.com)

It contains a tensin like domain as well as a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases. (ayassbioscience.com)

Ectopic up-regulation of PTPRD in neuroblastoma dephosphorylates tyrosine residues in AURKA resulting in a destabilization of this protein culminating in interfering with one of AURKA's primary functions in neuroblastoma, the stabilization of MYCN protein, the gene of which is amplified in approximately 25 to 30% of high risk neuroblastoma. (biomedcentral.com)
The sulfhydration of cysteine residues in proteins is an important mechanism involved in diverse biological processes. (pharmaceuticalintelligence.com)
Reactive cysteine residues in proteins have high nucleophilicity and low pKa values and serve as a major target for oxidative modifications, which can vary depending on the subcellular environment, including the type and intensity of intracellular or environmental cues. (pharmaceuticalintelligence.com)
The biological significance of the Cys150 modification by H2S is not well-studied, but H2S could serve as a biological switch for protein function acting via oxidative modification of specific cysteine residues in response to redox homeostasis (Paul and Snyder, 2012). (pharmaceuticalintelligence.com)
Negatively charged residues Asp and Glu are favoured at pY+1, making a salt bridge with an Arg at the βD3 position. (eu.org)
Position pY+4 is highly permissive favouring Ala, Thr, Ser and Tyr, and pY+6 favours negatively charged residues. (eu.org)
These distinctions were way more prominent when phospho precise antibodies for each of 2 distinct tyrosine residues have been made use of to the western blot evaluation. (hormonespathway.com)

PTPs have been implicated in regulation of many cellular processes, including, but not limited to: Cell growth Cellular differentiation Mitotic cycles Oncogenic transformation Receptor endocytosis PTP activity can be found in four protein families. (wikipedia.org)
The protein encoded by this gene is an unusual orphan receptor that contains a putative ligand-binding domain but lacks a conventional DNA-binding domain. (cancerindex.org)
Studies suggest that the protein represses nuclear hormone receptor-mediated transactivation via two separate steps: competition with coactivators and the direct effects of its transcriptional repressor function. (cancerindex.org)
Protein tyrosine phosphatase receptor delta ( PTPRD ) is an important regulator of axon growth and guidance and is highly expressed in the central nervous system where it functions as a transmembrane homophilic neuronal cell adhesion molecule [ 1 ]. (biomedcentral.com)
Programmed cell death protein 1 (PD-1, CD279) is a transmembrane glycoprotein that belongs to the CD28 receptor superfamily. (medicaltrend.org)
Our work in the past few years has uncovered an important regulator of invasive cell growth, the Met receptor tyrosine kinase. (mcgill.ca)
My lab has focused on and will continue to address these questions using the Met receptor tyrosine kinase and oncogene as a model. (mcgill.ca)
We will establish the molecular mechanism through which Cbl negatively regulates the Met receptor and establish if this is a mechanism for receptor deregulation in human cancers. (mcgill.ca)
CD45, previously called LCA (leukocyte common antigen), T200, or Ly5 in mouse, is member C of the class 1 (receptor-like) protein tyrosine phosphatase family (PTPRC) (1, 2). (rndsystems.com)
NCK is a major adaptor protein involved in membrane receptor signalling and modulation of actin cytoskeleton dynamics. (eu.org)

Unlike most of the protein tyrosine phosphatases, this protein preferentially dephosphorylates phosphoinositide substrates. (ayassbioscience.com)
Another PTP involved in the immune processes is PTPMEG, a cytosolic phosphatase expressed in the thymus that is able to dephosphorylates TCRζ ITAMs in vitro . (biomedcentral.com)
Within the IS, CD45 dephosphorylates and negatively regulates the src family kinase, LCK (8‑10). (rndsystems.com)

miR-328 down-regulates the expression of protein-tyrosine phosphatase PTPRJ. (unicz.it)
It negatively regulates intracellular levels of phosphatidylinositol-3,4,5-trisphosphate in cells and functions as a tumor suppressor by negatively regulating AKT/PKB signaling pathway. (ayassbioscience.com)
It encodes a lipid and protein phosphatase that negatively regulates the PI3K/AKT/mTOR pathway. (cornell.edu)

EC 3.1.3.48) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. (wikipedia.org)
2015). In the latter, an oxidized cysteine residue included glutathionylated, 60 sulfenylated and nitrosylated on a protein reacts with the sulfide anion to form a cysteine persulfide. (pharmaceuticalintelligence.com)
They are able to bind specific motifs containing a phosphorylated tyrosine residue, propagating the signal downstream by promoting protein-protein interactions and/or modifying enzymatic activities. (eu.org)

Protein tyrosine phosphatase nonreceptor type 2 (PTPN2) recently emerged as a promising cancer immunotherapy target. (jci.org)

What pathways are this gene/protein implicaed in? (cancerindex.org)
Suppressor of cytokine signaling (SOCS)-3 and protein-tyrosine phosphatase 1B (PTP-1B) are two endogenous inhibitors of tyrosine kinase signaling pathways and suppress both insulin and leptin signaling via different molecular mechanisms. (diabetesjournals.org)
In addition, they play important roles in gene transcription (via activation of mitogen activated protein (MAP) kinase pathways and, in higher eukaryotes, the transcription factor NFκB), generation of reactive oxygen species, apoptosis, and cell-cycle progression. (biomedcentral.com)
Src Homology 2 (SH2) domains are small modular domains found within a great number of proteins involved in different signalling pathways. (eu.org)

The class II PTPs contain only one member, low-molecular-weight phosphotyrosine phosphatase (LMPTP). (wikipedia.org)
Cdc25 phosphatases (dTyr and/or dThr) The Class III PTPs contains three members, CDC25 A, B, and C These are members of the HAD fold and superfamily, and include phosphatases specific to pTyr and pSer/Thr as well as small molecule phosphatases and other enzymes. (wikipedia.org)

Although dozens of proteins act downstream of these GTPases, a comparison of effector proteins from evolutionarily diverse organisms suggests that six groups of proteins serve as the core machinery for signaling from Cdc42 and Rac. (biomedcentral.com)
PTPRD has a tumor suppressor function in neuroblastoma through AURKA dephosphorylation and destabilization and a downstream destabilization of MYCN protein, representing a novel mechanism for the function of PTPRD in neuroblastoma. (biomedcentral.com)
We further demonstrate that PTPRD has a tumor suppressor function in neuroblastoma through dephosphorylating and destabilizing AURKA, leading to a downstream decrease of MYCN protein. (biomedcentral.com)
ATM inhibitor review by quite a few downstream proteins during the HGF c Met pathway. (hormonespathway.com)

PD-1 recruits SHP-2, promoting the dephosphorylation of CD3ζ and CD28 and negatively affecting TCR signaling strength. (medicaltrend.org)

In particular, stage II and III tumors displayed enhanced PTPN2 protein expression in tumor-infiltrating T cells, and increased PTPN2 levels negatively correlated with expression of PD-1, CTLA4, STAT1, and granzyme A. In vivo, T cell- and DC-specific PTPN2 deletion reduced tumor burden in several CRC models by promoting CD44+ effector/memory T cells, as well as CD8+ T cell infiltration and cytotoxicity in the tumor. (jci.org)
The rapid development of research on receptors that negatively regulate lymphocyte function is driven by the success of tumor immunotherapy. (medicaltrend.org)
miR-214 negatively regulated PTK6 expression to impair the JAK2/STAT3 pathway activation, thereby halting CC cell proliferation, migration, invasion, xenograft tumor growth and metastasis. (arcillaresearch.com)
The protein encoded by this gene is a cell cycle checkpoint regulator and putative tumor suppressor. (affbiotech.com)
An intracellular signaling and tumor suppressor protein that forms a complex with TUBEROUS SCLEROSIS COMPLEX 1 PROTEIN (TSC1) and other signaling factors to negatively regulate MTORC1 and affect cell growth and proliferation. (bvsalud.org)

SHP-2 can hamper the TRIF (TIR-domain-containing adapter-inducing interferon-β) adaptor protein-dependent TLR4 and TLR3 signal transduction with a consequent block of the pro-inflammatory cytokine production [ 7 ]. (biomedcentral.com)

ITIMs negatively modulate cell activation by recruiting phosphatases such as protein tyrosine phosphatases 1 and 2 (SHP-1 and SHP-2), as well as inositol 5′-phosphatases 1 and 2 (SHIP-1 and SHIP-2). (medicaltrend.org)

Ser/Thr and Tyr dual-specificity phosphatases are a group of enzymes with both Ser/Thr (EC 3.1.3.16) and tyrosine-specific protein phosphatase (EC 3.1.3.48) activity able to remove the serine/threonine or the tyrosine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase. (wikipedia.org)
We tested a model that AP achieves a portion of this preference by destabilizing ground state binding via charge repulsion between the anionic active site nucleophile, Ser102, and the negatively charged phosphate monoester substrate. (rcsb.org)
In the case of sulfhydration, a small number of proteins have been identified, among them the glycolytic enzyme glyceraldehyde phosphate dehydrogenase, GAPDH (Mustafa et al. (pharmaceuticalintelligence.com)

Glycans, either alone or complexed with glycan-binding proteins, can deliver intracellular signals or control extracellular processes that promote initiation, execution and resolution of cell death programs. (nature.com)

The mouse CD45RABC cDNA encodes 1291 amino acids (aa), including a 23 aa signal sequence, a 541 aa extracellular domain containing the splicing region, a cysteine-rich region and two fibronectin type III domains, a 22 aa transmembrane sequence, and a 705 aa cytoplasmic domain that contains two phosphatase domains, D1 and D2. (rndsystems.com)

SH2 domains are phosphotyrosine recognition domains, often mediating transient interactions with target proteins. (eu.org)

This activity is strongly conserved and probably represents a primordial function of these proteins. (biomedcentral.com)
The protein also contains an AAA domain, which is associated with ATPase activity. (cancerindex.org)
c-Abelson tyrosine kinase (c-Abl) is known to phosphorylate Cdk5 at Tyr15 (Tyr15-Cdk5) and thereby facilitates the Cdk5 activity. (frontiersin.org)
Only D1 has phosphatase activity. (rndsystems.com)
These studies found that brown fat activity increases in cold temperatures and is negatively correlated with BMI and age. (todoslifestyle.com)
We found that The level of PSTPIP2 in synovial macrophages is negatively correlated with RA disease activity, which is mediated by synovial macrophages polarization. (biomedcentral.com)

This gene encodes a protein containing a C3HC4-type RING finger domain, which is a specialized type of Zn-finger that binds two atoms of zinc and is thought to be involved in mediating protein-protein interactions. (cancerindex.org)

SRC homology 2 (SH2)-containing tyrosine phosphatase-2 (SHP-2) has a controversial effect on lymphocyte signaling. (biomedcentral.com)

Dual-specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. (wikipedia.org)

And last year, Dr. Fawaz Haj, professor at University of California, Davis, made an important discovery marking the link between the regulation of insulin signalling and brown fat cells through an enzyme called protein tyrosine phosphatase 1B (PTP1B). (todoslifestyle.com)

At that time, glycobiology, which is the study of carbohydrates and their recognition by motif-specific carbohydrate-binding proteins or lectins, lagged far behind the studies that defined the structural and cellular biology of cell death. (nature.com)
The Tir protein of EPEC binds NCK1/NCK2 SH2 domains through a high affinity pYDEV motif ( Frese,2006 ). (eu.org)

It is a variably glycosylated 180‑220 kDa transmembrane protein that is abundantly expressed on all nucleated cells of hematopoietic origin (1‑3). (rndsystems.com)
TJs, tightly fused regions between the outer membrane of adjacent cells, are formed by integral transmembrane proteins such as OCLN and claudins, anchoring proteins such as zonula occludens (ZO)1-3, and other TJ-associated/regulatory proteins [ 4 , 5 ]. (biomedcentral.com)

The cytoplasmic tails of these inhibitory receptors contain tyrosine-based inhibitory motifs (ITIMs) and switch motifs (ITSMs) with common sequence features. (medicaltrend.org)
The cytoplasmic tail of PD-1 contains two tyrosine-based motifs, an ITIM (VDY223GEL), and an ITSM (TEY248ATI). (medicaltrend.org)

The expression of transthyretin, a protein shown to sequester Aβ and prevent amyloid fibril formation in vitro , and several genes in the insulin-signaling pathway, e.g., insulin-like growth factor-2, were increased selectively in the hippocampus of APP Sw mice. (jneurosci.org)
Cancer-associated alterations in this gene often result in loss of PTEN protein and upregulation of the PI3K/AKT/mTOR pathway. (cornell.edu)
Protein Phosphatase, Mg 2+ /Mn 2+ Dependent 1D (PPM1D) is another negative regulator of the TP53 pathway and activating mutations in this gene are present in myeloid malignancies including MPNS. (medicalresearch.com)

Scope includes mutations and abnormal protein expression. (cancerindex.org)
In the present study, MEG3 upregulation was negatively associated with the International Staging System (ISS) status of the bone marrow samples of 39 patients with MM. MEG3 overexpression in an MM cell line resulted in elevated p53 expression. (spandidos-publications.com)
The aim of this selleck chemicals llc study was to assess the expression patterns of these three functionally relevant proteins, PAX5, c Met and paxillin, in the setting of neuroendocrine tumors with the lung. (hormonespathway.com)

Rho GTPases are small (20-30 kDa) GTP-binding proteins of the Ras superfamily. (biomedcentral.com)

Another negative regulator of hematopoietic cell development and function is SHP-1 (SRC homology 2 (SH2)-containing tyrosine phosphatase 1), that is mainly expressed in hematopoietic and lymphoid cells [ 8 ]. (biomedcentral.com)
The Src Homology 2 (SH2) domain is a major protein interaction module that is central to tyrosine kinase signaling. (eu.org)

As a molecular mechanism, we demonstrate that PTPRD interacts with aurora kinase A (AURKA), an oncogenic protein that is over-expressed in multiple forms of cancer, including neuroblastoma. (biomedcentral.com)
Analogous Pi binding measurements with a protein tyrosine phosphatase suggest the generality of this ground state destabilization mechanism. (rcsb.org)
Posttranslational modification is a fundamental mechanism in the regulation of structure and function of proteins. (pharmaceuticalintelligence.com)

Proximity ligation assay, immunoblotting, and phosphatase assay were performed to study the effect of DUSP3 on the TJ protein occludin (OCLN). (biomedcentral.com)
The cytotoxicity of mutant SOD1s was also measured by lactate dehydrogenase release assay at 48 h following the induction of SOD1 proteins. (hormonespathway.com)

For instance, familial AD is linked to mutations in the amyloid precursor protein (APP), presenilin 1, and presenilin 2, all of which lead to increased levels of Aβ. (jneurosci.org)
Mutations identified in many SH2 domain-containing proteins as well as the SH2 domain itself are associated with human diseases ranging from cancers, diabetes, to immunodeficiencies. (eu.org)

Alkaline Phosphatase (AP) and other nonspecific phosphatases are some of Nature's most impressive catalysts, achieving preferential transition state over ground state stabilization of more than 10²²-fold while utilizing interactions with only the five atoms attached to the transferred phosphorus. (rcsb.org)

The protein has been shown to interact with retinoid and thyroid hormone receptors, inhibiting their ligand-dependent transcriptional activation. (cancerindex.org)

In conclusion, the present study points out a slight potential role for PTPH1 in spontaneous pain sensitivity and it indicates that this phosphatase might play a role in the positive regulation of the LPS-induced cytokines release in vivo , in contrast to previous reports indicating PTPH1 as potential negative regulator of immune response. (biomedcentral.com)

Both motifs are phosphorylated by the tyrosine kinase Lck when PD-1 ligands bind to PD-1. (medicaltrend.org)

and proteins that interact with members of the Arp2/3 complex and hence the actin cytoskeleton (Table 1 ). (biomedcentral.com)

PTEN p.Y68H is a reported pathogenic variant that causes tyrosine to histidine substitution at codon 68 affecting NH2-terminal phosphatase domain. (cornell.edu)

What does this gene/protein do? (cancerindex.org)
these proteins are also important in regulating gene transcription. (biomedcentral.com)
The DEGs were analyzed by gene ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG), and protein-protein interaction (PPI) networks. (bvsalud.org)
The protein encoded by this gene is a phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase. (ayassbioscience.com)

Protein-protein interaction (PPI) networks and modules were constructed to identify hub genes with the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) and Cytoscape. (researchsquare.com)

Western blot assessment confirmed that myc tagged human SOD1 proteins were induced by doxycycline in these cell lines. (hormonespathway.com)
WB: For western blot detection of denatured protein samples. (affbiotech.com)

Tg2576 mice overexpress a mutant form of human amyloid precursor protein with the Swedish mutation (APP Sw ), resulting in high β-amyloid (Aβ) levels in the brain. (jneurosci.org)

Anaplastic lymphoma kinase (ALK) protein may be detected in most cases (60-70%) of systemic ALCL by immunohistochemistry. (medscape.com)

Understanding the physiological significance of protein sulfhydration requires the development of genome-wide innovative experimental approaches. (pharmaceuticalintelligence.com)

Space-filling model of the PTEN protein (blue) complexed with tartaric acid (brown). (ayassbioscience.com)
Functional studies demonstrate that individuals harboring this variant have decreased levels of the PTEN protein when compared to wild type controls. (cornell.edu)

The analysis of Cdc42 and Rac function in evolutionarily distant organisms is useful as a tool to uncover the basic activities of these proteins. (biomedcentral.com)
It can also function as GTPASE-ACTIVATING PROTEIN (GAP) for RHEB GTPASE to activate mTORC1 independent of its role in the complex. (bvsalud.org)

By regulating filamentous actin, Cdc42 and Rac exert a profound effect on cell shape, polarity, migration, cell:cell and cell:matrix adhesion, protein traffic, and cytokinesis. (biomedcentral.com)
One particular of them is paxillin, a crucial focal adhesion protein that is definitely important for cell matrix adhesion, cell motility and migration. (hormonespathway.com)

Anatomy24

Organisms11

Diseases3

Chemicals and Drugs150

Analytical, Diagnostic and Therapeutic Techniques and Equipment19

Phenomena and Processes45

Disciplines and Occupations1

Information Science3

Phosphorylation17

Kinases9

Dual-specificity protein-tyrosine pho1

Residues7

Receptor10

Dephosphorylates3

Regulates3

Residue3

Nonreceptor-type1

Pathways4

PTPs2

Downstream4

Dephosphorylation1

Tumor5

Adaptor protein1

Modulate1

Phosphate3

Intracellular1

Extracellular1

Phosphotyrosine1

Activity6

Encodes1

Lymphocyte1

Signal transduction1

Enzyme1

Motif2

Transmembrane2

Cytoplasmic2

Pathway3

Expression3

Superfamily1

Homology2

Mechanism3

Assay2

Mutations2

Interactions1

Receptors1

Regulation1

Ligands1

Actin cytoskeleton1

Pathogenic1

Gene4

Interaction1

Western blot2

Mutant1

Anaplastic1

Physiological1

PTEN2

Function2

Cell:matrix adhesion2