among the 36 PTP genes, gene ptp-h, which is proposed to be the origin of baculovirus ptp, belongs to atypical VH1-like dual-specific PTP subset and encodes a catalytic active protein. PTP variants and subfamilies in Bombyx mori, overview
analysis of molecular basis of substrate specificity in the FERM-containing subfamily of nonreceptor PTPs, overview. These enzymes are characterized by the presence of an N-terminal FERM plasma-membrane-localization domain and a C-terminal catalytic domain
enzyme Siw14 is a member of the protein tyrosine-phosphatase (PTP) superfamily. Siw14 has a cysteine-based, class I CX5R(S/T) motif that defines the family of protein-tyrosine phosphatases (PTPs). Bioinformatic studies lead to Siw14 being classified as belonging within a specialist subgroup of PTPs, the dual specific protein-tyrosine phosphatases (DUSPs). The DUSPs themselves include a distinct class of proteins that appears not to have substantial activity against phosphoproteins. These are usually described as nonprotein-specific or atypical phosphatases. The inclusion of Siw14 in this category is supported by biochemical analysis, the enzyme's catalytic activity against 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP7) is several orders of magnitude greater than that against 4-nitrophenyl phosphate, a generic protein phosphatase substrate. Other members of this atypical DUSP subgroup preferentially hydrolyze either phosphorylated carbohydrates, inositol lipids, or triphosphate groups in mRNA. Thus, this DUSP subfamily exhibits catalytic site diversity that is not observed for classical PTPs
group A Streptococcus (GAS) Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. GAS lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). SP-PTP falls into the category of low-molecular weight PTPases (LMW PTPases)
group A Streptococcus (GAS) Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. GAS lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). SP-PTP falls into the category of low-molecular weight PTPases (LMW PTPases)
protein tyrosine phosphatase N3 (PTPN3/PTPH1) belongs to a subfamily of five PTPs that contain an N-terminal 4.1 protein, ezrin, radixin, and moesin (FERM) plasma membrane-localization domain and a C-terminal catalytic domain. PTPs in this subfamily can be further divided into two types based on the presence of a PDZ domain
the enzyme is a member of the PTP superfamily. The Trp residue is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid
the enzyme is a member of the PTP superfamily. The Trp residue is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid
the enzyme is a member of the PTP superfamily. The Trp residue is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid
the enzyme is a member of the PTP superfamily. The Trp residue, W179 in PTP1B, is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid
the enzyme is a member of the PTP superfamily. The Trp residue, W354 in YopH, is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid
the pathogenic enzyme EhPRL protein possesses the classical HCX5R catalytic motif of PTPs and the CAAX box characteristic of the PRL family and exhibits 31-32% homology with the three human PRL isoforms
the enzyme is a member of the PTP superfamily. The Trp residue is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid
enzyme Siw14 is a member of the protein tyrosine-phosphatase (PTP) superfamily. Siw14 has a cysteine-based, class I CX5R(S/T) motif that defines the family of protein-tyrosine phosphatases (PTPs). Bioinformatic studies lead to Siw14 being classified as belonging within a specialist subgroup of PTPs, the dual specific protein-tyrosine phosphatases (DUSPs). The DUSPs themselves include a distinct class of proteins that appears not to have substantial activity against phosphoproteins. These are usually described as nonprotein-specific or atypical phosphatases. The inclusion of Siw14 in this category is supported by biochemical analysis, the enzyme's catalytic activity against 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP7) is several orders of magnitude greater than that against 4-nitrophenyl phosphate, a generic protein phosphatase substrate. Other members of this atypical DUSP subgroup preferentially hydrolyze either phosphorylated carbohydrates, inositol lipids, or triphosphate groups in mRNA. Thus, this DUSP subfamily exhibits catalytic site diversity that is not observed for classical PTPs
group A Streptococcus (GAS) Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. GAS lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). SP-PTP falls into the category of low-molecular weight PTPases (LMW PTPases)
the pathogenic enzyme EhPRL protein possesses the classical HCX5R catalytic motif of PTPs and the CAAX box characteristic of the PRL family and exhibits 31-32% homology with the three human PRL isoforms
the pathogenic enzyme EhPRL protein possesses the classical HCX5R catalytic motif of PTPs and the CAAX box characteristic of the PRL family and exhibits 31-32% homology with the three human PRL isoforms
bone marrow-derived macrophages lacking significant SHP-1 activity display a profound defect in interleukin-12p40 synthesis in response to lipopolysaccharide, peptidoglycan, and synthetic Toll-like receptor ligands, while producing normal amounts of other proinflammatory cytokines, such as TNFalpha and interleukin-6
neuronal protein tyrosine phosphatase 1B deficiency results in inhibition of hypothalamic AMP-activated protein kinase, AMPK, and isoform-specific activation of AMPK in peripheral tissues, overview
protein tyrosine phosphatases inactivate neurotrophic factor receptors and downstream intracellular signaling molecules causing neurodegeneration and loss of sensoric functions, overview
PTPs are integral components of key cell survival pathways, and are responsible for their inactivation, while PTP inhibition is are often associated with enhanced cell proliferation, overview. PTP inhibition in the presence of certain types of DNA damage may lead to increased genomic instability, via bypass of cell cycle checkpoints
improperly regulated PTP activity has been implicated in a range of human diseases including leukemia, solid-tumor cancers, diabetes, and several autoimmune disorders
loss of SHP-1 expression strongly augments the ability of regulatory T cells to suppress inflammation in a mouse model. Specific pharmacological inhibition of SHP-1 enzymatic activity via the cancer drug sodium stibogluconate potently augmented regulatory T cell suppressor activity both in vivo and ex vivo. SHP-1-deficient regulatory T cells are more efficient suppressors T-cell activation than wild-type regulatory T-cells
absence of SP-PTP and SP-PTP enzymatic activity adversely affects GAS cell morpholog, the slow growth of M1T1DELTAPTP is associated with defective cell divisiony. The GAS mutant lacking SP-PTP poorly adheres to and invades human respiratory cells and affects in vivo phosphorylation events in human respiratory cells, phenotype
absence of SP-PTP and SP-PTP enzymatic activity adversely affects GAS cell morpholog, the slow growth of M1T1DELTAPTP is associated with defective cell divisiony. The GAS mutant lacking SP-PTP poorly adheres to and invades human respiratory cells and affects in vivo phosphorylation events in human respiratory cells, phenotype
enzyme HD-PTP depletion causes a striking accumulation of tubulo-vesicular endosomal compartments that contain a build-up of ubiquitin-protein conjugates and reduces sorting of EGFR to the endosomal lumen
in the microglial cell line BV-2, DEP-1 depletion by shRNA-mediated knockdown results in enhanced phosphorylation of the Fyn activating tyrosine (Tyr420) and elevated specific Fyn-kinase activity in immunoprecipitates. Fyn mRNA and protein levels are reduced in DEP-1-deficient microglia cells. Knockdown of DEP-1 causes a small but significant decrease of phagocytosis of unstimulated microglial BV-2 cells. And the stimulatory effect on phagocytosis is significantly reduced in cells depleted for DEP-1, reduced phagocytic activity of microglial cells in DEP-1-/- mice brains
phosphorylation of PTPN12 at Ser19 by CDK2 impairs recruitment of the serine/threonine-protein kinase 1 (PAK1) to HER2, resulting in the blockade of the HER2-pY1196-PAK1-T423 signaling pathway, thus increases tumor cell motility. Decreased PTPN12 protein level is associated with poor prognosis of several types of cancers. Phosphorylation of Ser19 by CDK2 specifically increases EGF-induced HER2-pY1196 and PAK1-pT423 phosphorylation
the C1858T polymorphism within the protein tyrosine phosphatase PTPN22 (encoding PTPN22R619W) is a major risk factor for the development of multiple autoimmune diseases, including rheumatoid arthritis (RA), type I diabetes, lupus and juvenile idiopathic arthritis (JIA). The autoimmune associated PTPN22R619W variant displays reduced binding to the tyrosine kinase Csk, due to a missense mutation in the P1 domain. Ptpn22 variants do not alter BMDC receptor mediated phagocytosis
loss of SHP-1 expression strongly augments the ability of regulatory T cells to suppress inflammation in a mouse model. Specific pharmacological inhibition of SHP-1 enzymatic activity via the cancer drug sodium stibogluconate potently augmented regulatory T cell suppressor activity both in vivo and ex vivo. SHP-1-deficient regulatory T cells are more efficient suppressors T-cell activation than wild-type regulatory T-cells
the C1858T polymorphism within the protein tyrosine phosphatase PTPN22 (encoding PTPN22R619W) is a major risk factor for the development of multiple autoimmune diseases, including rheumatoid arthritis (RA), type I diabetes, lupus and juvenile idiopathic arthritis (JIA). The autoimmune associated PTPN22R619W variant displays reduced binding to the tyrosine kinase Csk, due to a missense mutation in the P1 domain. Ptpn22 variants do not alter BMDC receptor mediated phagocytosis
in the microglial cell line BV-2, DEP-1 depletion by shRNA-mediated knockdown results in enhanced phosphorylation of the Fyn activating tyrosine (Tyr420) and elevated specific Fyn-kinase activity in immunoprecipitates. Fyn mRNA and protein levels are reduced in DEP-1-deficient microglia cells. Knockdown of DEP-1 causes a small but significant decrease of phagocytosis of unstimulated microglial BV-2 cells. And the stimulatory effect on phagocytosis is significantly reduced in cells depleted for DEP-1, reduced phagocytic activity of microglial cells in DEP-1-/- mice brains
absence of SP-PTP and SP-PTP enzymatic activity adversely affects GAS cell morpholog, the slow growth of M1T1DELTAPTP is associated with defective cell divisiony. The GAS mutant lacking SP-PTP poorly adheres to and invades human respiratory cells and affects in vivo phosphorylation events in human respiratory cells, phenotype
MPtpA is a signalling protein belonging to the tyrosine phosphatase superfamily, and is involved in phagocytosis and is active in virulent mycobacterial form
a CDK2-mediated phosphorylation-based substrate recognition mechanism of PTPN12 orchestrated signaling crosstalk between the oncogenic CDK2 and HER2 pathways
analysis of multivesicular body (MVB) sorting, involving the enzyme, of internalised membrane proteins that have entered the early endosome, overview. The multivesicular body is an intermediate compartment en route to the degradative milieu of the lysosome
analysis of multivesicular body (MVB) sorting, involving the enzyme, of internalised membrane proteins that have entered the early endosome, overview. The multivesicular body is an intermediate compartment en route to the degradative milieu of the lysosome
cysteine residues Cys35, Cys104 and Cys243 in the catalytic core domain of PGP mediate the reversible inhibition of PGP activity and the associated, redox-dependent conformational changes. Cys35 oxidation weakens van-der-Waals interactions with Thr67, a conserved catalytic residue required for substrate coordination. Cys104 and Cys243 form a redox-dependent disulfide bridge between the PGP catalytic core and cap domains. Cys297 in the PGP cap domain is essential for redox-dependent PGP oligomerization, and PGP oxidation/oligomerization occurs in response to stimulation of cells with EGF
regulatory interaction of tyrosine kinase Wzc, and its opposing tyrosine phosphatase, Wzb. The phosphatase Wzb utilizes a surface distal to the catalytic elements of the kinase, Wzc, to dock onto its catalytic domain WzcCD. WzcCD binds in a fashion largely independent of the C-terminal tyrosine cluster near the Wzb catalytic site, inducing allosteric changes therein. YC dephosphorylation is proximity-mediated and reliant on the elevated concentration of phosphorylated YC near the Wzb active site resulting from WzcCD docking
isozyme p52shc plays an essential role in mediating IGF-I activation of MAP kinases in smooth muscle cells, involving also protein tyrosine phosphatase-2, while isozyme p66shc inhibits IGF-I signal transduction, overview. p66shc functions to negatively regulate the formation of a signaling complex that is required for p52shc activation in response to IGF-I, thus leading to attenuation of IGF-I-stimulated cell proliferation and migration
MptpA and MptpB selectively dephosphorylate human host proteins involved in interferon-gamma signaling pathways, thereby preventing the initiation of host defense mechanisms, overview
PTPH1 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
PTPs are integral components of key cell survival pathways, and are responsible for their inactivation, while PTP inhibition is are often associated with enhanced cell proliferation, overview
SHP-1 plays critical roles in regulation of many receptor-mediated signaling cascades in the immune system, and it represents a mechanism for host regulation of a specific proinflammatory cytokine important in both innate and adaptive immunity. It is required for SHP-1 in interleukin-12/23 p40 production in response to Toll-like receptor stimulation in macrophages. SHP-1 regulation of interleukin-12p40 transcription requires both its catalytic activity and phosphotyrosine binding by its N-terminal SH2 domain and is mediated via repression of, and interaction with, phosphatidylinositol 3-kinase, without affecting c-Rel activation, overview
the heat-resistant PTPase may play important roles in vivo in the adaptation of the microorganism to extreme temperatures and specific nutritional conditions
protein tyrosine phosphatases are a large and important class of signaling enzymes that catalyze the dephosphorylation of phosphotyrosine in protein substrates. A number of PTPs are tumor-suppressor proteins. PEST is a wide-ranging and ubiquitously expressed signaling molecule, which is involved in the regulation of osteoclast activation, cell motility and adhesion, the immune response, and apoptosis
PTP1B-mediated dephosphorylation of Gab1 negatively affects its EGF-induced association with the phosphatase SHP2. The dissociation of this signaling complex is accompanied by a decrease of ERK MAP kinase phosphorylation and activation. PTP1B specifically interferes with SHP2 recruitment by Gab1 and with ERK1/2 activation
the cytoplasmic tyrosine phosphatase Src homology region 2 domain-containing phosphatase 1, SHP-1, acts as an endogenous brake and modifier of the suppressive ability of regulatory T cells, which are important for immune tolerance. Regulatory T cells prevent the activation of conventional T cells. Regulatory T cell -mediated suppression of Tcon activation occurs by multiple mechanisms and is regulated by SHP-1, overview
low molecular weight protein-tyrosine phosphatase A is a key virulence factor of Mycobacterium tuberculosis, the enzyme is essential for infection of host macrophages
protein tyrosine phosphatase (PTP) alpha regulates integrin signaling, focal adhesion formation, and migration. PTPalpha-Tyr789 is necessary for efficient integrin-induced Cas tyrosine phosphorylation and Cas-Crk association, and regulates Cas downstream signaling events and Cas localization to focal adhesions
protein tyrosine phosphatase 1B is a negative regulator of systemic glucose and insulin homeostasis and inhibits adipocyte differentiation and mediates TNFalpha action in obesity
density-enhanced phosphatase-1 (DEP-1), also designated PTPRJ, receptor-type PTP eta or CD148, is a transmembrane PTP endowed with one intracellular catalytic domain, and an extracellular domain harboring eight fibronectin-like repeats. The protein-tyrosine phosphatase DEP-1 promotes migration and phagocytic activity of microglial cells in part through negative regulation of fyn tyrosine kinase. DEP-1 protein levels increase in several cell types at high-cell density, suggesting a role of the molecule in density-dependent growth control. A negative regulatory role of Fyn for microglial functions is inhibited by DEP-1. Determination of a role of DEP-1 in a potential DEP-1-Fyn axis in the regulation of microglial functions. Enzyme DEP-1 stimulates microglial phagocytosis and microglial cell migration, overview
EhPRL may play an important role in the biology and adaptive response of the parasite to the host environment during amoebic liver abscess development, thereby participating in the pathogenic mechanism in humans
in human cells, enzyme SHP-1's phosphatase activity is regulated through an autoinhibitory interaction between its catalytic PTP domain and one of its SH2 domains, in the autoinhibited state of SHP-1, the amino-terminal SH2 domain blocks the PTP-domain's active site
PGP depletion facilitates fatty acid flux through the intracellular triacylglycerol/fatty acid cycle, and phosphatidylinositol-4,5-bisphosphate is critical for the impact of PGP activity on EGF-induced signaling. Loss of endogenous PGP expression amplifies both EGF-induced EGF receptor autophosphorylation and Src-dependent tyrosine phosphorylation of phospholipase C-gamma1. EGF enhances the formation of circular dorsal ruffles in PGP-depleted cells via Src/PLCgamma1/protein kinase C (PKC)-dependent signaling to the cytoskeleton
protein tyrosine phosphatases (PTPs) play critical roles in cell signaling pathways. Together with the protein kinases, they control the balance of phosphorylated species, enabling specific and varied signaling responses
Ptpn22 in the mouse negatively regulates Src and Syk family kinase (SFK) activity downstream of the T-cell antigen receptor (TCR). In addition to TCR signalling, PTPN22 regulates many pathways in different cell types including the B-cell receptor, the alphaLbeta2 integrin LFA-1 and Toll-Like Receptor (TLR) signalling pathways. Ptpn22 also functions to alter SFK independent signalling events by modulating TRAF ubiquitination. Macropinocytosis does not require Ptpn22. Splenic dendritic cell uptake of ovalbumin occurs independently of Ptpn22. Ptpn22 is dispensable for antigen processing and presentation and is redundant for dendritic cell activation of antigen specific T-cells. Ptpn22 variants do not modulate BMDC dependent OT-II T-cell activation
recombinant overexpression of enzyme Bmptp-h enhances BmNPV replication in BmE cells. Enzyme BmPTP-h acts as a host factor facilitating baculovirus infection via promoting its DNA replication, the enzyme is involved in the host-virus interactions that control the viral replication
replacement of murine Pgp with its phosphatase-inactive PgpD34N mutant is embryonically lethal due to intrauterine growth arrest and developmental delay in midgestation. PGP inactivation attenuates triosephosphate isomerase activity, increases triglyceride levels at the expense of the cellular phosphatidylcholine content, and inhibits cell proliferation. These effects are prevented under hypoxic conditions or by blocking phosphoglycolate release from damaged DNA
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Enzyme PrpA is a PPP phosphatase
role of His domain protein tyrosine phosphatase/PTPN23 (HD-PTP) and ESCRTs (endosomal sorting complexes required for transport) in sorting activated epidermal growth factor receptor to the multivesicular body, interactions involving HD-PTP and ESCRTs. HD-PTP acts selectively at the endosome and is essential for the forward movement of epidermal growth factor receptor (EGFR) from the early endosome towards the lysosome. HD-PTP binds the EGFR adaptor Grb2, via the proline-rich region (PRR). The importance of HD-PTP for MVB sorting is highlighted by its necessity for the down-regulation of platelet-derived growth factor receptor and alpha5beta1 integrin, as well as MHC (major histocompatibility complex) class I targeted by the K3 ubiquitin ligase of Karposi's sarcoma-associated herpes virus. Consistent with a role in receptor downregulation, HD-PTP is a tumour suppressor and HD-PTP haploinsufficiency is linked to a poor clinical prognosis. HD-PTP works closely with ESCRT-0, and indeed is essential for releasing EGFR from ESCRT-0 and allowing it to engage ESCRT-III. The ESCRT-0 subunit STAM2 binds directly to HD-PTP at two sites. HD-PTP forms an open console on which ESCRTs can shuffle via competitive interactions. STAM2, SARA and endofin can potentially modulate the multivesicular body (MVB) sorting of multiple receptors by preventing HD-PTP from binding to CHMP4B. Meanwhile, their regulated release can conceivably leave an opened binding pocket into which the CHMP4B C-terminal peptide is then accepted. This binding switch may explain how HD-PTP moves EGFR from ESCRT-0 towards ESCRT-III. Potential mechanism for EGFR sorting to the MVB, overview
role of His domain protein tyrosine phosphatase/PTPN23 (HD-PTP) and ESCRTs (endosomal sorting complexes required for transport) in sorting activated epidermal growth factor receptor to the multivesicular body, interactions involving HD-PTP and ESCRTs. Potential mechanism for EGFR sorting to the MVB, comparisons to Homo sapiens, overview
SP-PTP is a secretory protein tyrosine phosphatase and plays a crucial role in group A Streptococcus (GAS) growth. As a group A Streptococcus, Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. It lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). Enzymatically active SP-PTP plays a crucial role in cell division, the function of SP-PTP is physiologically relevant for GAS growth and cell division. SP-PTP is essential for GAS virulence
SP-PTP is a secretory protein tyrosine phosphatase and plays a crucial role in group A Streptococcus (GAS) growth. As a group A Streptococcus, Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. It lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). Enzymatically active SP-PTP plays a crucial role in cell division, the function of SP-PTP is physiologically relevant for GAS growth and cell division. SP-PTP is essential for GAS virulence
the enzyme is active on protein substrates that play a relevant role in cell energy metabolism. PtpA-mediated dephosphorylation may affect pathways involved in cell energy metabolism, particularly the beta oxidation of fatty acids through modulation of TFP activity and/or cell distribution
the insulinoma associated protein tyrosine phosphatase 2 (IA-2) is one of the immunodominant autoantigens involved in the autoimmune attack to the beta-cell in type 1 diabetes mellitus
the parasite enzyme LmPRL-1 shows a strong structural similarity to the human phosphatases of regenerating liver, PRL-1, -2, and -3, that regulate the proliferation, differentiation, and motility of cells
the primary catalytic activity involves the hydrolysis of a phosphomonoester bond (C-O-P) with high catalytic efficiency, while the secondary activity is the hydrolysis of a glycosidic bond (C-O-C) with poorer catalytic efficiency. This enzyme also displays substrate promiscuity by hydrolyzing diester bonds while being highly discriminative for its monoester substrates. Additional distinct sugar hydrolase and diesterase activity for the phosphatase domain of PTPRdelta and its homologue PTPRomega
the primary catalytic activity involves the hydrolysis of a phosphomonoester bond (C-O-P) with high catalytic efficiency, while the secondary activity is the hydrolysis of a glycosidic bond (C-O-C) with poorer catalytic efficiency. This enzyme also displays substrate promiscuity by hydrolyzing diester bonds while being highly discriminative for its monoester substrates. Additional distinct sugar hydrolase and diesterase activity for the phosphatase domain of PTPRdelta and its homologue PTPRomega. PTPRdelta is known to be involved in the guidance and termination of motor neurons during embryonic development, PTPRdelta is essential for the organization of neural circuits
the protein tyrosine phosphatase (PTPase) plays an important role in insect immune system. The enzyme specifically dephosphorylate trans-Golgi p230 in vitro
the protein tyrosine phosphatase nonreceptor type 12 (PTPN12) is a multifunctional protein. A CDK2-mediated phosphorylation-based substrate recognition mechanism of PTPN12 orchestrated signaling crosstalk between the oncogenic CDK2 and HER2 pathways
the reversible phosphorylation of tyrosine residues in proteins, which depends on the balanced coordination between a multitude of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs), is an essential step in many cellular signaling pathways. Classical type I cysteine-based PTPs include both receptor and nonreceptor forms that catalyze the removal of the phosphate moiety from a targeted pTyr residue. The enzyme plays a positive role in the survival of human breast cancer cells
protein tyrosine kinase Wzc participates in the production of capsular (CPS) and released (RPS) polysaccharides. The phosphorylation state of Wzc is dependent on the activity of phosphatase Wzb. The absence of phosphatase Wzb affects the phosphorylation/dephosphorylation cycles of Wzc, altering released polysaccharides production, and this effect is not replicated when the Y-rich region of Wzc is truncated. The double mutant lacking both Wzc and Wzb activity exhibits 18% decrease in capsular polysaccharides and a 23% increase of released polysaccharides
the heat-resistant PTPase may play important roles in vivo in the adaptation of the microorganism to extreme temperatures and specific nutritional conditions
the cytoplasmic tyrosine phosphatase Src homology region 2 domain-containing phosphatase 1, SHP-1, acts as an endogenous brake and modifier of the suppressive ability of regulatory T cells, which are important for immune tolerance. Regulatory T cells prevent the activation of conventional T cells. Regulatory T cell -mediated suppression of Tcon activation occurs by multiple mechanisms and is regulated by SHP-1, overview
Ptpn22 in the mouse negatively regulates Src and Syk family kinase (SFK) activity downstream of the T-cell antigen receptor (TCR). In addition to TCR signalling, PTPN22 regulates many pathways in different cell types including the B-cell receptor, the alphaLbeta2 integrin LFA-1 and Toll-Like Receptor (TLR) signalling pathways. Ptpn22 also functions to alter SFK independent signalling events by modulating TRAF ubiquitination. Macropinocytosis does not require Ptpn22. Splenic dendritic cell uptake of ovalbumin occurs independently of Ptpn22. Ptpn22 is dispensable for antigen processing and presentation and is redundant for dendritic cell activation of antigen specific T-cells. Ptpn22 variants do not modulate BMDC dependent OT-II T-cell activation
density-enhanced phosphatase-1 (DEP-1), also designated PTPRJ, receptor-type PTP eta or CD148, is a transmembrane PTP endowed with one intracellular catalytic domain, and an extracellular domain harboring eight fibronectin-like repeats. The protein-tyrosine phosphatase DEP-1 promotes migration and phagocytic activity of microglial cells in part through negative regulation of fyn tyrosine kinase. DEP-1 protein levels increase in several cell types at high-cell density, suggesting a role of the molecule in density-dependent growth control. A negative regulatory role of Fyn for microglial functions is inhibited by DEP-1. Determination of a role of DEP-1 in a potential DEP-1-Fyn axis in the regulation of microglial functions. Enzyme DEP-1 stimulates microglial phagocytosis and microglial cell migration, overview
the enzyme is active on protein substrates that play a relevant role in cell energy metabolism. PtpA-mediated dephosphorylation may affect pathways involved in cell energy metabolism, particularly the beta oxidation of fatty acids through modulation of TFP activity and/or cell distribution
the enzyme is active on protein substrates that play a relevant role in cell energy metabolism. PtpA-mediated dephosphorylation may affect pathways involved in cell energy metabolism, particularly the beta oxidation of fatty acids through modulation of TFP activity and/or cell distribution
the parasite enzyme LmPRL-1 shows a strong structural similarity to the human phosphatases of regenerating liver, PRL-1, -2, and -3, that regulate the proliferation, differentiation, and motility of cells
SP-PTP is a secretory protein tyrosine phosphatase and plays a crucial role in group A Streptococcus (GAS) growth. As a group A Streptococcus, Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. It lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). Enzymatically active SP-PTP plays a crucial role in cell division, the function of SP-PTP is physiologically relevant for GAS growth and cell division. SP-PTP is essential for GAS virulence
the protein tyrosine phosphatase (PTPase) plays an important role in insect immune system. The enzyme specifically dephosphorylate trans-Golgi p230 in vitro
EhPRL may play an important role in the biology and adaptive response of the parasite to the host environment during amoebic liver abscess development, thereby participating in the pathogenic mechanism in humans
EhPRL may play an important role in the biology and adaptive response of the parasite to the host environment during amoebic liver abscess development, thereby participating in the pathogenic mechanism in humans
CRC cells homozygous for a paxillin Y88F knock-in mutant exhibit significantly reduced cell migration and impaired anchorage-independent growth, and they fail to form xenograft tumors in nude mice, and have decreased phosphorylation of p130CAS, SHP2, and AKT
Asp120 has an essentiality function as the general acid. Two adjacent tyrosine residues, Tyr122 and Tyr123, contribute to the deepening of the active-site pocket. Genetic deletion of ptpA or ptpB does not affect in vitro growth or cell wall integrity
GST pull-down experiment with pervanadate-treated, to increase and preserve tyrosine phosphorylation, RAW264.7 cell lysates with either GST alone, wild-type Lyp fused to GST (GST-Lyp), or the substrate-trapping fusion proteins GST-Lyp/C227S and GST-Lyp/D195A. Whereas no protein retained by GST or GST-Lyp is detectable, the GST-Lyp/C227S and GST-Lyp/D195A trapping mutants specifically bound SKAP-HOM, the failure to detect association of SKAP-HOM with wild-type Lyp indicates that the interaction between the Lyp trapping mutants and SKAP-HOM requires tyrosine phosphorylation
the crystal structures of the tail-truncated SHP-1 and SHP-2 reveal an autoinhibitory conformation, regulatory mechanism, overview. Interactions between two SH2 domains and between the N-SH2 and the catalytic domains can be responsible for the stabilization of SHP-1 in the open, active conformation
a conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs
a conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs
a conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs
a conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs
a conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs
a conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs, except for enzyme PTPN21, this critical residue in PTPN21 is substituted with a glutamic acid, thus resulting in a WPE loop instead. The WPE loop is a key region responsible for the catalytic inertness of PTPN21
a conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs, except for enzyme PTPN21, this critical residue in PTPN21 is substituted with a glutamic acid, thus resulting in a WPE loop instead. The WPE loop is a key region responsible for the catalytic inertness of PTPN21
a conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs, except for enzyme PTPN21, this critical residue in PTPN21 is substituted with a glutamic acid, thus resulting in a WPE loop instead. The WPE loop is a key region responsible for the catalytic inertness of PTPN21
a conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs, except for enzyme PTPN21, this critical residue in PTPN21 is substituted with a glutamic acid, thus resulting in a WPE loop instead. The WPE loop is a key region responsible for the catalytic inertness of PTPN21
a conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs, except for enzyme PTPN21, this critical residue in PTPN21 is substituted with a glutamic acid, thus resulting in a WPE loop instead. The WPE loop is a key region responsible for the catalytic inertness of PTPN21
active site architecture and substrate binding pocket structure, overview. The core catalytic domain of Siw14 is formed by residues 116-281. A loop between the alpha5 and alpha6 helices, corresponding to the Q-loop in PTPs, contains a lysine and an arginine that extend into the catalytic pocket due to displacement of the alpha5 helix orientation through intramolecular crowding caused by three bulky, hydrophobic residues. The general-acid loop in PTPs is replaced in Siw14 with a flexible loop that does not use an aspartate or glutamate as a general acid
active site architecture and substrate binding pocket structure, overview. The core catalytic domain of Siw14 is formed by residues 116-281. A loop between the alpha5 and alpha6 helices, corresponding to the Q-loop in PTPs, contains a lysine and an arginine that extend into the catalytic pocket due to displacement of the alpha5 helix orientation through intramolecular crowding caused by three bulky, hydrophobic residues. The general-acid loop in PTPs is replaced in Siw14 with a flexible loop that does not use an aspartate or glutamate as a general acid
determination of key interactions that likely determine both substrate recognition and the catalytic activity of the complex. e.g. an important interaction between H812 of the enzyme and a proline residue adjacent to the phosphotyrosine of the peptide substrate, which results in an atypical conformation of the C-terminal part of the peptide substrate. If the proline is replaced by valine, the atypical conformation is lost. Residues H812 and D811 of PTPN3 are not required to regulate Eps15-dependent EGFR signaling in cultured cells
in HD-PTP, the PRR is particularly extensive and is followed by a PTP domain and a PEST region. The PTP domain has no readily observable catalytic activity towards model PTPase substrates, but displays PTPase activity towards FYN kinase
osteoclastic protein tyrosine phosphatase (PTP-oc) is a structurally unique transmembrane protein tyrosine phosphatase (PTP) that contains only a relatively small intracellular PTP catalytic domain, does not have an extracellular domain, and lacks a signal peptide proximal to the N-terminus
osteoclastic protein tyrosine phosphatase (PTP-oc) is a structurally unique transmembrane protein tyrosine phosphatase (PTP) that contains only a relatively small intracellular PTP catalytic domain, does not have an extracellular domain, and lacks a signal peptide proximal to the N-terminus
phosphatases do not alter the transition state for phosphoryl transfer. Active site structure and WPD loop analysis. Slowlier loop dynamics in PTP1B may reflect its key physiological roles in which turnover rates must meet the requirements of other activities in the cell
phosphatases do not alter the transition state for phosphoryl transfer. Active site structure and WPD loop analysis. Slowlier loop dynamics in PTP1B may reflect its key physiological roles in which turnover rates must meet the requirements of other activities in the cell
phosphatases do not alter the transition state for phosphoryl transfer. Active site structure and WPD loop analysis. Slowlier loop dynamics in PTP1B may reflect its key physiological roles in which turnover rates must meet the requirements of other activities in the cell
specific recognition of Eps15 by enzyme PTPN3 and members in the FERM domain-containing PTP subfamily comprising PTPN4, N13, N14, and N21, overview. Pro850 of Eps15 and His812 of PTPN3 plays a central role in substrate specificity. E811 in WPE loop is unfavorable to act as a general acid during dephosphorylation. Identification of residues responsible for substrate specificity in the subfamily, overview. Critical role of the additional residue Tyr676 of PTPN3, which is replaced by Ile939 in PTPN14, in recognition of tyrosine phosphorylated Eps15. The WPD loop necessary for catalysis is present in all members but not PTPN21. A conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs. Superposition of the N3PTP D811A/C842SEps15846-854 complex structure with other known PTP phosphopeptide structures. Residues H812 and D811 in PTPN3 are essential for regulating Eps15-dependent EGFR/MAPK signaling In vivo
specific recognition of Eps15 by enzyme PTPN3 and members in the FERM domain-containing PTP subfamily comprising PTPN4, N13, N14, and N21, overview. Pro850 of Eps15 and His812 of PTPN3 plays a central role in substrate specificity. E811 in WPE loop is unfavorable to act as a general acid during dephosphorylation. Identification of residues responsible for substrate specificity in the subfamily, overview. Critical role of the additional residue Tyr676 of PTPN3, which is replaced by Ile939 in PTPN14, in recognition of tyrosine phosphorylated Eps15. The WPD loop necessary for catalysis is present in all members but not PTPN21. A conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs. Superposition of the N3PTP D811A/C842SEps15846-854 complex structure with other known PTP phosphopeptide structures. Residues H812 and D811 in PTPN3 are essential for regulating Eps15-dependent EGFR/MAPK signaling In vivo
specific recognition of Eps15 by enzyme PTPN3 and members in the FERM domain-containing PTP subfamily comprising PTPN4, N13, N14, and N21, overview. Pro850 of Eps15 and His812 of PTPN3 plays a central role in substrate specificity. E811 in WPE loop is unfavorable to act as a general acid during dephosphorylation. Identification of residues responsible for substrate specificity in the subfamily, overview. Critical role of the additional residue Tyr676 of PTPN3, which is replaced by Ile939 in PTPN14, in recognition of tyrosine phosphorylated Eps15. The WPD loop necessary for catalysis is present in all members but not PTPN21. A conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs. Superposition of the N3PTP D811A/C842SEps15846-854 complex structure with other known PTP phosphopeptide structures. Residues H812 and D811 in PTPN3 are essential for regulating Eps15-dependent EGFR/MAPK signaling In vivo
specific recognition of Eps15 by enzyme PTPN3 and members in the FERM domain-containing PTP subfamily comprising PTPN4, N13, N14, and N21, overview. Pro850 of Eps15 and His812 of PTPN3 plays a central role in substrate specificity. E811 in WPE loop is unfavorable to act as a general acid during dephosphorylation. Identification of residues responsible for substrate specificity in the subfamily, overview. Critical role of the additional residue Tyr676 of PTPN3, which is replaced by Ile939 in PTPN14, in recognition of tyrosine phosphorylated Eps15. The WPD loop necessary for catalysis is present in all members but not PTPN21. A conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs. Superposition of the N3PTP D811A/C842SEps15846-854 complex structure with other known PTP phosphopeptide structures. Residues H812 and D811 in PTPN3 are essential for regulating Eps15-dependent EGFR/MAPK signaling In vivo
specific recognition of Eps15 by enzyme PTPN3 and members in the FERM domain-containing PTP subfamily comprising PTPN4, N13, N14, and N21, overview. Pro850 of Eps15 and His812 of PTPN3 plays a central role in substrate specificity. E811 in WPE loop is unfavorable to act as a general acid during dephosphorylation. Identification of residues responsible for substrate specificity in the subfamily, overview. Critical role of the additional residue Tyr676 of PTPN3, which is replaced by Ile939 in PTPN14, in recognition of tyrosine phosphorylated Eps15. The WPD loop necessary for catalysis is present in all members but not PTPN21. A conserved aspartic acid, which functions as a general acid for nucleophilic attack on the substrate in the first step of catalysis, must appear in the WPD loop among active PTPs. Superposition of the N3PTP D811A/C842SEps15846-854 complex structure with other known PTP phosphopeptide structures. Residues H812 and D811 in PTPN3 are essential for regulating Eps15-dependent EGFR/MAPK signaling In vivo
Tk-PTP adopts a common dual-specificity phosphatase (DUSP) fold, but it undergoes an atypical temperature-dependent conformational change in its P-loop and alpha4-alpha5 loop regions, switching between the inactive and active forms. Tk-PTP contains a PTP signature motif HCxxGxxR, HC93MGGLGR99 in Tk-PTP constituting the phosphate binding loop (or simply called P-loop), contains the catalytic cysteine residue (Cys93) that functions as a nucleophile for dephosphorylation and the conserved arginine residue (Arg99) that anchors the phosphate group of the substrate during the enzyme reaction. Tk-PTP contains dual general acid/base residues, Asp63 or Glu132. Structural analysis of the conformation of the P-loop of Tk-PTP(form I), structure comparisons of PTPs, structure-function analysis of the two enzyme forms, overview. Molecular dynamics simulations
unlike the catalytic domain of SHP-1 (SHP-1cat), full-length SHP-1 is a multi-domain enzyme that contains two Src-homology 2 (SH2) domains in addition to its PTP domain
unlike the catalytic domain of SHP-1 (SHP-1cat), full-length SHP-1 is a multi-domain enzyme that contains two Src-homology 2 (SH2) domains in addition to its PTP domain
Tk-PTP adopts a common dual-specificity phosphatase (DUSP) fold, but it undergoes an atypical temperature-dependent conformational change in its P-loop and alpha4-alpha5 loop regions, switching between the inactive and active forms. Tk-PTP contains a PTP signature motif HCxxGxxR, HC93MGGLGR99 in Tk-PTP constituting the phosphate binding loop (or simply called P-loop), contains the catalytic cysteine residue (Cys93) that functions as a nucleophile for dephosphorylation and the conserved arginine residue (Arg99) that anchors the phosphate group of the substrate during the enzyme reaction. Tk-PTP contains dual general acid/base residues, Asp63 or Glu132. Structural analysis of the conformation of the P-loop of Tk-PTP(form I), structure comparisons of PTPs, structure-function analysis of the two enzyme forms, overview. Molecular dynamics simulations
active site architecture and substrate binding pocket structure, overview. The core catalytic domain of Siw14 is formed by residues 116-281. A loop between the alpha5 and alpha6 helices, corresponding to the Q-loop in PTPs, contains a lysine and an arginine that extend into the catalytic pocket due to displacement of the alpha5 helix orientation through intramolecular crowding caused by three bulky, hydrophobic residues. The general-acid loop in PTPs is replaced in Siw14 with a flexible loop that does not use an aspartate or glutamate as a general acid
Tk-PTP adopts a common dual-specificity phosphatase (DUSP) fold, but it undergoes an atypical temperature-dependent conformational change in its P-loop and alpha4-alpha5 loop regions, switching between the inactive and active forms. Tk-PTP contains a PTP signature motif HCxxGxxR, HC93MGGLGR99 in Tk-PTP constituting the phosphate binding loop (or simply called P-loop), contains the catalytic cysteine residue (Cys93) that functions as a nucleophile for dephosphorylation and the conserved arginine residue (Arg99) that anchors the phosphate group of the substrate during the enzyme reaction. Tk-PTP contains dual general acid/base residues, Asp63 or Glu132. Structural analysis of the conformation of the P-loop of Tk-PTP(form I), structure comparisons of PTPs, structure-function analysis of the two enzyme forms, overview. Molecular dynamics simulations