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Enzyme Nomenclature
Information on EC 3.1.3.48 - protein-tyrosine-phosphatase
for references in articles please use BRENDA:EC3.1.3.48
Word Map on EC 3.1.3.48
- 3.1.3.48
- diabetes
- arrest
-
mapks
-
cyclin
- carcinoma
- adhesion
- autoimmune
- leukemia
- endothelial
- vascular
- breast
-
okadaic
-
signal-regulated
- bone
- t-cells
- inflammation
-
checkpoint
- orthovanadate
- metastasis
- vanadate
- obesity
-
tyrosine-phosphorylated
-
cyclin-dependent
- myeloid
-
3-kinase
- phosphatidylinositol
- arthritis
-
adaptor
-
focal
-
hyperphosphorylation
-
autophosphorylation
-
rheumatoid
- genistein
-
integrins
-
receptor-like
- chondroitin
-
insulin-stimulated
-
nonreceptor
-
oncoproteins
-
phosphopeptide
-
platelet-derived
-
stats
-
paxillin
-
myelomonocytic
-
janus
-
insulin-induced
- herbimycin
- tyrphostins
-
substrate-1
-
polo-like
- medicine
- pharmacology
- drug development
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.1.3.48
-
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RECOMMENDED NAME
GeneOntology No.
protein-tyrosine-phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
mechanism, transition state of reaction, kinetic isotope effects, overview
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
mechanism, role of residue 182
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
thermodynamic parameters
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
mechanism, kinetic isotope effects
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[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
comparison of kinetic properties of different transmembrane and cytosolic isozymes
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[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
overview on mechanism and transition state
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
overview on mechanism and transition state
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
overview on mechanism and transition state
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
mechanism, overview
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
mechanism
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
mechanism, features required for substrate
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
activation mechanism
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
in addition to active site, enzyme has a low-affinity noncatalytic aryl phosphate-binding site
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
H148 acts as a general acid catalyst, D115 assists the protonation of the leaving group of a substrate, and D76 and D112 are involved in binding of magnesium ions
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
conformation of active site is favorable for phosphotyrosine binding. Interaction of D115 and R13 to stabilize the conformation of the active cavity. A41 and G45 form a noncharged surface around the active cavity, which is surrounded by a flexible wall made of the loop region from F40 to T48
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
arrangement of two metal ions, a phosphate ion, and amino acid residues in the catalytic site is identical to that of PS/Tpases
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
motif H74C(X)5R81 is involved in catalysis
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
ping-pong mechanism, catalysis proceeds through a two-step mechanism involving a phosphocysteine intermediate. In the first step, a nucleophilic cysteine thiolate attacks the phosphate ester moiety of the substrate, resulting in formation of a phosphoenzyme intermediate with release of the peptidyl tyrosine. The second step occurs via attack of water on the phosphoenzyme intermediate, and yields the final products inorganic phosphate and the regenerated enzyme. The central binding site for the substrate is the P-loop, a region at the bottom of a pocket that includes the nucleophilic cysteine and backbone amide groups oriented in a horseshoe fashion, catalytic cycle, detailed overview
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
mechanism of the dephosphorylation catalysed by MptpA
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
mechanism
-
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
protein-tyrosine-phosphate phosphohydrolase
Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2, non-specific protein-tyrosine kinase.
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CAS REGISTRY NUMBER
COMMENTARY
79747-53-8
-
97162-86-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. CvBV, gene CvBV202. Cotesia vestalis is a solitary endoparasitoid wasp of the larval stage of the diamondback moth, Plutella xylostella, and injects a polydnavirus, CvBV, into its host during oviposition
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the wild type strain DSM 639 missing 322 bp called MW001
UniProt
the wild type strain DSM 639 missing 322 bp called MW001
UniProt
-
651283, 652498, 665525, 666310, 666864, 677314, 678028, 678263, 678471, 678485, 678724, 678831, 679025, 679201, 680716, 680825, 682085, 682215, 682557, 682565, 682756, 690663, 691305, 691462, 692217, 692320, 692322, 692448, 692702, 693029, 693383, 693564, 693715, 693943, 694112, 694163, 694286, 694291, 694525, 694608, 694902, 694911, 707666, 707675, 707683, 707688, 707975, 708290, 709166, 709254, 709293, 709433, 709455, 709960, 710028, 710166, 710237, 710396, 710432, 714237, 714323, 714433, 714721, 715647, 715714, 728947, 729298, 729368, 729393, 730540, 730564, 730970, 737098, 94964, 94965, 94968, 94969, 94974, 94977, 94979, 94986, 94987, 94989, 94996, 95000, 95005, 95007, 95008, 95009, 95011, 95014, 95017, 95019
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-
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SwissProt
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UniProt
-
UniProt
isoform PTP1B, amino acids 1-400, catalytic domain plus 80-amino acid C-terminal tail
SwissProt
-
678052, 678978, 680916, 681516, 681830, 691726, 691836, 692163, 693154, 694165, 694204, 694827, 709385, 709938, 715793, 728947, 729290, 729989, 730380
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GenBank accession numbers are PTP36-A: AF170902, PTP36-B: AF170903, PTP36-C: AF170904
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GenBank accession numbers are PTP36-A: AF170902, PTP36-B: AF170903, PTP36-C: AF170904; GenBank D64141
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GenBank accession numbers are PTP36-A: AF170902, PTP36-B: AF170903, PTP36-C: AF170904; PTP36-D: Af170905, tissue-dependent expressions of isoforms
Uniprot
homozygous PTP1B-deficient animal, hyperresponsive to insulin and leptin and resistant to diet-induced obesity
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-
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652081, 664283, 665245, 666827, 677364, 681516, 692182, 708290, 729553, 94972, 94973, 94982, 94983, 94986, 94995, 95001
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alternative splicing produces 3 isoforms: PTPxi-A, the full-length form, PTPxi-B, the short form and PTPxi-S an extracellular variant
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two low-molecular-weight protein tyrosine phosphatases, PtpA and PtpB
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strain PCC 6803, isoforms SynPPP1 and SynPPM3 both acting on phosphotyrosine- as well as phosphoserine-containing proteins
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
Protein tyrosine phosphatases form a large family of enzymes involved in the regulation of numerous cellular functions in eukaryotes
evolution
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Protein tyrosine phosphatases form a large family of enzymes involved in the regulation of numerous cellular functions in eukaryotes
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malfunction
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the enzyme is involved in the negative regulation of several cancer relevant cellular signalling pathways
malfunction
-
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
malfunction
-
protein tyrosine phosphatases inactivate neurotrophic factor receptors and downstream intracellular signaling molecules causing neurodegeneration and loss of sensoric functions, overview
malfunction
-
CRYP-2 is involved in hepatic carcinomas, inhibition of CRYP-2 is of tremendous therapeutic importance
malfunction
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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
malfunction
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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
malfunction
-
the Cowden syndrome-associated G129E mutation abrogates the phospholipid phosphatase activity but not the phosphoprotein phosphatase activity of PTEN
malfunction
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improperly regulated PTP activity has been implicated in a range of human diseases including leukemia, solid-tumor cancers, diabetes, and several autoimmune disorders
malfunction
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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
malfunction
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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
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metabolism
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MPtpA is a signalling protein belonging to the tyrosine phosphatase superfamily, and is involved in phagocytosis and is active in virulent mycobacterial form
metabolism
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striatal-enriched protein-tyrosine phosphatase regulates proline-rich tyrosine kinase 2 activity
physiological function
the heat-resistant PTPase may play important roles in vivo in the adaptation of the microorganism to extreme temperatures and specific nutritional conditions
physiological function
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MptpA and MptpB selectively dephosphorylate human host proteins involved in interferon-gamma signaling pathways, thereby preventing the initiation of host defense mechanisms, overview
physiological function
protein tyrosine phosphatases are crucial elements in eukaryotic signal transduction
physiological function
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SHP-1 is important in the negative regulation of JAK/STAT signaling and is often silenced by methylation in leukemias and lymphomas
physiological function
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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
physiological function
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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
physiological function
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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
physiological function
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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
physiological function
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SHP-1 is involved in the PI3K-AKT pathway interacting with PI3K and regulating its activity and p110 catalytic subunit phosphorylation
physiological function
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PTPRT is involved in important signaling pathway that plays a critical role in colorectal tumorigenesis, overview
physiological function
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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
physiological function
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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
physiological function
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SHP-1 generally acts as a negative regulator in a variety of cellular signaling pathways
physiological function
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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
physiological function
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the enzyme is capable of rescuing the effects of v-Src toxicity
physiological function
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the enzyme is capable of rescuing the effects of v-Src toxicity
physiological function
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protein tyrosine phosphatase 1B is a negative regulator of systemic glucose and insulin homeostasis and inhibits adipocyte differentiation and mediates TNFalpha action in obesity
physiological function
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isoform TC48 inhibits proliferation and enhances sensitivity of K562 cells to STI571
physiological function
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protein tyrosine phosphatase-PEST regulates mast cell-activating signals in protein tyrosine phosphatase activity-dependent and -independent manners
physiological function
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low molecular weight protein-tyrosine phosphatase A is a key virulence factor of Mycobacterium tuberculosis, the enzyme is essential for infection of host macrophages
physiological function
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protein tyrosine phosphatase B is a virulence factor secreted into the host macrophage
physiological function
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isoform PTP1B (PTPN1) regulates the insulin and leptin signalling pathway and is implicated in cancer and obesity/diabetes
physiological function
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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
physiological function
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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
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physiological function
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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the heat-resistant PTPase may play important roles in vivo in the adaptation of the microorganism to extreme temperatures and specific nutritional conditions
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additional information
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small-molecule protein tyrosine phosphatase inhibition is a neuroprotective treatment after spinal cord injury in adult rats
additional information
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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
additional information
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PTP-H2 expression is restricted to hemocytes in Microplitis demolitor bracovirus -infected hosts
additional information
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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
additional information
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phosphatases interact only transiently with their substrates
additional information
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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
additional information
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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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-O-methylfluorescein phosphate + H2O
3-O-methylfluorescein + phosphate
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-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferol + phosphate
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
Ac-DGEEpYDDPF-NH2 + H2O
Ac-DGEEYDDPF-NH2 + phosphate
-
SKAP-HOM Tyr75 peptide
-
-
?
Ac-YGEEpYDDLY-NH2 + H2O
Ac-YGEEYDDLY-NH2 + phosphate
-
consensus peptide 1
-
-
?
Ac-YGYEpYDDEY-NH2 + H2O
Ac-YGYEYDDEY-NH2 + phosphate
-
consensus peptide 2
-
-
?
bis-(p-phosphophenyl) methane + H2O
?
synthetic high-affinity low-molecular weight nonpeptide substrate
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-
?
carrier protein-Cdc2-phosphotyrosine + H2O
carrier protein-Cdc2-tyrosine + phosphate
-
-
-
-
?
carrier protein-Y3-phosphotyrosine + H2O
carrier protein-Y3-tyrosine + phosphate
-
-
-
-
?
carrier protein-Y5-phosphotyrosine + H2O
carrier protein-Y5-tyrosine + phosphate
-
-
-
-
?
Cdk2-pTpY + H2O
Cdk2-TpY + phosphate
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dephosphorylates Cdk/cyclins on pThr14 and/or pTyr15 residues
-
-
?
difluoromethylumbelliferyl phosphate + H2O
difluoromethylumbelliferone + phosphate
-
-
-
?
epidermal growth factor receptor + H2O
? + phosphate
-
with phosphotyrosine Tyr992
-
-
?
FMN + H2O
? + phosphate
-
71.8% of the activity with 4-nitrophenyl phosphate, lung enzyme
-
-
?
GESDGGpYMDMSKD + H2O
GESDGGYMDMSKD + phosphate
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this peptide corresponds to the sequence containing Tyr740 of the human platelet-derived growth factor receptor
-
-
?
hirudin + H2O
? + phosphate
-
hirudin from leech, phosporylated on tyrosine
-
-
?
KRLIEDNE(pY)TARGQ + H2O
KRLIEDNEYTARGQ + phosphate
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phosphopeptide derived from autophosphorylation of mammalian tyrosine kinase Lck
-
-
?
lysozyme + H2O
? + phosphate
-
reduced, carboxymethylated and maleylated
-
-
?
nicotinic acetylcholine receptor + H2O
? + phosphate
-
i.e. nAChR
-
-
?
phosphorylated Abelson interacting protein + H2O
Abelson interacting protein + phosphate
-
-
-
-
?
phosphorylated Abl tyrosine kinase + H2O
Abl tyrosine kinase + phosphate
-
-
-
-
?
phosphorylated adenomatous Polyposis coli-protein + H2O
adenomatous Polyposis coli-protein + phosphate
-
-
-
-
?
phosphorylated AMP-activated protein kinase + H2O
AMP-activated protein kinase + phosphate
phosphorylated c-Kit + H2O
c-Kit + phosphate
-
dephosphorylation occurs at tyrosines 567/569 and 719
-
-
?
phosphorylated Cdk2-pTpY/CycA protein + H2O
Cdk2-pTpY/CycA protein + phosphate
-
-
-
?
phosphorylated colony-stimulating factor 1 receptor + H2O
colony-stimulating factor 1 + phosphate
-
-
-
-
?
phosphorylated Down syndrome cell adhesion molecule + H2O
Down syndrome cell adhesion molecule + phosphate
-
-
-
-
?
phosphorylated epidermal growth factor receptor + H2O
epidermal growth factor receptor + phosphate
phosphorylated ERK2 + H2O
ERK2 + phosphate
HePTP binds the phosphorylated tyrosine of the Erk2 peptide (pY185), Erk2 residue T183, which is phosphorylated in maximally activated Erk2, is not essential for substrate recognition and binding by HePTP
-
-
?
phosphorylated eukaryotic-initiation-factor-4G + H2O
eukaryotic-initiation-factor-4G + phosphate
-
-
-
-
?
phosphorylated extracellular signal regulated kinase + H2O
extracellular signal regulated kinase + phosphate
-
-
-
-
?
phosphorylated extracellular signal-regulated kinase 1 + H2O
extracellular signal-regulated kinase 1 + phosphate
phosphorylated extracellular signal-regulated kinase 2 + H2O
extracellular signal-regulated kinase 2 + phosphate
phosphorylated focal adhesion kinase + H2O
focal adhesion kinase + phosphate
-
dephosphorylation occurs at Tyr-397, PTPD1 activity is required for focal adhesion kinase autophosphorylation and adhesion plaque stability
-
-
?
phosphorylated fragile X related + H2O
fragile X related + phosphate
-
-
-
-
?
phosphorylated Gln3 + H2O
Gln3 + phosphate
-
Siw14, in combination with the protein kinase Npr1, regulates the intracellular localization of Gln3
-
-
?
phosphorylated hepatocyte growth factor regulated tyrosine kinase substrate + H2O
hepatocyte growth factor regulated tyrosine kinase substrate + phosphate
-
-
-
-
?
phosphorylated IGF-I receptor + H2O
IGF-I receptor + phosphate
-
isozyme p52shc
-
-
?
phosphorylated IGF-II mRNA-binding protein + H2O
IGF-II mRNA-binding protein + phosphate
-
-
-
-
?
phosphorylated insulin receptor substrate-1 + H2O
insulin receptor substrate-1 + phosphate
-
-
-
-
?
phosphorylated insulin receptor substrate-2 + H2O
insulin receptor substrate-2 + phosphate
-
-
-
-
?
phosphorylated JAK2 + H2O
JAK2 + phosphate
-
SHP2 dephosphorylates the Tyr1007 site, preventing the formation of the JAK2-Socs1 complex
-
-
?
phosphorylated Jun amino-terminal kinase + H2O
Jun amino-terminal kinase + phosphate
-
-
-
-
?
phosphorylated Lck + H2O
Lck + phosphate
-
component of the T cell receptor signaling pathway
-
-
?
phosphorylated mitogen-activated protein kinase + H2O
mitogen-activated protein kinase + phosphate
-
-
-
-
?
phosphorylated mitogen-activated protein kinase Pmk1p + H2O
mitogen-activated protein kinase Pmk1p + phosphate
phosphorylated Munc18c + H2O
Munc18c + phosphate
-
dephosporylation at Tyr218/219 and Tyr521
-
-
?
phosphorylated p130 Crk-associated substrate + H2O
p130 Crk-associated substrate + phosphate
-
-
-
-
?
phosphorylated p190B Rho-GTPase-activating protein + H2O
p190B Rho-GTPase-activating protein + phosphate
-
-
-
-
?
phosphorylated p38 mitogen-activated protein kinase + H2O
p38 mitogen-activated protein kinase + phosphate
phosphorylated PDGF- and VEGF-receptor related + H2O
PDGF- and VEGF-receptor related + phosphate
-
-
-
-
?
phosphorylated platelet-derived growth factor receptor + H2O
platelet-derived growth factor receptor + phosphate
-
-
-
-
?
phosphorylated poly(A)-binding protein + H2O
poly(A)-binding protein + phosphate
-
-
-
-
?
phosphorylated proline serine threonine-rich phosphatase interacting protein + H2O
proline serine threonine-rich phosphatase interacting protein + phosphate
-
-
-
-
?
phosphorylated proline-rich tyrosine kinase 2 + H2O
proline-rich tyrosine kinase 2 + phosphate
-
the enzyme directly binds to and dephosphorylates proline-rich tyrosine kinase 2 at Tyr402
-
-
?
phosphorylated protein kinase-like endoplasmic reticulum kinase + H2O
protein kinase-like endoplasmic reticulum kinase + phosphate
-
dephosphorylation at Tyr615
-
-
?
phosphorylated pyruvate kinase M2 + H2O
pyruvate kinase M2 + phosphate
-
-
-
-
?
phosphorylated RET(C634R) oncoprotein + H2O
RET(C634R) oncoprotein + phosphate
-
dephosphorylation at Tyr905 and Tyr1062
-
-
?
phosphorylated RET-MEN2A oncoprotein + H2O
RET-MEN2A oncoprotein + phosphate
-
dephosphorylation at Tyr905 and Tyr1062
-
-
?
phosphorylated RET/PTC1 oncoprotein + H2O
RET/PTC1 oncoprotein + phosphate
-
dephosphorylation at Tyr905 and Tyr1062
-
-
?
phosphorylated signal transducer and activator of transcription 3 + H2O
signal transducer and activator of transcription 3 + phosphate
-
-
-
-
?
phosphorylated specifically Rac1-associated protein 1 + H2O
specifically Rac1-associated protein 1 + phosphate
-
-
-
-
?
phosphorylated Src tyrosine kinase + H2O
Src tyrosine kinase + phosphate
-
PTPD1 associates with and activates Src tyrosine kinase
-
-
?
phosphorylated STAT5 + H2O
STAT5 + phosphate
-
purified SHP2 protein directly dephosphorylates STAT5 or tyrosine-phosphorylated peptides derived from STAT5
-
-
?
phosphorylated T cell antigen receptor chain zeta + H2O
T cell antigen receptor chain zeta + phosphate
-
-
-
-
?
phosphorylated T cell antigen receptor zeta + H2O
T cell antigen receptor zeta + phosphate
-
-
-
-
?
phosphorylated T-cell receptor-zeta subunit + H2O
T-cell receptor-zeta subunit + phosphate
-
dephosphorylates ITAMs of the T-cell receptor-zeta subunit
-
-
?
phosphorylated TCRzeta + H2O
TCRzeta + phosphate
-
PTPH1 dephosphorylates TCRzeta in vitro, inhibiting the downstream inflammatory signaling pathway
-
-
?
phosphorylated valosin containing protein + H2O
valosin containing protein + phosphate
-
-
-
-
?
phosphorylated vascular endothelial growth factor receptor 2 + H2O
vascular endothelial growth factor receptor 2 + phosphate
phosphorylated Vav + H2O
Vav + phosphate
-
component of the T cell receptor signaling pathway
-
-
?
phosphorylated voltage-gated potassium channel subunit Kv2.1 + H2O
voltage-gated potassium channel subunit Kv2.1 + phosphate
-
-
-
-
?
phosphorylated YwqD
YwqD + phosphate
-
protein implicated in UDP-glucuronate synthesis
-
-
?
phosphorylated YwqF
YwqF + phosphate
-
protein implicated in UDP-glucuronate synthesis
-
-
?
phosphotyrosyl myelin basic protein + H2O
tyrosyl-myelin basic protein + phosphate
-
-
-
-
?
phosphotyrosyl reduced carboxyamidomethylated and maleylated lysozyme + H2O
tyrosyl-reduced carboxyamidomethylated and maleylated lysozyme + phosphate
-
-
-
-
?
SKAP-HOM + H2O
?
-
a cytosolic adaptor protein required for proper activation of the immune system, a bona fide Lyp substrate
-
-
?
soluble N-ethylmaleimide-sensitive factor attachment protein receptor + H2O
soluble N-ethylmaleimide-sensitive factor attachment protein receptor + phosphate
-
-
-
-
?
TGFLTELpYVATRWY + H2O
TGFLTELYVATRWY + phosphate
-
this peptide corresponds to the sequence containing Tyr204 of the human extracellular signal-regulated kinase
-
-
?
tyrosine-phosphorylated myelin basic protein + H2O
myelin basic protein + phosphate
-
-
-
?
YCRPESQEHPEADPGAAPpYLK + H2O
YCRPESQEHPEADPGAAYLK + phosphate
-
YCRPESQEHPEADPGAApYLK is signal transducer and activator of transcription 3, is dephosphorylated at Y705
-
-
?
[EGF receptor]-tyrosine1018 phosphate + H2O
[EGF receptor]-tyrosine1018 + phosphate
highest activity
-
-
?
[insulin receptor kinase]-tyrosine phosphate + H2O
[insulin receptor kinase]-tyrosine + phosphate
-
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
89.3% of the activity with 4-nitrophenyl phosphate, lung enzyme
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
nitrophenol + phosphate
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferol + phosphate
-
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferol + phosphate
-
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
9.5% activity compared to TRDIpYETDYYRK
-
-
?
ATP + H2O
ADP + phosphate
-
9.5% activity compared to TRDIpYETDYYRK
-
-
?
bovine serum albumin + H2O
? + phosphate
-
reduced, carboxamide methylated and succinylated
-
-
?
D-fructose 1,6-diphosphate + H2O
?