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3.1.3.48: protein-tyrosine-phosphatase

This is an abbreviated version!
For detailed information about protein-tyrosine-phosphatase, go to the full flat file.

Word Map on EC 3.1.3.48

Reaction

[a protein]-tyrosine phosphate
+
H2O
=
[a protein]-tyrosine
 +
phosphate

Synonyms

70Z-SHP, acid phosphatase, acid phosphatase activity, acid phosphatase ortholog, acid tyrosine phosphatase, alpha-PTP-PEST, AUM, Bd1204, BDP, Bmptp-h, Brain-derived phosphatase, BVP, CAPTPase, CD148, CD148 antigen, CD45, CD45 antigen, CD45 protein tyrosine phosphatase, Cdc25 phosphatase, Cdc25-like protein, Cdc25A, Cdc25B, Cdc25B phosphatase, Cdc25C, CDK2-associated dual specificity phosphatase, Ch-1PTPase, chick retinal tyrosine phosphatase-2, cold-active protein tyrosine phosphatase, CPTP1, CQMa102 phosphatase, Cryp-2, CRYP-2/PTPRO, CRYP-2/receptor-type tyrosine-protein phosphatase O, cysteine-dependent protein tyrosine phosphatase, cyt-PTPepsilon, density-enhanced phosphatase-1, DEP-1, DEP-1 phosphatase, DLAR, dPTP61F, DSP, DSP18, dual specificity phosphatase, Dual specificity phosphatase Cdc25A, Dual specificity phosphatase Cdc25B, Dual specificity phosphatase Cdc25C, dual specificity protein phosphatase, dual specificity protein phosphatase 23, dual specificity protein phosphatase 3, Dual specificity protein phosphatase hVH1, Dual specificity protein phosphatase hVH2, Dual specificity protein phosphatase hVH3, Dual specificity protein phosphatase PYST1, Dual specificity protein phosphatase PYST2, Dual specificity protein phosphatase VHR, dual-specificity (Thr/Tyr) MAPK protein phosphatase, dual-specificity phosphatase, dual-specificity protein phosphatase, dual-specificity protein tyrosine phosphatase 18, Dual-specificity tyrosine phosphatase TS-DSP6, Dual-specificity tyrosine phosphatase YVH1, DUSP, ED-Eya2, EhPRL, EpsB, ES cell phosphatase, FAP-1, Fap1, FLP1, GLEPP-1, GLEPP1, HAP, HCP, HD-PTP, Hematopoietic cell protein-tyrosine phosphatase, Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, hematopoietic protein tyrosine phosphatase, Hematopoietic protein-tyrosine phosphatase, hematopoietic tyrosine phosphatase, HEPTP, His domain protein tyrosine phosphatase, histidine acid phosphatase, histidine domain-protein tyrosine phosphatase, HPTP beta-like tyrosine phosphatase, HPTP eta, HPTPbeta, HPTPbeta-CD, hPTPE1, IA-2, IA-2A, IA-2beta, IAR, ICAAR, IF1, IF2, insulinoma associated protein tyrosine phosphatase 2, islet cell antigen-related PTP, Islet cell autoantigen related protein, KIM-containing PTP, KIM-PTP, kinase associated phosphatase, kinase interaction motif phosphatase, kinase interaction motif-containing protein tyrosine phosphatases, L-CA, LAR, Late protein H1, LCA, LCA-related phosphatase, LDP-3, leucocyte common antigen-related protein tyrosine phosphatase, Leukocyte antigen related, leukocyte common antigen-related, LmACR2, LMJF_16_0230, LmPRL-1, LMW PTPase, LMW-PTP, LMWPTP, low molecular mass dual specificity phosphatase 3, Low molecular weight cytosolic acid phosphatase, Low molecular weight phosphotyrosine protein phosphatase, low molecular weight protein tyrosine phosphatase, low molecular weight protein-tyrosine phosphatase A, low molecular weight protein-tyrosine-phosphatase, low molecular weight-PTP, low-molecular weight PTPase, low-molecular-weight protein tyrosine phosphatase, Lpt1, LRP, Lymphoid phosphatase, lymphoid-specific tyrosine phosphatase, LyP, M1851, MAP kinase phosphatase, MAP-kinase phosphatase CPG21, MAPK-specific tyrosine phosphatase, MEG, mitogen-activated protein kinase phosphatase, mitogen-activated protein kinase phosphatase-1, mitogen-activated protein kinase-specific tyrosine phosphatase, Mitosis initiation protein, Mitosis initiation protein MIH1, Mitotic inducer homolog, MKP, MKP-1, MKP-1 like protein tyrosine phosphatase, MKP-2, MKP-3, MKP-4, MKP-5, MKP-7, MKP-X, MKP1, MKP5-C, More, MPTP, MPTP-PEST, MPtpA, MPtpB, MSP, N3PTP, NC-PTPCOM1, Neural-specific protein-tyrosine phosphatase, non-receptor protein tyrosine phosphatase, ORF5, orphan protein tyrosine phosphatase, OST-PTP, osteoclastic protein-tyrosine phosphatase, P19-PTP, p52shc, p65 PTPepsilon, p66shc, p67 PTPepsilon, P80, PC12-PTP1, PCPTP1, PEST, PGN_1525, Pgp, Phogrin, Phosphacan, phosphatase of regenerating liver-3, phosphatase, phosphoprotein (phosphotyrosine), phosphatase, phosphotyrosine, phosphoprotein phosphatase (phosphotyrosine), phosphotyrosine histone phosphatase, phosphotyrosine phosphatase, Phosphotyrosine phosphatase 13, phosphotyrosine phosphatase 1B, phosphotyrosine protein phosphatase, phosphotyrosine-specific PP, phosphotyrosylprotein phosphatase, Pmp1p, PP2A, PPase, pphA, PPM, PPT-phosphatase, PRL, PRL-1, PRL-3, PRL-related protein tyrosine phosphatase, probable low molecular weight protein-tyrosine-phosphatase, protein of regenerating liver-related protein tyrosine phosphatase, Protein phosphatase 1B, protein phosphatase 2A, protein phosphotyrosine phosphatase, protein Tyr phosphatase, protein tyrosine phosphatase, protein tyrosine phosphatase 1B, protein tyrosine phosphatase A, protein tyrosine phosphatase alpha, protein tyrosine phosphatase B, protein tyrosine phosphatase beta, protein tyrosine phosphatase epsilon, protein tyrosine phosphatase eta, protein tyrosine phosphatase H1, protein tyrosine phosphatase N12, protein tyrosine phosphatase N3, protein tyrosine phosphatase ny, Protein tyrosine phosphatase receptor-type T, protein tyrosine phosphatase SHP-1, protein tyrosine phosphatase sigma, protein tyrosine phosphatase xi, protein tyrosine phosphatase, non-receptor type 1, protein tyrosine phosphatase, receptor-type, Z polypeptide 1, protein tyrosine phosphatase-1B, protein tyrosine phosphatase-2, protein tyrosine phosphatase-BL, protein tyrosine phosphatase-H2, Protein tyrosine phosphatase-NP, protein tyrosine phosphatase-PEST, Protein-protein-tyrosine phosphatase HA2, protein-tyrosine phosphatase, Protein-tyrosine phosphatase 1B, Protein-tyrosine phosphatase 1C, Protein-tyrosine phosphatase 1E, Protein-tyrosine phosphatase 2C, Protein-tyrosine phosphatase 2E, Protein-tyrosine phosphatase 3CH134, protein-tyrosine phosphatase alpha, Protein-tyrosine phosphatase CL100, Protein-tyrosine phosphatase D1, Protein-tyrosine phosphatase ERP, Protein-tyrosine phosphatase G1, Protein-tyrosine phosphatase H1, Protein-tyrosine phosphatase LC-PTP, Protein-tyrosine phosphatase MEG1, Protein-tyrosine phosphatase MEG2, Protein-tyrosine phosphatase P19, Protein-tyrosine phosphatase PCPTP1, Protein-tyrosine phosphatase pez, Protein-tyrosine phosphatase PTP-RL10, Protein-tyrosine phosphatase PTP36, Protein-tyrosine phosphatase PTPL1, Protein-tyrosine phosphatase striatum-enriched, Protein-tyrosine phosphatase SYP, Protein-tyrosine-phosphatase SL, Protein-tyrosine-phosphate phosphohydrolase, Prp1, PrpA, PTEN, PTEN phosphoprotein phosphatase, PTK, PTP, PTP 1B, PTP epsilon, PTP IA-2beta, PTP-1B, PTP-1C, PTP-1D, PTP-2C, PTP-BAS, PTP-BL, PTP-E1, PTP-eta, PTP-F, PTP-H1, PTP-H2, PTP-HA2, PTP-like phytase, PTP-MEG2, PTP-NP, PTP-oc, PTP-PEST, PTP-phosphatase, PTP-SH2beta, PTP-SL, PTP-U2, PTP1, PTP1B, PTP1C, PTP1D, PTP1e, PTP1N13, PTP1N21, PTP2C, PTP3, PTP36, PtpA, PTPalpha, PTPase, PTPase YVH1, PTPase-MEG1, PTPase-MEG2, PtpB, PTPB1, PTPBAS, PTPbeta, PTPBR7, PTPD1, PTPepsilon, PTPepsilonC, PTPepsilonM, PTPeta, PTPetaCD, PTPG1, PTPgamma, PTPH1, PTPL1, PTPLP, PTPMEG, PTPN1, PTPN11, PTPN12, PTPN13, PTPN14, PTPN2, PTPN20 variant 15, PTPN21, PTPN22, PTPN23, PTPN3, PTPN4, PTPN4/PTP-MEG1, PTPN5, PTPN6, PTPN7, PTPN9, PTPNE6, PTPP, PTPPase, PTPPBSgamma, PTPPBSgamma-37, PTPPBSgamma-42, PTPRA, PTPRB, PTPRC, PTPRD, PTPRdelta, PTPRE, PTPRF, PTPRG, PTPRH, PTPRJ, PTPRK, PTPRM, PTPRN, PTPRN2, PTPRO, PTPRO, truncated, PTPRO-FL, PTPRomega, PTPROt, PTPRQ, PTPRR, PTPRS, PTPRT, PTPRU, PTPRV, PTPRZ, PTPRZ1, PTPS31, PTPsigma, PTPxi/RPTPbeta, PY protein phosphatase, Pyp1p, Pyp2p, R-PTP-alpha, R-PTP-beta, R-PTP-delta, R-PTP-epsilon, R-PTP-eta, R-PTP-gamma, R-PTP-kappa, R-PTP-mu, R-PTP-zeta, R2B phosphatase, receptor protein tyrosine phosphatase, receptor protein tyrosine phosphatase isoform delta, receptor protein tyrosine phosphatase isoform omega, receptor protein tyrosine phosphatase rho, receptor protein tyrosine phosphatase T, receptor protein tyrosine phosphatase {kappa}, receptor PTPepsilon, Receptor-linked protein-tyrosine phosphatase 10D, Receptor-linked protein-tyrosine phosphatase 99A, receptor-type protein tyrosine phosphatase J, Receptor-type protein-tyrosine phosphatase-kappa, receptor-type tyrosine-protein phosphatase R, reductant-inhibited PTPase1, RIP1, RNA/RNP complex-intereracting phosphatase, ROL B protein, RPTP, RPTP-BK, RPTPalpha, RPTPdelta, RPTPepsilon, RPTPgamma, RPTPkappa, RPTPlambda, RPTPmu, RPTPrho, RPTPrho/PTPRT, RPTPsigma, RPTPzeta, Saci-PTP, Saci0545, SAP1, Scr homology 2-containing tyrosine phosphatase, selective striatal enriched protein phosphatase, SH-PTP1, SH-PTP2, SH-PTP3, SH2 domain-containing tyrosine phosphatase-1, SH2 domain-containing tyrosine phosphatase-2, SHP, SHP-1, SHP-2, SHP1, SHP2, Siw14, Slr0328, Small tyrosine phosphatase, Small, acidic phosphotyrosine protein phosphatase, SP-PTP, Spd1837, SPD_1837, specific protein-tyrosine phosphatase, SPH-1, SPH-2, SPy_0036, SPy_0039, Src homology 2 domain-containing phosphatase-1, Src homology region 2 domain-containing phosphatase 1, Src homology-2 domain containing protein tyrosine phosphatase-1, Src homology-2 domain containing protein tyrosine phosphatase-2, STEP, STEP33, STEP46, STEP61, Stp1, striatal enriched protein tyrosine phosphatase, striatal-enriched protein-tyrosine phosphatase, striatal-enriched PTP, String protein, SynPTP, Syp, T cell protein tyrosine phosphatase, T-cell protein tyrosine phosphatase, T-cell protein-tyrosine phosphatase, T-cell PTP, T-DSP11, T200, TC PTP, TC-PTPase ´, TC48, TCPTP, TCPTP/TC45, TcPTP1, testis- and skeletal-muscle-specific DSP, testis- and skeletal-muscle-specific dual specificity protein phosphatase, Testis-and skeletal-muscle-specific DSP, Tk-PTP, TK0241, TMDP, TpbA, TypPT, tyrosine O-phosphate phosphatase, tyrosine phosphatase, tyrosine phosphatase alpha, Tyrosine phosphatase CBPTP, tyrosine phosphatase epsilon, tyrosine phosphatase IA-2, tyrosine phosphatase Src homology region 2 domain-containing phosphatase 1, tyrosine phosphatase-1B, tyrosine-protein phosphatase, tyrosine-protein phosphatase non-receptor type 22, tyrosine-protein phosphatase non-receptor type 5, tyrosine-specific MAPK phosphatase, tyrosylprotein phosphatase, vaccinia H1-related PTP, VE-PTP, VHR, VHZ, Wzb, YopH, YwlE, YwqE, [phosphotyrosine]protein phosphatase

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.48 protein-tyrosine-phosphatase

Crystallization

Crystallization on EC 3.1.3.48 - protein-tyrosine-phosphatase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
solution structure of enzyme
hanging drop vapor diffusion method, using 200 mM MgCl2, 100 mM Tris-HCl (pH 7.0), 8-10% (w/v) PEG 8000
hanging drop vapour diffusion method with 10% (v/v) Tascimate, 0.1 M HEPES pH 7.0 and 19% (w/v) PEG 3350
-
active site mutant C215S in complex with substrates bis-(para-phosphophenyl) methane and 4-nitrophenyl phosphate
both wild-type PTP-1B and its mutant L119V
-
C-terminal truncated form, ligand-free, in auto-inhibited conformation
-
catalytic domain and C455S mutant of catalytic domain, in complex with peptide substrates
catalytically active, monomeric D1 domain
-
cytoplasmic D1D2 segment of CD45, in native and phosphotyrosyl peptide-bound form
-
enzyme in oxovanadium-complexes, termed [VIVO(SAA)(2,2'-bipyridine)]0.25bpy and [VIVO(SAA)(1,10-phenanthroline)]0.33H2O, overview
-
hanging drop vapour diffusion method with 0.05 M Bis-Tris (pH 7.0), 24% (v/v) PEG3350, 0.1 M lithium sulfate, 0.2 M magnesium sulfate and 10 mM dithiothreitol
hanging drop vapour diffusion method with 0.1 M HEPES-NaOH pH 7.5, 10% 2-propanol, 10 mM magnesium acetate and 20% (w/v) PEG 4000 at 18°C
-
hanging drop vapour diffusion method with 0.2 M MgCl2, 4.5% PEG 10000 (w/v) and 0.1 M HEPES (pH 7.5)
-
hanging drop vapour diffusion method with 1.5 M sodium chloride, 10% (v/v) ethanol, and 10 mM dithiothreitol
-
hanging drop vapour diffusion method with 18-22% PEG 8000, 200 mM MgCl2, 100 mM Tris-HCl pH 8.0, and 1% (v/v) beta-mercaptoethanol
in complex with inhibitors 3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethyl-N,N-dimethyl-1-benzofuran-6-sulfonamide, 3-((3,5-dibromo-4-hydroxyphenyl)carbonyl)-2-ethyl-N-(4-(1,3-thiazol-2-ylsulfamoyl)phenyl)-1-benzofuran-6-sulfonamide and 3-((3,5-dibromo-4-hydroxyphenyl)carbonyl)-2-ethyl-N-(4-sulfamoylphenyl)-1-benzofuran-6-sulfonamide
in complex with monophosphorylated and dually phosphorylated Erk2 peptides, sitting drop vapour diffusion method, in 0.2 M ammonium tartrate, pH 6.6, and 20% (w/v) PEG 3350 or and 1.0 M lithium chloride, 0.1 M citrate, pH 5.0, and 20% (w/v) PEG 6000
molecular dynamics simulations of the crystal structure of the enzyme catalytic domain and of mutant R47V/D48N/M258C/G259Q, both in complex with substrate 4-nitrophenyl phosphate and as cysteine-phosphor complex
phosphotyrosine phosphatase 1B
-
PTP1B and PTP1B mutant F182H in complex with inhibitors
purified recombinant detagged enzyme, hanging drop vapor diffusion method, mixing of 0.0018 ml of protein solution, containing 18 mg/ml protein in 20 mM HEPES-NaOH, pH 7.0, 0.2 M NaCl, 5 mM MgCl2, 20 mM DTT, and 5% glycerol, with an equal volume of reservoir solution containing 0.1 M bis-Tris, pH 6.0, and 2.4 M NaCl, 18°C, 3 days, X-ray diffraction structure determination and analysis at 2.4 A resolution
purified recombinant enzyme mutants D811A/C842S, D811E/C842S, D811A/H812F/C842S/M883G, Y676I, and D811E in complex with substrate Eps15846-854, and with mutant Eps15846-854 P450V, X-ray diffraction structure determination and analysis at 1.26-1.72 A resolution
purified recombinant wild-type and mutant isolated membrane-proximal D1 and distal D2 domains of protein tyrosine phosphatase epsilon, and PTPepsilon (A455N/V457Y/E597D) D2 domain mutant, hanging drop vapour diffusion method, for PTPepsilon D1 domain mixing of 0.002 ml of 13.9 mg/ml protein solution with 0.002 ml of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 0.2 M sodium chloride, and 22% w/v PEG 3350, for wild-type PTPepsilon D2 domain mixing of 0.001 ml of 5.0 mg/ml protein solution with 0.003 ml of reservoir solution containing 0.1 M bicine/trizma base, pH 8.5, 0.03 mM diethylene glycol, 0.03 M triethylene glycol, 0.03 M tetraethylene glycol, 0.03 M pentaethylene glycol, 10% w/v PEG 4000, and 20% v/v glycerol, and for mutant A455N/V457Y/E597D PTPepsilon D2 domain mixing of 0.002 ml of 9.0 mg/ml protein solution with 0.002 ml of reservoir solution containing 0.1 M imidazole, pH 8.0, 0.2 M calcium acetate hydrate, 20% w/v PEG 1000, in all cases equilibration against 0.5 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.67-2.27 A resolution
recombinant N-terminally His-tagged inactive enzyme mutant C227S, im complex with the consensus peptide substrate or SKAP-HOM, a bona fide Lyp substrate, 3-5 days, X-ray diffraction structure determmination and analysis at 2.5 A and 2.9 A resolution, respectively, molecular replacement
-
SHP-1, in the open, active conformation, hanging-drop vapor diffusion, 4°C, mixing of 0.0025 ml of protein solution, containing 3.6 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 0-1 M NaCl,2 mM 2-mercaptoethanol, 1 mM EDTA, with 0.0025 ml of reservoir solution, containing 1.8 M ammonium sulfate, 0.1 M glycine, 0.1 M Tris-HCl, pH 7.0, and additon of 0.5 ml 14 mM deoxy Big Chap detergent, X-ray diffraction crystal structure determination and analysis at 3.1 A resolution, molecular replacement
-
sitting drop vapour diffusion method using 25% PEG-3350, 0.2 M LiSO4, and 100 mM Bis-Tris, pH 5.5, or 0.15 M malic acid, pH 7.0, 20% PEG-3350 and 2.0 M (NH4)H2PO4, 0.1 M Tris/HCl, pH 8.5
-
two transition-state analogues, by sitting drop vapor diffusion method, 4°C, mixing of 0.002 ml of protein solution, containing native PTPB1, peptide DADEYL, and Na3VO4 in 10 mM Tris, pH 7.5, 25 mM NaCl, 0.2 mM EDTA, and 3 mM DTT, with 0.0005 ml of sucrose 30% v/v solution, and 0.003 ml of precipitant solution, containing 0.1 M HEPES, pH 7.5, 0.2 M magnesium acetate and 15-17% PEG 8000, 3 days, X-ray diffraction structure determination and analysis at 2.25-2.3 A resolution
wild type and C215D mutant, both are structurally identical
protein-ligand interaction analysis. The Cys26 thiol group can engage in a van-der-Waals interaction with Ser58. The reduction-induced conformational change in wild-type is likely triggered by loss of the Cys104/Cys243 disulfide bridge between the PGP core and cap domains
and structural study, modeling of chloride ion and glycerol into active site
in complex with phosphate
hanging drop vapour diffusion method with 20% PEG 10000, 0.1 M MES pH 6.5
-
hanging drop vapour diffusion method with 0.1M citrate (pH 5.5) and 20% PEG 3000
-
purified recombinant catalytic core of Siw14 (residues 116-281), hanging drop vapor diffusion, mixing of 0.002 ml of 15 mg/ml protein in 150 mM NaCl, and 20 mM Tris-HCl, pH 7.5, with 0.002 ml of well solution containing 0.7 M sodium citrate, and 50 mM 2-mercaptoethanol, 25°C, X-ray diffraction structure determination and analysis at 2.35-2.38 A resolution, model building
hanging drop vapour diffusion method, using a reservoir solution containing 30% (w/v) polyethylene glycol 4000, 0.2 M ammonium acetate, and 0.1 M Tris-HCl (pH 8.5)
native form and bound with a phosphate ion
-
isozyme PtpA with a peptide bound in the active site mimicking a phosphotyrosine substrate, X-ray diffraction structure determination and analysis at 1.0 A resolution
-
purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 20 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 200 mM NaCl, 5 mM 2-mercaptoethanol, and 2 mM dithiothreitol, with 0.001 ml of precipitant solution containing 150 mM potassium thiocyanate, 100 mM Bis-Tris, pH 6.25, 8% PEG 3350, and 2% D-sorbitol, 18°C, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement method using the structure of the YfkJ from Bacillus subtilis as a search model
structure of Wzb to 2.28 A resolution. Wzb has a classical a low molecular weight protein tyrosine phosphatase conformation
purified recombinant enzyme Tk-PTP(form I) Tk-PTP(form II) Tk-PTP(G95A), sitting-drop vapor diffusion method, for enzyme form I: mixing 0.001 ml of 10 mg/ml protein solution with 0.001 ml of precipitant solution containing 0.1 M sodium citrate, pH 5.4, 8% w/v PEG 10000, and 14% v/v dioxane, for enzyme form II: mixing of 0.001 ml of 10 mg/ml protein solution with 0.001 ml of precipitant solution containing 0.03 M citric acid, 0.07 M Bis-Tris propane, pH 7.6, 8% w/v PEG 3350, and 0.08 M spermine tetrahydrochloride, and for mutant Tk-PTP(G95A): mixing of 0.001 ml of 10 mg/ml protein solution with 0.001 ml of precipitant solution containing 0.1 M Bis-Tris, pH 6.25, and 0.8 M magnesium formate dehydrate, all at 18°C, X-ray diffraction structure determination and analysis at 1.7-2.3 A resolution, molecular replacement method, model building
determination of three-dimensional structure by nuclear magnetic resonance spectroscopy, S37 and Q67 are located in the active site
-
in complex with phenyl vinyl sulfonate or phenyl vinyl sulfone, hanging drop vapour diffusion method, using 25% (w/v) PEG3350, 100 mM NaCl, and 100 mM HEPES buffer (pH 7.0-8.0)
-