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
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3.1.3.48
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pp2a
-
mapks
-
autoimmune
-
erk
-
cyclin
-
leukemia
-
endothelial
-
ras
-
signal-regulated
-
lysosomal
-
okadaic
-
t-cells
-
metastasis
-
checkpoint
-
sirna
-
obesity
-
myeloid
-
3-kinase
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adaptor
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arthritis
-
vanadate
-
stat3
-
tumorigenesis
-
prostate
-
mellitus
-
phosphatidylinositol
-
cyclin-dependent
-
c-jun
-
pkc
-
rheumatoid
-
tyrosine-phosphorylated
-
hyperphosphorylation
-
nonreceptor
-
chk1
-
cytochemical
-
autophosphorylation
-
receptor-like
-
genistein
-
irs-1
-
insulin-stimulated
-
phosphopeptide
-
tartrate-resistant
-
grb2
-
c-src
-
jak2
-
fyn
-
paxillin
-
substrate-1
-
myelomonocytic
-
polo-like
-
medicine
-
pharmacology
-
diagnostics
-
drug development
- 3.1.3.48
- pp2a
- mapks
- autoimmune
- erk
- cyclin
- leukemia
- endothelial
- ras
-
signal-regulated
- lysosomal
-
okadaic
- t-cells
- metastasis
-
checkpoint
- sirna
- obesity
- myeloid
- 3-kinase
- adaptor
- arthritis
- vanadate
- stat3
- tumorigenesis
- prostate
- mellitus
- phosphatidylinositol
-
cyclin-dependent
- c-jun
- pkc
-
rheumatoid
-
tyrosine-phosphorylated
-
hyperphosphorylation
-
nonreceptor
- chk1
-
cytochemical
- autophosphorylation
-
receptor-like
- genistein
- irs-1
-
insulin-stimulated
- phosphopeptide
-
tartrate-resistant
- grb2
- c-src
- jak2
- fyn
- paxillin
- substrate-1
-
myelomonocytic
-
polo-like
- medicine
- pharmacology
- diagnostics
- drug development
Reaction
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
3.1.3.48 protein-tyrosine-phosphataseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.1.3.48 - protein-tyrosine-phosphatase
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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
-
-
-
-
?
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
-
-
?
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
-
dephosphorylates Cdk/cyclins on pThr14 and/or pTyr15 residues
-
-
?
difluoromethylumbelliferyl phosphate + H2O
difluoromethylumbelliferone + phosphate
-
-
-
?
ENPE(pY)LGLD + H2O
ENPEYLGLD + phosphate
dephosphorylation at Tyr1248
-
-
?
ENPE(pY)LTPQ + H2O
ENPEYLTPQ + phosphate
dephosphorylation at Tyr1196
-
-
?
epidermal growth factor receptor + H2O
? + phosphate
-
with phosphotyrosine Tyr992
-
-
?
FDNL(pY)2WDQD + H2O
FDNLYYWDQD + 2 phosphate
dephosphorylation at Tyr1221/1222
-
-
?
FMN + H2O
? + phosphate
-
71.8% of the activity with 4-nitrophenyl phosphate, lung enzyme
-
-
?
GESDGGpYMDMSKD + H2O
GESDGGYMDMSKD + phosphate
-
this peptide corresponds to the sequence containing Tyr740 of the human platelet-derived growth factor receptor
-
-
?
H2O + O-phospho-L-tyrosyl-[Wzc]
L-tyrosyl-[Wzc] + phosphate
Wzb dephosphorylates protein tyrosine kinase Wzc
-
-
?
hirudin + H2O
? + phosphate
-
hirudin from leech, phosphorylated on tyrosine
-
-
?
KRLIEDNE(pY)TARGQ + H2O
KRLIEDNEYTARGQ + phosphate
-
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
-
dephosphorylation 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 bovine serum albumin + H2O
tyrosyl-bovine serum albumin + phosphate
-
-
-
-
?
phosphotyrosyl myelin basic protein + H2O
tyrosyl-myelin basic protein + phosphate
-
-
-
-
?
phosphotyrosyl reduced carboxyamidomethylated and maleylated lysozyme + H2O
tyrosyl-reduced carboxyamidomethylated and maleylated lysozyme + phosphate
-
-
-
-
?
PLQR(pY)SEDP + H2O
PLQRYSEDP + phosphate
dephosphorylation at Tyr1112
-
-
?
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
-
-
?
[casein]-tyrosine phosphate + H2O
[casein]-tyrosine + phosphate
-
-
-
?
[cytosolic 6-phosphofructokinase]-tyrosine phosphate + H2O
[cytosolic 6-phosphofructokinase]-tyrosine + phosphate
[diguanylate cyclase TpbB]-tyrosine phosphate + H2O
[diguanylate cyclase TpbB]-tyrosine + phosphate
[EGF receptor]-tyrosine1018 phosphate + H2O
[EGF receptor]-tyrosine1018 + phosphate
highest activity
-
-
?
[epidermal growth factor receptor 2]-tyrosine phosphate + H2O
[epidermal growth factor receptor 2]-tyrosine + phosphate
dephosphorylation of epidermal growth factor receptor 2 (HER2)-pY1196 site
-
-
?
[epidermal growth factor receptor]-tyrosine phosphate + H2O
[epidermal growth factor receptor]-tyrosine + phosphate
[Eps15 peptide846-854 P850V]-tyrosine phosphate + H2O
[Eps15 peptide846-854 P850V]-tyrosine + phosphate
-
-
-
?
[Eps15 peptide846-854]-tyrosine phosphate + H2O
[Eps15 peptide846-854]-tyrosine + phosphate
[FAK]-tyrosine phosphate + H2O
[FAK]-tyrosine + phosphate
dephosphorylation at Tyr397
-
-
?
[FYN kinase]-tyrosine phosphate + H2O
[FYN kinase]-tyrosine + phosphate
-
-
-
?
[HER2]-tyrosine phosphate + H2O
[HER2]-tyrosine + phosphate
dephosphorylation at Tyr1112, Tyr1196, Tyr1221, Tyr1222, and Tyr1248
-
-
?
[insulin receptor kinase]-tyrosine phosphate + H2O
[insulin receptor kinase]-tyrosine + phosphate
-
-
-
?
[myelin basic protein]-tyrosine phosphate + H2O
[myelin basic protein]-tyrosine + phosphate
-
-
-
?
[p130Cas]-tyrosine phosphate + H2O
[p130Cas]-tyrosine + phosphate
dephosphorylation at Tyr165
-
-
?
[p190RhoGAP]-tyrosine phosphate + H2O
[p190RhoGAP]-tyrosine + phosphate
dephosphorylation at Tyr1105
-
-
?
[paxillin]-tyrosine phosphate + H2O
[paxillin]-tyrosine + phosphate
dephosphorylation at Tyr118
-
-
?
[SRC]-tyrosine phosphate + H2O
[SRC]-tyrosine + phosphate
dephosphorylation at Tyr416
-
-
?
[sulfide quinone oxidoreductase]-tyrosine phosphate + H2O
[sulfide quinone oxidoreductase]-tyrosine + phosphate
[trifunctional enzyme]-tyrosine phosphate + H2O
[trifunctional enzyme]-tyrosine + phosphate
[VAV2]-tyrosine phosphate + H2O
[VAV2]-tyrosine + phosphate
dephosphorylation at Tyr172
-
-
?
[Wzb]-tyrosine phosphate + H2O
[Wzb]-tyrosine + phosphate
Wzb i.e. bacterial tyrosine kinase
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
89.3% of the activity with 4-nitrophenyl phosphate, lung enzyme
-
-
?
3-o-methyl fluorescein phosphate + H2O
3-o-methyl fluorescein + phosphate
-
-
-
?
3-o-methyl fluorescein phosphate + H2O
3-o-methyl fluorescein + phosphate
-
-
-
?
3-o-methyl fluorescein phosphate + H2O
3-o-methyl fluorescein + 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
-
-
663621, 665502, 692217, 693943, 694291, 694608, 694902, 707683, 708290, 709293, 710237, 714433, 729298, 729368, 729393, 730564, 730970
-
-
?
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
-
acid phosphatase activity, best tested substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Streptococcus pneumoniae D39 NCTC 7466
-
-
-
?
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
-
-
-
-
?
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-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
-
-
-
?
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
-
-
?
DADE(pY)LIPQQG + H2O
DADEYLIPQQG + phosphate
a physiological phosphopeptide substrate of enzyme PTP1B
-
-
?
DADE(pY)LIPQQG + H2O
DADEYLIPQQG + phosphate
a phosphopeptide substrate of enzyme PTP1B and the modified enzyme asPTP1B. asPTP1B dephosphorylates DADE(pY)LIPQQG at a rate that is only slightly lower than the rate of dephosphorylation induced by wild-type PTP1B
-
-
?
DADE(pY)LIPQQG + H2O
DADEYLIPQQG + phosphate
sequence equivalent to residues 988-998 of the epidermal growth factor receptor
-
-
?
DADE(pY)LIPQQG + H2O
DADEYLIPQQG + phosphate
phosphopeptide-2
-
-
?
DADE(pY)LIPQQG + H2O
DADEYLIPQQG + phosphate
Streptococcus pneumoniae D39 NCTC 7466
phosphopeptide-2
-
-
?
DADEpYIPQQG + H2O
DADEYIPQQG + phosphate
-
specific substrate for PTP1B
-
-
?
DADEpYLIPQQG + H2O
DADEYLIPQQG + phosphate
a phosphopeptide substrate
-
-
?
END(pY)INASL + H2O
ENDYINASL + phosphate
phosphopeptide-1
-
-
?
END(pY)INASL + H2O
ENDYINASL + phosphate
Streptococcus pneumoniae D39 NCTC 7466
phosphopeptide-1
-
-
?
insulin receptor phosphopeptide + H2O
insulin receptor peptide + phosphate
-
-
-
-
?
insulin receptor phosphopeptide + H2O
insulin receptor peptide + phosphate
-
-
-
-
?
O-phospho-L-tyrosine + H2O
tyrosine + phosphate
-
-
-
?
O-phospho-L-tyrosyl-[PTK1] + H2O
L-tyrosyl-[PTK1] + phosphate
-
-
-
?
O-phospho-L-tyrosyl-[PTK1] + H2O
L-tyrosyl-[PTK1] + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
60.3% activity compared to TRDIpYETDYYRK
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
60.3% activity compared to TRDIpYETDYYRK
-
-
?
paxilin tyrosine phosphate + H2O
paxilin tyrosine + phosphate
-
PTPRT specifically regulates paxillin phosphorylation at Tyr88 in colorectal cancer cells
-
-
?
paxilin tyrosine phosphate + H2O
paxilin tyrosine + phosphate
-
substrate of PTPRT, inactive with paxilin mutant Y88F
-
-
?
phosphorylated AMP-activated protein kinase + H2O
AMP-activated protein kinase + phosphate
-
PTPB1 is involved in AMPK regulation through its phosphorylation in a tissue-specific manner, overview
-
-
?
phosphorylated AMP-activated protein kinase + H2O
AMP-activated protein kinase + phosphate
-
phosphorylation of the AMPK alpha subunit at Thr172
-
-
?
phosphorylated c-MET + H2O
c-MET + phosphate
-
PTP1B and SHP-2 are bound to the c-Met receptor to control its activity, PTP1B acts as a negative regulator, increased binding and phosphorylation of SHP-2 coincide with maximal stimulation of c-Met, therefore acting as a positive regulator
-
-
?
phosphorylated c-MET + H2O
c-MET + phosphate
-
PTP1B and SHP-2 are bound to the c-Met receptor to control its activity, PTP1B acts as a negative regulator, increased binding and phosphorylation of SHP-2 coincide with maximal stimulation of c-Met, therefore acting as a positive regulator
-
-
?
phosphorylated c-Src + H2O
c-Src + phosphate
-
dephosphorylation activates c-Src
-
-
?
phosphorylated c-Src + H2O
c-Src + phosphate
-
dephosphorylation occurs at Tyr-527
-
-
?
phosphorylated epidermal growth factor receptor + H2O
epidermal growth factor receptor + phosphate
-
-
-
-
?
phosphorylated epidermal growth factor receptor + H2O
epidermal growth factor receptor + phosphate
-
-
preferential dephosphorylation at Y1068 and Y1173
-
?
phosphorylated epidermal growth factor receptor + H2O
epidermal growth factor receptor + phosphate
-
PTP1B negatively regulates EGF-induced signaling in HCEC cells by dephosphorylating the epidermal growth factor receptor
-
-
?
phosphorylated epidermal growth factor receptor + H2O
epidermal growth factor receptor + phosphate
-
inactivation of EGFR
-
-
?
phosphorylated epidermal growth factor receptor + H2O
epidermal growth factor receptor + phosphate
-
-
-
-
?
phosphorylated ERK + H2O
ERK + phosphate
-
the cleavage of STEP leads to a catalytically active form, but this cleaved form no longer binds to and dephosphorylates its substrate phosphorylated ERK
-
-
?
phosphorylated extracellular signal-regulated kinase 1 + H2O
extracellular signal-regulated kinase 1 + 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 extracellular signal-regulated kinase 2 + H2O
extracellular signal-regulated kinase 2 + phosphate
-
-
-
-
?
phosphorylated insulin receptor + H2O
insulin receptor + phosphate
-
-
-
?
phosphorylated insulin receptor + H2O
insulin receptor + phosphate
-
-
preferential dephosphorylation of Y1162/1163 of insulin receptor
-
?
phosphorylated mitogen-activated protein kinase Pmk1p + H2O
mitogen-activated protein kinase Pmk1p + phosphate
-
-
-
-
?
phosphorylated mitogen-activated protein kinase Pmk1p + H2O
mitogen-activated protein kinase Pmk1p + phosphate
-
-
-
-
?
phosphorylated p38 mitogen-activated protein kinase + H2O
p38 mitogen-activated protein kinase + phosphate
-
-
-
-
?
phosphorylated p38 mitogen-activated protein kinase + H2O
p38 mitogen-activated protein kinase + phosphate
-
-
-
?
phosphorylated phospholipase Cgamma + H2O
phospholipase Cgamma + phosphate
-
dephosphorylation occurs at Tyr-783
-
-
?
phosphorylated phospholipase Cgamma + H2O
phospholipase Cgamma + phosphate
-
dephosphorylation occurs at Tyr-783
-
-
?
phosphorylated Src + H2O
Src + phosphate
-
DEP-1 is able to dephosphorylate the inhibitory Y529 and activate Src
-
-
?
phosphorylated STAT1 + H2O
STAT1 + phosphate
-
purified GST-SHP2 dephosphorylates STAT1 at both tyrosine and serine residues when immunoprecipitated phosphorylated STAT1 or phosphor-peptides corresponding to the sequence surrounding Tyr701 or Ser727 of STAT1 are used as the substrates, SHP2 negatively regulates the interferon-induced JAK/STAT pathway by dephosphorylating STAT1
-
-
?
phosphorylated STAT1c + H2O
STAT1c + phosphate
-
mode of STAT activation, whereby serine-threonine phosphorylation of the cognate protein tyrosine phosphatase PTP3 results in the inhibition of its activity, shifting the phosphorylation-dephosphorylation equilibrium in favour of phosphorylation, overview
-
-
?
phosphorylated STAT3 + H2O
STAT3 + phosphate
-
SHP2 negatively regulates the activity of STAT3
-
-
?
phosphorylated vascular endothelial growth factor receptor 2 + H2O
vascular endothelial growth factor receptor 2 + phosphate
-
-
-
-
?
phosphorylated vascular endothelial growth factor receptor 2 + H2O
vascular endothelial growth factor receptor 2 + phosphate
-
dephosphorylation occurs at Tyr-1175, PTP1B binds to vascular endothelial growth factor receptor 2 cytoplasmic domain and directly dephosphorylates activated vascular endothelial growth factor receptor 2 immunoprecipitates
-
-
?
phosphotyrosine + H2O
tyrosine + phosphate
-
45.2% of the activity with 4-nitrophenyl phosphate, lung enzyme
-
-
?
phosphotyrosine + H2O
tyrosine + phosphate
O14522, P10586, P17706, P18031, P18433, P23467, P23468, P23469, P23470, P23471, P26045, P28827, P29074, P29350, P35236, P43378, P54829, Q05209, Q06124, Q0VAE8, Q12913, Q12923, Q13332, Q15256, Q15262, Q15678, Q16825, Q16827, Q16849, Q4JDK3, Q92729, Q92932, Q99952, Q9H3S7, Q9HD43, Q9UMZ3, Q9Y2R2
-
-
-
?
phosphotyrosyl-STAT3 + H2O
STAT3 + phosphate
-
signal transducers and activator of transcription 3, STAT3, is a transcription factor that is associated with survival, proliferation, chemoresistance, and angiogenesis of tumor cells
-
-
?
platelet-derived growth factor receptor + H2O
? + phosphate
-
with phosphotyrosine Tyr1021 or Tyr1009
-
-
?
TEVGKRI(pY)RLVGDKN + H2O
TEVGKRIYRLVGDKN + phosphate
-
-
-
?
TEVGKRI(pY)RLVGDKN + H2O
TEVGKRIYRLVGDKN + phosphate
-
-
-
?
TRDIpYETDYYRK + H2O
TRDIYETDYYRK + phosphate
-
100% activity
-
-
?
TSTEPQpYQPGENL + H2O
TSTEPQYQPGENL + phosphate
-
this sequence contains the C-terminal phosphorylation site of c-src with phosphorylated Tyr527
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
Leishmania major MHOM/IL/81/FEBNI
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
Streptococcus pneumoniae D39 NCTC 7466
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
-
?
[ATP synthase]-tyrosine phosphate + H2O
[ATP synthase]-tyrosine + phosphate
-
-
-
?
[ATP synthase]-tyrosine phosphate + H2O
[ATP synthase]-tyrosine + phosphate
-
-
-
?
[ATP synthase]-tyrosine phosphate + H2O
[ATP synthase]-tyrosine + phosphate
-
-
-
?
[cytosolic 6-phosphofructokinase]-tyrosine phosphate + H2O
[cytosolic 6-phosphofructokinase]-tyrosine + phosphate
-
-
-
?
[cytosolic 6-phosphofructokinase]-tyrosine phosphate + H2O
[cytosolic 6-phosphofructokinase]-tyrosine + phosphate
-
-
-
?
[cytosolic 6-phosphofructokinase]-tyrosine phosphate + H2O
[cytosolic 6-phosphofructokinase]-tyrosine + phosphate
-
-
-
?
[diguanylate cyclase TpbB]-tyrosine phosphate + H2O
[diguanylate cyclase TpbB]-tyrosine + phosphate
the substrate is involved in motility, biofilm formation
-
-
?
[diguanylate cyclase TpbB]-tyrosine phosphate + H2O
[diguanylate cyclase TpbB]-tyrosine + phosphate
the substrate is involved in motility, biofilm formation
-
-
?
[diguanylate cyclase TpbB]-tyrosine phosphate + H2O
[diguanylate cyclase TpbB]-tyrosine + phosphate
the substrate is involved in motility, biofilm formation
-
-
?
[diguanylate cyclase TpbB]-tyrosine phosphate + H2O
[diguanylate cyclase TpbB]-tyrosine + phosphate
the substrate is involved in motility, biofilm formation
-
-
?
[diguanylate cyclase TpbB]-tyrosine phosphate + H2O
[diguanylate cyclase TpbB]-tyrosine + phosphate
the substrate is involved in motility, biofilm formation
-
-
?
[diguanylate cyclase TpbB]-tyrosine phosphate + H2O
[diguanylate cyclase TpbB]-tyrosine + phosphate
the substrate is involved in motility, biofilm formation
-
-
?
[diguanylate cyclase TpbB]-tyrosine phosphate + H2O
[diguanylate cyclase TpbB]-tyrosine + phosphate
the substrate is involved in motility, biofilm formation
-
-
?
[diguanylate cyclase TpbB]-tyrosine phosphate + H2O
[diguanylate cyclase TpbB]-tyrosine + phosphate
the substrate is involved in motility, biofilm formation
-
-
?
[epidermal growth factor receptor]-tyrosine phosphate + H2O
[epidermal growth factor receptor]-tyrosine + phosphate
-
-
-
?
[epidermal growth factor receptor]-tyrosine phosphate + H2O
[epidermal growth factor receptor]-tyrosine + phosphate
-
-
-
?
[epidermal growth factor receptor]-tyrosine phosphate + H2O
[epidermal growth factor receptor]-tyrosine + phosphate
enzyme SP-PTP dephosphorylates the activated EGFR (170 kDa protein migrating at about 240 kDa) present in MDA-MB-231 cell lines
-
-
?
[epidermal growth factor receptor]-tyrosine phosphate + H2O
[epidermal growth factor receptor]-tyrosine + phosphate
-
-
-
?
[epidermal growth factor receptor]-tyrosine phosphate + H2O
[epidermal growth factor receptor]-tyrosine + phosphate
-
-
-
?
[Eps15 peptide846-854]-tyrosine phosphate + H2O
[Eps15 peptide846-854]-tyrosine + phosphate
-
-
-
?
[Eps15 peptide846-854]-tyrosine phosphate + H2O
[Eps15 peptide846-854]-tyrosine + phosphate
active with enzyme mutant F182H, wild-type shows poor activity
-
-
?
[Eps15 peptide]-tyrosine phosphate + H2O
[Eps15 peptide]-tyrosine + phosphate
substrate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for enzyme PTPN3
-
-
?
[Eps15 peptide]-tyrosine phosphate + H2O
[Eps15 peptide]-tyrosine + phosphate
substrate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for enzyme PTPN3
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[Eps15 peptide]-tyrosine phosphate + H2O
[Eps15 peptide]-tyrosine + phosphate
substrate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for enzyme PTPN3. 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. Critical role of the additional residue Tyr676 of PTPN3. The atypical binding conformation of Eps15 is mediated by its pTyr-Pro motif
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[FHA-1]-tyrosine phosphate + H2O
[FHA-1]-tyrosine + phosphate
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[FHA-1]-tyrosine phosphate + H2O
[FHA-1]-tyrosine + phosphate
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[FHA-1]-tyrosine phosphate + H2O
[FHA-1]-tyrosine + phosphate
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[FHA-1]-tyrosine phosphate + H2O
[FHA-1]-tyrosine + phosphate
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[FHA-1]-tyrosine phosphate + H2O
[FHA-1]-tyrosine + phosphate
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[FHA-1]-tyrosine phosphate + H2O
[FHA-1]-tyrosine + phosphate
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[FHA-1]-tyrosine phosphate + H2O
[FHA-1]-tyrosine + phosphate
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[FHA-1]-tyrosine phosphate + H2O
[FHA-1]-tyrosine + phosphate
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[protein Golgi p230]-tyrosine phosphate + H2O
[protein Golgi p230]-tyrosine + phosphate
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[protein Golgi p230]-tyrosine phosphate + H2O
[protein Golgi p230]-tyrosine + phosphate
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[protein]-L-tyrosine phosphate + H2O
[protein]-L-tyrosine + phosphate
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[protein]-L-tyrosine phosphate + H2O
[protein]-L-tyrosine + phosphate
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[protein]-tyrosine phosphate + H2O
[protein]-tyrosine + phosphate
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[protein]-tyrosine phosphate + H2O
[protein]-tyrosine + phosphate
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[protein]-tyrosine phosphate + H2O
[protein]-tyrosine + phosphate
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[protein]-tyrosine phosphate + H2O
[protein]-tyrosine + phosphate
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[protein]-tyrosine phosphate + H2O
[protein]-tyrosine + phosphate
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[protein]-tyrosine phosphate + H2O
[protein]-tyrosine + phosphate
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[protein]-tyrosine phosphate + H2O
[protein]-tyrosine + phosphate
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[protein]-tyrosine phosphate + H2O
[protein]-tyrosine + phosphate
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[sulfide quinone oxidoreductase]-tyrosine phosphate + H2O
[sulfide quinone oxidoreductase]-tyrosine + phosphate
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[sulfide quinone oxidoreductase]-tyrosine phosphate + H2O
[sulfide quinone oxidoreductase]-tyrosine + phosphate
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[sulfide quinone oxidoreductase]-tyrosine phosphate + H2O
[sulfide quinone oxidoreductase]-tyrosine + phosphate
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[trifunctional enzyme]-tyrosine phosphate + H2O
[trifunctional enzyme]-tyrosine + phosphate
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[trifunctional enzyme]-tyrosine phosphate + H2O
[trifunctional enzyme]-tyrosine + phosphate
also dephosphorylates the human trifunctional enzyme
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[trifunctional enzyme]-tyrosine phosphate + H2O
[trifunctional enzyme]-tyrosine + phosphate
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[trifunctional enzyme]-tyrosine phosphate + H2O
[trifunctional enzyme]-tyrosine + phosphate
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additional information
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PTP is an element of the abscisic acid signaling pathway that leads to stomatal closure
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additional information
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no substrate: phosphoeptides RRA(pS)VA, KR(pT)IRR
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additional information
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the enzyme does not display catalytic activity against some common protein tyrosine phosphatase substrates (O-nitrophenyl beta-D-galactopyranoside, O-phospho-L-threonine, D-fructose 6-phosphate, D-ribose 5-phosphate, D-glucose 6-phosphate, D-glucose 1-phosphate) but is highly specific for hydrolysis of phosphomonoester bonds of inositol hexakisphosphate
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additional information
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the enzyme does not display catalytic activity against some common protein tyrosine phosphatase substrates (O-nitrophenyl beta-D-galactopyranoside, O-phospho-L-threonine, D-fructose 6-phosphate, D-ribose 5-phosphate, D-glucose 6-phosphate, D-glucose 1-phosphate) but is highly specific for hydrolysis of phosphomonoester bonds of inositol hexakisphosphate
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additional information
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the enzyme does not display catalytic activity against some common protein tyrosine phosphatase substrates (O-nitrophenyl beta-D-galactopyranoside, O-phospho-L-threonine, D-fructose 6-phosphate, D-ribose 5-phosphate, D-glucose 6-phosphate, D-glucose 1-phosphate) but is highly specific for hydrolysis of phosphomonoester bonds of inositol hexakisphosphate
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additional information
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Bracoviriform demolitoris
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PTP-H2 functions as an inhibitor of phagocytosis, PTP-H2 mediates cell death of infected Sf-21 cells, expression of PTP-H2 triggers mitochondrial membrane depolarisation and caspase-dependent apoptosis
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additional information
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Bracoviriform demolitoris
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no activity with DADEpYLIPQQG, poor activity with 4-nitrophenyl phosphate
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additional information
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STATc becomes tyrosine phosphorylated and accumulates in the nucleus when Dictyostelium cells are exposed to the prestalk cell inducer Differentiation inducing factor 1, DIF-1, or are subjected to hyperosmotic stress
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additional information
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the enzyme is a dual-specificity Ser/Thr/Tyr phosphatase also exhibiting the activity of EC 3.1.3.16
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additional information
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no hydrolysis of serine phosphate, threonine phosphate, nicotinamide adenine dinucleotide phosphate
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additional information
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kinetic constants for several peptide substrates
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additional information
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study on substrate specificity, screen of peptide substrate library
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additional information
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PTPases regulate the ligand-induced autophosphorylation of PTK growth factor receptors, the phosphotyrosine-mediated binding s of src homology 2 (SH2)-domain-containing proteins to autophosphorylated PTK growth factor receptors and the activation state of the src family pf PTK
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additional information
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LMW-PTP is involved in the negative regulation of the mitogenic stimulus starting from the activated PDGF receptor. The interaction between LMW-PTP results in the dephosphorylation of the PDGF-R phosphortyrosine and a negative regulation of the mitogenic signal
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additional information
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regulation of the function of epidermal growth factor receptor in keratinocytes by its dephosphorylation
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additional information
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SHP-1 may regulate the tethering of receptors to the cytoskeleton and/or the extent of cross-linking of actin filaments in platelets
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additional information
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Cdc25 phosphatases prefer a bisanionic over a monoanionic substrate
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additional information
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activation of SPH-1 and SPH-2 is accompanied by reduced responsiveness to aggregating agents, phosphorylation of SPH-1 and SPH-2 introduces docking sites for adaptor molecules like growth factor receptor-bound protein 2 regulating further signaling to integrin alphaIIbbeta3
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additional information
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by modulating Src-focal adhesion kinase signaling at adhesion sites, PTPD1 promotes the cytoskeleton events that induce cell adhesion and migration
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additional information
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functional inactivation of the protein tyrosine phosphatase DEP-1 leads to increased endothelial cell proliferation and failure of vessels to remodel and branch
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additional information
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human LMW-PTP is critical in the regulation of mitogenic signalling and Rho-mediated cytoskeletal rearrangements after platelet derived growth factor stimulation
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additional information
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SHP-2, MKP-1, LAR, and PTEN are targets of platelet-derived growth factor-induced reversible oxidation
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additional information
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DEP-1 is a positive regulator of VEGF-mediated Src and Akt activation and endothelial cell survival
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additional information
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ED-Eya2 is bifunctional acting as protein tyrosine phosphatase and as transcription factor. The transcriptional activity of Eya proteins is regulated by a dephosphorylating activity within its Eya domain, structure-function analysis, overview
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additional information
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ED-Eya2 is bifunctional acting as protein tyrosine phosphatase and as transcription factor. The transcriptional activity of Eya proteins is regulated by a dephosphorylating activity within its Eya domain, structure-function analysis, overview
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additional information
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isozyme p52shc associates with the growth factor receptor-bound protein-2, Grb2. Overexpression of isozyme p66shc impaires IGF-I-stimulated p52shc tyrosine phosphorylation and p52shc-Grb2 association. Isozyme p66shc inhibits IGF-I signal transduction via competitively inhibiting the binding of Src homology 2 domain-containing SHP-2 to SHP substrate-1, leading to the disruption of SHPS-1/SHP-2/Src/p52shc complex formation, an event that is essential for p52shc phosphorylation and Grb2 recruitment, overview. p66shc inhibits IGF-I signal transduction via impairing membrane recruitment of Grb2
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additional information
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protein tyrosine phosphatase 1B, PTP1B, is an intracellular non-receptor type PTP
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additional information
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formation and structure of a transition state analogue for the first catalytic step comprising a ternary complex between the catalytic cysteine of PTP1B, vanadate, and the peptide DADEYL, a fragment of a physiological substrate, overview. The equatorial vanadate oxygen atoms bind to the P-loop, and the apical positions are occupied by the peptide tyrosine oxygen and by the PTP1B cysteine sulfur atom. The vanadate assumes a trigonal bipyramidal geometry in both transition state analogue structures, with very similar apical O-O distances, denoting similar transition states for both phosphoryl transfer steps
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additional information
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PTEN phosphoprotein phosphatase catalysis of phosphoprotein dephosphorylation follows a two-step mechanism with Cys124 transiently phosphorylated to form the phosphoenzyme intermediate
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additional information
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Ser380, Thr382 and Thr383 C-terminal tail residues do not affect the recruitment of the WPD-loop into the active site to participate in the phosphoprotein dephosphorylation reaction, catalytic mechanism of PTEN phosphoprotein phosphatase activity, overview. The phosphoPTEN protein is not the cysteinyl phosphoenzyme intermediate formed by transient phosphorylation of Cys124 in the course of phosphopeptide dephosphorylation reaction. PTEN can adopt the closed conformation to allow Asp92 to participate in catalysis when it dephosphorylates the physiological protein substrates such as FAK and Shc in cells
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additional information
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substrate specificity analysis using a trapping mutant of the phosphatase, which is a point mutation that maintains specificity but does not allow detachment of the phosphate, overview. The enzyme is also active on 4-nitrophenyl phosphate, but is not active on GRB2
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additional information
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substrate specificity of lymphoid-specific tyrosine phosphatase, identification of consensus sequence motifs for Lyp substrate recognition using an inverse alanine scanning combinatorial library approach, molecular determinants and molecular basis for Lyp substrate recognition, crystal structure analysis, overview
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additional information
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the PTP1B catalytic domain has modest preference for acidic residues on both sides of phosphotyrosine, is highly active toward multiply phosphorylated peptides, but disfavors basic residues at any position, a Gly at the phosphotyrosine-1 position, or a Pro at the pY-/-1 position. By contrast, SHP-1 and SHP-2 share similar but much narrower substrate specificities, with a strong preference for acidic and aromatic hydrophobic amino acids on both sides of the phosphotyrosine residue. An efficient SHP-1/2 substrate generally contains two or more acidic residues on the N-terminal side and one or more acidic residues on the C-terminal side of pY but no basic residues, substrate specificities of the protein tyrosine phosphatases PTP1B, RPTPalpha, SHP-1, and SHP-2, and reported PTP1B, SHP-1, and SHP-2 substrates and their dephosphorylation sites, overview. The catalytic domain of RPTPalpha has very weak sequence specificity and is approximately 2 orders of magnitude less active than the other three enzyme variants
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additional information
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PTP1B exhibits higher affinity (about 70fold) for tandem phosphotyrosine-containing peptides compared with mono-phosphotyrosine derivatives
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additional information
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activity detection by malachite green phosphatase method for phosphate determination
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additional information
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activity detection by malachite green phosphatase method for phosphate determination
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additional information
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development and optimization of non-radiometric immunoassays for the efficient detection of IA-2 autoantibodies (IA-2A)
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additional information
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human protein VHR is a dual specificity protein phosphatase 3, that also exhibits serine/threonine phosphatase activity, EC 3.1.3.16
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additional information
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human protein VHR is a dual specificity protein phosphatase 3, that also exhibits serine/threonine phosphatase activity, EC 3.1.3.16
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additional information
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human protein VHR is a dual specificity protein phosphatase 3, that also exhibits serine/threonine phosphatase activity, EC 3.1.3.16
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additional information
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PTP1B is a classical PTP with a deep active site pocket suited for phosphotyrosine, that also efficiently hydrolyzes other phosphorylated phenols
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additional information
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PTP1B is a classical PTP with a deep active site pocket suited for phosphotyrosine, that also efficiently hydrolyzes other phosphorylated phenols
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additional information
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PTP1B is a classical PTP with a deep active site pocket suited for phosphotyrosine, that also efficiently hydrolyzes other phosphorylated phenols
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additional information
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receptor protein tyrosine phosphatase isoform delta (PTPRdelta) displays substrate promiscuity by hydrolyzing the diester bond while showing a high-level of discrimination in its primary monoesterase substrate preference. The phosphatase domain of receptor protein tyrosine phosphatases catalyzes the hydrolysis of glycosidic (COC) bonds apart from its primary activity of cleaving phosphomonoester (COP) bond. This is important because the hydrolysis of COC bond in beta-galactosides and COP bond in phosphomonoesters require different functional groups and different mechanism of cleavage. No activity with adenosine monophosphate, inosine monophosphate, guanosine monophosphate, nicotinamide adenine dinucleotide phosphate, and pyridoxal 5'-phosphate, also no activity with tris-(4-nitrophenyl) phosphate, tris-(4-nitrobenzyl) phosphate, tetrakis-(4-nitrophenyl) diphosphate, NADP+, and peptide H-Gly-PNA. The enzyme shows low activity with several nitrophenyl glycosides cleaving the glycosidic bond. Substrate specificity, overview. No phosphocysteinyl hydrolysis of isozyme PTPRdelta
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additional information
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receptor protein tyrosine phosphatase isoform delta (PTPRdelta) displays substrate promiscuity by hydrolyzing the diester bond while showing a high-level of discrimination in its primary monoesterase substrate preference. The phosphatase domain of receptor protein tyrosine phosphatases catalyzes the hydrolysis of glycosidic (COC) bonds apart from its primary activity of cleaving phosphomonoester (COP) bond. This is important because the hydrolysis of COC bond in beta-galactosides and COP bond in phosphomonoesters require different functional groups and different mechanism of cleavage. No activity with adenosine monophosphate, inosine monophosphate, guanosine monophosphate, nicotinamide adenine dinucleotide phosphate, and pyridoxal 5'-phosphate, also no activity with tris-(4-nitrophenyl) phosphate, tris-(4-nitrobenzyl) phosphate, tetrakis-(4-nitrophenyl) diphosphate, NADP+, and peptide H-Gly-PNA. The enzyme shows low activity with several nitrophenyl glycosides cleaving the glycosidic bond. Substrate specificity, overview. No phosphocysteinyl hydrolysis of isozyme PTPRdelta
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additional information
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receptor protein tyrosine phosphatase isoform delta (PTPRdelta) shows catalytic and substrate promiscuity. The phosphatase domain of receptor protein tyrosine phosphatases catalyzes the hydrolysis of glycosidic (COC) bonds apart from its primary activity of cleaving phosphomonoester (COP) bond. This is important because the hydrolysis of COC bond in beta-galactosides and COP bond in phosphomonoesters require different functional groups and different mechanism of cleavage. No activity with adenosine monophosphate, inosine monophosphate, guanosine monophosphate, nicotinamide adenine dinucleotide phosphate, and pyridoxal 5'-phosphate, also no activity with tris-(4-nitrophenyl) phosphate, tris-(4-nitrobenzyl) phosphate, tetrakis-(4-nitrophenyl) diphosphate, NADP+, and peptide H-Gly-PNA. The enzyme shows low activity with several nitrophenyl glycosides cleaving the glycosidic bond. Substrate specificity, overview. Isozyme PD-PTPRomega shows rate-limiting phosphocysteinyl hydrolysis leading to a biphasic time-dependence of substrate to product conversion
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additional information
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receptor protein tyrosine phosphatase isoform delta (PTPRdelta) shows catalytic and substrate promiscuity. The phosphatase domain of receptor protein tyrosine phosphatases catalyzes the hydrolysis of glycosidic (COC) bonds apart from its primary activity of cleaving phosphomonoester (COP) bond. This is important because the hydrolysis of COC bond in beta-galactosides and COP bond in phosphomonoesters require different functional groups and different mechanism of cleavage. No activity with adenosine monophosphate, inosine monophosphate, guanosine monophosphate, nicotinamide adenine dinucleotide phosphate, and pyridoxal 5'-phosphate, also no activity with tris-(4-nitrophenyl) phosphate, tris-(4-nitrobenzyl) phosphate, tetrakis-(4-nitrophenyl) diphosphate, NADP+, and peptide H-Gly-PNA. The enzyme shows low activity with several nitrophenyl glycosides cleaving the glycosidic bond. Substrate specificity, overview. Isozyme PD-PTPRomega shows rate-limiting phosphocysteinyl hydrolysis leading to a biphasic time-dependence of substrate to product conversion
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. 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. Enzyme PTPN21 shows no activity with 4-nitrophenyl phosphate or Eps15846-854 peptide as substrate in the phosphatase activity assay. Once the glutamic acid in the WPE loop is replaced by an aspartic acid, the E1067D mutant form of PTPN21PTP exhibits a significantly higher level of phosphatase activity compared with its wild-type counterpart
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. 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. Enzyme PTPN21 shows no activity with 4-nitrophenyl phosphate or Eps15846-854 peptide as substrate in the phosphatase activity assay. Once the glutamic acid in the WPE loop is replaced by an aspartic acid, the E1067D mutant form of PTPN21PTP exhibits a significantly higher level of phosphatase activity compared with its wild-type counterpart
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. 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. Enzyme PTPN21 shows no activity with 4-nitrophenyl phosphate or Eps15846-854 peptide as substrate in the phosphatase activity assay. Once the glutamic acid in the WPE loop is replaced by an aspartic acid, the E1067D mutant form of PTPN21PTP exhibits a significantly higher level of phosphatase activity compared with its wild-type counterpart
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. 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. Enzyme PTPN21 shows no activity with 4-nitrophenyl phosphate or Eps15846-854 peptide as substrate in the phosphatase activity assay. Once the glutamic acid in the WPE loop is replaced by an aspartic acid, the E1067D mutant form of PTPN21PTP exhibits a significantly higher level of phosphatase activity compared with its wild-type counterpart
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. 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. Enzyme PTPN21 shows no activity with 4-nitrophenyl phosphate or Eps15846-854 peptide as substrate in the phosphatase activity assay. Once the glutamic acid in the WPE loop is replaced by an aspartic acid, the E1067D mutant form of PTPN21PTP exhibits a significantly higher level of phosphatase activity compared with its wild-type counterpart
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. Analysis of enzymes PTPN13 and PTPN14 within the FERM domain-containing PTP subfamily, overview. The catalytic domain of enzyme PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type PTPN3, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity. Enzyme PTPN13 binds to Eps15846-854 more strongly largely because of the unique H2379 responsible for substrate recognition. The other difference is an aspartic acid (D2380) in PTPN13 instead of a glycine residue in PTPN3 inside the WPD loop. The presence of an additional aspartic acid suggests that the side chain of H2379 in PTPN13 might interact with the side chains of D2378 and D2380. Such interaction likely causes a perturbation of H2379, rendering this particular residue unable to form a stable stacked-like contact to Eps15846-854, wild-type PTPN13 shows a 3fold increase in Km compared with PTPN3
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. Analysis of enzymes PTPN13 and PTPN14 within the FERM domain-containing PTP subfamily, overview. The catalytic domain of enzyme PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type PTPN3, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity. Enzyme PTPN13 binds to Eps15846-854 more strongly largely because of the unique H2379 responsible for substrate recognition. The other difference is an aspartic acid (D2380) in PTPN13 instead of a glycine residue in PTPN3 inside the WPD loop. The presence of an additional aspartic acid suggests that the side chain of H2379 in PTPN13 might interact with the side chains of D2378 and D2380. Such interaction likely causes a perturbation of H2379, rendering this particular residue unable to form a stable stacked-like contact to Eps15846-854, wild-type PTPN13 shows a 3fold increase in Km compared with PTPN3
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. Analysis of enzymes PTPN13 and PTPN14 within the FERM domain-containing PTP subfamily, overview. The catalytic domain of enzyme PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type PTPN3, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity. Enzyme PTPN13 binds to Eps15846-854 more strongly largely because of the unique H2379 responsible for substrate recognition. The other difference is an aspartic acid (D2380) in PTPN13 instead of a glycine residue in PTPN3 inside the WPD loop. The presence of an additional aspartic acid suggests that the side chain of H2379 in PTPN13 might interact with the side chains of D2378 and D2380. Such interaction likely causes a perturbation of H2379, rendering this particular residue unable to form a stable stacked-like contact to Eps15846-854, wild-type PTPN13 shows a 3fold increase in Km compared with PTPN3
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. Analysis of enzymes PTPN13 and PTPN14 within the FERM domain-containing PTP subfamily, overview. The catalytic domain of enzyme PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type PTPN3, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity. Enzyme PTPN13 binds to Eps15846-854 more strongly largely because of the unique H2379 responsible for substrate recognition. The other difference is an aspartic acid (D2380) in PTPN13 instead of a glycine residue in PTPN3 inside the WPD loop. The presence of an additional aspartic acid suggests that the side chain of H2379 in PTPN13 might interact with the side chains of D2378 and D2380. Such interaction likely causes a perturbation of H2379, rendering this particular residue unable to form a stable stacked-like contact to Eps15846-854, wild-type PTPN13 shows a 3fold increase in Km compared with PTPN3
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. Analysis of enzymes PTPN13 and PTPN14 within the FERM domain-containing PTP subfamily, overview. The catalytic domain of enzyme PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type PTPN3, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity. Enzyme PTPN13 binds to Eps15846-854 more strongly largely because of the unique H2379 responsible for substrate recognition. The other difference is an aspartic acid (D2380) in PTPN13 instead of a glycine residue in PTPN3 inside the WPD loop. The presence of an additional aspartic acid suggests that the side chain of H2379 in PTPN13 might interact with the side chains of D2378 and D2380. Such interaction likely causes a perturbation of H2379, rendering this particular residue unable to form a stable stacked-like contact to Eps15846-854, wild-type PTPN13 shows a 3fold increase in Km compared with PTPN3
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. Analysis of enzymes PTPN13 and PTPN14 within the FERM domain-containing PTP subfamily, overview. The catalytic domain of enzyme PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type PTPN3, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity. Enzyme PTPN14 shows a substitution of tyrosine in the pY loop with an isoleucin. The wild-type PTPN14PTP is catalytically inactive when four structurally characterized phosphopeptides are used as the substrate in the assay
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. Analysis of enzymes PTPN13 and PTPN14 within the FERM domain-containing PTP subfamily, overview. The catalytic domain of enzyme PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type PTPN3, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity. Enzyme PTPN14 shows a substitution of tyrosine in the pY loop with an isoleucin. The wild-type PTPN14PTP is catalytically inactive when four structurally characterized phosphopeptides are used as the substrate in the assay
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. Analysis of enzymes PTPN13 and PTPN14 within the FERM domain-containing PTP subfamily, overview. The catalytic domain of enzyme PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type PTPN3, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity. Enzyme PTPN14 shows a substitution of tyrosine in the pY loop with an isoleucin. The wild-type PTPN14PTP is catalytically inactive when four structurally characterized phosphopeptides are used as the substrate in the assay
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. Analysis of enzymes PTPN13 and PTPN14 within the FERM domain-containing PTP subfamily, overview. The catalytic domain of enzyme PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type PTPN3, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity. Enzyme PTPN14 shows a substitution of tyrosine in the pY loop with an isoleucin. The wild-type PTPN14PTP is catalytically inactive when four structurally characterized phosphopeptides are used as the substrate in the assay
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. Analysis of enzymes PTPN13 and PTPN14 within the FERM domain-containing PTP subfamily, overview. The catalytic domain of enzyme PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type PTPN3, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity. Enzyme PTPN14 shows a substitution of tyrosine in the pY loop with an isoleucin. The wild-type PTPN14PTP is catalytically inactive when four structurally characterized phosphopeptides are used as the substrate in the assay
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. The catalytic domain of PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type N3PTP, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. The catalytic domain of PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type N3PTP, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. The catalytic domain of PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type N3PTP, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. The catalytic domain of PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type N3PTP, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity
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additional information
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the [Eps15 peptide]-tyrosine phosphate is a phosphopeptide fragment of substrate epidermal growth factor receptor. Eps15 is a scaffolding adaptor that regulates endocytosis and trafficking of the EGFR and is a substrate for PTP enzyme PTPN3. The catalytic domain of PTP1B cannot dephosphorylate Eps15846-854 or Eps15836-858 efficiently compared with wild-type N3PTP, supporting a critical role of H812 in recognition of Eps15. The position of H812 in PTPN3 is a phenylalanine (F182) in PTP1B, His812 of PTPN3 plays a central role in substrate specificity
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additional information
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VHZ is an atypical PTP, with the deep active site of classical PTPs but several structural differences, including an immobile loop bearing the general acid
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additional information
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VHZ is an atypical PTP, with the deep active site of classical PTPs but several structural differences, including an immobile loop bearing the general acid
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additional information
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VHZ is an atypical PTP, with the deep active site of classical PTPs but several structural differences, including an immobile loop bearing the general acid
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additional information
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strict specificity of Spd1837 for phosphotyrosine residues
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additional information
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strict specificity of Spd1837 for phosphotyrosine residues
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Leishmania major MHOM/IL/81/FEBNI
strict specificity of Spd1837 for phosphotyrosine residues
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no activity against phytic acid, ADP, AMP, O-phospho-L-serine or O-phospho-L-threonine
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additional information
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substrate specificity evaluation, the purified recombinant enzyme exhibits high activity on O-phospho-L-tyrosine
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additional information
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substrate specificity evaluation, the purified recombinant enzyme exhibits high activity on O-phospho-L-tyrosine
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additional information
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no activity against phytic acid, ADP, AMP, O-phospho-L-serine or O-phospho-L-threonine
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additional information
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substrate specificity evaluation, the purified recombinant enzyme exhibits high activity on O-phospho-L-tyrosine
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additional information
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the isoforms of PRP36 may function as adapter molecules rather than as a phosphatase
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protein tyrosine phosphatase alpha regulates the activity of raft Fyn
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N-cadherin, VE-cadherin, desmoglein, alpha-catenin, beta-catenin, gamma-catenin, and alpha-actinin are not dephosphorylated by RPTPrho
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PTP-PEST most likely also participates in regulating osteoclast differentiation and adhesion to bone matrix
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additional information
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PTPalpha is required for stem cell factor-stimulated Src family kinase activation and signaling, and for mast cell migration
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SHP-1 is a negative regulator of osteoclastogenic signalling
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phospho-p38 mitogen-activated protein kinase and Akt are not dephosphorylated
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HePTP plays a role in regulating the level of p38 MAPK phosphorylation in B-lymphocytes, HePTP can be phosphorylated by PKA, which inactivates the phosphatase and causes it to release p38 MAPK into the cytoplasm
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additional information
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PTPN4 does not dephosphorylate Lck at tyrosine residue 394
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in vivo phagocytosis assay and in vivo microglial migration assay, overview
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additional information
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enzyme additionally catalyzes the hydrolysis of 2-phosphoglycolate, reaction of EC 3.1.3.18
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additional information
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PTP1 is a classical PTP with a deep active site pocket suited for phosphotyrosine, that also efficiently hydrolyzes other phosphorylated phenols
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additional information
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N-cadherin, VE-cadherin, desmoglein, alpha-catenin, beta-catenin, gamma-catenin, and alpha-actinin are not dephosphorylated by RPTPrho
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additional information
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in vivo phagocytosis assay and in vivo microglial migration assay, overview
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both isozymes act only on phosphotyrosine residues
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little or no effect on the residues of phosphoserine or phosphothreonine
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acts specifically on phosphorylated tyrosine
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protein-tyrosine phosphatases are signaling molecules that are involved in numerous cellular mechanisms such as cell growth and proliferation, cell cycle regulation, and cytoskeletal integrity
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LAR, PTPalpha and PTP1B may act upon cell surface insulin receptors
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enzyme activity is correlated with sperm thiol status and tyrosine phosphorylation of sperm proteins during maturation is promoted by thiol oxidation and diminished enzyme
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enzyme isoform Shp2 is required for complete activation of mitogen-activated protein kinases MAPKs by brain-derived neurotropic factor
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phosphoserine and phosphothreonine are no substrates
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the enzyme shows high activity and exquisite specificity for the 5-diphosphate group of inositol diphosphates (5-PP-InsP), substrate-binding pocket structure analysis, overview. Enzyme Siw14 also acts as a 5-PP-InsP phosphatase, EC 3.1.3.56 (inositol-polyphosphate 5-phosphatase)
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additional information
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the enzyme shows high activity and exquisite specificity for the 5-diphosphate group of inositol diphosphates (5-PP-InsP), substrate-binding pocket structure analysis, overview. Enzyme Siw14 also acts as a 5-PP-InsP phosphatase, EC 3.1.3.56 (inositol-polyphosphate 5-phosphatase)
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additional information
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the enzyme shows high activity and exquisite specificity for the 5-diphosphate group of inositol diphosphates (5-PP-InsP), substrate-binding pocket structure analysis, overview. Enzyme Siw14 also acts as a 5-PP-InsP phosphatase, EC 3.1.3.56 (inositol-polyphosphate 5-phosphatase)
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additional information
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Stp1 is a low molecular weight cytosolic acid phosphatase or phosphotyrosine protein phosphatase
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Stp1 is a low molecular weight cytosolic acid phosphatase or phosphotyrosine protein phosphatase
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substrate specificity of enzyme PRL, overview. The enzyme also hydrolyzes adenosine diphosphate, fructose 6-phosphate, sodium alpha-naphthyl phosphate, and phosphoenol pyruvate
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PtpA, PtpB act specifically on phosphotyrosine residues
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Spd1837 has activity against two phosphotyrosine-containing peptides, phosphopeptide-1 (END(pY)INASL) and phosphopeptide-2 (DADE(pY)LIPQQG), as the mutant protein Spd1837C8S lacks activity against these two phosphotyrosine-containing phosphopeptides
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Streptococcus pneumoniae D39 NCTC 7466
Spd1837 has activity against two phosphotyrosine-containing peptides, phosphopeptide-1 (END(pY)INASL) and phosphopeptide-2 (DADE(pY)LIPQQG), as the mutant protein Spd1837C8S lacks activity against these two phosphotyrosine-containing phosphopeptides
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additional information
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enzyme SP-PTP does not dephosphorylate the C-terminal fragment of EGFR with intact catalytic domain in vitro. SP-PTP possesses a tyrosine phosphatase activity that varies based on the type of substrates and reaction conditions. Enzyme SP-PTP also possesses Ser/Thr phosphatase activity dephosphorylating the autophosphorylated SP-STKK, i.e. the kinase domain of kinase SP-STK
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additional information
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enzyme SP-PTP shares high similarity with typical low molecular weight protein tyrosine phosphatases (LMWPTPs), which are specific for phosphotyrosine, but not with dual-specificity phosphatases, in overall folding and active site composition. In the dephosphorylation activity test, SP-PTP consistently acts on phosphotyrosine substrates, but not or only minimally on phosphoserine/phosphothreonine substrates. PTP as a canonical tyrosine-specific LMWPTP
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additional information
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enzyme SP-PTP does not dephosphorylate the C-terminal fragment of EGFR with intact catalytic domain in vitro. SP-PTP possesses a tyrosine phosphatase activity that varies based on the type of substrates and reaction conditions. Enzyme SP-PTP also possesses Ser/Thr phosphatase activity dephosphorylating the autophosphorylated SP-STKK, i.e. the kinase domain of kinase SP-STK
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additional information
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enzyme SP-PTP does not dephosphorylate the C-terminal fragment of EGFR with intact catalytic domain in vitro. SP-PTP possesses a tyrosine phosphatase activity that varies based on the type of substrates and reaction conditions. Enzyme SP-PTP also possesses Ser/Thr phosphatase activity dephosphorylating the autophosphorylated SP-STKK, i.e. the kinase domain of kinase SP-STK
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SynPTP displays catalytic activity towards all tyrosyl-phosphorylated proteins, but fails to dephosphorylate the same serylphosphorylated substrates, SynPTP functions as a protein tyrosine phosphatase not as a dual-specific phosphatase
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the enzyme is also active on 4-nitrophenyl phosphate
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the enzyme shows dual specificity, protein tyrosine/serine/threonine phosphatase activity
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the enzyme shows dual specificity, protein tyrosine/serine/threonine phosphatase activity
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additional information
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the enzyme shows dual specificity, protein tyrosine/serine/threonine phosphatase activity
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PPM displays little activity toward P-Ser/Thr histones
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essential for virulence of the bacteria responsible for the plague
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the enzyme contains a Cys(X5)Arg catalytic domain
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in the YopH PTP catalytic mechanism, the active site Cys403 sits at the bottom of the pTyr-binding pocket, i.e., the active site, such that its Sgamma atom is poised 3 A from the phosphorus atom of the substrate ready for nucleophilic attack
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YopH is a classical PTP with a deep active site pocket suited for phosphotyrosine, that also efficiently hydrolyzes other phosphorylated phenols
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