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Information on EC 3.1.3.48 - protein-tyrosine-phosphatase

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.48 protein-tyrosine-phosphatase
IUBMB Comments
Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2, non-specific protein-tyrosine kinase.
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This record set is specific for:
UNIPROT: P29350
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
ptp1b, protein tyrosine phosphatase, shp-1, shp-2, tyrosine phosphatase, protein phosphatase 2a, acid phosphatase activity, mkp-1, cdc25a, ptpn22, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
protein tyrosine phosphatase
-
protein tyrosine phosphatase 1B
-
70Z-SHP
-
-
-
-
Brain-derived phosphatase
-
-
-
-
BVP
-
-
-
-
CD148 antigen
-
-
-
-
CD45
-
-
-
-
CD45 antigen
-
-
-
-
Cdc25-like protein
-
-
-
-
CDK2-associated dual specificity phosphatase
-
-
-
-
Ch-1PTPase
-
-
-
-
CPTP1
-
-
-
-
DLAR
-
-
-
-
Dual specificity phosphatase Cdc25A
-
-
-
-
Dual specificity phosphatase Cdc25B
-
-
-
-
Dual specificity phosphatase Cdc25C
-
-
-
-
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 tyrosine phosphatase TS-DSP6
-
-
-
-
Dual-specificity tyrosine phosphatase YVH1
-
-
-
-
ES cell phosphatase
-
-
-
-
HCP
-
-
-
-
Hematopoietic cell protein-tyrosine phosphatase
-
-
-
-
Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP
-
-
-
-
Hematopoietic protein-tyrosine phosphatase
-
-
-
-
HEPTP
-
-
-
-
HPTP beta-like tyrosine phosphatase
-
-
-
-
HPTP eta
-
-
-
-
hPTPE1
-
-
-
-
ICAAR
-
-
-
-
Islet cell autoantigen related protein
-
-
-
-
kinase associated phosphatase
-
-
-
-
L-CA
-
-
-
-
Late protein H1
-
-
-
-
LCA
-
-
-
-
LCA-related phosphatase
-
-
-
-
Leukocyte antigen related
-
-
-
-
Low molecular weight cytosolic acid phosphatase
-
-
-
-
LRP
-
-
-
-
Lymphoid phosphatase
-
-
-
-
LyP
-
-
-
-
M1851
-
-
-
-
MAP-kinase phosphatase CPG21
-
-
-
-
MEG
-
-
-
-
Mitosis initiation protein
-
-
-
-
Mitosis initiation protein MIH1
-
-
-
-
Mitotic inducer homolog
-
-
-
-
MKP-1 like protein tyrosine phosphatase
-
-
-
-
MPTP
-
-
-
-
MPTP-PEST
-
-
-
-
NC-PTPCOM1
-
-
-
-
Neural-specific protein-tyrosine phosphatase
-
-
-
-
ORF5
-
-
-
-
OST-PTP
-
-
-
-
P19-PTP
-
-
-
-
P80
-
-
-
-
PC12-PTP1
-
-
-
-
Phogrin
-
-
-
-
Phosphacan
-
-
-
-
phosphatase, phosphoprotein (phosphotyrosine)
-
-
-
-
phosphatase, phosphotyrosine
-
-
-
-
phosphoprotein phosphatase (phosphotyrosine)
-
-
-
-
phosphotyrosine histone phosphatase
-
-
-
-
phosphotyrosine phosphatase
-
-
-
-
Phosphotyrosine phosphatase 13
-
-
-
-
phosphotyrosine protein phosphatase
-
-
-
-
phosphotyrosylprotein phosphatase
-
-
-
-
protein phosphotyrosine phosphatase
-
-
-
-
Protein tyrosine phosphatase-NP
-
-
-
-
Protein-protein-tyrosine phosphatase HA2
-
-
-
-
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 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
-
-
-
-
PTP IA-2beta
-
-
-
-
PTP-1B
-
-
-
-
PTP-1C
-
-
-
-
PTP-1D
-
-
-
-
PTP-2C
-
-
-
-
PTP-BAS
-
-
-
-
PTP-E1
-
-
-
-
PTP-H1
-
-
-
-
PTP-HA2
-
-
-
-
PTP-NP
-
-
-
-
PTP-SH2beta
-
-
-
-
PTP1C
-
-
-
-
PTP1D
-
-
-
-
PTP2C
-
-
-
-
PTPase YVH1
-
-
-
-
PTPase-MEG1
-
-
-
-
PTPase-MEG2
-
-
-
-
PTPG1
-
-
-
-
PTPN6
-
-
-
-
PTPNE6
-
-
-
-
PY protein phosphatase
-
-
-
-
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
-
-
-
-
Receptor-linked protein-tyrosine phosphatase 10D
-
-
-
-
Receptor-linked protein-tyrosine phosphatase 99A
-
-
-
-
RNA/RNP complex-intereracting phosphatase
-
-
-
-
ROL B protein
-
-
-
-
RPTPalpha
-
-
-
-
SH-PTP1
-
-
-
-
SH-PTP2
-
-
-
-
SH-PTP3
-
-
-
-
SHP
-
-
-
-
Small tyrosine phosphatase
-
-
-
-
Small, acidic phosphotyrosine protein phosphatase
-
-
-
-
STEP
-
-
-
-
String protein
-
-
-
-
Syp
-
-
-
-
T-cell protein-tyrosine phosphatase
-
-
-
-
T-DSP11
-
-
-
-
T200
-
-
-
-
TCPTP
-
-
-
-
Testis-and skeletal-muscle-specific DSP
-
-
-
-
tyrosine O-phosphate phosphatase
-
-
-
-
Tyrosine phosphatase CBPTP
-
-
-
-
tyrosylprotein phosphatase
-
-
-
-
[phosphotyrosine]protein phosphatase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-tyrosine-phosphate phosphohydrolase
Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2, non-specific protein-tyrosine kinase.
CAS REGISTRY NUMBER
COMMENTARY hide
79747-53-8
-
97162-86-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
DADE(pY)LIPQQG + H2O
DADEYLIPQQG + phosphate
show the reaction diagram
-
-
-
?
phosphorylated insulin receptor + H2O
insulin receptor + phosphate
show the reaction diagram
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
study on substrate specificity
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
28-(10-decanoic)-oleanolic acid
-
28-(12-dodecanoic)-oleanolic acid
-
28-(2-acetic)-oleanolic acid
-
28-(4-butyric)-oleanolic acid
-
28-(6-hexanoic)-oleanolic acid
-
28-(8-octanoic)-oleanolic acid
-
28-(glycine)-oleanolic acid amide
-
28-(L-glutamic acid)-oleanolic acid amide
-
28-(L-phenylalanine)-oleanolic acid amide
-
28-(p-carboxyphenyl)-oleanolic acid amide
-
28-[4-butyric((R)-1-carboxy-phenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric((S)-1-carboxy-3-indole-ethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric((S)-1-carboxy-5-imidazole-ethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric((S)-1-carboxy-methylthioethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric((S)-1-carboxy-phenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-2,3-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-3,4-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-3,4-oxymethyleneoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-3,5-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-m-chlorophenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-m-methoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-o-chlorophenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-o-methoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-o-methylphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-p-chlorophenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-p-fluorophenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-p-methoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-p-methylphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-p-nitrophenylethyl)-amide]-DELTA12-oleanene
-
3-(2,2'-dimethyl-carboxypropanoyloxy)-oleanolic acid
-
3-(2-carboxy-benzyloxy)-oleanolic acid
-
3-(2-carboxybenzoyloxy)-oleanolic acid
-
3-(3-carboxy-benzyloxy)-oleanolic acid
-
3-(4-carboxy-benzyloxy)-28-[4-butyric((s)-1-carboxyphenylethyl)-amide]-DELTA12-oleanene
-
3-(4-carboxy-benzyloxy)-oleanolic acid
-
3-benzyloxy-oleanolic acid
-
3-carboxypropanoyloxy-oleanolic acid
-
3-dehydroxy-oleanolic acid
-
3-ethyl oxalyl-oleanolic acid
-
3-methylene-oleanolic acid
-
3-oxalyl-oleanolic acid
-
3-oxo-oleanolic acid
-
3alpha-oleanolic acid
-
4,4'-[benzene-1,4-diylbis(methanediyloxy)]dibenzoic acid
-
benzyl oleanolic acid amide
-
benzyl oleanolic acid ester
-
methyl oleanolic acid amide
-
methyl oleanolic acid ester
-
oleanolic acid
-
oleanolic acid amide
-
oleanolic alcohol
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00072
28-(10-decanoic)-oleanolic acid
Homo sapiens
-
0.00059
28-(12-dodecanoic)-oleanolic acid
Homo sapiens
-
0.0021
28-(2-acetic)-oleanolic acid
Homo sapiens
-
0.00133
28-(4-butyric)-oleanolic acid
Homo sapiens
-
0.00088
28-(6-hexanoic)-oleanolic acid
Homo sapiens
-
0.00078
28-(8-octanoic)-oleanolic acid
Homo sapiens
-
0.01544
28-(glycine)-oleanolic acid amide
Homo sapiens
-
0.01635
28-(L-glutamic acid)-oleanolic acid amide
Homo sapiens
-
0.00331
28-(L-phenylalanine)-oleanolic acid amide
Homo sapiens
-
0.00319
28-(p-carboxyphenyl)-oleanolic acid amide
Homo sapiens
-
0.00074
28-[4-butyric((R)-1-carboxy-phenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00059
28-[4-butyric((S)-1-carboxy-3-indole-ethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00462
28-[4-butyric((S)-1-carboxy-5-imidazole-ethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00055
28-[4-butyric((S)-1-carboxy-methylthioethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00057
28-[4-butyric((S)-1-carboxy-phenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00066
28-[4-butyric(1-carboxy-2,3-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00082
28-[4-butyric(1-carboxy-3,4-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00044
28-[4-butyric(1-carboxy-3,4-oxymethyleneoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00063
28-[4-butyric(1-carboxy-3,5-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00051
28-[4-butyric(1-carboxy-m-chlorophenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00052
28-[4-butyric(1-carboxy-m-methoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00056
28-[4-butyric(1-carboxy-o-chlorophenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00053
28-[4-butyric(1-carboxy-o-methoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00055
28-[4-butyric(1-carboxy-o-methylphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00061
28-[4-butyric(1-carboxy-p-chlorophenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00057
28-[4-butyric(1-carboxy-p-fluorophenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.0006
28-[4-butyric(1-carboxy-p-methoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00065
28-[4-butyric(1-carboxy-p-methylphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00045
28-[4-butyric(1-carboxy-p-nitrophenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00233
3-(2,2'-dimethyl-carboxypropanoyloxy)-oleanolic acid
Homo sapiens
-
0.00272
3-(2-carboxy-benzyloxy)-oleanolic acid
Homo sapiens
-
0.00458
3-(2-carboxybenzoyloxy)-oleanolic acid
Homo sapiens
-
0.00062
3-(3-carboxy-benzyloxy)-oleanolic acid
Homo sapiens
-
0.00015
3-(4-carboxy-benzyloxy)-28-[4-butyric((s)-1-carboxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00054
3-(4-carboxy-benzyloxy)-oleanolic acid
Homo sapiens
-
0.00267
3-benzyloxy-oleanolic acid
Homo sapiens
-
0.00597
3-carboxypropanoyloxy-oleanolic acid
Homo sapiens
-
0.00261
3-dehydroxy-oleanolic acid
Homo sapiens
-
0.00289
3-ethyl oxalyl-oleanolic acid
Homo sapiens
-
0.00285
3-methylene-oleanolic acid
Homo sapiens
-
0.00286
3-oxalyl-oleanolic acid
Homo sapiens
-
0.00532
3-oxo-oleanolic acid
Homo sapiens
-
0.00505
3alpha-oleanolic acid
Homo sapiens
-
0.00573
4,4'-[benzene-1,4-diylbis(methanediyloxy)]dibenzoic acid
Homo sapiens
-
0.0081
benzyl oleanolic acid amide
Homo sapiens
-
0.00861
benzyl oleanolic acid ester
Homo sapiens
-
0.0092
methyl oleanolic acid amide
Homo sapiens
-
0.00444
methyl oleanolic acid ester
Homo sapiens
-
0.0037
oleanolic acid
Homo sapiens
-
0.00476
oleanolic acid amide
Homo sapiens
-
0.02
oleanolic alcohol
Homo sapiens
IC50 above 0.02 mM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
in human cells, enzyme SHP-1's phosphatase activity is regulated through an autoinhibitory interaction between its catalytic PTP domain and one of its SH2 domains, in the autoinhibited state of SHP-1, the amino-terminal SH2 domain blocks the PTP-domain's active site
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PTN6_HUMAN
595
0
67561
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain and C455S mutant of catalytic domain, in complex with peptide substrates
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C455S
crystallization data
V451M
site-directed mutagenesis, the mutation lies in a conserved motif adjacent to the protein tyrosine phosphatase (PTP) consensus sequence and alters catalytic function. Mutant V451M possesses increased catalytic activity as compared to the wild-type enzyme. When assayed with 4-nitrophenyl phosphatase as substrate, mutant V451M shows higher activity regardless of the pNPP substrate concentration used. The mutant shows increased thermolability compared to wild-type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42
above 42°C, the activity of the mutant proteins decreases substantially, dropping off to only a fraction of that of the corresponding wild-type enzymes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in CHO cells and L6 cells
gene PTPN6, recombinant expression of wild-type full-length enzyme and isolated catalytic enzyme domain SHP-1cat, and of V451M mutant full-length enzyme and isolated catalytic enzyme domain SHP-1cat in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, J.; Cheng, Z.; Niu, T.; Liang, X.; Zhao, Z.J.; Zhou, G.W.
Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1
J. Biol. Chem.
275
4066-4071
2000
Homo sapiens (P29350)
Manually annotated by BRENDA team
Zhang, Y.N.; Zhang, W.; Hong, D.; Shi, L.; Shen, Q.; Li, J.Y.; Li, J.; Hu, L.H.
Oleanolic acid and its derivatives: new inhibitor of protein tyrosine phosphatase 1B with cellular activities
Bioorg. Med. Chem.
16
8697-8705
2008
Homo sapiens (P29350)
Manually annotated by BRENDA team
Hendriks, W.J.; Elson, A.; Harroch, S.; Stoker, A.W.
Protein tyrosine phosphatases: functional inferences from mouse models and human diseases
FEBS J.
275
816-830
2008
Homo sapiens, Homo sapiens (O14522), Homo sapiens (P10586), Homo sapiens (P17706), Homo sapiens (P18031), Homo sapiens (P18433), Homo sapiens (P23467), Homo sapiens (P23468), Homo sapiens (P23469), Homo sapiens (P23470), Homo sapiens (P23471), Homo sapiens (P26045), Homo sapiens (P28827), Homo sapiens (P29074), Homo sapiens (P29350), Homo sapiens (P35236), Homo sapiens (P43378), Homo sapiens (P54829), Homo sapiens (Q05209), Homo sapiens (Q06124), Homo sapiens (Q0VAE8), Homo sapiens (Q12913), Homo sapiens (Q12923), Homo sapiens (Q13332), Homo sapiens (Q15256), Homo sapiens (Q15262), Homo sapiens (Q15678), Homo sapiens (Q16825), Homo sapiens (Q16827), Homo sapiens (Q16849), Homo sapiens (Q4JDK3), Homo sapiens (Q92729), Homo sapiens (Q92932), Homo sapiens (Q99952), Homo sapiens (Q9H3S7), Homo sapiens (Q9HD43), Homo sapiens (Q9UMZ3), Homo sapiens (Q9Y2R2)
Manually annotated by BRENDA team
Bishop, A.C.
A missense methionine mutation augments catalytic activity but reduces thermal stability in two protein tyrosine phosphatases
Biochem. Biophys. Res. Commun.
481
153-158
2016
Homo sapiens (P29350), Homo sapiens
Manually annotated by BRENDA team