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Information on EC 3.1.3.48 - protein-tyrosine-phosphatase and Organism(s) Rattus norvegicus and UniProt Accession Q64604
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EC Tree
3.1.3.48 protein-tyrosine-phosphataseIUBMB 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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Word Map
- 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
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
STEP33
-
STEP is processed into a 33 kDa isoform by calpain-mediated cleavage, STEP33 retains catalytic activity but is unable to bind to phosphorylated ERK
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
-
-
-
-
STEP
-
-
-
-
TCPTP
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
79747-53-8
-
97162-86-2
-
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
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + 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 2 + H2O
extracellular signal-regulated kinase 2 + phosphate
-
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
-
?
additional information
?
-
-
acts specifically on phosphorylated tyrosine
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
LAR, PTPalpha and PTP1B may act upon cell surface insulin receptors
-
?
additional information
?
-
-
enzyme activity is correlated with sperm thiol status and tyrosine phosphorylation of sperm proteins during maturation is promoted by thiol oxidation and diminished enzyme
-
-
?
additional information
?
-
-
enzyme isoform Shp2 is required for complete activation of mitogen-activated protein kinases MAPKs by brain-derived neurotropic factor
-
-
?
NATURAL SUBSTRATE
NATURAL 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
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
LAR, PTPalpha and PTP1B may act upon cell surface insulin receptors
-
?
additional information
?
-
-
enzyme activity is correlated with sperm thiol status and tyrosine phosphorylation of sperm proteins during maturation is promoted by thiol oxidation and diminished enzyme
-
-
?
additional information
?
-
-
enzyme isoform Shp2 is required for complete activation of mitogen-activated protein kinases MAPKs by brain-derived neurotropic factor
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
JTT-551
-
i.e. monosodium (([5-(1,1-dimethylethyl)thiazol-2-yl]methyl) ([(4-(4-[4-(1-propylbutyl)phenoxy]methyl)phenyl)thiazol-2-yl]methyl)amino)acetate, a specific protein tyrosine phosphatase 1B inhibitor in vitro and in vivo, mixed-type inhibition mode versus PTPB1, overview. The inhibitor shows a hypoglycaemic effect in rat L6 cells, overview
N-(4-([(6-methoxy-1,3-benzothiazol-2-yl)amino]sulfonyl)phenyl)acetamide
-
-
N-(6-ethoxy-1,3-benzothiazol-2-yl)-4-nitrobenzene sulfonamide
-
linear mixed-type inhibition, shows in vivo antihyperglycemic activity
N-(6-methyl-1,3-benzothiazol-2-yl)-4-nitrobenzenesulfonamide
-
linear mixed-type inhibition, shows in vivo antihyperglycemic activity
potassium bisperoxo(1,10-phenanthroline)oxovanadate(V)
-
i.e. [bpV(phen)], the peroxovanadium compound is a stable, potent and selective protein tyrosine phosphatase inhibitor. It protects dorsal column sensory axons and white matter and rescues sensory-evoked potentials in vivo after treatement with PTP or spinal cord injury, overview
additional information
-
in absence of externally added Ca2+, no effect of ethylene glycol bis(2-amino-ethylether) N,N,N,N-tetracetic acid or trifluoperazine. Not inhibitory: okadaic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
-
calculated, recombinant catalytic domain of protein tyrosine phosphatase ny, His-tag free
7.3
-
isoelectric focusing, recombinant catalytic domain of protein tyrosine phosphatase ny, His-tag free
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
epididymal spermatozoon, changes in thiol status during sperm maturation affect enzyme protein levels and activity. Tyrosine phosphorylation is significantly increased in several sperm tails during maturation. Enzyme activity is higher in the caput spermatozoa, which have a high thiol content, than in the cauda spermatozoa, with low thiol content
-
in global cerebral ischemia STEP mRNA is selectively down-regulated in brain areas susceptible to ischemic damage, while in regions of the brain that are relatively resistant to ischemic damage STEP mRNA levels are increased
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoforms STEP46 and STEP33 are found predominantly in the cytoplasmic fraction
-
there is a significant processing of STEP after ischemia to generate a novel species, STEP33, resulting in a redistribution of STEP from membrane-bound to soluble compartments
-
additional information
-
detailed study on subcellular distribution of isozymes
-
-
the PTPase family contains both cell surface transmembrane receptor forms and cytolasmic nonreceptor forms. The receptor forms generally have an extracellular domain, a single transmembrane region, and one or two cytoplasmic PTPase domains. The intracellular PTPases contain a single catalytic domain and various amino- or carboxy-terminal extensions including SH2-domains that may have targeting or regulatory functions. The catalytic domain is the only structural element with an amino acid sequence identical among all PTPases from bacteria to mammals
-
the majority of STEP61 is found in membrane-bound compartments
-
the PTPase family contains both cell surface transmembrane receptor forms and cytoplasmic nonreceptor forms. The receptor forms generally have an extracellular domain, a single transmembrane region, and one or two cytoplasmic PTPase domains. The intracellular PTPases contain a single catalytic domain and various amino- or carboxy-terminal extensions including SH2-domains that may have targeting or regulatory functions. The catalytic domain is the only structural element with an amino acid sequence identical among all PTPases from bacteria to mammals
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
protein tyrosine phosphatases inactivate neurotrophic factor receptors and downstream intracellular signaling molecules causing neurodegeneration and loss of sensoric functions, overview
physiological function
-
protein tyrosine phosphatase-PEST regulates mast cell-activating signals in protein tyrosine phosphatase activity-dependent and -independent manners
additional information
-
small-molecule protein tyrosine phosphatase inhibition is a neuroprotective treatment after spinal cord injury in adult rats
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PTPRF_RAT
1898
1
211494
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
190000
-
receptor-type protein tyrosine phosphatase, isoform RPTPgamma-A, treatment with N-glycanase reduce the value to 175000 Da
41000
-
x * 41000, SDS-PAGE, recombinant catalytic domain of protein tyrosine phosphatase ny, His-tag free
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
consists of two tandemly repeated phosphatase domains in the cytoplasmic region, domain CD1 is enzymatically active and is influenced by the catalytically inactive domain CD2
?
-
x * 41000, SDS-PAGE, recombinant catalytic domain of protein tyrosine phosphatase ny, His-tag free
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
receptor-type protein tyrosine phosphatase, isoforms RPTPgamma-A, RPTPgamma-B, RPTPgamma-C, RPTPgamma-S are glycoproteins
phosphoprotein
-
aggregation of the high-affinity IgE receptor FceRI induces the phosphorylation of PTP-PEST at Ser39, thus resulting in the suppression of enzyme activity
side-chain modification
-
alternative splicing of the brain enzyme produces 3 isoforms: PTPxi-A, the full-length form, PTPxi-B, the short form and PTPxi-S an extracellular variant, all three variants are chondroitin sulfate proteoglycans
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method with 20% PEG 10000, 0.1 M MES pH 6.5
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme activity is significantly suppressed in the liver microsomes of regucalcin transgenic rats
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged catalytic domain of protein tyrosine phosphatase ny
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
receptor-type protein tyrosine phosphatase, isoforms RPTPgamma-A, RPTPgamma-B, RPTPgamma-C, RPTPgamma-S, expression in COS7 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PTP-PEST mRNA expression is significantly induced upon the high-affinity IgE receptor FceRI-crosslinking
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
PTPalpha and PTP1B responsible for counteraction of insulin signaling, LAR and PTPalpha may act upon cell surface insulin receptors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tamura, S.; Suzuki, Y.; Kikuchi, K.; Tsuiki, S.
Identification and characterization of Mg2+-dependent phosphotyrosyl protein phosphatase from rat liver cytosol
Biochem. Biophys. Res. Commun.
140
212-218
1986
Rattus norvegicus
Okada, M.; Owada, K.; Nakagawa, H.
[Phosphotyrosine]protein phosphatase in rat brain. A major [phosphotyrosine]protein phosphatase is a 23 kDa protein distinct from acid phosphatase
Biochem. J.
239
155-162
1986
Rattus norvegicus
Brunati, A.M.; Pinna, L.A.
Isolation and partial characterization of distinct species of phosphotyrosyl protein phosphatases from rat spleen
Biochem. Biophys. Res. Commun.
133
929-936
1985
Rattus norvegicus
Gallis, B.; Bornstein, P.; Brautigan., D.L.
Tyrosylprotein kinase and phosphatase activities in membrane vesicles from normal and Rous sarcoma virus-transformed rat cells
Proc. Natl. Acad. Sci. USA
78
6689-6693
1981
Rattus norvegicus
Foulkes, J.G.; Howard, R.F.; Ziemiecki, A.
Detection of a novel mammalian protein phosphatase with activity for phosphotyrosine
FEBS Lett.
130
197-200
1981
Rattus norvegicus
Foulkes, J.G.
Phosphotyrosyl-protein phosphatases
Curr. Top. Microbiol. Immunol.
107
163-180
1983
Gallus gallus, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
Nishiwaki, T.; Maeda, N.; Noda, M.
Characterization and developmental regulation of proteoglycan-type protein-tyrosine phosphatase xi/RPTPbeta isoforms
J. Biochem.
123
458-467
1998
Rattus norvegicus
Shintani, T.; Maeda, N.; Nishiwaki, T.; Noda, M.
Characterization of rat receptor-like protein tyrosine phosphatase gamma isoforms
Biochem. Biophys. Res. Commun.
230
419-4235
1997
Rattus norvegicus
Zhang, Z.Y.
Kinetic and mechanistic characterization of a mammalian protein-tyrosine phosphatase, PTP1
J. Biol. Chem.
270
11199-11204
1995
Rattus norvegicus
Pot, D.A.; Woodford, T.A.; Remboutsika, E.; Haun, R.S.; Dixon, J.E.
Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase
J. Biol. Chem.
266
19688-19696
1991
Rattus norvegicus (Q64604)
Chengalvala, M.V.; Bapat, A.R.; Hurlburt, W.W.; Kostek, B.; Gonder, D.S.; Mastroeni, R.A.; Frail, D.E.
Biochemical characterization of osteo-testicular protein tyrosine phosphatase and its functional significance in rat primary osteoblasts
Biochemistry
40
814-821
2001
Rattus norvegicus
Calera, M.R.; Vallega, G.; Pilch, P.F.
Dynamics of protein-tyrosine phosphatases in rat adipocytes
J. Biol. Chem.
275
6308-6312
2000
Rattus norvegicus
Seligman, J.; Zipser, Y.; Kosower, N.S.
Tyrosine phosphorylation, thiol status, and protein tyrosine phosphatase in rat epididymal spermatozoa
Biol. Reprod.
71
1009-1015
2004
Rattus norvegicus
Fukaya, Y.; Yamaguchi, M.
Characterization of protein tyrosine phosphatase activity in rat liver microsomes: suppressive effect of endogenous regucalcin in transgenic rats
Int. J. Mol. Med.
14
427-432
2004
Rattus norvegicus
Easton, J.B.; Royer, A.R.; Middlemas, D.S.
The protein tyrosine phosphatase, Shp2, is required for the complete activation of the RAS/MAPK pathway by brain-derived neurotrophic factor
J. Neurochem.
97
834-845
2006
Rattus norvegicus
Santos, M.A.; Santos, S.M.; Matozo, H.C.; Portugal, R.V.; Iuliano, R.; Fusco, A.; Polikarpov, I.
Expression, purification, and characterization of rat protein tyrosine phosphatase eta catalytic domain
Protein Expr. Purif.
41
113-120
2005
Rattus norvegicus
Matozo, H.C.; Nascimento, A.S.; Santos, M.A.; Iuliano, R.; Fusco, A.; Polikarpov, I.
Crystallization and preliminary X-ray diffraction analysis of rat protein tyrosine phosphatase eta
Acta Crystallogr. Sect. F
62
923-925
2006
Rattus norvegicus
Noordman, Y.E.; Jansen, P.A.; Hendriks, W.J.
Tyrosine-specific MAPK phosphatases and the control of ERK signaling in PC12 cells
J. Mol. Signal.
1
2006
2006
Mus musculus, Rattus norvegicus
Braithwaite, S.P.; Xu, J.; Leung, J.; Urfer, R.; Nikolich, K.; Oksenberg, D.; Lombroso, P.J.; Shamloo, M.
Expression and function of striatal enriched protein tyrosine phosphatase is profoundly altered in cerebral ischemia
Eur. J. Neurosci.
27
2444-2452
2008
Rattus norvegicus
Navarrete-Vazquez, G.; Paoli, P.; Leon-Rivera, I.; Villalobos-Molina, R.; Medina-Franco, J.L.; Ortiz-Andrade, R.; Estrada-Soto, S.; Camici, G.; Diaz-Coutino, D.; Gallardo-Ortiz, I.; Martinez-Mayorga, K.; Moreno-Diaz, H.
Synthesis, in vitro and computational studies of protein tyrosine phosphatase 1B inhibition of a small library of 2-arylsulfonylaminobenzothiazoles with antihyperglycemic activity
Bioorg. Med. Chem.
17
3332-3341
2009
Rattus norvegicus
Fukuda, S.; Ohta, T.; Sakata, S.; Morinaga, H.; Ito, M.; Nakagawa, Y.; Tanaka, M.; Matsushita, M.
Pharmacological profiles of a novel protein tyrosine phosphatase 1B inhibitor, JTT-551
Diabetes Obes. Metab.
12
299-306
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Nakashima, S.; Arnold, S.A.; Mahoney, E.T.; Sithu, S.D.; Zhang, Y.P.; D'Souza, S.E.; Shields, C.B.; Hagg, T.
Small-molecule protein tyrosine phosphatase inhibition as a neuroprotective treatment after spinal cord injury in adult rats
J. Neurosci.
28
7293-7303
2008
Rattus norvegicus
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