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Information on EC 3.1.3.48 - protein-tyrosine-phosphatase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P40347
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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: Saccharomyces cerevisiae
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
-
-
-
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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
-
-
-
-
Siw14
Small tyrosine phosphatase
-
-
-
-
Small, acidic phosphotyrosine protein phosphatase
-
-
-
-
STEP
-
-
-
-
String protein
-
-
-
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Syp
-
-
-
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T-cell protein-tyrosine phosphatase
-
-
-
-
T-DSP11
-
-
-
-
T200
-
-
-
-
TCPTP
-
-
-
-
Testis-and skeletal-muscle-specific DSP
-
-
-
-
tyrosine O-phosphate phosphatase
-
-
-
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Tyrosine phosphatase CBPTP
-
-
-
-
tyrosylprotein phosphatase
-
-
-
-
[phosphotyrosine]protein phosphatase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
overview on mechanism and transition state
-
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-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
phosphorylated Gln3 + H2O
Gln3 + phosphate
-
Siw14, in combination with the protein kinase Npr1, regulates the intracellular localization of Gln3
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
-
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)
-
-
?
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
phosphorylated Gln3 + H2O
Gln3 + phosphate
-
Siw14, in combination with the protein kinase Npr1, regulates the intracellular localization of Gln3
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
enzyme Siw14 is a member of the protein tyrosine-phosphatase (PTP) superfamily. Siw14 has a cysteine-based, class I CX5R(S/T) motif that defines the family of protein-tyrosine phosphatases (PTPs). Bioinformatic studies lead to Siw14 being classified as belonging within a specialist subgroup of PTPs, the dual specific protein-tyrosine phosphatases (DUSPs). The DUSPs themselves include a distinct class of proteins that appears not to have substantial activity against phosphoproteins. These are usually described as nonprotein-specific or atypical phosphatases. The inclusion of Siw14 in this category is supported by biochemical analysis, the enzyme's catalytic activity against 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP7) is several orders of magnitude greater than that against 4-nitrophenyl phosphate, a generic protein phosphatase substrate. Other members of this atypical DUSP subgroup preferentially hydrolyze either phosphorylated carbohydrates, inositol lipids, or triphosphate groups in mRNA. Thus, this DUSP subfamily exhibits catalytic site diversity that is not observed for classical PTPs
metabolism
-
analysis of multivesicular body (MVB) sorting, involving the enzyme, of internalised membrane proteins that have entered the early endosome, overview. The multivesicular body is an intermediate compartment en route to the degradative milieu of the lysosome
physiological function
-
role of His domain protein tyrosine phosphatase/PTPN23 (HD-PTP) and ESCRTs (endosomal sorting complexes required for transport) in sorting activated epidermal growth factor receptor to the multivesicular body, interactions involving HD-PTP and ESCRTs. Potential mechanism for EGFR sorting to the MVB, comparisons to Homo sapiens, overview
additional information
additional information
active site architecture and substrate binding pocket structure, overview. The core catalytic domain of Siw14 is formed by residues 116-281. A loop between the alpha5 and alpha6 helices, corresponding to the Q-loop in PTPs, contains a lysine and an arginine that extend into the catalytic pocket due to displacement of the alpha5 helix orientation through intramolecular crowding caused by three bulky, hydrophobic residues. The general-acid loop in PTPs is replaced in Siw14 with a flexible loop that does not use an aspartate or glutamate as a general acid
additional information
-
active site architecture and substrate binding pocket structure, overview. The core catalytic domain of Siw14 is formed by residues 116-281. A loop between the alpha5 and alpha6 helices, corresponding to the Q-loop in PTPs, contains a lysine and an arginine that extend into the catalytic pocket due to displacement of the alpha5 helix orientation through intramolecular crowding caused by three bulky, hydrophobic residues. The general-acid loop in PTPs is replaced in Siw14 with a flexible loop that does not use an aspartate or glutamate as a general acid
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant catalytic core of Siw14 (residues 116-281), hanging drop vapor diffusion, mixing of 0.002 ml of 15 mg/ml protein in 150 mM NaCl, and 20 mM Tris-HCl, pH 7.5, with 0.002 ml of well solution containing 0.7 M sodium citrate, and 50 mM 2-mercaptoethanol, 25°C, X-ray diffraction structure determination and analysis at 2.35-2.38 A resolution, model building
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the DELTAsiw14 disruptant exhibits caffeine sensitivity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-MBP-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity and heparin affinityy chromatography, tag cleavage with TEV protease, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene siw14, recombinant expression of His6-MBP-tagged wild-type and mutant enzymes in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, S.; Tabernero, L.; Zhang, M.; Harms, E.; van Etten, R.L.; Stauffacher, C.V.
Crystal structure of a low-molecular weight protein tyrosine phosphatase from Saccharomyces cerevisiae and its complex with the substrate p-nitrophenyl phosphate
Biochemistry
39
1903-1914
2000
Saccharomyces cerevisiae (P40347), Saccharomyces cerevisiae
Kolmodin, K.; Aqvist, J.
The catalytic mechanism of protein tyrosine phosphatases revisited
FEBS Lett.
498
208-213
2001
Saccharomyces cerevisiae, Homo sapiens, Yersinia enterocolitica
Hirasaki, M.; Kaneko, Y.; Harashima, S.
Protein phosphatase Siw14 controls intracellular localization of Gln3 in cooperation with Npr1 kinase in Saccharomyces cerevisiae
Gene
409
34-43
2008
Saccharomyces cerevisiae
Tabernero, L.; Woodman, P.
Dissecting the role of His domain protein tyrosine phosphatase/PTPN23 and ESCRTs in sorting activated epidermal growth factor receptor to the multivesicular body
Biochem. Soc. Trans.
46
1037-1046
2018
Saccharomyces cerevisiae, Homo sapiens (Q9H3S7)
Wang, H.; Gu, C.; Rolfes, R.J.; Jessen, H.J.; Shears, S.B.
Structural and biochemical characterization of Siw14 a protein-tyrosine phosphatase fold that metabolizes inositol pyrophosphates
J. Biol. Chem.
293
6905-6914
2018
Saccharomyces cerevisiae (P53965), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P53965)
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