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Information on EC 3.1.3.56 - inositol-polyphosphate 5-phosphatase and Organism(s) Homo sapiens and UniProt Accession Q14642

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.56 inositol-polyphosphate 5-phosphatase
IUBMB Comments
One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q14642
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
inpp5k, ins(1,4,5)p3 5-phosphatase, inositol polyphosphate-5-phosphatase, inpp5a, insp 5-ptase, insp3 5-phosphatase, pip3 phosphatase, at5ptase1, 5pt13, inpp5j, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
InsP 5-ptase
-
type I inositol polyphosphate 5-phosphate
-
type I inositol-1,4,5-trisphosphate 5-phosphatase
-
D-myo-inositol 1,4,5-triphosphate 5-phosphatase
-
-
-
-
D-myo-inositol 1,4,5-trisphosphate 5-phosphatase
-
-
-
-
D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase
-
-
-
-
inosine triphosphatase
-
-
-
-
inositol 1,4,5-triphosphate 5-phosphatase
-
-
-
-
inositol 1,4,5-trisphosphate 5-monophosphatase
-
-
-
-
inositol 1,4,5-trisphosphate 5-phosphatase
inositol 1,4,5-trisphosphate phosphatase
-
-
-
-
inositol phosphate 5-phosphomonoesterase
-
-
-
-
inositol polyphosphate 5-phosphatase
inositol polyphosphate-5-phosphatase
-
-
-
-
inositol trisphosphate phosphomonoesterase
-
-
-
-
inositol(1,4,5)P3 5-phosphatase
-
-
inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase
-
-
-
-
Ins(1,4,5)P3 5-phosphatase
Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphatase
-
-
-
-
InsP3 5-phosphatase
-
-
L-myo-inositol 1,4,5-trisphosphate-monoesterase
-
-
-
-
myo-Inositol 1,4,5-trisphosphate 5-phosphatase
-
-
myo-inositol-1,4,5-trisphosphate 5-phosphatase
-
-
-
-
phosphatase, inosine tri-5PTASE
-
-
-
-
SHIP2
trisphosphate 5-phosphatase
-
-
type I inositol polyphosphate 5-phosphatase
-
-
type I inositol-1,4,5-trisphosphate 5-phosphatase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate
show the reaction diagram
catalytic and kinetic reaction mechanism, substrate binding, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
1D-myo-inositol-1,4,5-trisphosphate 5-phosphohydrolase
One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids.
CAS REGISTRY NUMBER
COMMENTARY hide
106283-14-1
-
9082-57-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
specific for
-
-
?
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
show the reaction diagram
-
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
1D-myo-inositol 1,2,3,4,5-pentakisphosphate + H2O
1D-myo-inositol 1,2,3,4-tetrakisphosphate + phosphate
show the reaction diagram
-
preferred substrate
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
show the reaction diagram
1D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O
1D-myo-inositol 1,4,6-trisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-disphosphate + phosphate
show the reaction diagram
-
-
-
-
?
1D-myo-inositol 2,4,5,6-tetrakisphosphate + H2O
1D-myo-inositol 2,4,6-trisphosphate + phosphate
show the reaction diagram
-
low activity
-
-
?
1D-myo-inositol 3,4,5-trisphosphate + H2O
1D-myo-inositol 3,4-bisphosphate + phosphate
show the reaction diagram
-
-
-
?
1D-myo-inositol 3,5-bisphosphate + H2O
1D-myo-inositol 3-phosphate + phosphate
show the reaction diagram
-
-
-
?
3-hydroxybenzene 1,2,4-trisphosphate + H2O
2,3-dihydroxybenzene 1,4-bisphosphate + phosphate
show the reaction diagram
-
this is the first example of its kind to illustrate that an unnatural aromatic polyphosphorylated molecule can be specifically dephosphorylated by type I Ins(1,4,5)P3 5-phosphatase. No reaction with benzene 1,2,4-trisphosphate
-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
show the reaction diagram
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
glycerophosphoinositol 4,5-bisphosphate + H2O
glycerophosphoinositol 4-phosphate + phosphate
show the reaction diagram
-
at 13% of the rate of inositol 1,4,5-trisphosphate hydrolysis
-
?
inositol 1,2-cyclic 4,5-trisphosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
inositol 4,5-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
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
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
specific for
-
-
?
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
show the reaction diagram
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
show the reaction diagram
-
-
-
?
1D-myo-inositol 3,4,5-trisphosphate + H2O
1D-myo-inositol 3,4-bisphosphate + phosphate
show the reaction diagram
-
-
-
?
1D-myo-inositol 3,5-bisphosphate + H2O
1D-myo-inositol 3-phosphate + phosphate
show the reaction diagram
-
-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
show the reaction diagram
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
inositol 4,5-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
no effect
Mn2+
-
can partially replace Mg2+, 50% of activity with Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
2,3-dihydroxybenzene 1,4-bisphosphate
-
-
3-benzyloxybenzene 1,2,4-trisphosphate
-
-
3-hydroxybenzene 1,2,4-trisphosphate
-
-
benzene 1,2,3,4-tetrakisphosphate
-
-
benzene 1,2,3,5-tetrakisphosphate
-
-
benzene 1,2,3-trisphosphate
-
-
benzene 1,2,4,5-tetrakisphosphate
-
-
benzene 1,2,4-trisphosphate
-
-
benzene 1,2-bisphosphate
-
-
benzene 1,3,5-trisphosphate
-
-
biphenyl 2,3',4,5',6-pentakisphosphate
-
-
CdCl2
-
-
D-fructose 1,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
-
D-glucose 6-phosphate
-
-
EDTA
-
no activity in presence of 1 mM EDTA
Glycerophosphoinositol 4,5-bisphosphate
-
competitive with D-myo-inositol 1,4,5-trisphosphate
Glycerophosphoinositol 4-phosphate
-
-
Inositol 1,3,4,5-tetrakisphosphate
inositol 1,4-bisphosphate
-
-
L-chiro-Inositol 1,4,6-trisphosphorothioate
-
very potent inhibitor
L-chiro-Inositol 2,3,5-trisphosphorothioate
-
very potent inhibitor
L-myo-inositol 1,3,5-trisphosphorothioate
-
very potent inhibitor
L-myo-inositol 1,4,5-trisphosphorothioate
-
very potent inhibitor
N-ethylmaleimide
-
-
p-hydroxymercuribenzoate
-
-
Phenylglyoxal
phosphate
-
-
additional information
-
inositol 1,4-bisphosphate does not inhibit enzyme activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 0.0075
D-myo-Inositol 1,3,4,5-tetrakisphosphate
0.006 - 0.32
D-myo-inositol 1,4,5-trisphosphate
additional information
additional information
-
kinetics, substrate specificity, overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
2,3-bisphosphoglycerate
-
-
0.0005 - 0.015
Inositol 1,3,4,5-tetrakisphosphate
0.0000003
L-chiro-Inositol 1,4,6-trisphosphorothioate
-
-
0.00000023
L-chiro-Inositol 2,3,5-trisphosphorothioate
-
-
0.00000052
L-myo-inositol 1,3,5-trisphosphorothioate
-
-
0.00000043
L-myo-inositol 1,4,5-trisphosphorothioate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021
2,3-dihydroxybenzene 1,4-bisphosphate
Homo sapiens
-
in the presence of 1 mM Ins-(1,4,5)P3 as substrate
0.068
3-benzyloxybenzene 1,2,4-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.021
3-hydroxybenzene 1,2,4-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.098
benzene 1,2,3,4-tetrakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate 6
0.078
benzene 1,2,3,5-tetrakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate 6
0.086
benzene 1,2,3-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.004
benzene 1,2,4,5-tetrakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.014
benzene 1,2,4-trisphosphate
0.016
benzene 1,3,5-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.001
biphenyl 2,3',4,5',6-pentakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
additional information
benzene 1,2-bisphosphate
Homo sapiens
-
IC value is higher than 0.2 mM, IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0028
-
Vmax, pH 7.0, 37°C
191
-
Vmax, native enzyme
2.7
-
purified membrane associated enzyme, pH 7.2, 37°C
237
-
Vmax, R350A mutant
25
-
purified enzyme
3.2
-
measured in the presence of 0.05 mM of labeled Ins(1,4,5)P3
31
-
Vmax, R343A mutant
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.4
-
assay at
7 - 7.5
-
-
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
-
-
6.25 - 8.25
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
-
assay at
7
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
I5P1_HUMAN
412
0
47820
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
SDS-PAGE, type I enzyme
70000
-
SDS-PAGE, gel filtration, membrane associated enzyme
75000
-
gel filtration, SDS-PAGE
90100
-
SDS-PAGE, maltose binding protein MBP-Type I ins(1,4,5)P3 5-phosphatase fusion protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
side-chain modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C409S
C939S
-
eliminates isoprenylation of enzyme which reduces activity towards phosphatidylinositol 4,5-bisphosphate
DELTA407-411
-
predominantly soluble
R343A
-
increased Km and dramatic loss of activity
R350A
-
increased Km
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, no loss of activity during long term storage
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
membrane associated enzyme
-
purification by a dual tag strategy: cDNA encoding human Type I Ins(1,4,5)P3 5-phosphatase is subcloned into a modified pMAL expression vector. This plasmid produces a recombinant protein in fusion with affinity tags located at its N-terminus, consisting in a maltose binding protein (MPB) and an octa-histidine stretch. The construction is transformed into Escherichia coli BL21 (DE3) expression strain. Yield: 18 mg of pure and stable enzyme starting from a 2 L
-
recombinant enzyme using His-tag
-
recombinant enzymes from Escherichia coli using His-tag
-
recombinant His-tagged catalytic domain from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the tag is cleaved off
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional expression of the enzyme in transgenic Arabidopsis thaliana plants using the Agrobacterium tumefaciens transfection system
expressed in CHO-K1 cells
-
expressed in COS-7 and CHO cells and Escherichia coli
-
expressed in HB 101 host bacteria
-
expressed in Sf9 insect cells
-
expression of His-tagged isolated catalytic domain in Escherichia coli strain BL21(DE3)
-
His-tagged version expressed in Solanum lycopersicum cv. Micro-Tom
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
genetic variation in INPP5A appears to have a role in susceptibility to arsenic toxicity. A single nucleotide polymorphism in the INPP5A gene (rs1133400) shows a significant gene-environment interaction with water arsenic on skin lesion risk
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Downes, C.P.; Mussat, M.C.; Michell, R.H.
The inositol trisphosphate phosphomonoesterase of the human erythrocyte membrane
Biochem. J.
203
169-177
1982
Homo sapiens
Manually annotated by BRENDA team
Connolly, T.M.; Bansal, V.S.; Bross, T.E.; Irvine, R.F.; Majerus, P.W.
The metabolism of tris- and tetraphosphates of inositol by 5-phosphomonoesterase and 3-kinase enzymes
J. Biol. Chem.
262
2146-2149
1987
Homo sapiens
Manually annotated by BRENDA team
Mitchell, C.A.; Connolly, T.M.; Majerus, P.W.
Identification and isolation of a 75-kDa inositol polyphosphate-5-phosphatase from human platelets
J. Biol. Chem.
264
8873-8877
1989
Homo sapiens
Manually annotated by BRENDA team
Fowler, C.J.; Brnnstrm, G.
Kinetic and inhibitor profiles of soluble and particulate inositol 1,4-5-trisphosphate 5-phosphatase from GH3 and IMR-32 cells
Biochem. J.
271
735-742
1990
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Hodgkin, M.; Parry, J.B.; Michell, R.H.; Kirk, C.J.
Generation of plasma membrane domains in polarized epithelial cells: role of cell-cell contacts and assembly of the membrane cytoskeleton
Biochem. Soc. Trans.
19
1055
1991
Bos taurus, Ovis aries, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Safrany, S.T.; Mills, S.J.; Liu, C.; Lampe, D.; Noble, N.J.; Nahorski, S.R.; Potter, B.V.L.
Design of potent and selective inhibitors of myo-inositol 1,4,5-trisphosphate 5-phosphatase
Biochemistry
33
10763-10769
1994
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Hodgkin, M.; Craxton, A.; Parry, J.B.; Hughes, P.J.; Potter, B.V.L.; Michell, R.H.; Kirk, C.J.
Bovine testis and human erythrocytes contain different subtypes of membrane-associated Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphomonoesterases
Biochem. J.
297
637-645
1994
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Jefferson, A.B.; Majerus, P.W.
Properties of type II inositol polyphosphate 5-phosphatase
J. Biol. Chem.
270
9370-9377
1995
Homo sapiens
Manually annotated by BRENDA team
De Smedt, F.; Boom, A.; Pesesse, X.; Schiffmann, S.N.; Erneux, C.
Post-translational modification of human brain type I inositol-1,4,5-trisphosphate 5-phosphatase by farnesylation
J. Biol. Chem.
271
10419-10424
1996
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Communi, D.; Lecocq, R.; Erneux, C.
Arginine 343 and 350 are two active site residues involved in substrate binding by human type I D-myo-inositol 1,4,5-trisphosphate 5-phosphatase
J. Biol. Chem.
271
11676-11683
1996
Homo sapiens
Manually annotated by BRENDA team
De Smedt, F.; Missiaen, L.; Parys, J.B.; Vanweyenberg, V.; De Smedt, H.; Erneux, C.
Isoprenylated human brain type I inositol 1,4,5-trisphosphate 5-phosphatase controls Ca2+ oscillations induced by ATP in Chinese hamster ovary cells
J. Biol. Chem.
272
17367-17375
1997
Homo sapiens
Manually annotated by BRENDA team
Erneux, C.; Govaerts, C.; Communi, D.; Pesesse, X.
The diversity and possible functions of the inositol polyphosphate 5-phosphatases
Biochim. Biophys. Acta
1436
185-199
1998
Homo sapiens
Manually annotated by BRENDA team
Whisstock, J.C.; Wiradjaja, F.; Waters, J.E.; Gurung, R.
The structure and function of catalytic domains within inositol polyphosphate 5-phosphatases
IUBMB Life
53
15-23
2002
Homo sapiens
Manually annotated by BRENDA team
Chi, Y.; Zhou, B.; Wang, W.Q.; Chung, S.K.; Kwon, Y.U.; Ahn, Y.H.; Chang, Y.T.; Tsujishita, Y.; Hurley, J.H.; Zhang, Z.Y.
Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2
J. Biol. Chem.
279
44987-44995
2004
Homo sapiens, Schizosaccharomyces pombe
Manually annotated by BRENDA team
Perera, I.Y.; Hung, C.Y.; Brady, S.; Muday, G.K.; Boss, W.F.
A universal role for inositol 1,4,5-trisphosphate-mediated signaling in plant gravitropism
Plant Physiol.
140
746-760
2006
Homo sapiens (Q14642), Homo sapiens
Manually annotated by BRENDA team
Mills, S.J.; Dozol, H.; Vandeput, F.; Backers, K.; Woodman, T.; Erneux, C.; Spiess, B.; Potter, B.V.
3-hydroxybenzene 1,2,4-trisphosphate, a novel second messenger mimic and unusual substrate for type-I myo-inositol 1,4,5-trisphosphate 5-phosphatase: Synthesis and physicochemistry
Chembiochem
7
1696-1706
2006
Homo sapiens
Manually annotated by BRENDA team
Wohlkoenig, A.; Senechal, M.; Dewitte, F.; Backers, K.; Erneux, C.; Villeret, V.
Expression and purification in high yield of a functionally active recombinant human Type I inositol(1,4,5)P3 5-phosphatase
Protein Expr. Purif.
55
69-74
2007
Homo sapiens
Manually annotated by BRENDA team
Mills, S.J.; Vandeput, F.; Trusselle, M.N.; Safrany, S.T.; Erneux, C.; Potter, B.V.
Benzene polyphosphates as tools for cell signalling: inhibition of inositol 1,4,5-trisphosphate 5-phosphatase and interaction with the pH domain of protein kinase Balpha
ChemBioChem
9
1757-1766
2008
Homo sapiens
Manually annotated by BRENDA team
Khodakovskaya, M.; Sword, C.; Wu, Q.; Perera, I.Y.; Boss, W.F.; Brown, C.S.; Winter Sederoff, H.
Increasing inositol (1,4,5)-trisphosphate metabolism affects drought tolerance, carbohydrate metabolism and phosphate-sensitive biomass increases in tomato
Plant Biotechnol. J.
8
170-183
2010
Homo sapiens
Manually annotated by BRENDA team
Braun, W.; Schein, C.
Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases
Structure
22
664-666
2014
Homo sapiens
Manually annotated by BRENDA team
Tresaugues, L.; Silvander, C.; Flodin, S.; Welin, M.; Nyman, T.; Graeslund, S.; Hammarstroem, M.; Berglund, H.; Nordlund, P.
Structural basis for phosphoinositide substrate recognition, catalysis, and membrane interactions in human inositol polyphosphate 5-phosphatases
Structure
22
744-755
2014
Homo sapiens (O15357)
Manually annotated by BRENDA team
Wiessner, M.; Roos, A.; Munn, C.J.; Viswanathan, R.; Whyte, T.; Cox, D.; Schoser, B.; Sewry, C.; Roper, H.; Phadke, R.; Marini Bettolo, C.; Barresi, R.; Charlton, R.; Boennemann, C.G.; Abath Neto, O.; Reed, U.C.; Zanoteli, E.; Araujo Martins Moreno, C.; Ertl-Wagner, B.; Stucka, R.; De Goede, C.; Borges de Silva, T.
Mutations in INPP5K, encoding a phosphoinositide 5-phosphatase, cause congenital muscular dystrophy with cataracts and mild cognitive impairment
Am. J. Hum. Genet.
100
523-536
2017
Danio rerio (A0A2R8QKI3), Danio rerio, Homo sapiens (Q9BT40)
Manually annotated by BRENDA team
Seow, W.J.; Pan, W.C.; Kile, M.L.; Tong, L.; Baccarelli, A.A.; Quamruzzaman, Q.; Rahman, M.; Mostofa, G.; Rakibuz-Zaman, M.; Kibriya, M.; Ahsan, H.; Lin, X.; Christiani, D.C.
A distinct and replicable variant of the squamous cell carcinoma gene inositol polyphosphate-5-phosphatase modifies the susceptibility of arsenic-associated skin lesions in Bangladesh
Cancer
121
2222-2229
2015
Homo sapiens (Q14642)
Manually annotated by BRENDA team
Ooms, L.M.; Binge, L.C.; Davies, E.M.; Rahman, P.; Conway, J.R.; Gurung, R.; Ferguson, D.T.; Papa, A.; Fedele, C.G.; Vieusseux, J.L.; Chai, R.C.; Koentgen, F.; Price, J.T.; Tiganis, T.; Timpson, P.; McLean, C.A.; Mitchell, C.A.
The inositol polyphosphate 5-phosphatase PIPP regulates AKT1-dependent breast cancer growth and metastasis
Cancer Cell
28
155-169
2015
Homo sapiens (Q15735)
Manually annotated by BRENDA team