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Information on EC 2.7.1.127 - inositol-trisphosphate 3-kinase and Organism(s) Homo sapiens and UniProt Accession Q96DU7

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EC Tree
IUBMB Comments
Activated by Ca2+. Three isoforms have been shown to exist .
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This record set is specific for:
Homo sapiens
UNIPROT: Q96DU7
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
itpka, itpkb, itpkc, insp3 3-kinase, ip3k, ip3k-a, ip3kb, insp3kinase, ins(1,4,5)p3 kinase, inositol 1,4,5-trisphosphate 3-kinase c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inositol(1,4,5)P3 3-kinase
-
inositol(1,4,5)trisphosphate 3-kinases
-
1D-myo-inositol-trisphosphate 3-kinase
-
-
-
-
D-myo-inositol 1,4,5-trisphosphate 3-kinase
-
-
-
-
inositol 1,4,5-trisphosphate 3-kinase
inositol 1,4,5-trisphosphate 3-kinase C
-
-
inositol 1,4,5-trisphosphate kinase
-
-
-
-
inositol 1,4,5-trisphosphate kinase 2
-
inositol 1,4,5-trisphosphate-3-kinase-A
-
inositol trisphosphate 3-kinase B
-
inositol(1,4,5)P3 3-kinase
-
inositol(1,4,5)trisphosphate 3-kinases
-
inositol-1,4,5-trisphosphate 3-kinase
inositol-1,4,5-trisphosphate 3-kinase A
-
inositol-1,4,5-trisphosphate 3-kinase-A
-
inositol-1,4,5-trisphosphate-3-kinase
-
-
-
-
inositol-1,4,5-trisphosphate-3-kinase A
-
inositol-trisphosphate 3-kinase B
UniProt
Ins(1,4,5)P3 3-kinase
Ins(1,4,5)P3 3-kinase isoform B
-
-
InsP3 3-kinase
-
-
-
-
IP3 3-kinase
-
-
IP3K-B
IP3K-C
-
-
IP3kin
-
-
-
-
kinase (phosphorylating), inositol 1,4,5-trisphosphate 3-
-
-
-
-
additional information
-
the enzyme belongs tot he IPK family, structure comparisons
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
show the reaction diagram
catalytic mechanism, ATP, substrate and product binding
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
phospho-group transfer
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol-1,4,5-trisphosphate 3-phosphotransferase
Activated by Ca2+. Three isoforms have been shown to exist [3].
CAS REGISTRY NUMBER
COMMENTARY hide
106283-10-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
show the reaction diagram
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
show the reaction diagram
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
the enzyme is activated by Ca2+/calmodulin
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1D-myo-inositol 1,4,5-trisphosphate
-
substrate inhibition of the catalytic domain
2-[3,5-dimethyl-1-(4-nitrophenyl)-1H-pyrazol-4-yl]-5,8-dinitro-1H-benzo[de]isoquinoline-1,3(2H)-dione
BIP-4, BIP-4 is competitive to Ins(1,4,5)P3 and shows high selectivity for the Ins(1,4,5)P3 binding pocket, BIP-4 does not block the actin bundling activity of ITPKA
-
3',4',7,8-tetrahydroxyflavone
7-methylsulfanyl-3-phenyl-[1,3,4]thiadiazolo[2,3-c][1,2,4]triazin-4-one
55% inhibition at 0.04 mM
aurintricarboxylic acid
Ca2+
-
at higher concentrations
chlorogenic acid
-
EGTA
-
Ca2+/calmodulin-activated enzyme
ellagic acid
epicatechin-3-gallate
epigallocatechin-3-gallate
F-actin
-
-
gossypol
hypericin
KN-62
KN-93
myricetin
N-(1,2-benzoxazol-3-yl)-4-methylbenzamide
68% inhibition at 0.04 mM, mixed type inhibitor, that is nearly completely taken up by H1299 cells and remains stable after cellular uptake, the compound exhibits a robust stability and a high membrane permeability. The inhibitor provides the possibility to partly inhibit the metastasis-promoting effect of ITPKA in lung tumor cells. Inhibition mechanism of BAMB-4, overview
N-(4-ethoxyphenyl)pyrazolo[1,5-a]pyridine-3-carboxamide
87% inhibition at 0.04 mM
Protein kinase C
-
quercetin
Rose bengal
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
the enzyme is activated by Ca2+/calmodulin. The isozyme contains a CaM binding domain
12-O-tetradecanoyl phorbol 13-acetate
-
stimulating in presence of cAMP
12-O-tetradecanoylphorbol-13-acetate
-
2fold activation, isoform B
Ca2+/calmodulin
for enzyme activation, Ca2+/calmodulin, 2.15 microg/ml calmodulin and 10-20 microM free CaCl2 is added to the assay mixture
-
Ca2+/CaM-dependent kinase II
-
i.e. CaMKII, activates the enzyme by phosphorylation of Thr311
-
Calmodulin
CaM kinase II
-
cAMP-dependent protein kinase
-
i.e. PKA, activates the enzyme by phosphorylation at a serine residue
-
Carbachol
Protein kinase C
-
phosphorylation of isoenzyme B by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, but protein kinase C alone inhibits in the presence of Ca2+ and calmodulin, no effect on the sensitivity to the Ca2+/calmodulin complex
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00076 - 0.004
1D-myo-inositol 1,4,5-trisphosphate
2.5
ATP
-
pH 7.4, 37°C, platelet enzyme
additional information
additional information
Michaelis-Menten kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000157
2-[3,5-dimethyl-1-(4-nitrophenyl)-1H-pyrazol-4-yl]-5,8-dinitro-1H-benzo[de]isoquinoline-1,3(2H)-dione
Homo sapiens
pH and temperature not specified in the publication
-
0.00018 - 0.0034
3',4',7,8-tetrahydroxyflavone
0.036
7-methylsulfanyl-3-phenyl-[1,3,4]thiadiazolo[2,3-c][1,2,4]triazin-4-one
Homo sapiens
pH 7.5, 30°C, recombinant enzyme
0.00011 - 0.000138
aurintricarboxylic acid
0.00022 - 0.00055
ellagic acid
0.0004 - 0.00056
epicatechin-3-gallate
0.00015 - 0.00278
epigallocatechin-3-gallate
0.000115 - 0.00034
gossypol
0.00018 - 0.00021
hypericin
0.00015 - 0.0042
myricetin
0.037
N-(1,2-benzoxazol-3-yl)-4-methylbenzamide
Homo sapiens
pH 7.5, 30°C, recombinant enzyme
0.017
N-(4-ethoxyphenyl)pyrazolo[1,5-a]pyridine-3-carboxamide
Homo sapiens
pH 7.5, 30°C, recombinant enzyme
0.0003 - 0.00125
quercetin
0.00052 - 0.00219
Rose bengal
additional information
chlorogenic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0048
-
37°C, isoenzyme A, rat cortical slices
0.283
-
pH 7.4, 37°C
0.75 - 1.45
-
pH 7.4, 37°C, platelet, in presence of free Ca2+ and calmodulin
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
in presence of Ca2+/calmodulin
7.4
-
assay at
7.6
-
in presence of EGTA
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 7.6
-
about half-maximal activity at pH 6.3 and 7.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene Itpkc
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
cloning and expression in Escherichia coli
Manually annotated by BRENDA team
Itpkb protein level is increased upon differentiation of human embryonic stem cells
Manually annotated by BRENDA team
-
human glioma cell line HTB-138, InsP3 3-kinase B mRNA
Manually annotated by BRENDA team
-
non-differentiated promyelocytic-leukaemia cell line, InsP3 3-kinase B mRNA
Manually annotated by BRENDA team
-
human cell line SH-SY5Y, InsP3 3-kinase B mRNA
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
not activated isoenzyme B: 65% soluble, 35% particulate fraction, carbachol-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction, only 10% remain soluble
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
inositol(1,4,5)trisphosphate 3-kinases (Itpks) occur in three isoenzyme forms, Itpka/b and c, in human, rat and mouse. They share a catalytic domain relatively well conserved at the C-terminal end and a quite isoenzyme specific regulatory domain at the N-terminal end of the protein
metabolism
1D-myo-inositol 1,3,4,5-tetrakisphosphate, Ins(1,3,4,5)P4 can interact with a relatively specific Ins(1,3,4,5)P4 binding protein Rasa3, alternatively, Ins(1,3,4,5)P4 can also compete with phosphoinositides to the binding of PH domain containing proteins such as Akt, protein kinase B. In neutrophils and hematopoietic progenitors, elevated levels of Ins(1,3,4,5)P4 inhibit the recruitment of Akt at the plasma membrane, and its activation, acting as a competitor of PtdIns(3,4,5)P3 binding to its PH domain
evolution
inositol(1,4,5)trisphosphate 3-kinases (Itpks) occur in three isoenzyme forms, Itpka/b and c, in human, rat and mouse. They share a catalytic domain relatively well conserved at the C-terminal end and a quite isoenzyme specific regulatory domain at the N-terminal end of the protein
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
IP3KC_HUMAN
683
0
75207
Swiss-Prot
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
-
1 * 36000, additional 53 kDa polypeptide with enzyme activity, SDS-PAGE
50000
53000
-
x * 53000, isoenzyme A, SDS-PAGE
53500
-
x * 50000, isozyme IP33K-A, x * 53500, isozyme IP33K-B, x * 75200, isozyme IP33K-C
58000
-
minor peaks with MW of 39 kDa and 32 kDa, HPLC gel filtration
75200
-
x * 50000, isozyme IP33K-A, x * 53500, isozyme IP33K-B, x * 75200, isozyme IP33K-C
88000
-
x * 88000, isoform B, SDS-PAGE, Western blot analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
proteolytic modification
Itpkb is very sensitive to proteolysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the complex between human Ca2+/CaM and the CaM-binding region of human IP3-3K isoform A (residues 158-183), modeling of the complex including the kinase domain
purified recombinant unlabeled or selennomethionine-labeled wild-type and mutant catalytic domain residues 187-461 free or complexed to ATP, substrate, and product, automated sitting drop vapour diffusion method, 17°C, 0.001 ml protein solution over reservoir solution containing 0.83-0.85 M tri-sodium citrate, 0.1 M Tris-HCl, pH 8.0, and 0.1 M NaCl, heavy atom derivative, substrates, or products complex formation by addition and removal of 0.001 ml of 2 M Li2SO4 and 100 mM Tris-HCl, pH 8.0, 4°C, containing the relevant compound, i.e. 3 mM ATP, 3 mM MnCl2, or 5 mM 1D-myo-inositol 1,3,4,5-tetrakisphosphate, for 7times, and final soaking for 2.5 h, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A187S
-
crystal structure determination and analysis
D262A
-
14% of wild-type enzyme activity
D262N
-
12% of wild-type enzyme activity
D416A
-
inactive mutant
K199A
-
80% of wild-type enzyme activity
L34P
a point mutant that blocks actin-binding is overexpressed in H1299 cells, the morphology of cells expressing the mutant and those of cells expressing green fluorescent protein do not show visible differences
R391A
-
0.5% of wild-type enzyme activity
R391D
-
inactive mutant
W188A
-
44% of wild-type enzyme activity
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
calpain inhibitors stabilize during purification
-
enzyme is more stable in Tris buffer than in potassium phosphate buffer
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 50 mM Tris-HCl, pH 7.5, 1 mM EGTA, 3 mM MgCl2, 1 mM DTT, 10% v/v glycerol, several months, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
4662fold
-
943fold
-
calmodulin-Sepharose affinity chromatography
-
His6-tagged fragment comprising residues 151-461 from Escherichia coli by nickel affinity chromatography, unlabeled or selenomethionine-labeled recombinant residues 185-459 of the catalytic domain of isozyme A fused to GST from Escherichia coli by glutathione affinity chromatography, removal of the GST-tag by recombinant TEV protease, further purification by a heparin affinity chromatography, and gel filtration
-
isoenzyme B
-
purification of GST-inositol 1,4,5-trisphosphate-3-kinase-A protein
Purification of IP3K isoform A is performed by phosphocellulose and calmodulin affinity chromatography.
Purification of IP3K isoform B is performed by phosphocellulose and calmodulin affinity chromatography.
recombinant isoenzyme A overexpressed in CHO cells
-
recombinant isozyme ITPKA from Escherichia coli strain BL21 by phosphocellulose chromatography and calmodulin affinity chromatography
recombinant wild-type or mutant fragments comprising the catalytic domain and the CaM binding domain of isozyme IP3K-A and IP3K-B from Escherichia coli strain BL21(DE3) by phosphocellulose and CaM affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding InsP3 3-kinase B is cloned from a hippocampus cDNA library and expressed in Escherichia coli, amino acid sequence
-
Cloning and expression of isoform A and of a fragment comprising the catalytic calmodulin binding domain (amino acids 165-462) in Escherichia coli BL21(DE3).
Cloning and expression of isoform B and of a fragment comprising the catalytic calmodulin binding domain (amino acids 165-462) in Escherichia coli BL21(DE3).
cloning and expression of the isoenzymes A, B and C in COS-7 cells, the 3 isoenzymes A, B and C can be distinguished by their localization on transfection in COS-7 cells
-
establishment of A549 or H1299 cells overexpressing the enzyme: the cDNA fragment encoding for ITPKAis cloned into the retroviral vector MigRI, for virus production this construct is co-transfected with SVgp (M57) and pHCMV-VSV-G (M75) into HEK293 phoenix ampho cells, after 48 h of incubation the supernatant containing the viruses is filtered and transferred to A549 or H1299 cells
expression of full length enzyme in Escherichia coli: a cDNA fragment encoding the full length form of ITPKA is inserted into the vector pGEX-4T-3 encoding a N-terminal Glutathione S-transferase-tag
expression of His6-tagged fragment comprising residues 151-461 in Escherichia coli, expression of wild-type and mutant cDNA fragments encoding for residues 187-461 of the catalytic domain of isozyme A as unlabeled or selenomethionine-labeled GST fusion proteins in Escherichia coli strains C41(DE3) and B834(DE3)
-
for stable knock-down of enzyme expression in MDA231 and H1299 cells a lentiviral transduction approach is employed
fusion protein of HsIP3K-C with an N-terminal EGFP tag (EGFP/HsIP3KC) is transiently expressed in NRK52E cells
-
gene IP3k2, quantitative real-time PCR expression analysis
gene Itpka
gene ITPKA, recombinant expression in Escherichia coli strain BL21
isoenzyme A is cloned and overexpressed in CHO cells
-
isozymes IP3K-A and IP3K-B, expression of a fragment comprising the catalytic domain and the CaM binding domain, residues 165-462 of isozyme A, of the wild-type and mutant isozyme A and isozyme B, respectively, in Escherichia coli strain BL21(DE3)
-
transient expression of isozyme B fragment 108-170 fused to EGFP in NRK 52E and PC12 cells co-localizes with F-actin, overexpression of isozyme B fused to EGFP in Escherichia coli, the enzyme co-localizes in with the cytoskeleton as well as with the endoplasmic reticulum and the plasma membrane, overexpression of inactive isozyme B lacking the F-actin target sequence at the noncatalytical N-terminus
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cancer cell lines show large differences in their enzyme levels: whereas SKBR-3 and T47D cells expressed very low enzyme levels, very high expression levels are found in the highly metastatic cell lines H1299, MDA231, and HepG2, most of the transformed cell lines (H1299, MDA231, Mevo, Jurkat T-cells, HEK293, HepG2) examined express increased levels of ITPKA compared to the low levels in non-transformed cells (IMR-90, HmEpc, HSF-14, leucocytes)
H1299 control and H1299 cells overexpressing inositol 1,4,5-trisphosphate-3-kinase-A (H1299-ITPKA) cells are injected subcutaneously in BALB/c severe combined immunodeficient SCID mice, high expression of ITPKA increases invasive migration in vitro and metastasis in a xenograft SCID mouse model, high expression of ITPKA during invasion of tumour cells from the primary tumour to the neighbouring tissue
in lung and breast cancer expression of ITPKA is stimulated by gene body methylation, ITPKA gene body methylation occurs early in tumor development
IP3K2 expression and Ca2+ entry are upregulated in osteosarcoma cells following treatment with chemotherapeutic drugs, e.g. doxorubicin and cisplatin
phenotypic consequences of enzyme expression in tumour cells: enzyme is stably knocked-downed in 2 cell lines with high enzyme expression levels (MDA231, H1299) and is stably overexpressed in low enzyme expressing A549 cells. MDA231, H1299 and A549-ITPKA cells show dramatically changed phenotypes compared with their respective control cells: highly metastatic MDA231 control cells migrate completely through the matrix and grow in an evenly scattered pattern, knock down variants grow as cell clusters inside the gelatin layer or adhered to the bottom of the culture dish in tight aggregates. Also H1299 control cells completely migrate through the gelatin. H1299 kd cells by contrast remain inside the gelatin matrix, forming tight aggregates of round cells. In cells with up-regulated enzyme expression, the opposite behaviour as in cells with low enzyme expression is observed. Most of the A549-ITPKA cells migrate through the gelatin layer and adhered to the bottom of the culture dish. Fewer A549 control cells migrated through the gelatin. Non-migrating cells remain in the matrix and cell clusters have a rounded morphology. To analyze the influence of enzyme on invasive migration, transwell migration assays are performed. Transwell migration of MDA231 kd cells is reduced by 73%, and that of H1299 kd cells by 58%, as compared to the respective control cells exhibiting high levels of enzyme. Approximately twice as many A549-ITPKA cells penetrate as A549 control cells (101%). A549-ITPKA cells show 2.5fold higher migration compared to control A549 cells, while migration of H1299 kd cells is reduced 3.4fold relative to H1299 control cells
the microRNA miR-140-5p inhibits IP3k2 expression in osteosarcoma cells via predicted 3'-UTR target sites and mRNA destabilization. Inhibiting IP3k2 protein expression promotes autophagy in response to anticancer drug treatment
Western blot analysis reveals that nontransformed cells express low (IMR-90, HSF-14) to nearly undetectable (HmEpc, leucocytes) levels of ITPKA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
in lung and breast cancer expression of ITPKA is stimulated by gene body methylation, ITPKA gene body methylation occurs early in tumor development. ITPKA enzyme expression may serve as biomarker for early detection of lung cancer
medicine
the actin bundling enzyme inositol-trisphosphate 3-kinase A (ITPKA) is a target in tumor therapy, because it is upregulated in tumor but not in corresponding normal cells. Downregulation of ITPKA in lung adenocarcinoma cancers reduced both, tumor growth and metastasis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Communi, D.; Vanweyenberg, V.; Erneux, C.
Purification and biochemical properties of a high-molecular-mass inositol 1,4,5-trisphosphate 3-kinase isoenzyme in human platelets
Biochem. J.
298
669-673
1994
Homo sapiens
-
Manually annotated by BRENDA team
Lin, A.; Wallace, R.W.; Barnes, S.
Purification and properties of a human platelet inositol 1,4,5-trisphosphate 3-kinase
Arch. Biochem. Biophys.
303
412-420
1993
Homo sapiens
Manually annotated by BRENDA team
Vanweyenberg, V.; Communi, D.; D'Santos, C.S.; Erneux, C.
Tissue- and cell-specific expression of Ins(1,4,5)P3 3-kinase isoenzymes
Biochem. J.
306
429-435
1995
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Irvine, R.F.; Schell, M.J.
Back in the water: The return of the inositol phosphates
Nat. Rev. Mol. Cell Biol.
2
327-338
2001
Homo sapiens, Mammalia
Manually annotated by BRENDA team
Dewaste, V.; Moreau, C.; De Smedt, F.; Bex, F.; De Smedt, H.; Wuytack, F.; Missiaen, L.; Erneux, C.
The three isoenzymes of human inositol-1,4,5-trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in COS-7 cells
Biochem. J.
374
41-49
2003
Homo sapiens
Manually annotated by BRENDA team
Communi, D.; Vanweyenberg, V.; Erneux, C.
D-myo-inositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calcium:calmodulin-dependent protein kinase II phosphorylation mechanism
EMBO J.
16
1943-1952
1997
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Communi, D.; Dewaste, V.; Erneux, C.
Calcium-calmodulin-dependent protein kinase II and protein kinase C-mediated phosphorylation and activation of D-myo-inositol 1,4, 5-trisphosphate 3-kinase B in astrocytes
J. Biol. Chem.
274
14734-14742
1999
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Brehm, M.A.; Schreiber, I.; Bertsch, U.; Wegner, A.; Mayr, G.W.
Identification of the actin-binding domain of Ins(1,4,5)P3 3-kinase isoform B (IP3K-B)
Biochem. J.
382
353-362
2004
Homo sapiens, Rattus norvegicus (P42335)
Manually annotated by BRENDA team
Xia, H.J.; Yang, G.
Inositol 1,4,5-trisphosphate 3-kinases: functions and regulations
Cell Res.
15
83-91
2005
Drosophila melanogaster, Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Mayr, G.W.; Windhorst, S.; Hillemeier, K.
Antiproliferative plant and synthetic polyphenolics are specific inhibitors of vertebrate inositol-1,4,5-trisphosphate 3-kinases and inositol polyphosphate multikinase
J. Biol. Chem.
280
13229-13240
2005
Gallus gallus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Gonzalez, B.; Schell, M.J.; Letcher, A.J.; Veprintsev, D.B.; Irvine, R.F.; Williams, R.L.
Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase
Mol. Cell
15
689-701
2004
Homo sapiens
Manually annotated by BRENDA team
Nalaskowski, M.M.; Windhorst, S.; Stockebrand, M.C.; Mayr, G.W.
Subcellular localisation of human inositol 1,4,5-trisphosphate 3-kinase C: species-specific use of alternative export sites for nucleo-cytoplasmic shuttling indicates divergent roles of the catalytic and N-terminal domains
Biol. Chem.
387
583-593
2006
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Mayr, G.W.; Windhorst, S.; Hillemeier, K.
Antiproliferative plant and synthetic polyphenolics are specific inhibitors of vertebrate inositol-1,4,5-trisphosphate 3-kinases and inositol polyphosphate multikinase. [Erratum to document cited in CA143:003106]
J. Biol. Chem.
282
35424
2007
Gallus gallus, Homo sapiens (P23677), Homo sapiens (P27987), Rattus norvegicus (Q80ZG2)
-
Manually annotated by BRENDA team
Windhorst, S.; Fliegert, R.; Blechner, C.; Mollmann, K.; Hosseini, Z.; Gunther, T.; Eiben, M.; Chang, L.; Lin, H.Y.; Fanick, W.; Schumacher, U.; Brandt, B.; Mayr, G.W.
Inositol-1,4,5-trisphosphate-3-kinase-A is a new cell motility-promoting protein that increases the metastatic potential of tumour cells by two functional activities
J. Biol. Chem.
285
5541-5554
2009
Homo sapiens (P23677), Homo sapiens
Manually annotated by BRENDA team
Windhorst, S.; Minge, D.; Baehring, R.; Hueser, S.; Schob, C.; Blechner, C.; Lin, H.Y.; Mayr, G.W.; Kindler, S.
Inositol-1,4,5-trisphosphate 3-kinase A regulates dendritic morphology and shapes synaptic Ca2+ transients
Cell. Signal.
24
750-757
2012
Homo sapiens (P23677)
Manually annotated by BRENDA team
Nalaskowski, M.M.; Fliegert, R.; Ernst, O.; Brehm, M.A.; Fanick, W.; Windhorst, S.; Lin, H.; Giehler, S.; Hein, J.; Lin, Y.N.; Mayr, G.W.
Human inositol 1,4,5-trisphosphate 3-kinase isoform B (IP3KB) is a nucleocytoplasmic shuttling protein specifically enriched at cortical actin filaments and at invaginations of the nuclear envelope
J. Biol. Chem.
286
4500-4510
2011
Homo sapiens (P27987), Homo sapiens
Manually annotated by BRENDA team
Erneux, C.; Ghosh, S.; Koenig, S.
Inositol(1,4,5)P3 3-kinase isoenzymes: catalytic properties and importance of targeting to F-actin to understand function
Adv. Biol. Regul.
60
135-143
2016
Homo sapiens (P23677), Homo sapiens (P27987), Homo sapiens (Q96DU7), Homo sapiens, Mus musculus (B2RXC2), Mus musculus (Q7TS72), Mus musculus (Q8R071), Mus musculus, Rattus norvegicus (P17105), Rattus norvegicus (P42335), Rattus norvegicus (Q80ZG2)
Manually annotated by BRENDA team
Schroeder, D.; Rehbach, C.; Seyffarth, C.; Neuenschwander, M.; Kries, J.V.; Windhorst, S.
Identification of a new membrane-permeable inhibitor against inositol-1,4,5-trisphosphate-3-kinase A
Biochem. Biophys. Res. Commun.
439
228-234
2013
Homo sapiens (P23677)
Manually annotated by BRENDA team
Franco-Echevarria, E.; Banos-Sanz, J.I.; Monterroso, B.; Round, A.; Sanz-Aparicio, J.; Gonzalez, B.
A new calmodulin-binding motif for inositol 1,4,5-trisphosphate 3-kinase regulation
Biochem. J.
463
319-328
2014
Homo sapiens (P23677), Homo sapiens
Manually annotated by BRENDA team
Stygelbout, V.; Leroy, K.; Pouillon, V.; Ando, K.; DAmico, E.; Jia, Y.; Luo, H.R.; Duyckaerts, C.; Erneux, C.; Schurmans, S.; Brion, J.P.
Inositol trisphosphate 3-kinase B is increased in human Alzheimer brain and exacerbates mouse Alzheimer pathology
Brain
137
537-552
2014
Homo sapiens (P27987), Homo sapiens, Mus musculus (B2RXC2), Mus musculus
Manually annotated by BRENDA team
Ashour, D.J.; Pelka, B.; Jaaks, P.; Wundenberg, T.; Blechner, C.; Zobiak, B.; Failla, A.V.; Windhorst, S.
The catalytic domain of inositol-1,4,5-trisphosphate 3-kinase-a contributes to ITPKA-induced modulation of F-actin
Cytoskeleton (Hoboken)
72
93-100
2015
Homo sapiens (P23677)
Manually annotated by BRENDA team
Windhorst, S.; Song, K.; Gazdar, A.F.
Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types
Biochem. Pharmacol.
137
1-9
2017
Homo sapiens (P23677), Homo sapiens, Mus musculus (Q8R071)
Manually annotated by BRENDA team
Wei, R.; Cao, G.; Deng, Z.; Su, J.; Cai, L.
miR-140-5p attenuates chemotherapeutic drug-induced cell death by regulating autophagy through inositol 1,4,5-trisphosphate kinase 2 (IP3k2) in human osteosarcoma cells
Biosci. Rep.
36
art:e00392
2016
Homo sapiens (P27987), Homo sapiens
Manually annotated by BRENDA team
Balabin, F.A.; Sveshnikova, A.N.
Computational biology analysis of platelet signaling reveals roles of feedbacks through phospholipase C and inositol 1,4,5-trisphosphate 3-kinase in controlling amplitude and duration of calcium oscillations
Mathr. Biosci.
276
67-74
2016
Homo sapiens
Manually annotated by BRENDA team