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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
additional information
?
-
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
r
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
regulatory mechanism of isoenzyme B involving phosphorylation by both protein kinase C and CaM kinase II
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
regulation mechanism of isoenzyme A involving CaM kinase II-mediated phosphorylation
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
role of the 3 isoforms as direct InsP3 metabolizing enzymes and direct regulators of Ca2+ responses to extracellular signals
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
regulation mechanism of isoenzyme A in brain involving CaM kinase II-mediated phosphorylation, role of Ins(1,4,5)P3 3-kinase in brain
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
key enzyme in inositol phosphate signaling pathway
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
the enzyme plays a key role in maintaining Ca2+ homeostasis by regulating the concentrations of 1D-myo-inositol 1,4,5-trisphosphate and 1D-myo-inositol 1,3,4,5-tetrakisphosphate, the enzyme has an important regulatory function in the inositol phosphate metabolism which is important for several cellular functions and signaling, overview
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
substrate and product binding site structure
-
-
?
additional information
?
-
-
the 3 isoenzymes A, B and C can be distinguished by their N-terminal sequence, sensitivity to Ca2+/calmodulin and localization on transfection in COS-7 cells
-
-
?
additional information
?
-
-
the enzyme might be involved in brain development, memory, and learning
-
-
?
additional information
?
-
-
the enzyme binds to F-actin in the cellular actin cytoskeleton with its F-actin domain at the N-terminus, the C-terminal fragment cannot bind to F-actin
-
-
?
additional information
?
-
ITPKA is a bifunctional protein; it phosphorylates Ins(1,4,5)P3 by its kinase activity and cross-links F-actin by its F-actin bundling activity
-
-
-
additional information
?
-
-
ITPKA is a bifunctional protein; it phosphorylates Ins(1,4,5)P3 by its kinase activity and cross-links F-actin by its F-actin bundling activity
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
additional information
?
-
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
r
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
regulatory mechanism of isoenzyme B involving phosphorylation by both protein kinase C and CaM kinase II
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
role of the 3 isoforms as direct InsP3 metabolizing enzymes and direct regulators of Ca2+ responses to extracellular signals
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
regulation mechanism of isoenzyme A in brain involving CaM kinase II-mediated phosphorylation, role of Ins(1,4,5)P3 3-kinase in brain
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
key enzyme in inositol phosphate signaling pathway
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
the enzyme plays a key role in maintaining Ca2+ homeostasis by regulating the concentrations of 1D-myo-inositol 1,4,5-trisphosphate and 1D-myo-inositol 1,3,4,5-tetrakisphosphate, the enzyme has an important regulatory function in the inositol phosphate metabolism which is important for several cellular functions and signaling, overview
-
-
?
additional information
?
-
-
the enzyme might be involved in brain development, memory, and learning
-
-
?
additional information
?
-
ITPKA is a bifunctional protein; it phosphorylates Ins(1,4,5)P3 by its kinase activity and cross-links F-actin by its F-actin bundling activity
-
-
-
additional information
?
-
-
ITPKA is a bifunctional protein; it phosphorylates Ins(1,4,5)P3 by its kinase activity and cross-links F-actin by its F-actin bundling activity
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Ca2+
-
at higher concentrations
EGTA
-
Ca2+/calmodulin-activated enzyme
epigallocatechin-3-gallate
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
3',4',7,8-tetrahydroxyflavone
-
3',4',7,8-tetrahydroxyflavone
-
inhibition of isozyme A, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
aurintricarboxylic acid
-
aurintricarboxylic acid
-
inhibition of isozyme A and isozyme B, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
ellagic acid
-
ellagic acid
-
inhibition of isozyme B, slight inhibition of isozyme A, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
epicatechin-3-gallate
-
epicatechin-3-gallate
-
slight inhibition of isozyme A and isozyme B, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
epigallocatechin-3-gallate
-
epigallocatechin-3-gallate
-
inhibition of isozyme A, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
gossypol
-
gossypol
-
inhibition of isozyme A and isozyme B, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
hypericin
-
hypericin
-
inhibition of isozyme A and isozyme B, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
KN-62
-
calmodulin-dependent protein kinase II inhibitor
KN-62
-
prevents the carbachol- or UTP-mediated activation
KN-93
-
calmodulin-dependent protein kinase II inhibitor
KN-93
-
prevents the carbachol- or UTP-mediated activation
myricetin
-
myricetin
-
inhibition of isozyme A, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
Protein kinase C
-
-
-
Protein kinase C
-
phosphorylates and inactivates enzyme
-
Protein kinase C
-
negative regulatory function, phosphorylates the enzyme at a serine residue
-
quercetin
-
quercetin
-
inhibition of isozyme A, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
Rose bengal
-
Rose bengal
-
slight inhibition of isozyme B, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
additional information
-
IC50 values, overiew, inhibitory potency of the synthetic and plant phenolics, no inhibition by chlorogenic acid
-
additional information
All inhibitors display a mixed-type inhibition with respect to ATP and a noncompetitive inhibition with respect to inositol-1,4,5-trisphosphate. Mutagenesis studies reveal that both the calmodulin binding and the ATP binding domains in IP3K are involved in inhibitor binding. Most discovered potent IP3K inhibitors exert antiproliferative effects on cultured cells in vitro or in animal experiments and tumor treatment studies in vivo.
-
additional information
All inhibitors display a mixed-type inhibition with respect to ATP and a noncompetitive inhibition with respect to inositol-1,4,5-trisphosphate. Mutagenesis studies reveal that both the calmodulin binding and the ATP binding domains in IP3K are involved in inhibitor binding. Most discovered potent IP3K inhibitors exert antiproliferative effects on cultured cells in vitro or in animal experiments and tumor treatment studies in vivo.
-
additional information
All inhibitors display a mixed-type inhibition with respect to ATP and a noncompetitive inhibition with respect to Ins(1,4,5)P3. Mutagenesis studies reveal that both the calmodulin binding and the ATP binding domains in IP3K are involved in inhibitor binding. Most discovered potent IP3K inhibitors exert antiproliferative effects on cultured cells in vitro or in animal experiments and tumor treatment studies in vivo.
-
additional information
All inhibitors display a mixed-type inhibition with respect to ATP and a noncompetitive inhibition with respect to Ins(1,4,5)P3. Mutagenesis studies reveal that both the calmodulin binding and the ATP binding domains in IP3K are involved in inhibitor binding. Most discovered potent IP3K inhibitors exert antiproliferative effects on cultured cells in vitro or in animal experiments and tumor treatment studies in vivo.
-
additional information
in order to inhibit the metastasis-promoting activity of ITPKA, both its actin bundling and its InsP3kinase activity has to be blocked, inhibitor library screening, overview
-
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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
-
cAMP-dependent protein kinase
-
i.e. PKA, activates the enzyme by phosphorylation at a serine residue
-
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
-
Calmodulin
-
2-3fold activation of isozyme IP33K-A and 7-8fold of isozyme IP33K-B, in a Ca2+-dependent manner, the binding site contains amphiphilic alpha-helices with cluster of positively charged and hydrophobic amino acids
Calmodulin
-
i.e. CaM, regulatory function, in concert with Ca2+
Calmodulin
the enzyme is activated by Ca2+/calmodulin. The human isozyme IP3-3K A contains a CaM binding domain at residues 158-183, binding structure and identification all of the key residues involved in the interaction, overview
Calmodulin
the enzyme is activated by Ca2+/calmodulin. The isozyme contains a CaM binding domain
Calmodulin
the enzyme is highly activated by Ca2+/calmodulin, ten to twentyfold increase in activity in human platelets. The isozyme contains a CaM binding domain
CaM kinase II
-
phosphorylation of isoenzyme B by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, no effect on the sensitivity to the Ca2+/calmodulin complex, CaM kinase II alone activates 35-40fold in the presence of Ca2+ and calmodulin
-
CaM kinase II
-
phosphorylation of Thr-311 results in 8-10fold enzyme activation in the presence of 0.01 mM free Ca2+ and 0.002 mM calmodulin and in a 25fold increase in sensitivity to the Ca2+/calmodulin complex
-
Carbachol
-
-
Carbachol
-
6-8fold okadaic acid-sensitive activation, maximal at 0.01 mM, isoform B, carbachol-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction
UTP
-
-
UTP
-
activation, recombinant isoenzyme A overexpressed in CHO cells
additional information
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
-
additional information
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
-
additional information
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
-
additional information
-
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
-
additional information
-
no activation by Triton X-100
-
additional information
-
isoenzyme B of 1321N1 cells is not activated by UTP
-
additional information
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
-
additional information
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
-
additional information
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
-
additional information
-
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
-
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Adenocarcinoma
Functional role of inositol-1,4,5-trisphosphate-3-kinase-A for motility of malignant transformed cells.
Adenocarcinoma of Lung
Functional role of inositol-1,4,5-trisphosphate-3-kinase-A for motility of malignant transformed cells.
Adenocarcinoma of Lung
Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types.
Adenocarcinoma of Lung
TFAP2A Induced ITPKA Serves as an Oncogene and Interacts with DBN1 in Lung Adenocarcinoma.
Alzheimer Disease
Inositol trisphosphate 3-kinase B is increased in human Alzheimer brain and exacerbates mouse Alzheimer pathology.
Alzheimer Disease
Microglia-Derived Extracellular Vesicles Carrying miR-711 Alleviate Neurodegeneration in a Murine Alzheimer's Disease Model by Binding to Itpkb.
Aneurysm
ITPKC functional polymorphism associated with Kawasaki disease susceptibility and formation of coronary artery aneurysms.
Aneurysm
ITPKC single nucleotide polymorphism associated with the Kawasaki disease in a Taiwanese population.
Aneurysm
Management of Kawasaki disease.
Aneurysm
Single-Nucleotide Polymorphism rs7251246 in ITPKC Is Associated with Susceptibility and Coronary Artery Lesions in Kawasaki Disease.
Arthritis
Inhibition of the Inositol Kinase Itpkb Augments Calcium Signaling in Lymphocytes and Reveals a Novel Strategy to Treat Autoimmune Disease.
Arthritis
Inositol 1,4,5-trisphosphate 3-kinase B promotes Ca2+ mobilization and the inflammatory activity of dendritic cells.
Autoimmune Diseases
Inhibition of the Inositol Kinase Itpkb Augments Calcium Signaling in Lymphocytes and Reveals a Novel Strategy to Treat Autoimmune Disease.
Breast Neoplasms
Expression Regulation of the Metastasis-Promoting Protein InsP3-Kinase-A in Tumor Cells.
Breast Neoplasms
Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types.
Breast Neoplasms
ITPKC as a Prognostic and Predictive Biomarker of Neoadjuvant Chemotherapy for Triple Negative Breast Cancer.
Breast Neoplasms
Relationship of ITPKA expression with the prognosis of breast cancer.
Carcinogenesis
Down-regulation of 1D-myo-inositol 1,4,5-trisphosphate 3-kinase A protein expression in oral squamous cell carcinoma.
Carcinogenesis
ITPKA Gene Body Methylation Regulates Gene Expression and Serves as an Early Diagnostic Marker in Lung and Other Cancers.
Carcinogenesis
ITPKA induces cell senescence, inhibits ovarian cancer tumorigenesis and can be downregulated by miR-203.
Carcinoma
Expression Regulation of the Metastasis-Promoting Protein InsP3-Kinase-A in Tumor Cells.
Carcinoma
Genetic polymorphisms in the ITPKC gene and cervical squamous cell carcinoma risk.
Carcinoma
ITPKA Gene Body Methylation Regulates Gene Expression and Serves as an Early Diagnostic Marker in Lung and Other Cancers.
Carcinoma
The Expression of miR-375 Is Associated with Carcinogenesis in Three Subtypes of Lung Cancer.
Carcinoma
The new InsP3Kinase inhibitor BIP-4 is competitive to InsP3 and blocks proliferation and adhesion of lung cancer cells.
Carcinoma, Hepatocellular
ITPKA expression is a novel prognostic factor in hepatocellular carcinoma.
Carcinoma, Squamous Cell
Genetic polymorphisms in the ITPKC gene and cervical squamous cell carcinoma risk.
Colorectal Neoplasms
Immune-related genes STIM1, ITPKC and PELI1 polymorphisms are associated with risk of colorectal cancer.
Common Variable Immunodeficiency
Common variable immunodeficiency associated with microdeletion of chromosome 1q42.1-q42.3 and inositol 1,4,5-trisphosphate kinase B (ITPKB) deficiency.
Erythema
ITPKC and SLC11A1 Gene Polymorphisms and Gene-Gene Interactions in Korean Patients with Kawasaki Disease.
Glioma
Mining the glioma susceptibility genes in children from gene expression profiles and a methylation database.
Graft vs Host Disease
Inhibition of inositol kinase B controls acute and chronic graft-versus-host disease.
Hirschsprung Disease
Potential association between ITPKC genetic variations and Hirschsprung disease.
Hodgkin Disease
Diagnostic utility of STAT6YE361 expression in classical Hodgkin lymphoma and related entities.
Immune System Diseases
New therapeutic targets in immune disorders: ItpkB, Orai1 and UNC93B.
Influenza, Human
Identification of Host Kinase Genes Required for Influenza Virus Replication and the Regulatory Role of MicroRNAs.
inositol-trisphosphate 3-kinase deficiency
Tonic BCR signaling represses receptor editing via Raf- and calcium-dependent signaling pathways.
Lung Neoplasms
Effect of the actin- and calcium-regulating activities of ITPKB on the metastatic potential of lung cancer cells.
Lung Neoplasms
Functional role of inositol-1,4,5-trisphosphate-3-kinase-A for motility of malignant transformed cells.
Lung Neoplasms
Identification of a new membrane-permeable inhibitor against inositol-1,4,5-trisphosphate-3-kinase A.
Lung Neoplasms
Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types.
Lung Neoplasms
ITPKA Gene Body Methylation Regulates Gene Expression and Serves as an Early Diagnostic Marker in Lung and Other Cancers.
Lung Neoplasms
TFAP2A Induced ITPKA Serves as an Oncogene and Interacts with DBN1 in Lung Adenocarcinoma.
Lung Neoplasms
The new InsP3Kinase inhibitor BIP-4 is competitive to InsP3 and blocks proliferation and adhesion of lung cancer cells.
Lymphatic Metastasis
Relationship of ITPKA expression with the prognosis of breast cancer.
Mucocutaneous Lymph Node Syndrome
A functional polymorphism, rs28493229, in ITPKC and risk of Kawasaki disease: an integrated meta-analysis.
Mucocutaneous Lymph Node Syndrome
A replication study for association of ITPKC and CASP3 two-locus analysis in IVIG unresponsiveness and coronary artery lesion in Kawasaki disease.
Mucocutaneous Lymph Node Syndrome
Clinical Implication of the C Allele of the ITPKC Gene SNP rs28493229 in Kawasaki Disease: Association With Disease Susceptibility and BCG Scar Reactivation.
Mucocutaneous Lymph Node Syndrome
ITPKC and CASP3 polymorphisms and risks for IVIG unresponsiveness and coronary artery lesion formation in Kawasaki disease.
Mucocutaneous Lymph Node Syndrome
ITPKC and SLC11A1 Gene Polymorphisms and Gene-Gene Interactions in Korean Patients with Kawasaki Disease.
Mucocutaneous Lymph Node Syndrome
ITPKC as a Prognostic and Predictive Biomarker of Neoadjuvant Chemotherapy for Triple Negative Breast Cancer.
Mucocutaneous Lymph Node Syndrome
ITPKC functional polymorphism associated with Kawasaki disease susceptibility and formation of coronary artery aneurysms.
Mucocutaneous Lymph Node Syndrome
ITPKC gene SNP rs28493229 and Kawasaki disease in Taiwanese children.
Mucocutaneous Lymph Node Syndrome
ITPKC single nucleotide polymorphism associated with the Kawasaki disease in a Taiwanese population.
Mucocutaneous Lymph Node Syndrome
ITPKC susceptibility in Kawasaki syndrome as a sensitizing factor for autoimmunity and coronary arterial wall relaxation induced by thimerosal's effects on calcium signaling via IP3.
Mucocutaneous Lymph Node Syndrome
Kawasaki disease: update on pathogenesis.
Mucocutaneous Lymph Node Syndrome
PPP3CC feedback regulates IP3-Ca2+ pathway through preventing ITPKC degradation.
Mucocutaneous Lymph Node Syndrome
Single-nucleotide Polymorphism rs2290692 in the 3'UTR of ITPKC Associated With Susceptibility to Kawasaki Disease in a Han Chinese Population.
Mucocutaneous Lymph Node Syndrome
Single-Nucleotide Polymorphism rs7251246 in ITPKC Is Associated with Susceptibility and Coronary Artery Lesions in Kawasaki Disease.
Mucocutaneous Lymph Node Syndrome
Superantigen involvement and susceptibility factors in Kawasaki disease: profiles of TCR V?2+ T cells and HLA-DRB1, TNF-? and ITPKC genes among Filipino patients.
Mucocutaneous Lymph Node Syndrome
[Association study of a functional SNP rs28493229 of ITPKC gene and Kawasaki disease in a Chinese population].
Neoplasm Metastasis
Inositol 1,4,5-trisphosphate 3-kinase-A is a new cell motility-promoting protein that increases the metastatic potential of tumor cells by two functional activities.
Neoplasm Metastasis
Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types.
Neoplasm Metastasis
Relationship of ITPKA expression with the prognosis of breast cancer.
Neoplasms
DNA methylation profiling in nonfunctioning pituitary adenomas.
Neoplasms
Effect of the actin- and calcium-regulating activities of ITPKB on the metastatic potential of lung cancer cells.
Neoplasms
Expression Regulation of the Metastasis-Promoting Protein InsP3-Kinase-A in Tumor Cells.
Neoplasms
Functional role of inositol-1,4,5-trisphosphate-3-kinase-A for motility of malignant transformed cells.
Neoplasms
Identification of a new membrane-permeable inhibitor against inositol-1,4,5-trisphosphate-3-kinase A.
Neoplasms
Inositol 1,4,5-trisphosphate 3-kinase-A is a new cell motility-promoting protein that increases the metastatic potential of tumor cells by two functional activities.
Neoplasms
Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types.
Neoplasms
Inositol-triphosphate 3-kinase B confers cisplatin resistance by regulating NOX4-dependent redox balance.
Neoplasms
ITPKA expression is a novel prognostic factor in hepatocellular carcinoma.
Neoplasms
ITPKA Gene Body Methylation Regulates Gene Expression and Serves as an Early Diagnostic Marker in Lung and Other Cancers.
Neoplasms
ITPKA induces cell senescence, inhibits ovarian cancer tumorigenesis and can be downregulated by miR-203.
Neoplasms
ITPKA1 Promotes Growth, Migration and Invasion of Renal Cell Carcinoma via Activation of mTOR Signaling Pathway.
Neoplasms
ITPKC as a Prognostic and Predictive Biomarker of Neoadjuvant Chemotherapy for Triple Negative Breast Cancer.
Neoplasms
Pervasive mutations of JAK-STAT pathway genes in classical Hodgkin lymphoma.
Neoplasms
Physiological relevance of the neuronal isoform of inositol-1,4,5-trisphosphate 3-kinases in mice.
Neoplasms
Relationship of ITPKA expression with the prognosis of breast cancer.
Neoplasms
TFAP2A Induced ITPKA Serves as an Oncogene and Interacts with DBN1 in Lung Adenocarcinoma.
Neoplasms
The catalytic domain of inositol-1,4,5-trisphosphate 3-kinase-a contributes to ITPKA-induced modulation of F-actin.
Neoplasms
The new InsP3Kinase inhibitor BIP-4 is competitive to InsP3 and blocks proliferation and adhesion of lung cancer cells.
Nephrolithiasis
Study of the association between ITPKC genetic polymorphisms and calcium nephrolithiasis.
Neuroblastoma
Inositol trisphosphate 3-kinase B is increased in human Alzheimer brain and exacerbates mouse Alzheimer pathology.
Neuroblastoma
Tissue- and cell-specific expression of Ins(1,4,5)P3 3-kinase isoenzymes.
Osteosarcoma
miR-140-5p attenuates chemotherapeutic drug induced cell death by regulating autophagy through IP3k2 in human osteosarcoma cells.
Ovarian Neoplasms
ITPKA induces cell senescence, inhibits ovarian cancer tumorigenesis and can be downregulated by miR-203.
Parkinson Disease
Association of ITPKB, IL1R2 and COQ7 with Parkinson's disease in Taiwan.
Parkinson Disease
Association of ZNF184, IL1R2, LRRK2, ITPKB, and PARK16 with sporadic Parkinson's disease in Eastern China.
Parkinson Disease
ITPKB and ZNF184 are associated with Parkinson's disease risk in East Asians.
Parkinson Disease
The Parkinson's disease-associated gene ITPKB protects against ?-synuclein aggregation by regulating ER-to-mitochondria calcium release.
Severe Combined Immunodeficiency
Severe combined immunodeficiency caused by inositol-trisphosphate 3-kinase B (ITPKB) deficiency.
Small Cell Lung Carcinoma
The Expression of miR-375 Is Associated with Carcinogenesis in Three Subtypes of Lung Cancer.
Triple Negative Breast Neoplasms
ITPKC as a Prognostic and Predictive Biomarker of Neoadjuvant Chemotherapy for Triple Negative Breast Cancer.
Uterine Cervical Neoplasms
Genetic polymorphisms in the ITPKC gene and cervical squamous cell carcinoma risk.
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cloning and expression in Escherichia coli
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Itpkb protein level is increased upon differentiation of human embryonic stem cells
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human glioma cell line HTB-138, InsP3 3-kinase B mRNA
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non-differentiated promyelocytic-leukaemia cell line, InsP3 3-kinase B mRNA
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human cell line SH-SY5Y, InsP3 3-kinase B mRNA
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1321N1 cells, isoform B
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isoenzyme A is the major isoform present in neuronal cells
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IP3K-A
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Itpka is particularly active in neurons of the hippocampus and cerebellum
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Itpkb protein level is increased in the cerebral cortex of most patients with Alzheimer's disease compared with control subjects
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high expression level in pyramidal neurons of the CA1 region and the dentate gyrus of the hippocampus
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high expression
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hippocampal neuron
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localized to the post-dendritic spines of neurons. Itpka is particularly active in neurons of the hippocampus and cerebellum
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neuron-specific isozyme
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pyramidal, in neurons, ITPKA is concentrated at postsynaptic densities (PSD) of hippocampal dendritic spines
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IP3K-A is identified mainly in brain and testis and shows an exclusive F-actin localization
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
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enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
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isoenzymes A and B are specifically expressed in different tissues and cells, expression pattern
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additional information
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isoenzyme C is not found in brain
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine
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additional information
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enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
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enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
ITPKA is expressed in a broad range of tumor types but shows limited expression in normal cells. ITPKA enzyme expression analysis, overview
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additional information
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ITPKA is expressed in a broad range of tumor types but shows limited expression in normal cells. ITPKA enzyme expression analysis, overview
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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
downregulation of ITPKA in lung adenocarcinoma cancers reduced both, tumor growth and metastasis. Re-expression of wild-type ITPKA completely restores reduced transmigration of ITPKA-depleted cells. Combined inhibition of F-actin bundling and InsP3Kinase activity should inhibit metastasis at early (adhesion, invasion) and late steps (colonization at secondary sites) of metastasis. Inhibition of cellular InsP3Kinase by BIP-4 reduces important steps in the metastatic cascade
malfunction
the expression of microRNA-140, termed miR-140-5p, is highly induced during chemotherapy of osteosarcoma cells accompanied by upregulated autophagy. The increased miR-140-5p expression levels upregulate anticancer drug-induced autophagy in osteosarcoma cells and ameliorate the anticancer drug-induced cell proliferation and viability decrease. miR-140-5p regulates this context-specific autophagy through its target, inositol 1,4,5-trisphosphate kinase 2 (IP3k2). miR-140-5p mediated drug-resistance in osteosarcoma cells occurs by inducing autophagy, and miRNA regulation of autophagy through modulation of IP3 signalling. IP3K2 expression and Ca2+ entry are upregulated in osteosarcoma cells following treatment with chemotherapeutic drugs
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
metabolism
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main mechanisms of platelet calcium signaling implemented in the model. The model includes two main compartments: cytosol and dense tubular system (DTS). Thrombin binding to PAR1 receptor leads to phospholipase C (PLC) activation and inositol-3-phosphate (IP3) release into cytosol. IP3 binding to its receptors (IP3R) in the DTS membrane opens this channels for release of calcium that is normally contained in the DTS because of the SERCA pump action. Cytosolic IP3 is being phosphorylated by inositol triphosphate-kinase (IP3K) into IP4 that might be included in the phosphoinositide turnover. Two feedback loops: a PLC-dependent positive feedback loop and the IP3K-dependent negative loop. System modeling, overview
physiological function
inositol-1,4,5-trisphosphate-3-kinase-A is a cell motility-promoting protein that increases the metastatic potential of tumour cells by 2 functional activities: it promotes migration of tumour cells by 2 different mechanisms: growth factor independently, high levels of inositol-1,4,5-trisphosphate-3-kinase-A induce the formation of large cellular protrusions by directly modulating the actin cytoskeleton, the F-actin binding activity of inositol-1,4,5-trisphosphate-3-kinase-A stabilizes and bundles actin filaments and thus increases the levels of cellular F-actin, in growth factor stimulated cells, the catalytically active domain enhances basal inositol-1,4,5-trisphosphate-3-kinase-A induced migration by activating store-operated calcium entry through production of inositol-1,3,4,5-tetrakisphosphate and subsequent inhibition of inositol-phosphate-5-phosphatase
physiological function
isoform inositol 1,4,5-trisphosphate 3-kinase A is ectopically expressed in different human tumor cell lines and during tumor progression in the metastatic tumor model Balb-neuT. High expression of isoform 1,4,5-trisphosphate 3-kinase A increases invasive migration in vitro and metastasis in a xenograft SCID mouse model. 1,4,5-Trisphosphate 3-kinase A promotes migration of tumor cells by two different mechanisms: growth factor independently high levels of enzyme induce the formation of large cellular protrusions by directly modulating the actin cytoskeleton. The F-actin binding activity of 1,4,5-trisphosphate 3-kinase A stabilizes and bundles actin filaments and thus increases the levels of cellular F-actin. In growth factor-stimulated cells, the catalytically active domain enhances basal 1,4,5-trisphosphate 3-kinase A-induced migration by activating store-operated calcium entry through production of inositol 1,3,4,5-tetrakisphosphate and subsequent inhibition of inositol phosphate 5-phosphatase
physiological function
overexpression of isoform inositol-1,4,5-trisphosphate 3-kinase A increases the number of dendritic protrusions by 71% in immature primary neurons. In mature neurons, the effect of inositol-1,4,5-trisphosphate 3-kinase A overexpression on formation of dendritic spines is weaker and depletion of the enzyme does not alter spine density and synaptic contacts. In synaptosomes of mature neurons, enzyme loss results in decreased duration of Ins(1,4,5)P3 signals and shorter Ins(1,4,5)P3-dependent Ca2+ transients. At synapses of inositol-1,4,5-trisphosphate 3-kinase A deficient neurons the levels of Ins(1,4,5)P3-5-phosphatase and sarcoplasmic/endoplasmic reticulum calcium ATPase pump-2b are increased
physiological function
1D-myo-inositol 1,4,5-trisphosphate is a key point in Ca2+ metabolism that promotes Ca2+ release from intracellular stores and together with 1D-myo-inositol 1,3,4,5-tetrakisphosphate regulates Ca2+ homoeostasis. In addition, 1D-myo-inositol 1,3,4,5-tetrakisphosphate is involved in immune cell development. Ca2+ and calmodulin regulate the activity of inositol(1,4,5)trisphosphate 3-kinases via direct interaction
physiological function
ectopic expression of the neuron-specific inositol-1,4,5-trisphosphate-3-kinase A in lung cancer cells increases their metastatic potential because the protein exhibits two actin regulating activities. The isozyme ITPKA bundles actin filaments and regulates inositol-1,4,5-trisphosphate (InsP3)-mediated calcium signals by phosphorylating InsP3
physiological function
in natural killer (NK) cells, isozyme Itpkb promotes NK-cell terminal maturation but limits NK-cell effector functions
physiological function
isozyme Itpka contains an F-actin binding site at the N-terminal part that confers to Itpka the properties of an F-actin bundling protein with two major consequences: it can reorganize the cytoskeletal network, particularly in dendritic spines, and it can provide an opportunity for Ins(1,3,4,5)P4 to act very locally as second messenger. Isozyme Itpka is an F-actin bundling protein regulating dendritic spines structural plasticity and a scaffold protein for synaptic rac signaling, Itpka overexpression induces cytoskeletal reorganization, high expression of Itpka in cancer cells increases invasion and migration in vitro
physiological function
isozyme ITPKA induces formation of complex actin networks, but exibits only one N-terminal actin binding domain, the C-terminus of ITPKA acts as spacer between actin filaments, overview. ITPKA induces the formation of a dense network of branched actin filaments, not of linear filaments. Overexpression of ITPKA induces the formation of lamellipodia-like protrusions which consist of cross-linked actin filaments. 1D-myo-inositol 1,3,4,5-tetrakisphosphate inhibits actin polymerization, but does not show a significant effect on bundling activity of ITPKA, while binding of ITPKA to actin stimulates inositol-1,4,5-trisphosphate 3-kinase-a activity
physiological function
among the ITPK-isoforms ITPKA is the most specialized one. In cells it is exclusively bound to F-actin resulting in cross-linking of actin filaments. ITPKA has two very distinct functions, regulating both, calcium signaling and actin dynamics. Isoform A of ITPK is an oncogene, it is involved in cancer progression, tumor growth is stimulated by the InsP3Kinase activity of ITPKA and metastasis by its actin bundling activity. ITPKA regulates actin dynamics by binding with its homodimeric N-terminal actin binding domain (ABD) to F-actin. The bulky C-terminus, which includes the InsP3Kinase-domain, acts as spacer between actin filaments resulting in formation of loose networks of F-actin bundles. Cellular calcium signals are regulated by the InsP3Kinase activity of ITPKA. Calcium is an ubiquitous second messenger that is involved in many signal transduction pathways, including protein kinase C and CAMKII signaling. ITPKA phosphorylates the calcium-mobilizing second messenger Ins(1,4,5)P3 at 3'-position, thereby producing Ins(1,3,4,5)P4. Since the Ins(1,4,5)P3 loop binds Ins(1,4,5)P3 with high affinity, but no other InsP-isomers or phosphatidylinositol phosphates, ITPKA is a highly specialized enzyme. Ins(1,3,4,5)P4 is substantially involved in the control of Ins(1,4,5)P3-mediated calcium release. The (1,4,5)P3 phosphatase INPP5A binds Ins(1,3,4,5)P4 with tenfold higher affinity than Ins(1,4,5)P3, resulting in decreased (1,4,5)P3 dephosphorylation. Therefore, production of Ins (1,3,4,5)P4 increases half-life of Ins(1,4,5)P3, thus Ins(1,4,5)P3-mediated calcium release from the endoplasmic reticulum. Based on this property, in the absence of ITPKA calcium release is shortened and calcium-induced calcium entry abrogated. ITPKA is involved in both, the control of calcium signals and the control of dendritic spine morphology. ITPKA belongs to the invasive signature of p130Cas/ErbB2 transformed breast cancer cells showing that in different tumor entities expression of ITPKA is associated with malignancy of tumor cells. Regulation of ITPKA expression in tumor cells, overview
physiological function
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analysis of the roles of feedbacks through phospholipase C and inositol 1,4,5-trisphosphate 3-kinase (IP3K) by means of a computer model of calcium signal transduction in platelets
additional information
ITPKC functional polymorphism associates with Kawasaki disease susceptibility
additional information
ITPKC functional polymorphism associates with Kawasaki disease susceptibility
additional information
ITPKC functional polymorphism associates with Kawasaki disease susceptibility
additional information
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ITPKC functional polymorphism associates with Kawasaki disease susceptibility
additional information
isozyme Itpkb contains an F-actin binding site at the N-terminal part
additional information
isozyme Itpkb contains an F-actin binding site at the N-terminal part
additional information
isozyme Itpkb contains an F-actin binding site at the N-terminal part
additional information
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isozyme Itpkb contains an F-actin binding site at the N-terminal part
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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
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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
brenda
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
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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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
-
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda