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Information on EC 2.7.1.153 - phosphatidylinositol-4,5-bisphosphate 3-kinase and Organism(s) Rattus norvegicus and UniProt Accession Q9Z1L0
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2.7.1.153 phosphatidylinositol-4,5-bisphosphate 3-kinaseIUBMB Comments
This enzyme also catalyses the phosphorylation of PtdIns4P to PtdIns(3,4)P2, and of PtdIns to PtdIns3P. Four mammalian isoforms are known to exist.
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Word Map
- 2.7.1.153
- wortmannin
- pten
- mapks
- mtor
- rapamycin
- endothelial
- erk
- colorectal
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signal-regulated
- subtypes
-
insulin-like
- pkc
- tumour
- adenocarcinoma
- phospholipase
- akt1
-
insulin-stimulated
- irs-1
- erbb2
-
mitogen
- adipocytes
- integrins
-
tensin
-
insulin-induced
- 3-kinases
-
dominant-negative
-
platelet-derived
-
hotspot
-
pi3k-akt
-
progression-free
- substrate-1
- igf-i
- sh2
-
ctnnb1
-
tyrosine-phosphorylated
-
phosphatidylinositol-3
-
pleckstrin
-
cdkn2a
- rac1
-
pi3k-dependent
-
her2-negative
- cetuximab
-
phosphatidylinositol-3-kinase
-
everolimus
-
anti-egfr
-
pdgfra
- trastuzumab
-
her2-positive
-
phospho-akt
-
endometrioid
- medicine
- pharmacology
- analysis
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pik3ca, phosphoinositide 3-kinase, pi 3-kinase, pi3-kinase, pi3-k, pi-3k, pik3r1, phosphatidylinositol 3'-kinase, p110alpha, pi 3-k, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
class I phosphoinositide 3-kinase
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-
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class I PI3K
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kinase (phosphorylating), phosphatidylinositol 4,5-diphosphate 3-
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p101-PI3K
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p110delta
P120-PI3K
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-
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phosphatidylinositol (4,5)-bisphosphate 3-hydroxykinase
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-
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phosphatidylinositol 3-hydroxyl kinase
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PI3K
PI3Kbeta
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-
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PI3Kgamma
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-
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PtdIns(4,5)P2 3-OH kinase
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-
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PtdIns-3-kinase p101
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PtdIns-3-kinase p110
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PtdInsP 3-OH-kinase
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type I phosphoinositide 3-kinase
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p110delta
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PI3K
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho-group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP:1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 3-phosphotransferase
This enzyme also catalyses the phosphorylation of PtdIns4P to PtdIns(3,4)P2, and of PtdIns to PtdIns3P. Four mammalian isoforms are known to exist.
CAS REGISTRY NUMBER
COMMENTARY
103843-30-7
-
115926-52-8
cf. EC 2.7.1.137
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
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-
-
-
?
additional information
?
-
-
a p110alpha/beta-subunit binds to a p85 regulatory subunit, and this heterodimer is recruited to the membrane through the association with phosphotyrosyl proteins, leading to production of phosphatidylinositol 3,4,5-triphosphate, PIP3, followed by activation of downstream signal pathway(s)
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-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
G-protein beta,gamma subunit
purified from bovine brain, 16fold activitation at 0.016 mM
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guanosine 5'-3-O-(thio)triphosphate
up to 3fold increase in activity, activation is blocked by high concentrations of guanosine-5-2-O-(thio)diphosphate
thrombin
activation of enzyme in intact cells, blocked by pertussis toxin
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cAMP
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PI 3-kinase is activated in response to cAMP or IGF-I, the PI 3-kinase activity bound to its p85 regulatory subunit increases by 1.7fold. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1
IGF-I
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PI 3-kinase is activated in response to cAMP or IGF-I. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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a pivotal region in reflex regulation of arterial pressure in the brain stem. Quantitative determination of expression levels of specific class I PI3K subunits, p85alpha, p85beta, p110alpha, p110beta, p110delta, and p110gamma, in the nucleus tractus solitarii of spontaneously hypertensive rats, overview
additional information
additional information
-
expression and platelet-derived growth factor beta receptor (betaPDGFR) binding of p110 isoforms in smooth muscle cells (SMCs), overview
additional information
expression and platelet-derived growth factor beta receptor (betaPDGFR) binding of p110 isoforms in smooth muscle cells (SMCs), overview
additional information
expression and platelet-derived growth factor beta receptor (betaPDGFR) binding of p110 isoforms in smooth muscle cells (SMCs), overview
additional information
-
expression and platelet-derived growth factor beta receptor (betaPDGFR) binding of p110 isoforms in smooth muscle cells (SMCs), overview
additional information
expression and platelet-derived growth factor beta receptor (betaPDGFR) binding of p110 isoforms in smooth muscle cells (SMCs), overview
additional information
expression and platelet-derived growth factor beta receptor (betaPDGFR) binding of p110 isoforms in smooth muscle cells (SMCs), overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
both nuclear membrane and soluble fraction, presence of an autonomous phosphoinositide 3-kinase cycle
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
class Ia phosphatidylinositol 3-kinase isoform p110beta is disensible for receptor tyrosine kinases signaling, not affecting proliferation, migration, and survival of smooth muscle cells
malfunction
physiological function
malfunction
-
chronic blockade of phosphatidylinositol 3-kinase in the nucleus tractus solitarii is prohypertensive in the spontaneously hypertensive rat
malfunction
p110delta deficiency did not affect vascular remodeling in vivo
physiological function
-
PI 3-kinase activated in response to cAMP or IGF-I stimulus plays important roles in increasing the translation rate or mRNA levels of cyclin D1, respectively. Activation of PI 3-kinase in response to cAMP or IGF-I are essential for marked increases in G1 CDK activities and DNA synthesis. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1
physiological function
class Ia phosphatidylinositol 3-kinase isoform p110alpha is crucial for receptor tyrosine kinases signaling, thus affecting proliferation, migration, and survival of smooth muscle cells, Receptor tyrosine kinasesinduced phosphatidylinositol 3'-kinase signaling via the p110alpha isoform plays a central role for vascular remodeling
physiological function
class Ia phosphatidylinositol 3-kinase isoform p110delta is disensible for receptor tyrosine kinases signaling, p110delta exerts noncatalytic functions in smooth muscle cell proliferation, but had no effect on migration
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PK3CB_RAT
1070
0
122608
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
1 * 110000, subunit p110, + 1 * 85000, subunit p85, class IA PI3K isoforms are heterodimers consisting of a catalytic subunit (p110beta) and a smaller regulatory subunit (p85)
heterodimer
heterodimer
-
a p110alpha/beta-subunit binds to a p85 regulatory subunit, and this heterodimer is recruited to the membrane through the association with phosphotyrosyl proteins, leading to production of phosphatidylinositol 3,4,5-triphosphate, PIP3, followed by activation of downstream signal pathway(s)
heterodimer
1 * 110000, subunit p110, + 1 * 85000, subunit p85, class IA PI3K isoforms are heterodimers consisting of a catalytic subunit (p110alpha) and a smaller regulatory subunit (p85)
heterodimer
1 * 110000, subunit p110, + 1 * 85000, subunit p85, class IA PI3K isoforms are heterodimers consisting of a catalytic subunit (p110delta) and a smaller regulatory subunit (p85)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
p110 subunit knockdown via specific siRNA application
additional information
p110 subunit knockdown via specific siRNA application
additional information
p110 subunit knockdown via specific siRNA application
additional information
-
p110 subunit knockdown via specific siRNA application
additional information
p110 subunit knockdown via specific siRNA application
additional information
p110 subunit knockdown via specific siRNA application
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme subunit isoform expression analysis in the nucleus tractus solitarii of the brain stem, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lu, P.J.; Hsu, A.L.; Wang, D.S.; Yan, H.Y.; Yin, H.L.; Chen, C.S.
Phosphoinositide 3-kinase in rat liver nuclei
Biochemistry
37
5738-5745
1998
Rattus norvegicus
Morris, A.J.; Rudge, S.A.; Mahlum, C.E.; Jenco.John, M.
Regulation of phosphoinositide-3-kinase by G protein bg subunits in a rat osteosarcoma cell line
Mol. Pharmacol.
48
532-539
1995
Rattus norvegicus (Q9Z1L0)
Fukushima, T.; Nedachi, T.; Akizawa, H.; Akahori, M.; Hakuno, F.; Takahashi, S.
Distinct modes of activation of phosphatidylinositol 3-kinase in response to cyclic adenosine 3',5'-monophosphate or insulin-like growth factor I play different roles in regulation of cyclin D1 and p27Kip1 in FRTL-5 cells
Endocrinology
149
3729-3742
2008
Rattus norvegicus
Zubcevic, J.; Waki, H.; Diez-Freire, C.; Gampel, A.; Raizada, M.K.; Paton, J.F.
Chronic blockade of phosphatidylinositol 3-kinase in the nucleus tractus solitarii is prohypertensive in the spontaneously hypertensive rat
Hypertension
53
97-103
2009
Rattus norvegicus
Vantler, M.; Jesus, J.; Leppaenen, O.; Scherner, M.; Berghausen, E.M.; Mustafov, L.; Chen, X.; Kramer, T.; Zierden, M.; Gerhardt, M.; Ten Freyhaus, H.; Blaschke, F.; Sterner-Kock, A.; Baldus, S.; Zhao, J.J.; Rosenkranz, S.
Class IA phosphatidylinositol 3-kinase isoform p110alpha mediates vascular remodeling
Arterioscler. Thromb. Vasc. Biol.
35
1434-1444
2015
Rattus norvegicus, Rattus norvegicus (A0A0G2K344), Rattus norvegicus (Q9Z1L0), Homo sapiens (O00329), Homo sapiens (P42336), Homo sapiens (P42338), Homo sapiens, Mus musculus (O35904), Mus musculus (P42337), Mus musculus
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