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Information on EC 2.7.1.68 - 1-phosphatidylinositol-4-phosphate 5-kinase and Organism(s) Rattus norvegicus
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2.7.1.68 1-phosphatidylinositol-4-phosphate 5-kinaseIUBMB Comments
This enzyme can also phosphorylate PtdIns3P in the 4-position, and PtdIns, PtdIns3P and PtdIns(3,4)P2 in the 5-position in vitro, but to a lesser extent. The last of these reactions occurs in vivo and is physiologically relevant. Three different isoforms are known.
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Word Map
- 2.7.1.68
- 4,5-bisphosphate
- phosphoinositide
- fracture
- pip2
- actin
- femoral
- phospholipase
-
ptdins4,5p2
- phospholipid
- cytoskeleton
- dislocation
- phosphatidylinositol-4,5-bisphosphate
-
phosphatidic
-
posterior
- gtpases
- diacylglycerol
-
4-kinase
-
polyphosphoinositides
-
acetabular
-
accident
-
ossification
- talin
-
avascular
- rac1
-
fracture-dislocation
- bisphosphate
-
screw
- arf6
-
5-phosphatase
-
heterotopic
-
arthroplasty
- 3,4,5-trisphosphate
-
ptdins5p
-
trochanteric
-
ovcar-5
- osteonecrosis
-
inositide
-
osteotomy
-
kinase-dead
-
osteochondral
- tiazofurin
-
3hinositol
-
insps
-
merle
-
ptdins3,4,5p3
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
pipkin, pip5k, pip kinase, ptdinsp, phosphatidylinositol 4-phosphate 5-kinase, phosphatidylinositol-4-phosphate 5-kinase, pipk, pipkigamma, pip5ks, pip5k1a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Diphosphoinositide kinase
-
-
-
-
MSS4p
-
-
-
-
phosphatidylinositol 4-phosphate kinase
-
-
-
-
phosphatidylinositol-4-phosphate 5-kinase
-
-
-
-
PI4P 5-kinase
-
-
-
-
PI4P5K
-
-
-
-
PIP kinase
-
-
-
-
PIP-5kin
-
-
-
-
PIP5K
-
-
-
-
PIP5Ks
-
-
-
-
PtdIns(4)P 5-kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 5-phosphotransferase
This enzyme can also phosphorylate PtdIns3P in the 4-position, and PtdIns, PtdIns3P and PtdIns(3,4)P2 in the 5-position in vitro, but to a lesser extent. The last of these reactions occurs in vivo and is physiologically relevant. Three different isoforms are known.
CAS REGISTRY NUMBER
COMMENTARY
104645-76-3
-
9032-61-5
-
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-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
GTP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
GDP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
50% of the activity with ATP
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
641773, 641822, 641824, 641828, 641829, 641830, 641831, 641833, 641850, 641852, 660641, 660965, 675006, 676808, 738176
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate has several important physiological functions, overview
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
the enzyme from liver membrane is possible regulated by a G-protein
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
the enzyme form PIPKIgamma may cooperate with synaptojanin in the regulation of actin and synaptic vesicle traffic
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-bisphosphate synthesis in the Golgi compartment
-
-
?
additional information
?
-
-
ARF6-dependent enzyme activation plays an important role in signal transduction of membrane ruffling formation through 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
?
additional information
?
-
-
splicing form a of the isozyme gamma is inactive, splicing form c is involved in maintenance of some neuronal cellular processes
-
-
?
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-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate has several important physiological functions, overview
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
the enzyme from liver membrane is possible regulated by a G-protein
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
the enzyme form PIPKIgamma may cooperate with synaptojanin in the regulation of actin and synaptic vesicle traffic
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-bisphosphate synthesis in the Golgi compartment
-
-
?
additional information
?
-
-
ARF6-dependent enzyme activation plays an important role in signal transduction of membrane ruffling formation through 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
?
additional information
?
-
-
splicing form a of the isozyme gamma is inactive, splicing form c is involved in maintenance of some neuronal cellular processes
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heparin
-
IC50: 0.002 mg/ml, competitive towards 1-phosphatidyl-1D-myo-inositol 4-phosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Acetylcholine
-
0.01 mM or 0.1 mM, each in presence of 0.1 mM eserine, stimulates the enzyme in homogenates by 30-40%
AP-2mu-endocytic cargo complex
-
clathrin adaptor complex, leads to a potent stimulation of PIPK activity
-
myelin basic protein
-
enhances activity when phosphatidylinositol 4-phosphate/phosphatidylethanolamine vesicles are used as substrate
-
small G proteins ARF
-
ARF activation absolutely requires the presence of phosphatidic acid, which cannot be substituted by phosphatidylserine, phosphatidylethanolamine, or lysophosphatidic acid, but by competitive phosphatidylcholine
-
spermine
-
enhances activity severalfold. Causes a shift in the MgCl2 saturation curve from sigmoidal to hyperbolic, lowering the Mg2+ concentration required for optimum kinase activity to the physiological range. 0.6 mM, 4fold increase of phosphorylation activity in phosphatidylinositol/phosphatidylethanolamine vesicles
spermine
-
1 mM, 3fold stimulation. Stimulation decreases to half at physiological ionic strength and is not affected appreciably by variations in the concentration of ATP and MgCl2
spermine
-
strong activation in presence of micromolar concentrations, at 2 mM Mg2+ optimal spermine concentration is 0.1-0.2 mM spermine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km-value for 1-phosphatidyl-1D-myo-inositol 4-phosphate is 0.0033 mg/ml
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
pH 5.0: about 65% of maximal activity, pH 8.0: about 75% of maximal activity
6.1 - 7.9
-
pH 6.1: about 85% of maximal activity, pH 7.9: about 85% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
641773, 641822, 641824, 641828, 641829, 641830, 641831, 641833, 641850, 641852, 675006, 676808, 721497, 738176
-
-
type I phosphatidylinositol 4-phosphate 5-kinase isozyme gamma, 3 splicing forms a-c
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in the pyramidal cells of the hippocampus and of the cerebral cortex, splicing form c of isozyme gamma is neuronal-specific
-
phosphatidylinositol 4-phosphate 5-kinase Igamma_v6 splice variant
additional information
-
PIP5KIgamma_v6 tissue expression pattern, overview
-
phosphatidylinositol 4-phosphate 5-kinase Igamma_v6 is not a major brain variant
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
translocation to the plasma membrane of isozyme alpha is dependent on ARF6 and EGF
-
phosphatidylinositol 4-phosphate 5-kinase Igamma_v6 splice variant
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
enzyme PIP5Kalpha acts as a negative regulator of nerve growth factor-induced neurite outgrowth by inhibiting phosphatidylinositol 3-kinase/Akt signaling pathway in PC-12 cells
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). PI51A_RAT
546
0
60605
Swiss-Prot
other Location (Reliability: 3)
PI51B_RAT
539
0
60733
Swiss-Prot
other Location (Reliability: 1)
PI51C_RAT
688
0
75594
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme possesses a central socalled kinase core domain containing the activation loop which is responsible for substrate specificity and subcellular targeting of the enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D316K
-
site-directed mutagenesis, overexpression of the catalytically inactive construct of isozyme gamma splicing form c in rat cerebellar granule cells causes progressive loss of their neuronal processes, not observed with expression of isozyme gamma splicing form a
K188A
-
site-directed mutagenesis, overexpression of the catalytically inactive construct of isozyme gamma splicing form c in rat cerebellar granule cells causes progressive loss of their neuronal processes, not observed with expression of isozyme gamma splicing form a
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant isozyme gamma, partially by immunoprecipitation and protein G affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of splice variant phosphatidylinositol 4-phosphate 5-kinase Igamma_v6 from hippocampus, expression in COS-7 cells
-
identification of splicing form c of type I phosphatidylinositol 4-phosphate 5-kinase isoform gamma possessing additional 26 amino acids at the C-terminus from a hippocampus library, DNA and amino acid sequence determination and analysis, overvexpression of the catalytically inactive mutants D316K and K188A of isozyme gamma splicing form c in rat cerebellar granule cells, expression of isozyme gamma splicing form a, expression of wild-type and FLAG-tagged isozyme gamma splicing form c in COS-7 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cooper, P.H.; Hawthorne, J.N.
Phosphatidylinositol kinase and diphosphoinositide kinase of rat kidney cortex: properties and subcellular localization
Biochem. J.
160
97-105
1976
Rattus norvegicus
Kai, M.; Salway, J.G.; Hawthorne, J.N.
The diphosphoinositide kinase of rat brain
Biochem. J.
106
791-801
1968
Rattus norvegicus
Smith, P.M.; Wreggett, K.A.; Irvine, R.F.
The phosphatidylinositol 4-phosphate kinase of rat brain and human platelets
Biochem. Soc. Trans.
14
1145-1146
1986
Homo sapiens, Rattus norvegicus
-
Lundberg, G.A.; Sundler, R.; Jergil, B.
Activation of phosphatidylinositol-4-phosphate kinase in rat liver plasma membranes by polyamines
Biochim. Biophys. Acta
922
1-7
1987
Rattus norvegicus
Cochet, C.; Chambaz, E.M.
Catalytic properties of a purified phosphatidylinositol-4-phosphate kinase from rat brain
Biochem. J.
237
25-31
1986
Rattus norvegicus
Lundberg, G.A.; Jergil, B.; Sundler, R.
Phosphatidylinositol-4-phosphate kinase from rat brain. Activation by polyamines and inhibition by phosphatidylinositol 4,5-bisphosphate
Eur. J. Biochem.
161
257-262
1986
Rattus norvegicus
Urumow, T.; Wieland, O.H.
Purification and partial characterization of phosphatidylinositol-4-phosphate kinase from rat liver plasma membranes. Further evidence for a stimulatory G-protein
Biochim. Biophys. Acta
1052
152-158
1990
Rattus norvegicus
Van Dongen, C.J.; Zwiers, H.; Gispen, W.H.
Purification and partial characterization of the phosphatidylinositol 4-phosphate kinase from rat brain
Biochem. J.
223
197-203
1984
Rattus norvegicus
Jones, D.H.; Morris, J.B.; Morgan, C.P.; Kondo, H.; Irvine, R.F.; Cockcroft, S.
Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-bisphosphate synthesis in the golgi compartment
J. Biol. Chem.
275
13962-13966
2000
Rattus norvegicus
Wenk, M.R.; Pellegrini, L.; Klenchin, V.A.; Di Paolo, G.; Chang, S.; Daniell, L.; Arioka, M.; Martin, T.F.; De Camilli, P.
PIP kinase Ig is the major PI(4,5)P2 synthesizing enzyme at the synapse
Neuron
32
79-88
2001
Rattus norvegicus
Kanaho, Y.; Miyazaki, H.; Yamazaki, M.
Activation of PI(4)P 5-kinase by small G proteins
Adv. Enzyme Regul.
43
107-119
2003
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
Giudici, M.L.; Emson, P.C.; Irvine, R.F.
A novel neuronal-specific splice variant of Type I phosphatidylinositol 4-phosphate 5-kinase isoform gamma
Biochem. J.
379
489-496
2004
Rattus norvegicus
Powner, D.J.; Payne, R.M.; Pettitt, T.R.; Giudici, M.L.; Irvine, R.F.; Wakelam, M.J.
Phospholipase D2 stimulates integrin-mediated adhesion via phosphatidylinositol 4-phosphate 5-kinase Igamma b
J. Cell Sci.
118
2975-2986
2005
Rattus norvegicus
Krauss, M.; Kukhtina, V.; Pechstein, A.; Haucke, V.
Stimulation of phosphatidylinositol kinase type I-mediated phosphatidylinositol (4,5)-bisphosphate synthesis by AP-2mu-cargo complexes
Proc. Natl. Acad. Sci. USA
103
11934-11939
2006
Rattus norvegicus
Xia, Y.; Irvine, R.F.; Giudici, M.L.
Phosphatidylinositol 4-phosphate 5-kinase Igamma_v6, a new splice variant found in rodents and humans
Biochem. Biophys. Res. Commun.
411
416-420
2011
Homo sapiens, Mus musculus, Rattus norvegicus
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