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Information on EC 2.7.1.151 - inositol-polyphosphate multikinase and Organism(s) Mus musculus and UniProt Accession Q7TT16

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EC Tree
IUBMB Comments
This enzyme also phosphorylates Ins(1,4,5)P3 to Ins(1,3,4,5)P4, Ins(1,3,4,5)P4 to Ins(1,3,4,5,6)P5, and Ins(1,3,4,5,6)P4 to Ins(PP)P4, isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P4 and Ins(1,2,3,4,6)P5 at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP6), respectively . Yeast produce InsP6 from Ins(1,4,5)P3 by the actions of this enzyme and EC 2.7.1.158, inositol-pentakisphosphate 2-kinase .
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Mus musculus
UNIPROT: Q7TT16
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
5-kinase, arg82, ins(1,4,5)p3 3-kinase, inositol polyphosphate multikinase, itpk1, inositol 1,4,5-trisphosphate 3-kinase, argriii, inositol polyphosphate kinase, ip3 3-kinase, atipk2beta, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inositol 1,4,5-trisphosphate 3-kinase
-
inositol polyphosphate multikinase
-
inositol polyphosphate kinase
inositol polyphosphate multikinase
-
-
Ipk2
-
-
phosphoinositol kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho-group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol-1,4,5-trisphosphate 6-phosphotransferase
This enzyme also phosphorylates Ins(1,4,5)P3 to Ins(1,3,4,5)P4, Ins(1,3,4,5)P4 to Ins(1,3,4,5,6)P5, and Ins(1,3,4,5,6)P4 to Ins(PP)P4, isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P4 and Ins(1,2,3,4,6)P5 at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP6), respectively [3]. Yeast produce InsP6 from Ins(1,4,5)P3 by the actions of this enzyme and EC 2.7.1.158, inositol-pentakisphosphate 2-kinase [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9077-69-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
inositol (1,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
show the reaction diagram
-
inositol polyphosphate multikinase is a key mediators in the production of inositol (1,3,4,5,6)-pentakisphosphate
-
-
?
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
inositol (1,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
show the reaction diagram
-
inositol polyphosphate multikinase is a key mediators in the production of inositol (1,3,4,5,6)-pentakisphosphate
-
-
?
additional information
?
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
immediate early gene induction by electroconvulsive stimulation is virtually abolished in the brains of IPMK-deleted mice, which also display deficits in spatial memory. Dominant-negative constructs, which prevent IPMK-CBP binding, substantially decrease immediate early gene induction
physiological function
inositol polyphosphate multikinase is a transcriptional coactivator required for immediate early gene induction. Inositol polyphosphate multikinase acts noncatalytically as a transcriptional coactivator to mediate induction of numerous immediate early genes, IEGs. Neural activity stimulates binding of IPMK to the histone acetyltransferase CBP and enhances its recruitment to IEG promoters, but IPMK regulation of CBP recruitment and IEG induction does not require its catalytic activities. The enzyme's epigenetic regulation of immediate early genes may influence diverse nonneural and neural biologic processes
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
IPMK_MOUSE
396
0
44453
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
IPMK physiologically binds AMP-activated kinase, with binding enhanced by glucose treatment
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of mutants by disrution of gene ipk2, the resulting enzyme-deficient Ipk2 null mice die around embryonic day 9.5 with multiple morphological defects, including abnormal folding of the neural tube, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ipk2 is located on chromosome 10
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Frederick, J.P.; Mattiske, D.; Wofford, J.A.; Megosh, L.C.; Drake, L.Y.; Chiou, S.T.; Hogan, B.L.; York, J.D.
An essential role for an inositol polyphosphate multikinase, Ipk2, in mouse embryogenesis and second messenger production
Proc. Natl. Acad. Sci. USA
102
8454-8459
2005
Mus musculus
Manually annotated by BRENDA team
Leyman, A.; Pouillon, V.; Bostan, A.; Schurmans, S.; Erneux, C.; Pesesse, X.
The absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate in mouse embryonic fibroblasts
Cell. Signal.
19
1497-1504
2007
Mus musculus (Q7TT16), Mus musculus
Manually annotated by BRENDA team
Gao, Y.; Wang, H.Y.
Inositol pentakisphosphate mediates Wnt/beta-catenin signaling
J. Biol. Chem.
282
26490-26502
2007
Mus musculus
Manually annotated by BRENDA team
Kim, S.; Kim, S.F.; Maag, D.; Maxwell, M.J.; Resnick, A.C.; Juluri, K.R.; Chakraborty, A.; Koldobskiy, M.A.; Cha, S.H.; Barrow, R.; Snowman, A.M.; Snyder, S.H.
Amino acid signaling to mTOR mediated by inositol polyphosphate multikinase
Cell Metab.
13
215-221
2011
Mus musculus
Manually annotated by BRENDA team
Maag, D.; Maxwell, M.J.; Hardesty, D.A.; Boucher, K.L.; Choudhari, N.; Hanno, A.G.; Ma, J.F.; Snowman, A.S.; Pietropaoli, J.W.; Xu, R.; Storm, P.B.; Saiardi, A.; Snyder, S.H.; Resnick, A.C.
Inositol polyphosphate multikinase is a physiologic PI3-kinase that activates Akt/PKB
Proc. Natl. Acad. Sci. USA
108
1391-1396
2011
Mus musculus
Manually annotated by BRENDA team
Bang, S.; Kim, S.; Dailey, M.J.; Chen, Y.; Moran, T.H.; Snyder, S.H.; Kim, S.F.
AMP-activated protein kinase is physiologically regulated by inositol polyphosphate multikinase
Proc. Natl. Acad. Sci. USA
109
616-620
2012
Mus musculus
Manually annotated by BRENDA team
Xu, R.; Paul, B.D.; Smith, D.R.; Tyagi, R.; Rao, F.; Khan, A.B.; Blech, D.J.; Vandiver, M.S.; Harraz, M.M.; Guha, P.; Ahmed, I.; Sen, N.; Gallagher, M.; Snyder, S.H.
Inositol polyphosphate multikinase is a transcriptional coactivator required for immediate early gene induction
Proc. Natl. Acad. Sci. USA
110
16181-16186
2013
Mus musculus (Q7TT16)
Manually annotated by BRENDA team