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Information on EC 2.7.4.21 - inositol-hexakisphosphate 5-kinase
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2.7.4.21 inositol-hexakisphosphate 5-kinaseIUBMB Comments
Three mammalian isoforms are known to exist.
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Word Map
- 2.7.4.21
- pyrophosphate
- polyphosphate
-
pp-insps
- tetrakisphosphate
- ppip5ks
-
bis-diphosphoinositol
-
pyrophosphorylation
-
5-insp7
-
5-diphosphoinositol
- medicine
-
ptdins3,4,5p3
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
Synonyms
ip6k1, ip6k2, ip6k3, ppip5k1, ppip5k2, insp6k2, inositol hexakisphosphate kinase, inositol hexakisphosphate kinase 1, ihpk2, atvip1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP:1D-myo-inositol-hexakisphosphate phosphotransferase
-
-
-
-
AtVip1
AtVip2
diphosphoinositol pentakisphosphate synthetase
-
-
-
-
EC 2.7.1.152
-
-
formerly
-
IHPK2
inositol hexakisphosphate kinase
inositol hexakisphosphate kinase 1
inositol hexakisphosphate kinase 2
inositol hexakisphosphate kinase 3
inositol hexakisphosphate kinase type 2
inositol hexakisphosphate kinase-1
inositol hexakisphosphate kinase-2
inositol-hexakisphosphate kinase
-
-
ambiguous
-
InsP6 kinase
InsP6-kinase
InsP6K1
InsP6K2
InsP6K3
-
-
-
-
IP6 kinase
-
-
-
-
IP6 kinase 1
IP6K
IP6K1
IP6K2
IP6K3
kinase (phosphorylating), inositol hexakisphosphate
-
-
-
-
PPIP5K2
RID-2
RID-2, regulator of interferon-induced death, is identical to inositol hexakisphosphate kinase 2, IP6K2
additional information
inositol hexakisphosphate kinase
-
-
-
-
inositol hexakisphosphate kinase 1
-
InsP6 kinase
-
-
-
-
IP6K
-
-
-
-
IP6K1
-
additional information
-
IP6K1 belongs to the family of inositol hexakisphosphate kinases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
(2)
-
-
-
ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
(1)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho-group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol-hexakisphosphate 5-phosphotransferase
Three mammalian isoforms are known to exist.
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CAS REGISTRY NUMBER
COMMENTARY
176898-37-6
-
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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
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
r
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,3-bis(diphosphate) 2,4,5,6-tetrakisphosphate
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1-triphosphate 2,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol 1-diphosphate pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
ATP + 1D-myo-inositol 5-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate
-
-
-
r
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 3-diphosphate 1,2,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol (1,2,3,4,6)-pentakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
ADP + diphosphoinositol pentakisphosphate + bisdiphosphoinositol tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol-1,3,4,5,6-pentakisphosphate
ADP + diphospho-1D-myo-inositol tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,3-bis(diphosphate) 2,4,5,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,3-bis(diphosphate) 2,4,5,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1-triphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1-triphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1-diphosphate pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1-diphosphate pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
r
ATP + 1D-myo-inositol 5-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol (1,2,3,4,6)-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol (1,2,3,4,6)-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol (1,2,3,4,6)-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol (1,2,3,4,6)-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
apoptosis regulation
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
forward and reverse reaction are random bireactant systems
-
-
?, r
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
enzyme is responsible for the biosynthesis of diphospho-myo-inositol pentakisphosphate. The enzyme also has a ATP synthase activity, implying that 5-diphospho-1D-myo-inositol pentakisphosphate functions as high-energy phosphate donor
-
r
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
-
-
-
?
additional information
?
-
the consensus PxxxDxKxG motif is responsible for substrate binding and is highly conserved in all known IPK2s
-
-
?
additional information
?
-
the consensus PxxxDxKxG motif is responsible for substrate binding and is highly conserved in all known IPK2s
-
-
?
additional information
?
-
secondary to its InsP6 kinase activity, also phosphorylates the 6-OH of Ins(1,4,5)P3, an inositol phosphate multikinase (IPMK)-like activity. IPMK itself is positionally promiscuous in that it is a 3-, 5- and 6-kinase. The enzyme also shows significant InsP3 kinase activity
-
-
?
additional information
?
-
-
secondary to its InsP6 kinase activity, also phosphorylates the 6-OH of Ins(1,4,5)P3, an inositol phosphate multikinase (IPMK)-like activity. IPMK itself is positionally promiscuous in that it is a 3-, 5- and 6-kinase. The enzyme also shows significant InsP3 kinase activity
-
-
?
additional information
?
-
EhIP6KA, like mammalian IP6Ks, converts InsP6 to 5-InsP7. The 5-phosphate group on InsP6 is diphosphorylated by EhIP6KA. The enzyme phosphorylates Ins(1,3,4,5,6)P5, and the major product co-elutes with a PP-[3H]InsP4 standard, no InsP6 is formed. The first order rate constant for Ins(1,3,4,5,6)P5 phosphorylation is 40fold lower than that for InsP6. The rate of phosphorylation of Ins(1,4,5)P3, is 220fold slower than that for InsP6, either the 2- or the 6-OH of Ins(1,4,5)P3 are phosphorylated. Ins(1,4,5,6)P4 is the major InsP4 product formed from Ins(1,4,5)P, with phosphorylation of an inositol phosphate at the 2-position. Steric restrictions prevent InsP6 from occupying the same space as Ins(1,4,5)P3 in the substrate-binding pocket. Substrate binding and specificities, overview
-
-
?
additional information
?
-
-
EhIP6KA, like mammalian IP6Ks, converts InsP6 to 5-InsP7. The 5-phosphate group on InsP6 is diphosphorylated by EhIP6KA. The enzyme phosphorylates Ins(1,3,4,5,6)P5, and the major product co-elutes with a PP-[3H]InsP4 standard, no InsP6 is formed. The first order rate constant for Ins(1,3,4,5,6)P5 phosphorylation is 40fold lower than that for InsP6. The rate of phosphorylation of Ins(1,4,5)P3, is 220fold slower than that for InsP6, either the 2- or the 6-OH of Ins(1,4,5)P3 are phosphorylated. Ins(1,4,5,6)P4 is the major InsP4 product formed from Ins(1,4,5)P, with phosphorylation of an inositol phosphate at the 2-position. Steric restrictions prevent InsP6 from occupying the same space as Ins(1,4,5)P3 in the substrate-binding pocket. Substrate binding and specificities, overview
-
-
?
additional information
?
-
role of the enzyme as a mediator of growth inhibition and apoptosis in response to interferon-beta treatment. The cellular level of the enzyme is posttranscriptionally enhanced by interferon-beta, in ovarian carcinoma cells
-
-
?
additional information
?
-
-
role of the enzyme as a mediator of growth inhibition and apoptosis in response to interferon-beta treatment. The cellular level of the enzyme is posttranscriptionally enhanced by interferon-beta, in ovarian carcinoma cells
-
-
?
additional information
?
-
-
IP6Ks change their kinase activity towards InsP6 at a decreasing ATP/ADP ratio to an ADP phosphotransferase activity and dephosphorylate InsP6. Enantioselective analysis reveals that Ins(2,3,4,5,6)P5 is the main InsP5 product of the IP6K reaction
-
-
?
additional information
?
-
the bifunctional enzyme also catalyzes the reaction of EC 2.7.4.24. The enzyme exhibits an unusual, nonproductive, substrate-stimulated ATPase activity, that is stimulated by the natural substratesand by 5-O-alpha-phosphonoacetyl-myo-inositol 1,2,3,4,6-pentakisphosphate and 2-O-benzyl-5-O-alpha-phosphonoacetyl-myo-inositol 1,3,4,6-tetrakisphosphate. The enzyme has two adjacent ligand-binding sites
-
-
?
additional information
?
-
enzyme additionally catalyzes the reaction of EC 2.7.4.24, i.e. conversion of 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate to 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate. The kinase activities toward 1D-myo-inositol hexakisphosphate are 4fold lower than the kinase activites toward 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
-
-
additional information
?
-
enzyme additionally catalyzes the reaction of EC 2.7.4.24, i.e. conversion of 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate to 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate. The kinase activities toward 1D-myo-inositol hexakisphosphate are 4fold lower than the kinase activites toward 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
-
-
additional information
?
-
-
IHPK2 binds to tumor necrosis factor receptor-associated factor 2 and interferes with phosphorylation of transforming growth factor beta-activated kinase 1, TAK1, thereby inhibiting NF-kappaB signaling. IHPK2 contains two sites required for TRAF2 binding, Ser347 and Ser359. IHPK2-TRAF2 binding leads to attenuation of TAK1- and NF-kappa B-mediated signaling and is partially responsible for the apoptotic activity of IHPK2. A portion of the death-promoting function of IHPK2 is independent of its kinase activity
-
-
?
additional information
?
-
-
IP6K2 belongs to a family of enzymes generating the inositol pyrophosphate IP7 [diphosphoinositol pentakisphosphate (5-PP-IP5)], it mediates apoptosis, increased IP6K2 activity sensitizes cancer cells to stressors, whereas its depletion blocks cell death
-
-
?
additional information
?
-
enzyme IP6K3 physiologically binds to the cytoskeletal proteins adducin and spectrin in mouse cerebellum
-
-
?
additional information
?
-
the enzyme generates inositol 1,3,4,5-tetrakisphosphate (InsP4) and InsP5
-
-
?
additional information
?
-
the enzyme generates inositol 1,3,4,5-tetrakisphosphate (InsP4) and InsP5
-
-
?
additional information
?
-
the enzyme generates inositol 1,3,4,5-tetrakisphosphate (InsP4) and InsP5
-
-
?
additional information
?
-
-
isoforms IP6K1 and IP6K2 bind to AP3B1protein
-
-
?
additional information
?
-
-
IP6Ks change their kinase activity towards InsP6 at a decreasing ATP/ADP ratio to an ADP phosphotransferase activity and dephosphorylate InsP6. Enantioselective analysis reveals that Ins(2,3,4,5,6)P5 is the main InsP5 product of the IP6K reaction
-
-
?
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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 + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1-diphosphate pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
ATP + 1D-myo-inositol 5-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
ATP + 1D-myo-inositol 1-diphosphate pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1-diphosphate pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate 2,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
apoptosis regulation
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
-
enzyme is responsible for the biosynthesis of diphospho-myo-inositol pentakisphosphate. The enzyme also has a ATP synthase activity, implying that 5-diphospho-1D-myo-inositol pentakisphosphate functions as high-energy phosphate donor
-
r
additional information
?
-
secondary to its InsP6 kinase activity, also phosphorylates the 6-OH of Ins(1,4,5)P3, an inositol phosphate multikinase (IPMK)-like activity. IPMK itself is positionally promiscuous in that it is a 3-, 5- and 6-kinase. The enzyme also shows significant InsP3 kinase activity
-
-
?
additional information
?
-
-
secondary to its InsP6 kinase activity, also phosphorylates the 6-OH of Ins(1,4,5)P3, an inositol phosphate multikinase (IPMK)-like activity. IPMK itself is positionally promiscuous in that it is a 3-, 5- and 6-kinase. The enzyme also shows significant InsP3 kinase activity
-
-
?
additional information
?
-
role of the enzyme as a mediator of growth inhibition and apoptosis in response to interferon-beta treatment. The cellular level of the enzyme is posttranscriptionally enhanced by interferon-beta, in ovarian carcinoma cells
-
-
?
additional information
?
-
-
role of the enzyme as a mediator of growth inhibition and apoptosis in response to interferon-beta treatment. The cellular level of the enzyme is posttranscriptionally enhanced by interferon-beta, in ovarian carcinoma cells
-
-
?
additional information
?
-
-
IHPK2 binds to tumor necrosis factor receptor-associated factor 2 and interferes with phosphorylation of transforming growth factor beta-activated kinase 1, TAK1, thereby inhibiting NF-kappaB signaling. IHPK2 contains two sites required for TRAF2 binding, Ser347 and Ser359. IHPK2-TRAF2 binding leads to attenuation of TAK1- and NF-kappa B-mediated signaling and is partially responsible for the apoptotic activity of IHPK2. A portion of the death-promoting function of IHPK2 is independent of its kinase activity
-
-
?
additional information
?
-
-
IP6K2 belongs to a family of enzymes generating the inositol pyrophosphate IP7 [diphosphoinositol pentakisphosphate (5-PP-IP5)], it mediates apoptosis, increased IP6K2 activity sensitizes cancer cells to stressors, whereas its depletion blocks cell death
-
-
?
additional information
?
-
enzyme IP6K3 physiologically binds to the cytoskeletal proteins adducin and spectrin in mouse cerebellum
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,3,4,5,6-inositol pentakisphosphate
-
IC50 for inositol hexakisphosphate kinase activity is 0.022 mM, IC50 for ATP synthase activity is 0.0128 mM
2,5-O-benzyl-myo-inositol 1,3,4,6-tetrakisphosphate
activates the ATP hydrolysis activity and inhibits the PPIP5K2 activity and InsP6 kinase activity, and the 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme. The compound can inhibit inositol phosphate kinase activity without occupying the catalytic site
2-O-benzyl-5-O-alpha-phosphonoacetyl-myo-inositol 1,3,4,6-tetrakisphosphate
stimulates ATP hydrolysis 9fold, but inhibits 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme. The compound can inhibit inositol phosphate kinase activity without occupying the catalytic site
2-O-benzyl-5-O-diphosphate-myo-inositol 1,3,4,6-tetrakisphosphate
activates ATP hydrolysis activity but inhibits 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme
2-O-benzyl-myo-inositol 1,2,3,4,6-pentakisphosphate
activates ATP hydrolysis activity but inhibits 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme
5-O-alpha-diphosphate-myo-inositol 1,3,4,6-tetrakisphosphate
activates ATP hydrolysis activity but inhibits 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme
5-O-alpha-phosphonoacetyl-myo-inositol 1,2,3,4,6-pentakisphosphate
stimulates ATP hydrolysis 5fold, but inhibits 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme
C8-PtdIns(4,5)P2
0.05 mM, inhibits 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate dephosphorylation by approximately 60%
-
diphosphoinositol pentakisphosphate
-
IC50 for inositol hexakisphosphate kinase activity is 0.0066 mM, IC50 for ATP synthase activity is 0.0018 mM
heat shock protein Hsp90
-
binding of HSP90 inhibits IP6K2 catalytic activity, IP6K2 binds to HSP90's C terminus. Depletion of HSP90 by RNAi in HEK-293 cells increases IP6K catalytic activity about 2.5fold, specificity of IP6K2-HSP90 interaction, overview. Drugs and selective mutations that abolish HSP90IP6K2 binding elicit activation of IP6K2, leading to cell death. Overexpression of HSP90 markedly and specifically reduces IP6K catalytic activity in HEK-293 cells, overexpression of HSP90 does not influence catalytic activity of IP6K1
-
inositol 1,2,4,5,6-pentakisphosphate
-
IC50 for inositol hexakisphosphate kinase activity is 0.022 mM
Inositol 1,3,4,5-tetrakisphosphate
-
IC50 for inositol hexakisphosphate kinase activity is 0.061 mM, IC50 for ATP synthase activity is 0.0325 mM
Inositol hexakisphosphate
-
IC50 for inositol hexakisphosphate kinase activity is 0.0008 mM, IC50 for ATP synthase activity is 0.0018 mM
N2-(m-(trifluoromethy)lbenzyl)N6-(p-nitrobenzyl)purine
potent and selective inhibitor
N2-(m-(trifluoromethyl) benzyl) N6-(p-nitrobenzyl) purine
TNP, a selective inhibitor, abolishes the basal and Cx43-potentiated Runx2 activity in response to FGF2 treatment relative to DMSO treated controls
phosphate
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate phosphatase activities of PPIP5Ks are 40-90% inhibited by phosphate within the 0-1 mM range; 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate phosphatase activities of PPIP5Ks are 40-90% inhibited by phosphate within the 0-1 mM range
N(2)-(m-(trifluoromethyl)benzyl) N(6)-(p-nitrobenzyl)purine
-
selective inhibitor in vitro
N(2)-(m-(trifluoromethyl)benzyl) N(6)-(p-nitrobenzyl)purine
-
selective inhibitor in vitro
N2-(3-trifluorobenzyl)-N6-(4-nitrobenzyl)purine
-
TNP, a selective IP6K inhibitor, abolishes the production of enantiomer Ins(2,3,4,5,6)P5 in different types of cells
N2-(3-trifluorobenzyl)-N6-(4-nitrobenzyl)purine
inhibiting IP6Ks by the compound decreases 5-diphosphoinositol pentakisphosphate synthesis and increases phosphorylation of Akt at T308 and S473 in mesenchymal stem cells, indicating the downregulation of 5-diphosphoinositol pentakisphosphate expression by IP6K inhibition enhance the activation of Akt in mesenchymal stem cells; inhibiting IP6Ks by the compound decreases 5-diphosphoinositol pentakisphosphate synthesis and increases phosphorylation of Akt at T308 and S473 in mesenchymal stem cells, indicating the downregulation of 5-diphosphoinositol pentakisphosphate expression by IP6K inhibition enhance the activation of Akt in mesenchymal stem cells; inhibiting IP6Ks by the compound decreases 5-diphosphoinositol pentakisphosphate synthesis and increases phosphorylation of Akt at T308 and S473 in mesenchymal stem cells, indicating the downregulation of 5-diphosphoinositol pentakisphosphate expression by IP6K inhibition enhance the activation of Akt in mesenchymal stem cells
N2-(3-trifluorobenzyl)-N6-(4-nitrobenzyl)purine
a selective inhibitor, abolishes the basal and Cx43-potentiated Runx2 activity in response to FGF2 treatment relative to DMSO treated controls; a selective inhibitor, abolishes the basal and Cx43-potentiated Runx2 activity in response to FGF2 treatment relative to DMSO treated controls
N2-(3-trifluorobenzyl)-N6-(4-nitrobenzyl)purine
-
TNP, a selective IP6K inhibitor, abolishes the production of enantiomer Ins(2,3,4,5,6)P5 in different types of cells
N2-(m-trifluorobenzyl),N6-(p-nitrobenzyl)purine
ATP competitive inhibitor
-
additional information
isoform PPIP5K2 is insensitive to physiological changes in either [AMP] or [ATP]/[ADP] ratios
-
additional information
-
isoform PPIP5K2 is insensitive to physiological changes in either [AMP] or [ATP]/[ADP] ratios
-
additional information
synthesis and effects of inositol phosphates and analogues upon ATPase activity, overview. The compounds are also inhibitors of [PP]2-InsP4 dephosphorylation. Binding structures, overview
-
additional information
radiation virtually abolishes binding of wild-type IP6K1 to the signalosome
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,5-O-benzyl-myo-inositol 1,3,4,6-tetrakisphosphate
activates the ATP hydrolysis activity and inhibits the InsP6 kinase activity of the enzyme
2-O-benzyl-5-O-alpha-phosphonoacetyl-myo-inositol 1,3,4,6-tetrakisphosphate
stimulates ATP hydrolysis 9fold
5-O-alpha-phosphonoacetyl-myo-inositol 1,2,3,4,6-pentakisphosphate
stimulates ATP hydrolysis 5fold
interferon beta
-
treatment with interferon beta enhances binding of IHPK2 to TNF receptor-associated factor 2
-
PtdIns(4,5)P2
increases net 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate kinase activity 5fold
-
additional information
synthesis and effects of inositol phosphates and analogues upon ATPase activity, overview. The compounds are also inhibitors of [PP]2-InsP4 dephosphorylation. Binding structures, overview
-
additional information
-
drugs and selective mutations that abolish HSP90IP6K2 binding elicit activation of IP6K2, leading to cell death
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Contribution of polymorphic variation of inositol hexakisphosphate kinase 3 (IP6K3) gene promoter to the susceptibility to late onset Alzheimer's disease.
Amyotrophic Lateral Sclerosis
Inositol Hexakisphosphate Kinase 2 is a Presymptomatic Biomarker for Amyotrophic Lateral Sclerosis.
Amyotrophic Lateral Sclerosis
Inositol hexakisphosphate kinase 2 promotes cell death of anterior horn cells in the spinal cord of patients with amyotrophic lateral sclerosis.
Autoimmune Diseases
Genetics of gene expression in primary immune cells identifies cell type-specific master regulators and roles of HLA alleles.
Breast Neoplasms
miR-125a-5p impairs the metastatic potential in breast cancer via IP6K1 targeting.
Carcinogenesis
Deletion of inositol hexakisphosphate kinase 1 (IP6K1) reduces cell migration and invasion, conferring protection from aerodigestive tract carcinoma in mice.
Carcinoma
Apo2L/TRAIL induction and nuclear translocation of inositol hexakisphosphate kinase 2 during IFN-beta-induced apoptosis in ovarian carcinoma.
Carcinoma
Deletion of inositol hexakisphosphate kinase 1 (IP6K1) reduces cell migration and invasion, conferring protection from aerodigestive tract carcinoma in mice.
Carcinoma
Effect of inositol hexakisphosphate kinase 2 on transforming growth factor beta-activated kinase 1 and NF-kappaB activation.
Carcinoma
Gene deletion of inositol hexakisphosphate kinase 2 predisposes to aerodigestive tract carcinoma.
Carcinoma
Inositol hexakisphosphate kinase 2 mediates growth suppressive and apoptotic effects of interferon-beta in ovarian carcinoma cells.
Carcinoma
Inositol hexakisphosphate kinase 2 sensitizes ovarian carcinoma cells to multiple cancer therapeutics.
Confusion
Multiple aspects of male germ cell development and interactions with Sertoli cells require inositol hexakisphosphate kinase-1.
Fatty Liver
Targeting the Inositol Pyrophosphate Biosynthetic Enzymes in Metabolic Diseases.
Hearing Loss
Mutations in Diphosphoinositol-Pentakisphosphate Kinase PPIP5K2 are associated with hearing loss in human and mouse.
Hyperinsulinism
Targeting the Inositol Pyrophosphate Biosynthetic Enzymes in Metabolic Diseases.
Hypersensitivity
A G-protein ? subunit, AGB1, negatively regulates the ABA response and drought tolerance by down-regulating AtMPK6-related pathway in Arabidopsis.
Infections
Human genome-wide RNAi screen identifies an essential role for inositol pyrophosphates in Type-I interferon response.
Infertility
IP6K1 is essential for chromatoid body formation and temporal regulation of Tnp2 and Prm2 expression in mouse spermatids.
Influenza, Human
Human genome-wide RNAi screen identifies an essential role for inositol pyrophosphates in Type-I interferon response.
Insulin Resistance
Adipocyte-specific deletion of Ip6k1 reduces diet-induced obesity by enhancing AMPK-mediated thermogenesis.
Insulin Resistance
Akt/PKB activation and insulin signaling: a novel insulin signaling pathway in the treatment of type 2 diabetes.
Insulin Resistance
Global IP6K1 deletion enhances temperature modulated energy expenditure which reduces carbohydrate and fat induced weight gain.
Insulin Resistance
High intensity exercise decreases IP6K1 muscle content & improves insulin sensitivity (SI2*) in glucose intolerant individuals.
Insulin Resistance
Ingestion of lean meat elevates muscle inositol hexakisphosphate kinase 1 protein content independent of a distinct post-prandial circulating proteome in young adults with obesity.
Insulin Resistance
Inositol hexakisphosphate kinase-1 interacts with perilipin1 to modulate lipolysis.
Insulin Resistance
Inositol pyrophosphates inhibit Akt signaling, thereby regulating insulin sensitivity and weight gain.
Insulin Resistance
IP6K1 Reduces Mesenchymal Stem/Stromal Cell Fitness and Potentiates High Fat Diet-Induced Skeletal Involution.
Insulin Resistance
Targeting the Inositol Pyrophosphate Biosynthetic Enzymes in Metabolic Diseases.
Insulin Resistance
The Role of the IGF-1 Signaling Cascade in Muscle Protein Synthesis and Anabolic Resistance in Aging Skeletal Muscle.
Insulin Resistance
TNP [N2-(m-Trifluorobenzyl), N6-(p-nitrobenzyl)purine] ameliorates diet induced obesity and insulin resistance via inhibition of the IP6K1 pathway.
Neoplasm Metastasis
Inositol pyrophosphates promote tumor growth and metastasis by antagonizing liver kinase B1.
Neoplasm Metastasis
miR-125a-5p impairs the metastatic potential in breast cancer via IP6K1 targeting.
Neoplasms
Deletion of inositol hexakisphosphate kinase 1 (IP6K1) reduces cell migration and invasion, conferring protection from aerodigestive tract carcinoma in mice.
Neoplasms
Effect of inositol hexakisphosphate kinase 2 on transforming growth factor beta-activated kinase 1 and NF-kappaB activation.
Neoplasms
Identification of novel Sp1 targets involved in proliferation and cancer by functional genomics.
Neoplasms
Inositol hexakisphosphate kinase 2 sensitizes ovarian carcinoma cells to multiple cancer therapeutics.
Neoplasms
Inositol pyrophosphates promote tumor growth and metastasis by antagonizing liver kinase B1.
Neoplasms
miR-125a-5p impairs the metastatic potential in breast cancer via IP6K1 targeting.
Neoplasms
Serum miR-1181 and miR-4314 associated with ovarian cancer: MiRNA microarray data analysis for a pilot study.
Neurodegenerative Diseases
Contribution of polymorphic variation of inositol hexakisphosphate kinase 3 (IP6K3) gene promoter to the susceptibility to late onset Alzheimer's disease.
Obesity
Adipocyte-specific deletion of Ip6k1 reduces diet-induced obesity by enhancing AMPK-mediated thermogenesis.
Obesity
Global IP6K1 deletion enhances temperature modulated energy expenditure which reduces carbohydrate and fat induced weight gain.
Obesity
Ingestion of lean meat elevates muscle inositol hexakisphosphate kinase 1 protein content independent of a distinct post-prandial circulating proteome in young adults with obesity.
Obesity
Inositol hexakisphosphate kinase-1 interacts with perilipin1 to modulate lipolysis.
Obesity
Inositol pyrophosphates inhibit Akt signaling, thereby regulating insulin sensitivity and weight gain.
Obesity
IP6K1 Reduces Mesenchymal Stem/Stromal Cell Fitness and Potentiates High Fat Diet-Induced Skeletal Involution.
Obesity
TNP [N2-(m-Trifluorobenzyl), N6-(p-nitrobenzyl)purine] ameliorates diet induced obesity and insulin resistance via inhibition of the IP6K1 pathway.
Pancreatitis
Platelet IP6K1 regulates neutrophil extracellular trap-microparticle complex formation in acute pancreatitis.
Pneumonia, Bacterial
Inhibition of IP6K1 suppresses neutrophil-mediated pulmonary damage in bacterial pneumonia.
Sarcopenia
The Role of the IGF-1 Signaling Cascade in Muscle Protein Synthesis and Anabolic Resistance in Aging Skeletal Muscle.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00039
1D-myo-inositol hexakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 m MKCl, at 37°C
0.00197
5-diphospho-1D-myo-inositol (1,2,3,4,6)pentakisphosphate
-
pH 6.8, 37°C
0.037
ATP
isoform PPIP5K2, using 1D-myo-inositol hexakisphosphate as cosubstrate, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
1D-myo-inositol hexakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
76
1D-myo-inositol hexakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
0.79
ATP
isoform PPIP5K2, using 1D-myo-inositol hexakisphosphate as cosubstrate, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0128
1,3,4,5,6-inositol pentakisphosphate
Rattus norvegicus
-
IC50 for inositol hexakisphosphate kinase activity is 0.022 mM, IC50 for ATP synthase activity is 0.0128 mM
0.0018
diphosphoinositol pentakisphosphate
Rattus norvegicus
-
IC50 for inositol hexakisphosphate kinase activity is 0.0066 mM, IC50 for ATP synthase activity is 0.0018 mM
0.0325
His3Cd-GST-protein
Rattus norvegicus
-
IC50 for inositol hexakisphosphate kinase activity is 0.061 mM, IC50 for ATP synthase activity is 0.0325 mM
-
0.022
inositol 1,2,4,5,6-pentakisphosphate
Rattus norvegicus
-
IC50 for inositol hexakisphosphate kinase activity is 0.022 mM
0.0018
Inositol hexakisphosphate
Rattus norvegicus
-
IC50 for inositol hexakisphosphate kinase activity is 0.0008 mM, IC50 for ATP synthase activity is 0.0018 mM
0.0095
N2-(m-trifluorobenzyl),N6-(p-nitrobenzyl)purine
Homo sapiens
pH 6.95, 37°C, in presence of 0.4 mM 1D-myo-inositol hexakisphosphate
-
0.016
N2-(m-trifluorobenzyl),N6-(p-nitrobenzyl)purine
Homo sapiens
pH 6.95, 37°C, in presence of 0.25 mM ATP
-
0.02
N2-(m-trifluorobenzyl),N6-(p-nitrobenzyl)purine
Homo sapiens
pH 6.95, 37°C, in presence of 0.1 mM 1D-myo-inositol hexakisphosphate
-
0.021
N2-(m-trifluorobenzyl),N6-(p-nitrobenzyl)purine
Homo sapiens
pH 6.95, 37°C, in presence of 0.2 mM 1D-myo-inositol hexakisphosphate
-
0.024
N2-(m-trifluorobenzyl),N6-(p-nitrobenzyl)purine
Homo sapiens
pH 6.95, 37°C, in presence of 0.05 mM 1D-myo-inositol hexakisphosphate
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.007
pH 7.2, 37°C, 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozymes IP6K1; Fluc+-eGFP+ transgenic mice, isozymes IP6K1
SwissProt
brenda
isozymes IP6K2; Fluc+-eGFP+ transgenic mice, isozymes IP6K2
UniProt
brenda
isozymes IP6K3; Fluc+-eGFP+ transgenic mice, isozymes IP6K3
UniProt
brenda
isozymes IP6K1; Fluc+-eGFP+ transgenic mice, isozymes IP6K1
SwissProt
brenda
isozymes IP6K2; Fluc+-eGFP+ transgenic mice, isozymes IP6K2
UniProt
brenda
isozymes IP6K3; Fluc+-eGFP+ transgenic mice, isozymes IP6K3
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
male, isozymes AtIPK2alpha and AtIPK2beta have overlapping expression in male gametophyte
brenda
isozyme IP6K3 is highly concentrated in the brain in cerebellar Purkinje cells
brenda
additional information
immunohistochemic analysis of the enzyme in wild-type and mutant mouse brains, overview
brenda
highest activity occurs in Purkinje cells with somewhat lower levels in granule cells. In hippocampus substantial densities occur in CA1-CA4 layers of the hippocampus as well as the dentate gyrus
brenda
MC-3T3 osteoblasts express IP6K1 and IP6K2 mRNA more than 25fold more abundantly than IP6K3
brenda
MC3T3 osteoblasts express IP6K1 and IP6K2 mRNA more than 25fold more abundantly than IP6K3
brenda
inositol hexakisphosphate kinase 3 is highly expressed at the leading edge of migrating cells
brenda
inositol hexakisphosphate kinase 3 is highly expressed at the leading edge of migrating cells
brenda
co-localization with phosphorylated TDP-43 of InsP6K2 in the cytoplasm of anterior horn cells of the spinal cord
brenda
additional information
in vitro and in vivo analysis of pollen germination and pollen tube growth of wild-type and mutant strains, detection of pollen tube guidance in cross-pollination, overview
brenda
additional information
in vitro and in vivo analysis of pollen germination and pollen tube growth of wild-type and mutant strains, detection of pollen tube guidance in cross-pollination, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
IP6K1 exhibits dual localization in the cytoplasm and nucleus
-
brenda
predominate in cytoplasm with only modest nuclear levels
brenda
-
isoform InsP6K2 is localized mainly in the cytoplasm of lymphoblast cells from patients with Huntington disease
brenda
-
comparable amounts of activity in the nucleus and cytoplasm
brenda
enzyme InsP6K2 is translocated from the nucleus to the cytosol during apoptosis
brenda
predominate in cytoplasm with only modest nuclear levels
brenda
-
after treatment of transfected cells (fusion protein consisting of IKPK2 and enhanced green fluorescent protein) with interferon-beta the protein translocated to the nucleus, additionally treatment of HEK-293T cells with tamoxifen (30 microM, 24 h) causes translocation of IHPK2 into the condensing nucleus, transfection with NLS-eGFP results in restricted expression of the fusion protein in the cytoplasm in untreated and in apoptotic cells
brenda
-
cytotoxicity is associated with a translocation of InsP6K2 from nuclei to mitochondria
brenda
-
isoform InsP6K2 is localized mainly in the nucleus of normal lymphoblast cells
brenda
enzyme InsP6K2 is translocated from the nucleus to the cytosol during apoptosis
brenda
-
comparable amounts of activity in the nucleus and cytoplasm
brenda
enzyme IP6K1 requires phosphatidic acid binding for nuclear localization and repression of mIno1 transcription. Deletion of the Q2 domain results in decreased nuclear localization in more than 60% of cells
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
in Dictyostelium discoideum, the IP7 target Ser is conserved, but the neighboring Asp and Glu residues are replaced with Thr. These Thr residues may undergo phosphorylation to mimic Asp/Glu and create a consensus site for diphosphorylation
evolution
IP6Ks are members of a wider inositol phosphate kinase family (Pfam PF03770) that includes IPMKs and IP3Ks. These enzymes all share a PxxxDxKxG, PDKG, catalytic motif. Phylogenetic analysis indivates that this kinase family arose from a primordial IP6K precursor
evolution
the absence of diphosphorylation in the IC(1-70)fragment suggests that the Ser-Pro cluster (residues 71-111) is required to facilitate pyrophosphorylation on Ser51. The site of diphosphorylation in mouse IC-2C is well conserved in human and rat, suggesting that the effect of IP7 on dynein is likely to be conserved in these species
evolution
the absence of diphosphorylation in the IC(1-70)fragment suggests that the Ser-Pro cluster (residues 71-111) is required to facilitate pyrophosphorylation on Ser51. The site of diphosphorylation in mouse IC-2C is well conserved in human and rat, suggesting that the effect of IP7 on dynein is likely to be conserved in these species
evolution
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the absence of diphosphorylation in the IC(1-70)fragment suggests that the Ser-Pro cluster (residues 71-111) is required to facilitate pyrophosphorylation on Ser51. The site of diphosphorylation in mouse IC-2C is well conserved in human and rat, suggesting that the effect of IP7 on dynein is likely to be conserved in these species
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malfunction
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cells lacking isoform IP6K1 arrest after genotoxic stress, and markers associated with DNA repair are recruited to DNAdamage sites indicating that homologous recombination repair is initiated in these cells. However, repair does not proceed to completion. Enzyme loss increases chromosomal damage susceptibility
malfunction
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deletion of isoform IP6K2 prevents the apoptotic actions of interferon beta and gamma-irradiation and cisplatin in different cancer cell lines
malfunction
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gene disruption of isoform IP6K2 in colorectal cancer cells selectively impairs p53-mediated apoptosis, instead favoring cell-cycle arrest
malfunction
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glycogen synthase kinase 3 activity is inhibited in the brains of IP6K1-deleted mice. Enzyme deletion disrupts social behavior
malfunction
-
isoform InsP6K1 disruption augments phosphatidylinositol-(3,4,5)-trisphosphate signaling and enhances superoxide production in neutrophils
malfunction
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isoform InsP6K1 disruption augments phosphatidylinositol-(3,4,5)-trisphosphate signaling and enhances superoxide production in neutrophils
malfunction
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isoform IP6K2 depletion inhibits Hh target gene expression. Inhibiting enzyme activity results in altered Hedgehog signal transduction. Isoform IP6K2 knockdown alters craniofacial and somite structures and inhibits the development and migration of neural crest cells
malfunction
analysis of the impact of siRNA-mediated knockdown of the two more abundant IP6Ks on Runx2 transcriptional activity. Knockdown of IP6K1 inhibits the FGF2-induced Runx2 activity, both basally and in response to Cx43 overexpression, more potently than knockdown of IP6K2. Knockdown of expression and/or inhibition of function of phospholipase Cgamma1, inositol polyphosphate multikinase, which generates inositol 1,3,4,5-tetrakisphosphate (InsP4) and InsP5, and inositol hexakisphosphate kinase 1/2, which generates inositol pyrophosphates, prevented the ability of Cx43 to potentiate FGF2 induced signaling through Runx2. Overexpression of phospholipase Cgamma1 and inositol hexakisphosphate kinase 1/2 enhances FGF2 activation of Runx2 and the effect of Cx43 overexpression on this response. Enzyme inhibition by TNP abolishes the basal and Cx43-potentiated Runx2 activity in response to FGF2 treatment relative to DMSO treated controls
malfunction
analysis of the impact of siRNA-mediated knockdown of the two more abundant IP6Ks on Runx2 transcriptional activity. Knockdown of IP6K1 inhibits the FGF2-induced Runx2 activity, both basally and in response to Cx43 overexpression, more potently than knockdown of IP6K2Knockdown of expression and/or inhibition of function of phospholipase Cgamma1, inositol polyphosphate multikinase, which generates inositol 1,3,4,5-tetrakisphosphate (InsP4) and InsP5, and inositol hexakisphosphate kinase 1/2, which generates inositol pyrophosphates, prevented the ability of Cx43 to potentiate FGF2 induced signaling through Runx2. Overexpression of phospholipase Cgamma1 and inositol hexakisphosphate kinase 1/2 enhances FGF2 activation of Runx2 and the effect of Cx43 overexpression on this response. Enzyme inhibition by TNP abolishes the basal and Cx43-potentiated Runx2 activity in response to FGF2 treatment relative to DMSO treated controls
malfunction
deletion of inositol hexakisphosphate kinase-1 (IP6K1) protects mice from high fat diet induced obesity and insulin resistance in mice. IP6K1-KO mice are lean due to enhanced energy expenditure. IP6K1-KO mice display enhanced basal lipolysis. IP6K1 modulates lipolysis via its interaction with the lipolytic regulator protein perilipin1 (PLIN1)
malfunction
deletion of KCS1, which blocks synthesis of inositol diphosphates on the 5-hydroxyl of the inositol ring, causes inositol auxotrophy and decreased intracellular inositol and phosphatidylinositol levels. These defects are caused by a profound decrease in transcription of INO1, which encodes myo-inositol-3-phosphate synthase. Expression of genes that function in glycolysis, transcription, and protein processing is not affected in kcs1DELTA. Deletion of OPI1, the INO1 transcription repressor, does not fully rescue INO1 expression in kcs1DELTA. Decreased inositol biosynthesis in kcs1DELTA is due to downregulation of INO1 transcription, but decreased inositol biosynthesis in kcs1DELTA is not because of perturbation of the UASINO regulatory complex Opi1-Ino2-Ino4, overview
malfunction
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endosomes derived from slime mold lacking inositol diphosphates display reduced dynein-directed microtubule transport. Intermediate chain recruitment to membranes is reduced in cells lacking IP6K1
malfunction
enzyme deletion reduces cell migration and invasion, conferring protection from aerodigestive tract carcinoma
malfunction
expressing either catalytically inactive or substrate specificity-altered variants of AtIPK2beta cannot rescue the male gametophyte and embryogenesis defects of the atipk2alpha/atipk2beta double mutant. The mutation of AtIPK2alpha and AtIPK2beta results in severely reduced transmission of male gametophyte as a result of abnormal pollen development and defective pollen tube guidance. Overexpression or reduction of the expression of AtIPK2alpha and AtIPK2beta reveal their roles in auxiliary shoot branching, abiotic stress responses and root growth. Phenotype, detailed overview
malfunction
iInositol synthesis is up-regulated in IP6K1 knockout MEF cells. Ip6k1 ablation leads to profound changes in DNA methylation and expression of Isyna1 (designated mIno1), which encodes the rate-limiting enzyme inositol-3-phosphate synthase. Expression of Q3DELTA, which lacks both the HOPA domain and the catalytic motif, leads to increased mIno1 mRNA levels in IP6K1-KO cells. In the mIno1 promoter region, most of the CpG sites exhibit a similar, but slightly decreased, pattern of methylation in IP6K1 knockout cells compared with wild-type cells. The CpG sites between the first and second ATGs exhibit markedly less methylation in IP6K1 knockout cells. Deletion of the Q4 domain of the enzyme results in increased mIno1 expression
malfunction
IP6K3 knock-out cerebella manifest abnormalities in Purkinje cell structure and synapse number, and the mutant mice display deficits in motor learning and coordination. Diminished cerebellar synapses in IP6K3 mutants
malfunction
knockdown of expression and/or inhibition of function of phospholipase Cgamma1, inositol polyphosphate multikinase, which generates inositol 1,3,4,5-tetrakisphosphate (InsP4) and InsP5, and inositol hexakisphosphate kinase 1/2, which generates inositol pyrophosphates, prevented the ability of Cx43 to potentiate FGF2 induced signaling through Runx2. Overexpression of phospholipase Cgamma1 and inositol hexakisphosphate kinase 1/2 enhances FGF2 activation of Runx2 and the effect of Cx43 overexpression on this response. Enzyme inhibition by TNP abolishes the basal and Cx43-potentiated Runx2 activity in response to FGF2 treatment relative to DMSO treated controls
malfunction
mammalian cells lacking IP6K1 display defects in dynein-dependent trafficking pathways, including endosomal sorting, vesicle movement, and Golgi maintenance. Expression of catalytically active but not inactive IP6K1 reverses the defects. Intermediate chain recruitment to membranes is reduced in cells lacking IP6K1
malfunction
mammalian cells lacking IP6K1 display defects in dynein-dependent trafficking pathways, including endosomal sorting, vesicle movement, and Golgi maintenance. Expression of catalytically active but not inactive IP6K1 reverses the defects. Intermediate chain recruitment to membranes is reduced in cells lacking IP6K1. Decreased Tfn distribution in the ERC in Ip6k1-/- MEFs might be due to a delay in Tfn trafficking from endosomes. Tfn is held back in early endosomes in cells lacking IP6K1
malfunction
selective inhibition of inositol hexakisphosphate kinase enhances mesenchymal stem cell engraftment and improves therapeutic efficacy for myocardial infarction. IP6K inhibition may increase Akt activation in mesenchymal stem cells, resulting in enhanced cardiac protective effect after transplantation. Inhibiting IP6Ks by N2-(3-trifluorobenzyl)-N6-(4-nitrobenzyl)purine decreases 5-diphosphoinositol pentakisphosphate synthesis and increases phosphorylation of Akt at T308 and S473 in mesenchymal stem cells, indicating the downregulation of 5-diphosphoinositol pentakisphosphate expression by IP6K inhibition enhances the activation of Akt in mesenchymal stem cells. IP6K inhibition by N2-(3-trifluorobenzyl)-N6-(4-nitrobenzyl)purine is also associated with decreased apoptosis
malfunction
significant reduction in platelet polyP levels in enzyme-deficient Ip6k1-/- mice, along with slower platelet aggregation and lengthened plasma clotting time. Incorporation of polyP into fibrin clots is reduced in Ip6k1-/- mice, thereby altering clot ultrastructure, which is rescued on the addition of exogenous polyP. In vivo assays reveal longer tail bleeding time and resistance to thromboembolism in Ip6k1-/- mice. No alteration in P-selectin surface expression in Ip6k1-/- platelets implies that IP6K1 does not influence platelet alpha-granule content or its thrombin-stimulated release No difference in the extent of fibrinogen binding to activated wild-type or Ip6k1-/- platelets, and no difference in serotonin content. Knockout Ip6k1-/- mice show altered clot homogeneity and architecture and a significant increase in the number of fibers per unit length in Ip6k1-/- derived clots compared to wild-type. Hemostasis defects in Ip6k1-/- mice, overview
malfunction
the UV-induced CRL4-mediated CDT1 degradation is substantially more rapid in IP6K1-deleted murine embryonic fibroblasts, MEFs, indicating enhanced CRL4 activity in the absence of IP6K1. CRL4-CSN binding is stimulated more by kinase-dead than wild-type IP6K1. IP6K1 knockdown greatly diminishes CRL4-CSN binding, an effect rescued by expressing shRNA-resistant mouse IP6K1 in IP6K1 knockdown cells. IP6K1 depletion augments Cul4A neddylation. The binding of substrate receptor DDB2 to Cul4A is diminished upon IP6K1 depletion
malfunction
deletion of inositol hexakisphosphate kinase 1 ( IP6K1) alters probability of presynaptic vesicle release and short-term facilitation of glutamatergic synapses in mouse hippocampus. IP6K1-knockout mice exhibit decreased prepulse inhibition with no defects in Y-maze and elevated plus maze tests. IP6K1 knockout leads to impaired shortterm memory formation in a contextual fear memory retrieval test with no effect on long-term memory. Both hippocampal long-term potentiation and long-term depression in IP6K1-knockout mice are similar to those in the wild-type control
malfunction
deletion of inositol hexakisphosphate kinase 3 (IP6K3) causes defects in cell motility and neuronal dendritic growth, eventually leading to brain malformations
malfunction
deletion of inositol hexakisphosphate kinase 3 (IP6K3) causes defects in cell motility and neuronal dendritic growth, eventually leading to brain malformations
malfunction
deletion of IP6K2 in male/female mice elicits substantial defects in synaptic influences of granule cells upon Purkinje cells as well as notable impairment of locomotor function. The disruption of IP6K2- 4.1N interactions impairs cell viability
malfunction
IP6K1 deletion leads to brain malformation and abnormalities of neuronal migration. IP6K1 deletion disrupts intracellular localization and function of alpha-actinin. The IP6K1 deleted cells display substantial decreases of stress fiber formation and impaired cell migration and spreading. Focal adhesion kinase phosphorylation is substantially decreased in IP6K1 deleted cells
malfunction
IP6K1/2-knockout cells have nondetectable levels of the IP6-derived 5-diphosphoinositol pentakisphosphate and bisdiphosphoinositol tetrakisphosphate and also exhibit reduced synthesis of the 5-diphosphoinositol pentakisphosphate-derived diphosphoinositol tetrakisphosphate. Knockout cells contain increased amounts of ATP, and elevated levels of free intracellular phosphate. Phosphate import and export of phosphate are decreased in the knockout cells
malfunction
Ip6k3-/- mice demonstrate lower blood glucose, reduced circulating insulin, deceased fat mass, lower body weight, increased plasma lactate, enhanced glucose tolerance, lower glucose during an insulin tolerance test, and reduced muscle Pdk4 expression under normal diet conditions. Ip6k3 deletion extends animal lifespan with concomitant reduced phosphorylation of S6 ribosomal protein in the heart. In contrast, Ip6k3-/- mice show unchanged skeletal muscle mass and no resistance to the effects of high fat diet
malfunction
RNAi mediated knock down of the IP6K1 isoform inhibits both glucose-mediated increase in diphosphoinositol pentakisphosphate and first phase insulin secretion
malfunction
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mammalian cells lacking IP6K1 display defects in dynein-dependent trafficking pathways, including endosomal sorting, vesicle movement, and Golgi maintenance. Expression of catalytically active but not inactive IP6K1 reverses the defects. Intermediate chain recruitment to membranes is reduced in cells lacking IP6K1. Decreased Tfn distribution in the ERC in Ip6k1-/- MEFs might be due to a delay in Tfn trafficking from endosomes. Tfn is held back in early endosomes in cells lacking IP6K1
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malfunction
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significant reduction in platelet polyP levels in enzyme-deficient Ip6k1-/- mice, along with slower platelet aggregation and lengthened plasma clotting time. Incorporation of polyP into fibrin clots is reduced in Ip6k1-/- mice, thereby altering clot ultrastructure, which is rescued on the addition of exogenous polyP. In vivo assays reveal longer tail bleeding time and resistance to thromboembolism in Ip6k1-/- mice. No alteration in P-selectin surface expression in Ip6k1-/- platelets implies that IP6K1 does not influence platelet alpha-granule content or its thrombin-stimulated release No difference in the extent of fibrinogen binding to activated wild-type or Ip6k1-/- platelets, and no difference in serotonin content. Knockout Ip6k1-/- mice show altered clot homogeneity and architecture and a significant increase in the number of fibers per unit length in Ip6k1-/- derived clots compared to wild-type. Hemostasis defects in Ip6k1-/- mice, overview
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malfunction
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selective inhibition of inositol hexakisphosphate kinase enhances mesenchymal stem cell engraftment and improves therapeutic efficacy for myocardial infarction. IP6K inhibition may increase Akt activation in mesenchymal stem cells, resulting in enhanced cardiac protective effect after transplantation. Inhibiting IP6Ks by N2-(3-trifluorobenzyl)-N6-(4-nitrobenzyl)purine decreases 5-diphosphoinositol pentakisphosphate synthesis and increases phosphorylation of Akt at T308 and S473 in mesenchymal stem cells, indicating the downregulation of 5-diphosphoinositol pentakisphosphate expression by IP6K inhibition enhances the activation of Akt in mesenchymal stem cells. IP6K inhibition by N2-(3-trifluorobenzyl)-N6-(4-nitrobenzyl)purine is also associated with decreased apoptosis
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metabolism
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isoform inositol hexakisphosphate kinase-2 acts as an effector of the vertebrate Hedgehog pathway. IP6K2 activity is required at the level or downstream of Smoothened but upstream of the transcription activator Gli1
metabolism
the enzyme is involved in the phospholipase Cgamma1/inositol polyphosphate/protein kinase C delta (PKCd) cascade which contributes to the Cx43-dependent transcriptional response of MC3T3 osteoblasts to FGF2. FGF2-signaling involves the inositol polyphosphate cascade, including inositol hexakisphosphate kinase (IP6K). FGF2 is an important regulator of skeletal tissue with complex action, acting at several stages of differentiation to differentially affect osteoblast function. Molecular mechanisms by which inositol diphosphates impact signaling in osteoblastic cells, overview
physiological function
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inositol hexakisphosphate kinase 1 regulates neutrophil function in innate immunity by inhibiting phosphatidylinositol-(3,4,5)-trisphosphate signaling. The enzyme does not regulate neutrophil trafficking and survival
physiological function
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inositol hexakisphosphate kinase 1 regulates neutrophil function in innate immunity by inhibiting phosphatidylinositol-(3,4,5)-trisphosphate signaling. The enzyme does not regulate neutrophil trafficking and survival
physiological function
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inositol hexakisphosphate kinase induces cell death in Huntington disease. The enzyme mediates apoptotic cell death via its translocation from the nucleus to the cytoplasm. Overexpression of the enzyme leads to the depletion of Akt phosphorylation and the induction of cell death
physiological function
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IP6K1 binds and stimulates (4fold) glycogen synthase kinase 3 alpha and beta isoforms enzymatic activity in vitro in a catalytically independent mechanism (physiological activator)
physiological function
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isoform IP6K2 is required for p53-mediated apoptosis and modulates the outcome of the p53 response. IP6K2 acts by binding directly to p53 and decreasing expression of proarrest gene targets such as the cyclin-dependent kinase inhibitor p21
physiological function
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isoform IP6K2 plays a specific role in regulating cell death. Isoform IP6K2 overexpression, that causes 10 to 20fold increase in IP7 level, enhances cell death
physiological function
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isoform P6K2 activity is required for normal development of craniofacial structures, somites, and neural crest cells
physiological function
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loss of inositol pyrophosphate synthesis by inositol hexakisphosphate kinase 1 impairs homologous recombination in mammalian cells, leading to increased cell death
physiological function
generated predominantly by inositol hexakisphosphate kinases (IP6Ks), inositol pyrophosphates can modulate protein function by posttranslational serine diphosphorylation. Ser51 in the dynein intermediate chain is a target for diphosphorylation by IP7, and this modification promotes the interaction of the intermediate chain N-terminus with the p150Glued subunit of dynactin. Involvement of IP6Ks in dynein function, inositol pyrophosphate-mediated diphosphorylation may act as a regulatory signal to enhance dynein-driven transport. Endosomal sorting of Tfn in fibroblasts requires IP6K1 activity, the enzyme activity also is required to maintain Golgi morphology. IP6K1 activity regulates Tfn trafficking, overview
physiological function
generated predominantly by inositol hexakisphosphate kinases (IP6Ks), inositol pyrophosphates can modulate protein function by posttranslational serine diphosphorylation. Ser51 in the dynein intermediate chain is a target for diphosphorylation by IP7, and this modification promotes the interaction of the intermediate chain N-terminus with the p150Glued subunit of dynactin. Involvement of IP6Ks in dynein function, inositol pyrophosphate-mediated diphosphorylation may act as a regulatory signal to enhance dynein-driven transport. IP6K1 activity regulates Tfn trafficking, overview
physiological function
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generated predominantly by inositol hexakisphosphate kinases (IP6Ks), inositol pyrophosphates can modulate protein function by posttranslational serine diphosphorylation. Ser51 in the dynein intermediate chain is a target for diphosphorylation by IP7, and this modification promotes the interaction of the intermediate chain N-terminus with the p150Glued subunit of dynactin. Involvement of IP6Ks in dynein function, inositol pyrophosphate-mediated diphosphorylation may act as a regulatory signal to enhance dynein-driven transport. Phagosomal motility requires IP6K1. IP6K1 activity regulates Tfn trafficking, overview
physiological function
hypoxia increases IP6Ks activity and 5-diphosphoinositol pentakisphosphate production
physiological function
inositol hexakisphosphate kinase 1 maintains hemostasis in mice by regulating platelet polyphosphate levels. Role for IP6K1 in regulation of mammalian hemostasis via its control of platelet polyP levels
physiological function
inositol hexakisphosphate kinase type 2 (InsP6K2), which converts inositol hexakisphosphate (InsP6) to InsP7, mediates cell death in mammalian cells. Cell death is augmented in the presence of cytoplasmic TDP-43 aggregations and activated InsP6K2, while cells with only cytoplasmic TDP-43 aggregation survive because Akt activity increases. Enzyme InsP6K2 causes neuronal cell death in patients suffering frontotemporal lobar degeneration with ubiquitinated inclusions (FTLD-U) or amyotrophic lateral sclerosis (ALS). InsP6K2 and cytoplasmic TDP-43 induce depletion of Akt phosphorylation and decrease casein kinase 2
physiological function
inositol hexakisphosphate kinase-3 regulates the morphology and synapse formation of cerebellar Purkinje cells via spectrin/adducin, isozyme IP6K3 is a major determinant of cytoskeletal disposition and function of cerebellar Purkinje cells. Spectrin/adducin binding is substantially increased by IP6K3, independent of the enzyme's kinase activity, catalytically inactive IP6K3 K217A mutant binds spectrin/adducin similarly to the wild-type enzyme
physiological function
inositol hexakisphosphate kinases (IP6Ks) primarily generate the signaling molecule, inositol diphosphate, 5-IP7. Phosphorylation of IP6K1 at a PKC/PKA motif modulates its interaction with PLIN1 and lipolysis. Enzyme IP6K1 is a regulator of PLIN1 mediated lipolysis. The PKA/PKC phosphorylation motif in IP6K1 regulates its interaction with PLIN1 and lipolysis
physiological function
inositol pyrophosphates containing seven (IP7) or more phosphate groups on a myo-inositol ring are synthesized from inositol hexakisphosphate (IP6) primarily by a family of IP6 kinases. Inositol hexakisphosphate kinase-1 mediates assembly/disassembly of the CRL4-signalosome complex. Under basal conditions, IP6K1 forms a ternary complexwith CSN and CRL4 in which IP6K1 and CRL4 are inactive. UV dissociates IP6K1 to generate IP7, which then dissociates CSN-CRL4 to activate CRL4. IP6K1 is a CRL4 subunit that transduces UV signals to mediate disassembly of the CRL4-CSN complex, thereby regulating nucleotide excision repair and cell death. IP6K1 directly binds to DDB1 and inhibits CRL4. IP6K1 inhibits CRL4 substrate, e.g. c-Jun, ubiquitylation and degradation. CDT1 ubiquitylation is markedly enhanced by overexpressing DDB1/Cul4A, an effect abolished in the presence of IP6K1. CRL4-CSN binding is stimulated more by kinase-dead than wild-type IP6K1
physiological function
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InsP6 (inositol hexakisphosphate), the most abundant inositol phosphate in metazoa, is pyrophosphorylated to InsP7 [5PP-InsP5 (diphosphoinositol pentakisphosphate)] by cytosolic and nuclear IP6Ks (InsP6 kinases) and to 1PP-InsP5 by another InsP6/InsP7 kinase family. IP6Ks are also nuclear and cytosolic InsP6- (and InsP5-)dephosphorylating enzymes whose activity is sensitively driven by a decrease in the cellular ATP/ADP ratio, thus suggesting a role for IP6Ks as cellular adenylate energy sensors
physiological function
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InsP6 (inositol hexakisphosphate), the most abundant inositol phosphate in metazoa, is pyrophosphorylated to InsP7 [5PP-InsP5 (diphosphoinositol pentakisphosphate)] by cytosolic and nuclear IP6Ks (InsP6 kinases) and to 1PP-InsP5 by another InsP6/InsP7 kinase family. IP6Ks are also nuclear and cytosolic InsP6- (and InsP5-)dephosphorylating enzymes whose activity is sensitively driven by a decrease in the cellular ATP/ADP ratio, thus suggesting a role for IP6Ks as cellular adenylate energy sensors
physiological function
IP6K regulates Runx2 and osteoblast gene expression
physiological function
IP6K regulates Runx2 and osteoblast gene expression. The nuclear translocation and association of PKCdelta with Runx2 is dependent upon IP6K1
physiological function
IP6K1, an inositol hexakisphosphate kinase that catalyzes the synthesis of inositol diphosphate, regulates inositol synthesis in mammalian cells. Enzyme IP6K1 may negatively regulate mIno1 transcription by increasing the methylation of mIno1 DNA. The catalytic function of IP6K1 is necessary for repression of mIno1 transcription
physiological function
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isozymes AtVip1 and AtVip2 are differentially expressed in plant tissues, suggesting nonredundant or non-overlapping functions in plants. Both AtVip1 and AtVip2 encode proteins capable of restoring InsP7 synthesis in Saccharomyces cerevisiae mutants, AtVip1 and AtVip2 can function as bonafide InsP6 kinases. The plant paralogues of the yeast Vip genes can catalyze the synthesis of InsP7 and correct the phenotypic consequences of a yeast vip1 null mutation
physiological function
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isozymes AtVip1 and AtVip2 are differentially expressed in plant tissues, suggesting nonredundant or non-overlapping functions in plants. Both AtVip1 and AtVip2 encode proteins capable of restoring InsP7 synthesis in yeast mutants, thus AtVip1 and AtVip2 can function as bonafide InsP6 kinases. The plant paralogues of the Saccharomyces cerevisiae Vip genes can catalyze the synthesis of InsP7 and correct the phenotypic consequences of a yeast vip1 null mutation
physiological function
modulation of Kcs1 controls INO1 transcription by regulating synthesis of inositol diphosphates, model of regulation of INO1 transcription by Kcs1 and inositol diphosphates, overview. bZIP and inositol pyrophosphate kinase (DINS) domains of enzyme Kcs1 are required for INO1 transcription. The Kcs1 protein, but not transcription, is regulated in response to inositol
physiological function
the enzyme is a key component for inositol polyphosphate turnover. The kinase activity of AtIPK2 is required for pollen development, pollen tube guidance and embryogenesis, requirement of inositol polyphosphate signaling in plant sexual reproduction. Isozymes AtIPK2alpha and AtIPK2beta act redundantly during pollen development, pollen tube guidance and embryogenesis
physiological function
the enzyme is involved in early cytoskeleton remodeling events during cancer progression and essential for 4-nitroquinoline-1-oxide-induced invasive carcinoma
physiological function
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate kinase activity is dominant when PPIP5K1 is expressed in intact cells. 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate phosphatase activity prevails when the enzyme is isolated from its cellular environment. Exogenous expression of PPIP5K1 in Drosophila melanogaster S3 cells elevates levels of 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate and 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
physiological function
inositol hexakisphosphate kinase (IP6K1) and IP6K2 together control inositol pyrophosphate metabolism and thereby physiologically regulate phosphate export and other aspects of mammalian cellular phosphate homeostasis
physiological function
inositol hexakisphosphate kinase 1 is a metabolic sensor in pancreatic beta-cells
physiological function
inositol hexakisphosphate kinase 3 promotes focal adhesion turnover via interactions with dynein intermediate chain 2
physiological function
inositol hexakisphosphate kinase 3 promotes focal adhesion turnover via interactions with dynein intermediate chain 2
physiological function
inositol hexakisphosphate kinase-2 in cerebellar granule cells regulates Purkinje cells and motor coordination via protein 4.1N
physiological function
islets from patients with T2D (a multifactorial, polygenetic disease) show impaired ATP generation in response to nutrients, in association with mitochondrial dysfunction. The regulation of IP6K1 activity is likely to be a vulnerable point in early disease development
physiological function
levels of both 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate and ATP decrease upon phosphate starvation and subsequently recover during phosphate replenishment
physiological function
physiological roles of the enzyme (IP6K1) and the associated inositol pyrophosphate metabolism in regulating sensorimotor gating as well as short-term memory
physiological function
product 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate promotes physiological endocytosis and downstream degradation of Na+/K+-ATPase-alpha1. Deletion of IP6K1 elicits a twofold enrichment of Na+/K+-ATPase-alpha1 in plasma membranes of multiple tissues and cell types. 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate binds the RhoGAP domain of phosphatidylinositol 3-kinase (PI3K) p85alpha to disinhibit its interaction with Na+/K+-ATPase-alpha1. This recruits adaptor protein 2 (AP2) and triggers the clathrin-mediated endocytosis of Na+/K+-ATPase-alpha1
physiological function
the enzyme (IP6K1) integrates glucose metabolism and insulin exocytosis
physiological function
the enzyme (IP6K1) integrates glucose metabolism and insulin exocytosis
physiological function
the enzyme (IP6K1) physiologically regulates neuronal migration by binding to alpha-actinin and influencing phosphorylation of both focal adhesion kinase and alpha-actinin through its product 5-diphosphoinositol pentakisphosphate
physiological function
the enzyme is important in numerous areas of cell physiology such as DNA repair and glucose homeostasis. It is implicated in the pathology of diabetes and other human diseases
physiological function
the enzyme promotes cell death of anterior horn cells in the spinal cord of patients with amyotrophic lateral sclerosis
physiological function
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isozymes AtVip1 and AtVip2 are differentially expressed in plant tissues, suggesting nonredundant or non-overlapping functions in plants. Both AtVip1 and AtVip2 encode proteins capable of restoring InsP7 synthesis in Saccharomyces cerevisiae mutants, AtVip1 and AtVip2 can function as bonafide InsP6 kinases. The plant paralogues of the yeast Vip genes can catalyze the synthesis of InsP7 and correct the phenotypic consequences of a yeast vip1 null mutation
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physiological function
-
isozymes AtVip1 and AtVip2 are differentially expressed in plant tissues, suggesting nonredundant or non-overlapping functions in plants. Both AtVip1 and AtVip2 encode proteins capable of restoring InsP7 synthesis in yeast mutants, thus AtVip1 and AtVip2 can function as bonafide InsP6 kinases. The plant paralogues of the Saccharomyces cerevisiae Vip genes can catalyze the synthesis of InsP7 and correct the phenotypic consequences of a yeast vip1 null mutation
-
physiological function
-
generated predominantly by inositol hexakisphosphate kinases (IP6Ks), inositol pyrophosphates can modulate protein function by posttranslational serine diphosphorylation. Ser51 in the dynein intermediate chain is a target for diphosphorylation by IP7, and this modification promotes the interaction of the intermediate chain N-terminus with the p150Glued subunit of dynactin. Involvement of IP6Ks in dynein function, inositol pyrophosphate-mediated diphosphorylation may act as a regulatory signal to enhance dynein-driven transport. Endosomal sorting of Tfn in fibroblasts requires IP6K1 activity, the enzyme activity also is required to maintain Golgi morphology. IP6K1 activity regulates Tfn trafficking, overview
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physiological function
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inositol hexakisphosphate kinase 1 maintains hemostasis in mice by regulating platelet polyphosphate levels. Role for IP6K1 in regulation of mammalian hemostasis via its control of platelet polyP levels
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physiological function
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hypoxia increases IP6Ks activity and 5-diphosphoinositol pentakisphosphate production
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additional information
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a small amount of InsP7 and InsP8 is accumulated in seeds of higher plants. Residue D292 of AtVIP1 is critical for activity of the kinase domain. The kinase domains alone does not show InsP7 synthesis activity to same levels as the intact AtVIP1
additional information
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a small amount of InsP7 and InsP8 is accumulated in seeds of higher plants. The kinase domains alone does not show InsP7 synthesis activity to same levels as the intact AtVIP2
additional information
enzyme InsP6K2 is translocated from the nucleus to the cytosol during apoptosis
additional information
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enzyme InsP6K2 is translocated from the nucleus to the cytosol during apoptosis
additional information
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lentiviral RNAi-based depletion of MINPP1 at falling cellular ATP/ADP ratios has no significant impact on Ins(2,3,4,5,6)P5 production
additional information
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lentiviral RNAi-based depletion of MINPP1 at falling cellular ATP/ADP ratios has no significant impact on Ins(2,3,4,5,6)P5 production
additional information
structural analysis of the IP6K from Entamoeba histolytica
additional information
-
structural analysis of the IP6K from Entamoeba histolytica
additional information
the catalytic motif of enzyme IP6K1 lies in the Q3 domain
additional information
a homogenous coupled bioluminescence assay is developed for measuring inositol hexakisphosphate kinase 1 activity in a 384-well format
additional information
-
a homogenous coupled bioluminescence assay is developed for measuring inositol hexakisphosphate kinase 1 activity in a 384-well format
additional information
-
a small amount of InsP7 and InsP8 is accumulated in seeds of higher plants. Residue D292 of AtVIP1 is critical for activity of the kinase domain. The kinase domains alone does not show InsP7 synthesis activity to same levels as the intact AtVIP1
-
additional information
-
a small amount of InsP7 and InsP8 is accumulated in seeds of higher plants. The kinase domains alone does not show InsP7 synthesis activity to same levels as the intact AtVIP2
-
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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). IP6K1_HUMAN
441
0
50236
Swiss-Prot
other Location (Reliability: 2)
IP6K1_MOUSE
433
0
49307
Swiss-Prot
other Location (Reliability: 2)
IP6K1_RAT
433
0
49366
Swiss-Prot
other Location (Reliability: 2)
IP6K3_HUMAN
410
0
46417
Swiss-Prot
other Location (Reliability: 2)
IP6K3_MOUSE
396
0
44418
Swiss-Prot
other Location (Reliability: 3)
KCS1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1050
0
119550
Swiss-Prot
other Location (Reliability: 1)
A0A061HYZ2_CRIGR
99
0
11093
TrEMBL
other Location (Reliability: 1)
A0A086LVE7_TOXGO
2221
0
238692
TrEMBL
other Location (Reliability: 2)
A0A0B2RPJ4_GLYSO
183
0
20275
TrEMBL
other Location (Reliability: 3)
A0A8M1N0H1_DANRE
430
0
48733
TrEMBL
other Location (Reliability: 1)
A0A8M1PCI0_DANRE
463
0
52425
TrEMBL
other Location (Reliability: 2)
VIP2_MOUSE
1129
0
128427
Swiss-Prot
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
55000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
enzyme structure determinaion and comparisons, similarities to enzymes human IP3KA, human IP6K, and Saccharomyces cerevisiae IPMK, overview
additional information
-
enzyme structure determinaion and comparisons, similarities to enzymes human IP3KA, human IP6K, and Saccharomyces cerevisiae IPMK, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
the phosphorylation of IP6K1 at a PKC/PKA motif modulates its interaction with PLIN1 and lipolysis. GST-IP6K1 phosphorylation in HEK293 cells is enhanced by forskolin-mediated PKA activation. Endogenous IP6K1 phosphorylation in HEK293 cells is enhanced to a greater extent by PKC activation compared to PKA activation as evidenced by PMA and FSK treatments. No phosphorylation of IP6K1 mutant S118A-S121A in HEK293 cells
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant MBP-tagged EhIP6KA residues 32-270, several crystal complexes of the IP6K including those that contain either large (Ins(1,3,4,5,6)P5 /InsP6) or small (Ins(1,4,5)P3) substrates, hanging drop vapor diffusion, 60 mg/ml protein in solution is mixed with reservoir solution containing 12% w/v PEG 3350, 50 mM NaH2PO4, pH 5.5 at 18°C, or by hanging drop vapor diffusion for one week against a well buffer containing 8% w/v PEG 3350, 100 mM Na3citrate, pH 5.2 at 25°C, followed by dilution microseeding for two weeks with a well buffer of 8% w/v PEG 3350, 100 mM Na3citrate, pH 5.2, and 8% ethylene glycol at 25°C, soaking of crystals in 22% w/v PEG 3350, 10 mM MgCl2, 10 mM ATP, 0.1 M sodium acetate, pH 5.2, and 20 mM InsP6, 10 mM Ins(1,3,4,5,6)P5 or 10 mM Ins(1,4,5)P3 for 3 days, X-ray diffraction structure determination and analysis, molecular replacement using MBP (1ez9) and IP3K (1w2c) as search models
N-terminally truncated enzyme mutant, residues 41-366, hanging drop vapor diffusion against a well buffer of 12% w/v PEG 3350, 20 mM MgCl2, 0.1 M HEPES, pH 7.0, 0,1 mM AMP-PNP, and 2 mM CdCl2 at 4°C, 3 days, 4°C, X-ray diffraction structure determination and analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D292A
K248A
the mutant shows a reduction in 1D-myo-inositol hexakisphosphate-stimulated ATPase activity of isofom PPIP5K2. The mutant shows a significant reduction in the rate of 1D-myo-inositol phosphate-independent ATPase activity of isofom PPIP5K2
R213A
the mutant shows a reduction in 1D-myo-inositol hexakisphosphate-stimulated ATPase activity of isofom PPIP5K2
R332A
2.4-4fold larger net formation of 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate, but mutation nearly completely impaires its hydrolysis
R388A
2.4-4fold larger net formation of 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate, but mutation nearly completely impaires its hydrolysis
R837H
variant R837H segregates with DFNB100-associated hearing loss. Mutation reduces the phosphatase activity of PPIP5K2 and elevates its kinase activity
K217A
a kinase-dead mutant IP6K3, the catalytically inactive IP6K3 K217A mutant binds spectrin/adducin similarly to the wild-type enzyme
R133A
-
mutation of IP6K2 in its putative HSP90-binding motif, mutation of Arg133 abolishes IP6K2-HSP90 binding
R136A
-
mutation of IP6K2 in its putative HSP90-binding motif, mutation of Arg136 abolishes IP6K2-HSP90 binding
S118A/S121A
site-directed mutagenesis, no phosphorylation of IP6K1 mutant S118A-S121A in HEK293 cells. The mutant does not efficiently bind Myc-PLIN1 in HEK293 cells
S347A/S359A
-
site-directed mutagenesis, the mutant displays 3.5fold greater TAK1 activation following TNF-alpha, the mutant demonstrates a 6-10fold increase in NF-kappaB DNA binding following TNF-alpha compared with wild type IHPK2-expressing cells in which NF-kappa B DNA binding is inhibited
S85A
site-directed mutagenesis, the mutation does not influence its binding to Myc-PLIN1 in HEK293 cells
W131A
-
mutation of IP6K2 in its putative HSP90-binding motif, mutation of Trp131 modestly diminishes IP6K2-HSP90 binding, the catalytically impaired IP6K2-W131A does not induce cell death
additional information
additional information
construction of a atipk2alpha/atipk2beta double mutant with male gametophyte and embryogenesis defects, the mutant cannot be rescued by either catalytically inactive or substrate specificity-altered variants of AtIPK2beta. The single knock-out mutant of atipk2alpha is indistinguishable from the wild-type. Transmission analysis of atipk2alpha and atipk2beta mutant alleles and Segregation analysis of atipk2alpha and atipk2beta mutants, overview. Complementation analysis of the atipk2alpha/atipk2beta double mutant, development-defective phenotype
additional information
construction of a atipk2alpha/atipk2beta double mutant with male gametophyte and embryogenesis defects, the mutant cannot be rescued by either catalytically inactive or substrate specificity-altered variants of AtIPK2beta. The single knock-out mutant of atipk2alpha is indistinguishable from the wild-type. Transmission analysis of atipk2alpha and atipk2beta mutant alleles and Segregation analysis of atipk2alpha and atipk2beta mutants, overview. Complementation analysis of the atipk2alpha/atipk2beta double mutant, development-defective phenotype
additional information
construction of a atipk2alpha/atipk2beta double mutant with male gametophyte and embryogenesis defects, the mutant cannot be rescued by either catalytically inactive or substrate specificity-altered variants of AtIPK2beta. The single knock-out mutant of atipk2beta is indistinguishable from the wild-type. Transmission analysis of atipk2alpha and atipk2beta mutant alleles and Segregation analysis of atipk2alpha and atipk2beta mutants, overview. Complementation analysis of the atipk2alpha/atipk2beta double mutant, development-defective phenotype
additional information
construction of a atipk2alpha/atipk2beta double mutant with male gametophyte and embryogenesis defects, the mutant cannot be rescued by either catalytically inactive or substrate specificity-altered variants of AtIPK2beta. The single knock-out mutant of atipk2beta is indistinguishable from the wild-type. Transmission analysis of atipk2alpha and atipk2beta mutant alleles and Segregation analysis of atipk2alpha and atipk2beta mutants, overview. Complementation analysis of the atipk2alpha/atipk2beta double mutant, development-defective phenotype
additional information
construction of an Entamoeba histolytica hybrid IP6K/IP3K chimeric hybrid through molecular modeling and mutagenesis
additional information
-
construction of an Entamoeba histolytica hybrid IP6K/IP3K chimeric hybrid through molecular modeling and mutagenesis
additional information
-
NLS (nuclear localization sequence) mutant of IHPK2 (4 point mutations in the NLS) remains in the cytoplasm, even after interferon-beta treatment
additional information
construction of an N-terminally truncated mutant PPIP5K2KD comprising residues 41-366
additional information
-
construction of an inactive enzyme mutant, overexpression of wild-type IHPK2 sensitizes ovarian carcinoma cell lines to the growth-suppressive and apoptotic effects of interferon beta, IFN-alpha2, and gamma-irradiation. Expression of a kinase-dead mutant abrogates 50% of the apoptosis induced by IFN-beta
additional information
-
depletion of IP6K2 in HEK-293 cells by RNAi leads to 40-50% reduced cell death, overview. Deletion mapping of IP6K2 to identify HSP90-binding motif, overview. The yeast Saccharomyces cerevisiae possesses constitutive and inducible homologues of HSP90, designated HSC82 and HSP82, respectively. In HSC82 KO yeast, IP6K activity is 2.5fold higher than murine wild-type, in yeast HSP82 null mutant, IP6K catalytic activity is increased but to a lesser extent. Overexpression of HSP90 markedly reduces IP6K catalytic activity in HEK-293 cells
additional information
-
gene deletion of IP6K1 in mice leads to markedly diminished production of inositol diphosphates. Male mutant mice are sterile with defects in spermiogenesis. Mutant mice are smaller than wild-type despite normal food intake. The mutants display markedly lower circulating insulin, phenotype, overview
additional information
construction of IP6K1 knockout MEF cells. Deletion of the Q2 domain results in decreased nuclear localization in more than 60% of cells
additional information
generation of enzyme-deficient Ip6k1-/- mice, phenotype, overview
additional information
IP6K3 knockdown HEK293 cells are generated by lentiviral transduction. Diminished cerebellar synapses in IP6K3 mutants
additional information
-
generation of enzyme-deficient Ip6k1-/- mice, phenotype, overview
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli and HEK-293T cells, additionally wild-type IHPK2 and the NLS mutant is cloned into the pCXN2 mammalian expression vector and electroporated into NIH-OVCAR-3 cells
-
expression in Escherichia coli, NIH-OVCAR-3 and Hey ovarian carcinoma cells, IP6K2 mRNA is not induced in NIH-OVCAR-3 cells following treatment with interferon-beta or gamma-irradiation, both gamma-irradiation and interferon-beta induce IP6K2 protein via a post-translational mechanism
-
expression in HeLa cells, PC12 cells, Jurkat T cells, OVCAR-3 cells, HL-60 cells and HEK-293 cells
-
expression of the wild-type enzyme in Saccharomyces cerevisiae mutant strains, overexpression of the GST-tagged or Myc-tagged enzyme in HEK-293, HeLa, and HCT116 cells, expression of wild-type and mutant enzymes in HEK-293 cells
-
gene Ihpk1, located on chromosome 9, has 6 exons, of which exon 1 is exclusively noncoding, the start codon is located in exon 2, and the stop codon is located in exon 6, DNA and amino acid sequence determination and analysis. Expressionin MEF cell lines
-
gene IP6K1
gene Ip6k1, expression of murine IP6K1 rescues yeast kcs1DELTA inositol auxotrophy. Nuclear recombinant expression of GFP-tagged wild type IP6K1 in IP6K1 knockout cells
gene ip6k1, quantitative real-time PCr enzyme expression analysis
gene IP6K1, recombinant coexpression of GST-tagged wild-type and mutant enzymes with Myc-tagged PLIN1 in HEK-293 cells, recombinant expression of Myc-tagged enzyme
gene IP6K1, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3), coexpression of IP6K1 prevents enhancement of ubiquitylation by the expression of DDB1/Cul4A in HEK293 cells. IP6K1 expression of shRNA-resistant mouse IP6K1 in IP6K1 knockdown cells, overexpression of TAP-IP6K1 in HEK-293 cells
gene ip6k2, quantitative real-time PCr enzyme expression analysis
gene ip6k3, quantitative real-time PCr enzyme expression analysis
gene vip1, phylogenetic analysis, AtVip1 restores InsP7 synthesis in a Saccharomyces cerevisiae kcs1 mutant
-
gene vip2, phylogenetic analysis, AtVip2 restores InsP7 synthesis in a Saccharomyces cerevisiae kcs1 mutant
-
GST fusion protein is transfected into HEK293T cells
overexpression of wild-type and inactive mutant IHPK2 in ovarian carcinoma cell lines
-
recombinant co-overexpression of InsP6K2 and C-terminal residues 219-414 of TDP-43 from InsP6K2-pDsRed tag and TDP219-pEGFP tag plasmids in SHSY-5Y cells. Transfection of SHSY-5Y cells with a plasmid encoding a catalytically inactive, dominant-negative InsP6K2 (K2 K/A). HSP90 protein expression is reduced in the cytoplasmic fraction of TDP219- and InsP6K2-transfected cells. HSP90 expression is also significantly reduced in cells doubly transfected with TDP219M and InsP6K2 compared with control cells
recombinant expression of wild-type and mutant enzymes with a Flag-tag beta-adducin tail and MARCKS domain tagged to it, or tagged with actin-binding domain (1-275 aa), repeat domain (303-525 aa), and PH domain (2197-2307 aa) of beta2-spectrin. Tag cleavage by prescission protease
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
IP6K3 is upregulated by dexamethasone. Ip6k3 expression is elevated under diabetic, fasting, and disuse conditions in mouse skeletal muscles
IP6K3 is upregulated by dexamethasone. Ip6k3 expression is elevated under diabetic, fasting, and disuse conditions in mouse skeletal muscles
IP6K3 is upregulated by dexamethasone. Ip6k3 expression is elevated under diabetic, fasting, and disuse conditions in mouse skeletal muscles
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
dialysis against renaturing buffer (25% sucrose, 0.1% Tween 40, 84 mM HEPES pH 7.5) after elution with denaturing buffer containing 150 mM imidazole
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
selectively blocking HSP90-IP6K2 binding could provide effective and safer modes of chemotherapy to block apoptosis
medicine
transition variant R837H segregates with DFNB100-associated hearing loss
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saiardi, A.; Erdjument-Bromage, H.; Snowman, A.M.; Tempst, P.; Snyder, S.H.
Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases
Curr. Biol.
9
1323-1326
1999
Mus musculus (Q6PD10), Homo sapiens (Q9UHH9)
brenda
Voglmaier, S.M.; Bembenek, M.E.; Kaplin, A.I.; Dorman, G.; Olszewski, J.D.; Prestwich, G.D.; Snyder, S.H.
Purified inositol hexakisphosphate kinase is an ATP synthase: diphosphoinositol pentakisphosphate as a high-energy phosphate donor
Proc. Natl. Acad. Sci. USA
93
4305-4310
1996
Rattus norvegicus
brenda
Albert, C.; Safrany, S.T.; Bembenek, M.E.; Reddy, K.M.; Reddy, K.K.; Falck, J.R.; Brcker, M.; Shears, S.B.; Mayr, G.W.
Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells
Biochem. J.
327
553-560
1997
Cricetulus griseus, Homo sapiens, Mus musculus
-
brenda
Morrison, B.H.; Bauer, J.A.; Kalvakolanu, D.V.; Lindner, D.J.
Inositol hexakisphosphate kinase 2 mediates growth suppressive and apoptotic effects of interferon-beta in ovarian carcinoma cells
J. Biol. Chem.
276
24965-24970
2001
Homo sapiens (Q9UHH9), Homo sapiens
brenda
Saiardi, A.; Nagata, E.; Luo, H.R.; Snowman, A.M.; Snyder, S.H.
Identification and characterization of a novel inositol hexakisphosphate kinase
J. Biol. Chem.
276
39179-39185
2001
Homo sapiens (Q96PC2), Mus musculus
brenda
Morrison, B.H.; Tang, Z.; Jacobs, B.S.; Bauer, J.A.; Lindner, D.J.
Apo2L/TRAIL induction and nuclear translocation of inositol hexakisphosphate kinase 2 during IFN-beta-induced apoptosis in ovarian carcinoma
Biochem. J.
385
595-603
2005
Homo sapiens
brenda
Schell, M.J.; Letcher, A.J.; Brearley, C.A.; Biber, J.; Murer, H.; Irvine, R.F.
PiUS (Pi uptake stimulator) is an inositol hexakisphosphate kinase
FEBS Lett.
461
169-172
1999
Xenopus sp.
brenda
Nagata, E.; Luo, H.R.; Saiardi, A.; Bae, B.I.; Suzuki, N.; Snyder, S.H.
Inositol hexakisphosphate kinase-2, a physiologic mediator of cell death
J. Biol. Chem.
280
1634-1640
2005
Homo sapiens
brenda
Morrison, B.H.; Bauer, J.A.; Hu, J.; Grane, R.W.; Ozdemir, A.M.; Chawla-Sarkar, M.; Gong, B.; Almasan, A.; Kalvakolanu, D.V.; Lindner, D.J.
Inositol hexakisphosphate kinase 2 sensitizes ovarian carcinoma cells to multiple cancer therapeutics
Oncogene
21
1882-1889
2002
Homo sapiens
brenda
Morrison, B.H.; Bauer, J.A.; Lupica, J.A.; Tang, Z.; Schmidt, H.; DiDonato, J.A.; Lindner, D.J.
Effect of inositol hexakisphosphate kinase 2 on transforming growth factor beta-activated kinase 1 and NF-kappaB activation
J. Biol. Chem.
282
15349-15356
2007
Homo sapiens, Mus musculus
brenda
Chakraborty, A.; Koldobskiy, M.A.; Sixt, K.M.; Juluri, K.M.; Mustafa, A.K.; Snowman, A.M.; van Rossum, D.B.; Patterson, R.L.; Snyder, S.H.
HSP90 regulates cell survival via inositol hexakisphosphate kinase-2
Proc. Natl. Acad. Sci. USA
105
1134-1139
2008
Mus musculus
brenda
Bhandari, R.; Juluri, K.R.; Resnick, A.C.; Snyder, S.H.
Gene deletion of inositol hexakisphosphate kinase 1 reveals inositol pyrophosphate regulation of insulin secretion, growth, and spermiogenesis
Proc. Natl. Acad. Sci. USA
105
2349-2353
2008
Mus musculus
brenda
Azevedo, C.; Szijgyarto, Z.; Saiardi, A.
The signaling role of inositol hexakisphosphate kinases (IP6Ks)
Adv. Enzyme Regul.
51
74-82
2011
Rattus norvegicus
brenda
Weaver, J.D.; Wang, H.; Shears, S.B.
The kinetic properties of a human PPIP5K reveal that its kinase activities are protected against the consequences of a deteriorating cellular bioenergetic environment
Biosci. Rep.
33
e00022
2013
Homo sapiens (O43314), Homo sapiens
brenda
Nagata, E.; Saiardi, A.; Tsukamoto, H.; Okada, Y.; Itoh, Y.; Satoh, T.; Itoh, J.; Margolis, R.L.; Takizawa, S.; Sawa, A.; Takagi, S.
Inositol hexakisphosphate kinases induce cell death in Huntington disease
J. Biol. Chem.
286
26680-26686
2011
Homo sapiens
brenda
Jadav, R.S.; Chanduri, M.V.; Sengupta, S.; Bhandari, R.
Inositol pyrophosphate synthesis by inositol hexakisphosphate kinase 1 is required for homologous recombination repair
J. Biol. Chem.
288
3312-3321
2013
Mus musculus
brenda
Chakraborty, A.; Latapy, C.; Xu, J.; Snyder, S.H.; Beaulieu, J.M.
Inositol hexakisphosphate kinase-1 regulates behavioral responses via GSK3 signaling pathways
Mol. Psychiatry
19
284-293
2014
Mus musculus
brenda
Prasad, A.; Jia, Y.; Chakraborty, A.; Li, Y.; Jain, S.K.; Zhong, J.; Roy, S.G.; Loison, F.; Mondal, S.; Sakai, J.; Blanchard, C.; Snyder, S.H.; Luo, H.R.
Inositol hexakisphosphate kinase 1 regulates neutrophil function in innate immunity by inhibiting phosphatidylinositol-(3,4,5)-trisphosphate signaling
Nat. Immunol.
12
752-760
2011
Homo sapiens, Mus musculus
brenda
Sarmah, B.; Wente, S.R.
Inositol hexakisphosphate kinase-2 acts as an effector of the vertebrate Hedgehog pathway
Proc. Natl. Acad. Sci. USA
107
19921-19926
2010
Danio rerio
brenda
Koldobskiy, M.A.; Chakraborty, A.; Werner, J.K.; Snowman, A.M.; Juluri, K.R.; Vandiver, M.S.; Kim, S.; Heletz, S.; Snyder, S.H.
p53-mediated apoptosis requires inositol hexakisphosphate kinase-2
Proc. Natl. Acad. Sci. USA
107
20947-20951
2010
Homo sapiens
brenda
Zhang, Z.; Liang, D.; Gao, X.; Zhao, C.; Qin, X.; Xu, Y.; Su, T.; Sun, D.; Li, W.; Wang, H.; Liu, B.; Cao, F.
Selective inhibition of inositol hexakisphosphate kinases (IP6Ks) enhances mesenchymal stem cell engraftment and improves therapeutic efficacy for myocardial infarction
Basic Res. Cardiol.
109
417
2014
Mus musculus (Q6PD10), Mus musculus (Q6ZQB6), Mus musculus (Q80V72), Mus musculus C57BL/6a (Q6PD10), Mus musculus C57BL/6a (Q6ZQB6), Mus musculus C57BL/6a (Q80V72)
brenda
Wundenberg, T.; Grabinski, N.; Lin, H.; Mayr, G.W.
Discovery of InsP6-kinases as InsP6-dephosphorylating enzymes provides a new mechanism of cytosolic InsP6 degradation driven by the cellular ATP/ADP ratio
Biochem. J.
462
173-184
2014
Homo sapiens, Rattus norvegicus
brenda
Chanduri, M.; Rai, A.; Malla, A.B.; Wu, M.; Fiedler, D.; Mallik, R.; Bhandari, R.
Inositol hexakisphosphate kinase 1 (IP6K1) activity is required for cytoplasmic dynein-driven transport
Biochem. J.
473
3031-3047
2016
Dictyostelium discoideum, Mus musculus (Q6PD10), Homo sapiens (Q92551), Mus musculus C57BL/6 (Q6PD10)
brenda
Ghosh, S.; Shukla, D.; Suman, K.; Lakshmi, B.J.; Manorama, R.; Kumar, S.; Bhandari, R.
Inositol hexakisphosphate kinase 1 maintains hemostasis in mice by regulating platelet polyphosphate levels
Blood
122
1478-1486
2013
Mus musculus (Q6PD10), Mus musculus C57BL/6 (Q6PD10)
brenda
Jadav, R.S.; Kumar, D.; Buwa, N.; Ganguli, S.; Thampatty, S.R.; Balasubramanian, N.; Bhandari, R.
Deletion of inositol hexakisphosphate kinase 1 (IP6K1) reduces cell migration and invasion, conferring protection from aerodigestive tract carcinoma in mice
Cell. Signal.
28
1124-1136
2016
Mus musculus (Q6PD10), Mus musculus
brenda
Wang, H.; Godage, H.Y.; Riley, A.M.; Weaver, J.D.; Shears, S.B.; Potter, B.V.
Synthetic inositol phosphate analogs reveal that PPIP5K2 has a surface-mounted substrate capture site that is a target for drug discovery
Chem. Biol.
21
689-699
2014
Homo sapiens (O43314)
brenda
Ghoshal, S.; Tyagi, R.; Zhu, Q.; Chakraborty, A.
Inositol hexakisphosphate kinase-1 interacts with perilipin1 to modulate lipolysis
Int. J. Biochem. Cell Biol.
78
149-155
2016
Mus musculus (Q6PD10)
brenda
Ye, C.; Bandara, W.M.; Greenberg, M.L.
Regulation of inositol metabolism is fine-tuned by inositol pyrophosphates in Saccharomyces cerevisiae
J. Biol. Chem.
288
24898-24908
2013
Saccharomyces cerevisiae (Q12494)
brenda
Yu, W.; Ye, C.; Greenberg, M.L.
Inositol hexakisphosphate kinase 1 (IP6K1) regulates inositol synthesis in mammalian cells
J. Biol. Chem.
291
10437-10444
2016
Mus musculus (Q6PD10)
brenda
Niger, C.; Luciotti, M.A.; Buo, A.M.; Hebert, C.; Ma, V.; Stains, J.P.
The regulation of runt-related transcription factor 2 by fibroblast growth factor-2 and connexin43 requires the inositol polyphosphate/protein kinase Cdelta cascade
J. Bone Miner. Res.
28
1468-1477
2013
Mus musculus (Q6PD10), Mus musculus (Q80V72), Mus musculus (Q8BWD2)
brenda
Fu, C.; Xu, J.; Li, R.J.; Crawford, J.A.; Khan, A.B.; Ma, T.M.; Cha, J.Y.; Snowman, A.M.; Pletnikov, M.V.; Snyder, S.H.
Inositol hexakisphosphate kinase-3 regulates the morphology and synapse formation of cerebellar Purkinje cells via spectrin/adducin
J. Neurosci.
35
11056-11067
2015
Mus musculus (Q8BWD2)
brenda
Nagata, E.; Nonaka, T.; Moriya, Y.; Fujii, N.; Okada, Y.; Tsukamoto, H.; Itoh, J.; Okada, C.; Satoh, T.; Arai, T.; Hasegawa, M.; Takizawa, S.
Inositol hexakisphosphate kinase 2 promotes cell death in cells with cytoplasmic TDP-43 aggregation
Mol. Neurobiol.
53
5377-5383
2016
Homo sapiens (Q9UHH9), Homo sapiens
brenda
Wang, H.; DeRose, E.F.; London, R.E.; Shears, S.B.
IP6K structure and the molecular determinants of catalytic specificity in an inositol phosphate kinase family
Nat. Commun.
5
4178
2014
Entamoeba histolytica (C4M387), Entamoeba histolytica
brenda
Desai, M.; Rangarajan, P.; Donahue, J.L.; Williams, S.P.; Land, E.S.; Mandal, M.K.; Phillippy, B.Q.; Perera, I.Y.; Raboy, V.; Gillaspy, G.E.
Two inositol hexakisphosphate kinases drive inositol pyrophosphate synthesis in plants
Plant J.
80
642-653
2014
Arabidopsis thaliana, Arabidopsis thaliana Col-0
brenda
Zhan, H.; Zhong, Y.; Yang, Z.; Xia, H.
Enzyme activities of Arabidopsis inositol polyphosphate kinases AtIPK2? and AtIPK2? are involved in pollen development, pollen tube guidance and embryogenesis.
Plant J.
82
758-771
2015
Arabidopsis thaliana (Q9FLT2), Arabidopsis thaliana (Q9LY23)
brenda
Rao, F.; Xu, J.; Khan, A.B.; Gadalla, M.M.; Cha, J.Y.; Xu, R.; Tyagi, R.; Dang, Y.; Chakraborty, A.; Snyder, S.H.
Inositol hexakisphosphate kinase-1 mediates assembly/disassembly of the CRL4-signalosome complex to regulate DNA repair and cell death
Proc. Natl. Acad. Sci. USA
111
16005-16010
2014
Mus musculus (Q6PD10)
brenda
Nair, V.; Gu, C.; Janoshazi, A.; Jessen, H.; Wang, H.; Shears, S.
Inositol pyrophosphate synthesis by diphosphoinositol pentakisphosphate kinase-1 is regulated by phosphatidylinositol(4,5)bisphosphate
Biosci. Rep.
38
BSR20171549
2018
Homo sapiens (Q6PFW1)
brenda
Rajasekaran, S.S.; Kim, J.; Gaboardi, G.C.; Gromada, J.; Shears, S.B.; Dos Santos, K.T.; Nolasco, E.L.; Ferreira, S.S.; Illies, C.; Koehler, M.; Gu, C.; Ryu, S.H.; Martins, J.O.; Dare, E.; Barker, C.J.; Berggren, P.O.
Inositol hexakisphosphate kinase 1 is a metabolic sensor in pancreatic beta-cells
Cell. Signal.
46
120-128
2018
Mus musculus (Q6PD10), Homo sapiens (Q92551)
brenda
Gu, C.; Nguyen, H.N.; Hofer, A.; Jessen, H.J.; Dai, X.; Wang, H.; Shears, S.B.
The significance of the bifunctional kinase/phosphatase activities of diphosphoinositol pentakisphosphate kinases (PPIP5Ks) for coupling inositol pyrophosphate cell signaling to cellular phosphate homeostasis
J. Biol. Chem.
292
4544-4555
2017
Homo sapiens (O43314), Homo sapiens (Q6PFW1)
brenda
Wilson, M.S.; Jessen, H.J.; Saiardi, A.
The inositol hexakisphosphate kinases IP6K1 and -2 regulate human cellular phosphate homeostasis, including XPR1-mediated phosphate export
J. Biol. Chem.
294
11597-11608
2019
Homo sapiens (Q92551), Homo sapiens (Q9UHH9), Homo sapiens
brenda
Nagpal, L.; Fu, C.; Snyder, S.H.
Inositol hexakisphosphate kinase-2 in cerebellar granule cells regulates Purkinje cells and motor coordination via protein 4.1N
J. Neurosci.
38
7409-7419
2018
Mus musculus (Q80V72)
brenda
Nagata, E.; Fujii, N.; Kohara, S.; Okada, C.; Satoh, T.; Takekoshi, S.; Takao, M.; Mihara, B.; Takizawa, S.
Inositol hexakisphosphate kinase 2 promotes cell death of anterior horn cells in the spinal cord of patients with myotrophic lateral sclerosis
Mol. Biol. Rep.
47
6479-6485
2020
Homo sapiens (Q9UHH9), Homo sapiens
brenda
Kim, M.G.; Zhang, S.; Park, H.; Park, S.J.; Kim, S.; Chung, C.
Inositol hexakisphosphate kinase-1 is a key mediator of prepulse inhibition and short-term fear memory
Mol. Brain
13
72
2020
Mus musculus (Q6PD10), Mus musculus
brenda
Yousaf, R.; Gu, C.; Ahmed, Z.M.; Khan, S.N.; Friedman, T.B.; Riazuddin, S.; Shears, S.B.; Riazuddin, S.
Mutations in diphosphoinositol-pentakisphosphate kinase PPIP5K2 are associated with hearing loss in human and mouse
PLoS Genet.
14
e1007297
2018
Homo sapiens (O43314), Homo sapiens
brenda
Wormald, M.; Liao, G.; Kimos, M.; Barrow, J.; Wei, H.
Development of a homogenous high-throughput assay for inositol hexakisphosphate kinase 1 activity
PLoS ONE
12
e0188852
2017
Homo sapiens (Q92551), Homo sapiens
brenda
Fu, C.; Xu, J.; Cheng, W.; Rojas, T.; Chin, A.C.; Snowman, A.M.; Harraz, M.M.; Snyder, S.H.
Neuronal migration is mediated by inositol hexakisphosphate kinase 1 via alpha-actinin and focal adhesion kinase
Proc. Natl. Acad. Sci. USA
114
2036-2041
2017
Mus musculus (Q6PD10)
brenda
Rojas, T.; Cheng, W.; Gao, Z.; Liu, X.; Wang, Y.; Malla, A.P.; Chin, A.C.; Romer, L.H.; Snyder, S.H.; Fu, C.
Inositol hexakisphosphate kinase 3 promotes focal adhesion turnover via interactions with dynein intermediate chain 2
Proc. Natl. Acad. Sci. USA
116
3278-3287
2019
Mus musculus (Q8BWD2), Homo sapiens (Q96PC2)
brenda
Chin, A.; Gao, Z.; Riley, A.; Furkert, D.; Wittwer, C.; Dutta, A.; Rojas, T.; Semenza, E.; Felder, R.; Pluznick, J.; Jessen, H.; Fiedler, D.; Potter, B.; Snyder, S.; Fu, C.
The inositol pyrophosphate 5-InsP7drives sodium-potassium pump degradation by relieving an autoinhibitory domain of PI3K p85alpha
Sci. Adv.
6
eabb8542
2020
Mus musculus (Q6PD10)
brenda
Moritoh, Y.; Oka, M.; Yasuhara, Y.; Hozumi, H.; Iwachidow, K.; Fuse, H.; Tozawa, R.
Inositol hexakisphosphate kinase 3 regulates metabolism and lifespan in mice
Sci. Rep.
6
32072
2016
Mus musculus (Q8BWD2), Mus musculus, Homo sapiens (Q96PC2), Homo sapiens
brenda
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