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Information on EC 2.7.1.134 - inositol-tetrakisphosphate 1-kinase
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EC Tree
2.7.1.134 inositol-tetrakisphosphate 1-kinaseIUBMB Comments
This enzyme also phosphorylates Ins(1,3,4)P3 on O-5 and O-6. The phosphotransfer from ATP to either inositol 1,3,4-trisphosphate or inositol 3,4,5,6-tetrakisphosphate appears to be freely reversible to the extent that the enzyme can act like an inositol polyphosphate phosphatase in the presence of ADP. It can also catalyse an isomerization between Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP. The enzymes from animals and plants also have the activity of EC 2.7.1.159, inositol-1,3,4-trisphosphate 5/6-kinase.
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Word Map
- 2.7.1.134
- hexakisphosphate
-
2-kinase
-
itpks
- polyphosphate
- 1,3,4,6-tetrakisphosphate
-
atp-grasp
- signalosome
-
phytic
- phytate
- agriculture
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
Synonyms
inositol 1,3,4-trisphosphate 5/6-kinase, osipk, itpk2, ositpk6, hvipk, inositol 1,3,4-trisphosphate 5/6 kinase, inositol tris/tetrakisphosphate kinase 1, inositol-tetrakisphosphate 1-kinase, inositol 1,4,5,6-tetrakisphosphate 3-kinase, inositol 1,3,4-trisphosphate 5/6-kinase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-myo-inositol-trisphosphate 6-kinase
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-
-
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1D-myo-inositol-tetrakisphosphate 1-kinase
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-
-
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1D-myo-inositol-trisphosphate 5-kinase
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-
-
-
ATP:1D-myo-inositol-1,3,4-trisphosphate 5-phosphoransferase
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-
-
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ATP:1D-myo-inositol-1,3,4-trisphosphate 6-phosphoransferase
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-
-
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EC 2.7.1.133
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-
formerly
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EC 2.7.1.139
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formerly
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inositol 1,3,4-trisphosphate 5/6 kinase
inositol 1,3,4-trisphosphate 5/6-kinase
inositol 1,4,5,6-tetrakisphosphate 3-kinase
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-
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inositol-trisphosphate 5-kinase
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-
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inositol-trisphosphate 6-kinase
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-
-
-
Ipk kinase
ITPK1
ITPK3
kinase, inositol 1,4,5,6-tetrakisphosphate 3- (phosphorylating)
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-
-
-
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol-3,4,5,6-tetrakisphosphate 1-phosphotransferase
This enzyme also phosphorylates Ins(1,3,4)P3 on O-5 and O-6. The phosphotransfer from ATP to either inositol 1,3,4-trisphosphate or inositol 3,4,5,6-tetrakisphosphate appears to be freely reversible to the extent that the enzyme can act like an inositol polyphosphate phosphatase in the presence of ADP. It can also catalyse an isomerization between Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP. The enzymes from animals and plants also have the activity of EC 2.7.1.159, inositol-1,3,4-trisphosphate 5/6-kinase.
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CAS REGISTRY NUMBER
COMMENTARY
113356-25-5
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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
ATP + 1D-myo-inositol 1,4,6-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
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-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol 3,4,6-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
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-
-
?
ATP + myo-inositol-1,3,4,6-tetrakisphosphate
ADP + myo-inositol-1,3,4,5-tetrakisphosphate
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-
r
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,2,3,4-tetrakisphosphate
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-
minor product
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
enzyme ITPK1 has robust enantiospecific hydroxykinase activity against Ins(3,4,5,6)P4
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-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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no activity with inositol-1,3,4,5-tetrakisphosphate
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?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
enzyme has both inositol-3,4,5,6-tetrakisphosphate 1-kinase and inositol-1,3,4-trisphosphate 5/6 kinase activity, 2 times higher activity than with inositol-1,3,4-trisphosphate, no activity with inositol-1,4-bisphosphate, inositol-1,4,5-trisphosphate, inositol-1,3,4,5-tetrakisphosphate, inositol-1,3,4,6-tetrakisphosphate or inositol-1,3,4,5,6-pentakisphosphate
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?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
enzyme has 1-kinase and 1-phosphatase activity as well as phosphomutase activity
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r
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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no activity with D-myo-inositol 1,3,4,5-tetrakisphosphate
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?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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i.e. L-myo-inositol 1,4,5,6-tetrakisphosphate, phosphorylation site: L-3 or D-1 substitution position
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?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
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?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
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?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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no activity with D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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i.e. L-myo-inositol 1,4,5,6-tetrakisphosphate, phosphorylation site: L-3 or D-1 substitution position
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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involved in synthesis of higher phosphorylated inositol phosphates
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?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
involved in synthesis of higher phosphorylated inositol phosphates
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?
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,3,4,5-tetrakisphosphate
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-
-
?
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,3,4,5-tetrakisphosphate
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-
major product
ir
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,3,4,5-tetrakisphosphate
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-
?
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,3,4,5-tetrakisphosphate
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r
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,3,4,6-tetrakisphosphate
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-
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?
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,3,4,6-tetrakisphosphate
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-
minor product
?
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,3,4,6-tetrakisphosphate
enzyme has both inositol-1,3,4-trisphosphate 5-kinase and inositol-1,3,4-trisphosphate 6-kinase activity
5:1 ratio of inositol-tetrakis-1,3,4,6-phosphate and inositol-1,2,4,5-tetrakisphosphate
?
ATP + myo-inositol-3,4,6-trisphosphate
ADP + myo-inositol-1,3,4,6-tetrakisphosphate
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-
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?
ATP + myo-inositol-3,4,6-trisphosphate
ADP + myo-inositol-1,3,4,6-tetrakisphosphate
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r
additional information
?
-
the enzyme also performs the reactions of EC 2.7.1.159, phosphorylation of position 5 and/or 6 of 1D-myo-inositol 1,3,4-trisphosphate
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-
?
additional information
?
-
the enzyme also performs the reactions of EC 2.7.1.159, phosphorylation of position 5 and/or 6 of 1D-myo-inositol 1,3,4-trisphosphate
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-
?
additional information
?
-
-
the enzyme also performs the reactions of EC 2.7.1.159, phosphorylation of position 5 and/or 6 of 1D-myo-inositol 1,3,4-trisphosphate
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-
?
additional information
?
-
substrate docking calculations, substrate specificity of Arabidopsis thaliana ITPK1, overview. Lack of Ins(1,4,5,6)P4/Ins(3,4,5,6) P4 product for Ins(1,4,6)P3 or Ins(3,4,6)P3 substrates. Consistent with the phosphorylation of the enantiomeric pair Ins(1,4,5,6)P4/Ins (3,4,5,6)P4, ITPK1 shows phosphorylation of Ins(1,4,6)P3 at the 3-position and Ins(3,4,6)P3 at the 1-position. ITPK1 has robust enantiospecific hydroxykinase activity against Ins(3,4,5,6)P4. With inositol tris/tetrakisphosphate kinase 1 (ITPK1, EC 2.7.1.134) and inositol pentakisphosphate 2-kinase (IPK1, EC 2.7.1.158) combined at a 1:20 ATP:ADP ratio, InsP6 is converted via Ins(1,3,4,5,6)P5 to Ins(3,4,5,6) P4 and/or Ins(1,4,5,6)P4 with concomitant generation of ATP
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-
-
additional information
?
-
the enzyme also performs the reactions of EC 2.7.1.159, phosphorylation of position 5 and/or 6 of 1D-myo-inositol 1,3,4-trisphosphate
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-
?
additional information
?
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-
phosphate is transferred between inositol phosphates via ITPK1-bound nucleotide. Intersubstrate phosphate transfer explains how competing substrates are able to stimulate each others catalysis by ITPK1
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-
?
additional information
?
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Ipk kinase plays a significant role in the inositol phosphate interacting network in plants
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-
?
additional information
?
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-
Ipk kinase plays a significant role in the inositol phosphate interacting network in plants
-
-
?
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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 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
involved in synthesis of higher phosphorylated inositol phosphates
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
involved in synthesis of higher phosphorylated inositol phosphates
-
?
additional information
?
-
-
phosphate is transferred between inositol phosphates via ITPK1-bound nucleotide. Intersubstrate phosphate transfer explains how competing substrates are able to stimulate each others catalysis by ITPK1
-
-
?
additional information
?
-
-
Ipk kinase plays a significant role in the inositol phosphate interacting network in plants
-
-
?
additional information
?
-
-
Ipk kinase plays a significant role in the inositol phosphate interacting network in plants
-
-
?
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
inositol-1,3,4-trisphosphate
activation of inositol-1,3,4,5,6-phosphate 1-phosphatase activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
OsITL1 gene encoding an inositol 1,3,4-trisphosphate 5/6-kinase is a negative regulator of osmotic stress signaling.
Neoplasms
Increased levels of inositol hexakisphosphate (InsP6) protect HEK293 cells from tumor necrosis factor (alpha)- and Fas-induced apoptosis.
Neoplasms
Inositol 1,3,4-trisphosphate 5/6-kinase inhibits tumor necrosis factor-induced apoptosis.
Neural Tube Defects
Expression of inositol 1,3,4-trisphosphate 5/6-kinase (ITPK1) and its role in neural tube defects.
Neural Tube Defects
Neural tube defects in mice with reduced levels of inositol 1,3,4-trisphosphate 5/6-kinase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
myo-inositol-3,4,5,6-tetrakisphosphate
pH 7.2, 37°C, recombinant enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
expression pattern of isozyme ITPK2, no or very poor expression in stem
brenda
3.6 kilobases transcript detected by Northern blot
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
substrate/product analysis using anion exchange chromatography on an acid- and hydroxide-stable quaternary amine functionalized latex, substrate docking calculations, resolvement and measurement of diphosphoinositol phosphates beside lower inositol phosphates without the use of radiolabel, method, overview. Modeling of the binding of the enantiomers Ins(1,4,5,6)P4 and Ins(3,4,5,6)P4 to ITPK1. Significant interaction of the 4-phosphate of Ins(1,4,5,6)P4 and of the 6-phosphate of the Ins(3,4,5,6)P4 in site F. The respective 1- and 3-phosphates of Ins(1,4,5,6)P4 and Ins(3,4,5,6)P4 make contacts in site C. These subsites are likely determinants of the reactivity of ITPK1
evolution
Arabidopsis thaliana ITPK1, belongs to a class of enzyme that has been shown to possess 1-, 5- and 6-hydroxykinase and (InsP6) 5-phosphokinase activities
evolution
OsITPK6 belongs to subgroup III, with 12 exons and 11 introns, of the OsITPK gene family. ITPK6 is a unique gene in the ITPK gene family
malfunction
-
generation of a mouse strain harboring a beta-galactosidase gene trap cassette in the second intron of the Itpk1 gene leads to animals, homozygous for this gene trap, which are viable, fertile, they produce less ITPK1 protein than wild-type and heterozygous animals, embryos resulting from homozygous matings uncovered neural tube defects in some animals and axial skeletal defects or growth retardation in others
malfunction
loss of this gene in itpk3-1 does neither affect phytate seed levels, nor seed Zn, Fe, and Mn but the micronutrient bioavailability is strongly reduced by seed phytate that forms complexes with seed cations. Low seed zinc is primarily caused by plant growth in Zn-deficient soil
malfunction
the epidermis structure of seed coat is irregularly formed in seeds of itpk2-1 mutant, resulting in the increased permeability of seed coat to tetrazolium salts. The cell wall shows a dramatic decrease in composition of suberin and cutin, which relate to the permeability of seed coat and the formation of which is accompanied with seed coat development. ITPK2 deficiency results in the distorted seed coat and crumpled columellas. Seed coat of itpk2-1 mutant presents high permeability to 2,3,5-triphenyltetrazolium and has less mucilage
malfunction
although both ipk1-1 and itpk1 mutants exhibit decreased levels of InsP6 (phytate) and diphosphoinositol pentakisphosphate (PP-InsP5, InsP7), disruption of another ITPK family enzyme, ITPK4, which correspondingly causes depletion of InsP6 and InsP7, does not display similar phosphate-related phenotypes, which precludes these InsP species from being effectors. Notably, the level of D/L-Ins(3,4,5,6)P4 is concurrently elevated in both ipk1-1 and itpk1 mutants, which demonstrates a specific correlation with the misregulated phosphate phenotypes. The level of D/L-Ins(3,4,5,6)P4 is not responsive to phosphate starvation that instead manifests a shoot-specific increase in the InsP7 level. ITPK1 overexpression significantly decreases phosphate uptake activity, in contrast to the elevated uptake activity shown by itpk1 mutants. In addition, several PSR genes are downregulated in ITPK1-overexpressing lines compared with the wild-type (e.g. PHT1:2, SPX1, AT4, IPS1 and PAP17)
malfunction
mutation of OsITPK6 not only significantly reduces the accumulation of IP6 in rice grains but also impairs plant growth and tolerance to abiotic stress. Nucleotide substitutions of gene OsITPK6 can significantly lower the phytic acid content in rice grains. Impact of ositpk6 mutations on plant growth and seed germination, panicle phenotype of mutant OsITPK6 and wild-type plants, overview. There is no significant difference in the number of leaves and roots with or without stress treatment between ositpk6_1 and wild-type
malfunction
-
loss of this gene in itpk3-1 does neither affect phytate seed levels, nor seed Zn, Fe, and Mn but the micronutrient bioavailability is strongly reduced by seed phytate that forms complexes with seed cations. Low seed zinc is primarily caused by plant growth in Zn-deficient soil
-
malfunction
-
generation of a mouse strain harboring a beta-galactosidase gene trap cassette in the second intron of the Itpk1 gene leads to animals, homozygous for this gene trap, which are viable, fertile, they produce less ITPK1 protein than wild-type and heterozygous animals, embryos resulting from homozygous matings uncovered neural tube defects in some animals and axial skeletal defects or growth retardation in others
-
metabolism
measurement of Fe, Zn, and Mn concentrations in seeds of Arabidopsis thaliana accessions grown in Zn-deficient and Zn-amended conditions, overview. Inositol 1,3,4-trisphosphate 5/6-kinase 3 gene (ITPK3), located close to a significant nucleotide polymorphism associated with relative Zn seed concentrations, is dispensable for seed micronutrients accumulation in ecotype Col-0
metabolism
inositol tris/tetrakisphosphate kinase 1 (ITPK1, EC 2.7.1.134) and inositol pentakisphosphate 2-kinase (IPK1, EC 2.7.1.158) comprise a reversible metabolic cassette converting Ins(3,4,5,6)P4 into 5-InsP7 and back in a nucleotide-dependent manner. Ability of Arabidopsis inositol tris/tetrakisphosphate kinase 1 to discriminate between symmetric and enantiomeric substrates in the production of diverse symmetric and asymmetric myo-inositol phosphate and diphospho-myo-inositol phosphate (inositol pyrophosphate) products
metabolism
the kinase activity of inositol pentakisphosphate 2-kinase (IPK1) is required for phytate (inositol hexakisphosphate, InsP6) synthesis, and is indispensable for maintaining phosphate homeostasis under phosphate-replete conditions. Inositol 1,3,4-trisphosphate 5/6-kinase 1 (ITPK1) plays an equivalent role. Genetic dissection of the roles for InsP and PP-InsP biosynthesis enzymes in regulation of phosphate homeostasis, overview
metabolism
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measurement of Fe, Zn, and Mn concentrations in seeds of Arabidopsis thaliana accessions grown in Zn-deficient and Zn-amended conditions, overview. Inositol 1,3,4-trisphosphate 5/6-kinase 3 gene (ITPK3), located close to a significant nucleotide polymorphism associated with relative Zn seed concentrations, is dispensable for seed micronutrients accumulation in ecotype Col-0
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physiological function
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key regulatory enzyme at the branch point for the synthesis of inositol hexakisphosphate, an intracellular signaling molecule implicated in the regulation of ion channels, endocytosis, exocytosis, transcription, DNA repair, and RNA export from the nucleus
physiological function
enzyme ITPK2 plays an essential role in seed coat development and lipid polyester barrier formation
physiological function
the enzyme is required for phytate (inositol hexakisphosphate, InsP6) synthesis and involved in maintaining phosphate homeostasis under phosphate-replete conditions
physiological function
-
key regulatory enzyme at the branch point for the synthesis of inositol hexakisphosphate, an intracellular signaling molecule implicated in the regulation of ion channels, endocytosis, exocytosis, transcription, DNA repair, and RNA export from the nucleus
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Show AA Sequence and Transmembrane Helices (2297 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H162D
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loss-of-function for Ins(1,3,4)P3 in the H162D mutant is matched by a 200fold reduction in its Ins(1,3,4)P3 kinase activity. The H162D mutant dephosphorylats Ins(1,3,4,5,6)P5 almost twice as fast as the wild-type enzyme. The H162D mutant also displays very limited ability to transfer phosphate from Ins(1,3,4,5,6)P5 to Ins(1,3,4)P3 in the presence of physiological concentrations of nucleotide
P522L
ositpk6 mutant, the line with the P522L amino acid substitution has agronomic performance (seed weight, germination, and seedling growth) similar to that of its wild-type parent
additional information
additional information
construction of the homogenous At4g08170 mutant (SALK_120653C,NASCcode N653925) carrying a T-DNA insertion in the intron in wild-type line Col-0
additional information
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construction of the homogenous At4g08170 mutant (SALK_120653C,NASCcode N653925) carrying a T-DNA insertion in the intron in wild-type line Col-0
additional information
functional analysis of itpk2-1 mutant (SAIL_25_H09), phenotype, overview
additional information
generation of itpk1-1 mutants, phenotype, overview. Genetic interaction analysis of bifunctional ITPK1 (EC 2.7.1.159/EC 2.7.1.134) and IPK1 (EC 2.7.1.158) with a genetic cross between ipk1-1 and itpk1 mutants. The ipk1-1 itpk1 double mutants exhibit more severe growth defects than single mutants and those that proceed to the reproductive stage bore aborted seeds. Common elevation of D/L-Ins(3,4,5,6)P4 in itpk1 and ipk1-1 mutants
additional information
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generation of itpk1-1 mutants, phenotype, overview. Genetic interaction analysis of bifunctional ITPK1 (EC 2.7.1.159/EC 2.7.1.134) and IPK1 (EC 2.7.1.158) with a genetic cross between ipk1-1 and itpk1 mutants. The ipk1-1 itpk1 double mutants exhibit more severe growth defects than single mutants and those that proceed to the reproductive stage bore aborted seeds. Common elevation of D/L-Ins(3,4,5,6)P4 in itpk1 and ipk1-1 mutants
additional information
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construction of the homogenous At4g08170 mutant (SALK_120653C,NASCcode N653925) carrying a T-DNA insertion in the intron in wild-type line Col-0
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additional information
OsITPK6 mutants are generated by CRISPR/Cas9-mediated mutagenesis, generation of 23 hygromycin phosphotransferase (HPT)-positive T0 plants transformed with the CRISPR/Cas9 vector pH-itpk6. Genotyping of gene ITPK6, the ositpk6_1 (a 6-nt in-frame deletion) mutation results in the loss of two amino acids at positions 91 to 92. In contrast, all the other three mutations, i.e. ositpk6_2 (a 1-nt insertion), ositpk6_3 (a 5-nt deletion), and ositpk6_4 (a 2-nt deletion), generate a premature stop codon almost right after the mutation site and, hence, significantly shorten the encoded proteins. Consequently, the ositpk6_2, _3 and _4 mutant alleles are predicted to produce proteins of only 105, 103, and 104 amino acids, respectively. The two amino acids missing in the ositpk6_1 mutant are located in a highly conserved segment, suggesting the mutation of ositpk6_1 might have a potential functional consequence. Plant growth of mutants ositpk6_2, _3, and _4 is significantly impaired. Their panicles are significantly shorter (30.1%, 28.8%, and 29.1%, respectively) compared to wild-type parental cultivar Xidao 1, phenotypes, overview. Numbers and lengths of root from mutant plants are reduced under salt stress compared to wild-type
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10 mM sodium diphosphate stabilizes ammonium sulfate precipitated enzyme, no loss of activity after 2 days at 4°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 1 mg/ml bovine serum albumin, 20% glycerol, 6 months, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged enzyme from Escherichia coli strain Rosetta 2(DE3)pLysS by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a recombinant fusion protein between GST and residues 124-311 of human ITPK1 is prepared in Escherichia coli to produce antibodies for Western blotting
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expressed in Escherichia coli
gene ITPK1, sequence comparisons, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain Rosetta 2(DE3)pLysS
gene ITPK2, expression analysis of wild-type and mutant enzymes by quantitative real-time PCR analysis
gene itpk3-1, genotyping, 108 different accessions, the Arabidopsis accessions differ in their response to Zn deficiency, quantitative real-time PCR enzyme expression anaysis, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
there is no significant difference in the number of leaves and roots with or without stress treatment between ositpk6_1 and wild-type
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
OsITPK6 can be a desirable target of mutagenesis for breeding yield-competitive lpa rice
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Craxton, A.; Erneux, C.; Shears, S.B.
Inositol 1,4,5,6-tetrakisphosphate is phosphorylated in rat liver by a 3-kinase that is distinct from inositol 1,4,5-trisphosphate 3-kinase
J. Biol. Chem.
269
4337-4342
1994
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Stephens, L.R.; Hawkins, P.T.; Morris, A.J.; Downes, C.P.
L-myo-inositol 1,4,5,6-tetrakisphosphate (3-hydroxy)kinase
J. Biol. Chem.
249
283-292
1988
Mus musculus, Rattus norvegicus
brenda
Balla, T.; Hunyadi, L.; Baukal, A.J.; Catt, K.J.
Structures and metabolism of inositol tetrakisphosphates and inositol pentakisphosphate in bovine adrenal glomerulosa cells
J. Biol. Chem.
264
9386-9390
1989
Bos taurus
brenda
Wilson, M.P.; Majerus, P.W.
Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning, and expression of the recombinant enzyme
J. Biol. Chem.
271
11904-11910
1996
Bos taurus, Homo sapiens (Q13572), Homo sapiens
brenda
Tan, Z.; Bruzik, K.S.; Shears, S.B.
Properties of the inositol 3,4,5,6-tetrakisphosphate 1-kinase purified from rat liver. Regulation of enzyme activity by inositol 1,3,4-trisphosphate
J. Biol. Chem.
272
2285-2290
1997
Rattus norvegicus
brenda
Phillippy, B.Q.
Identification of inositol 1,3,4-trisphosphate 5-kinase and inositol 1,3,4,5-tetrakisphosphate 6-kinase in immature soybean seeds
Plant Physiol.
116
291-297
1998
Glycine max
-
brenda
Brearley, C.A.; Hanke, D.E.
Metabolic relations of inositol 3,4,5,6-tetrakisphosphate revealed by cell permeabilization. Identification of inositol 3,4,5, 6-tetrakisphosphate 1-kinase and inositol 3,4,5,6-tetrakisphosphate phosphatase activities in mesophyll cells
Plant Physiol.
122
1209-1216
2000
Commelina communis
brenda
Yang, X.; Shears, B.S.
Multitasking in signal transduction by a promiscuous human ins(3,4,5,6)P4 1-kinase/ins(1,3,4)P3 5/6-kinase
Biochem. J.
351
551-555
2000
Homo sapiens (Q13572)
-
brenda
Ho, M.W.Y.; Yang, X.; Carew, M.A.; Zhang, T.; Hua, L.; Kwon, Y-U.; Chung, S-K.; Adelt, S.; Vogel, G.; Riley, a.M.; Potter, B.V.L.; Shears, S.B.
Regulation of ins(3,4,5,6)P4 signaling by a reversible kinase/phosphatase
Curr. Biol.
12
477-482
2002
Homo sapiens (Q13572)
brenda
Josefsen, L.; Bohn, L.; Sorensen, M.B.; Rasmussen, S.K.
Characterization of a multifunctional inositol phosphate kinase from rice and barley belonging to the ATP-grasp superfamily
Gene
397
114-125
2007
Hordeum vulgare, Oryza sativa
brenda
Chamberlain, P.P.; Qian, X.; Stiles, A.R.; Cho, J.; Jones, D.H.; Lesley, S.A.; Grabau, E.A.; Shears, S.B.; Spraggon, G.
Integration of inositol phosphate signaling pathways via human ITPK1
J. Biol. Chem.
282
28117-28125
2007
Homo sapiens
brenda
Wilson, M.P.; Hugge, C.; Bielinska, M.; Nicholas, P.; Majerus, P.W.; Wilson, D.B.
Neural tube defects in mice with reduced levels of inositol 1,3,4-trisphosphate 5/6-kinase
Proc. Natl. Acad. Sci. USA
106
9831-9835
2009
Mus musculus, Mus musculus C57BL6
brenda
Tang, Y.; Tan, S.; Xue, H.
Arabidopsis inositol 1,3,4-trisphosphate 5/6 kinase 2 is required for seed coat development
Acta Biochim. Biophys. Sin. (Shanghai)
45
549-560
2013
Arabidopsis thaliana (O81893)
brenda
Chen, X.; Yuan, L.; Ludewig, U.
Natural genetic variation of seed micronutrients of Arabidopsis thaliana grown in zinc-deficient and zinc-amended soil
Front. Plant Sci.
7
1070
2016
Arabidopsis thaliana (Q9SUG3), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9SUG3)
brenda
Whitfield, H.; White, G.; Sprigg, C.; Riley, A.M.; Potter, B.V.L.; Hemmings, A.M.; Brearley, C.A.
An ATP-responsive metabolic cassette comprised of inositol tris/tetrakisphosphate kinase 1 (ITPK1) and inositol pentakisphosphate 2-kinase (IPK1) buffers diphosphosphoinositol phosphate levels
Biochem. J.
477
2621-2638
2020
Arabidopsis thaliana (Q9SBA5)
brenda
Kuo, H.; Hsu, Y.; Lin, W.; Chen, K.; Munnik, T.; Brearley, C.; Chiou, T.
Arabidopsis inositol phosphate kinases IPK1 and ITPK1 constitute a metabolic pathway in maintaining phosphate homeostasis
Plant J.
95
613-630
2018
Arabidopsis thaliana (Q9SBA5), Arabidopsis thaliana
brenda
Jiang, M.; Liu, Y.; Liu, Y.; Tan, Y.; Huang, J.; Shu, Q.
Mutation of inositol 1,3,4-trisphosphate 5/6-kinase6 impairs plant growth and phytic acid synthesis in rice
Plants (Basel)
8
114
2019
Oryza sativa Japonica Group (Q0J0B2)
brenda
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