Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.1.149 - 1-phosphatidylinositol-5-phosphate 4-kinase and Organism(s) Rattus norvegicus

for references in articles please use BRENDA:EC2.7.1.149
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphatidylinositol 4-kinase, type ii kinase, pip4k2a, type ii ptdins 4-kinase, pip4k, pip4k2b, pip4k2c, mss4p, type ii phosphatidylinositol 4-kinase, phosphatidylinositol 5-phosphate 4-kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-phosphatidylinositol-4-phosphate 5-kinase
-
-
-
-
1-phosphatidylinositol-4-phosphate kinase
-
-
-
-
Diphosphoinositide kinase
-
-
-
-
phosphatidylinositol 4-phosphate 5-kinase gamma
-
-
PIP(4)K
-
-
-
-
PIP4Kalpha
-
-
PIP4Kbeta
-
-
PIP5Kgamma
-
-
PIP5KII-alpha
-
-
-
-
PIP5KIII
-
-
-
-
PIPKII
-
-
-
-
PIPKIIalpha
-
-
PtdIns(4)P-5-kinase B isoform
-
-
-
-
PtdIns(4)P-5-kinase C isoform
-
-
-
-
PtdIns5P-4-kinase
-
-
type II alpha phosphatidylinositol-5-phosphate 4-kinase
-
-
type II PIP kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
ATP:1-phosphatidyl-1D-myo-inositol-5-phosphate 4-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
104645-76-3
-
247907-17-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
show the reaction diagram
additional information
?
-
-
isozyme PIP4Kbeta interacts in vitro and in vivo with the PIP4Kalpha isoform. PIP4Kbeta has 2000fold less activity towards 1-phosphatidyl-1D-myo-inositol 5-phosphate compared with PIP4Kalpha, the majority of enzyme activity associated with PIP4Kbeta comes from its interaction with PIP4Kalpha
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
show the reaction diagram
additional information
?
-
-
isozyme PIP4Kbeta interacts in vitro and in vivo with the PIP4Kalpha isoform. PIP4Kbeta has 2000fold less activity towards 1-phosphatidyl-1D-myo-inositol 5-phosphate compared with PIP4Kalpha, the majority of enzyme activity associated with PIP4Kbeta comes from its interaction with PIP4Kalpha
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
light-driven translocation of PIPKIIalpha from the rod inner segment to rod outer segment, and subsequent binding to the ROS membrane
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
PIPKIIbeta and PIPKIIalpha
Manually annotated by BRENDA team
-
isozyme PIP4Kbeta can modulate the nuclear localization of isozyme PIP4Kalpha
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
two subfamilies of phosphatidylinositol 5-phosphate 4-kinases produce 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate from independent pools of substrates. In addition, type I and II subfamilies of PIPK can localize in different subcellular compartments and are involved in the synthesis of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate in distinct sites within cell
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PI42A_RAT
406
0
46210
Swiss-Prot
other Location (Reliability: 5)
PI42B_RAT
416
0
47264
Swiss-Prot
other Location (Reliability: 5)
PI42C_RAT
420
0
47049
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
crystal structure of isozyme PIP4Kbeta
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
enzyme PIPKIIgamma is phosphorylated in vivo. Phosphorylation is induced by treatment of mitogens such as serum and epidermal growth factor
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
knockdown of both isozymes, enzyme activity associated with kinase-inactive Myc-PIP4Kbeta is reduced to 24% compared with that associated with the active Myc-PIP4Kbeta
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant Myc-tagged isozymes by affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in COS-7 cells
-
recombinant expression of Myc-tagged isozymes, co-expression of the wild-type PIP4Kalpha isozyme suppresses ubiquitination of isozyme PIP4Kbeta
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Itoh, T.; Ijuin, T.; Takenawa, T.
A novel phosphatidylinositol-5-phosphate 4-kinase (phosphatidylinositol-phosphate kinase IIgamma) is phosphorylated in the endoplasmic reticulum in response to mitogenic signals
J. Biol. Chem.
273
20292-20299
1998
Rattus norvegicus
Manually annotated by BRENDA team
Bultsma, Y.; Keune, W.J.; Divecha, N.
PIP4Kbeta interacts with and modulates nuclear localization of the high-activity PtdIns5P-4-kinase isoform PIP4Kalpha
Biochem. J.
430
223-235
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Huang, Z.; Anderson, R.E.; Cao, W.; Wiechmann, A.F.; Rajala, R.V.
Light-induced tyrosine phosphorylation of rod outer segment membrane proteins regulate the translocation, membrane binding and activation of type II alpha phosphatidylinositol-5-phosphate 4-kinase
Neurochem. Res.
36
627-635
2011
Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Xu, J.X.; Si, M.; Zhang, H.R.; Chen, X.J.; Zhang, X.D.; Wang, C.; Du, X.N.; Zhang, H.L.
Phosphoinositide kinases play key roles in norepinephrine- and angiotensin II-induced increase in phosphatidylinositol 4,5-bisphosphate and modulation of cardiac function
J. Biol. Chem.
289
6941-6948
2014
Rattus norvegicus
Manually annotated by BRENDA team