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Enzyme Nomenclature
Information on EC 2.7.1.150 - 1-phosphatidylinositol-3-phosphate 5-kinase
for references in articles please use BRENDA:EC2.7.1.150
Word Map on EC 2.7.1.150
- 2.7.1.150
- vacuole
- endosomes
-
ptdins3,5p2
- 3,5-bisphosphate
-
ptdins5p
-
endolysosomal
-
multivesicular
- phosphatidylinositol-3,5-bisphosphate
-
charcot-marie-tooth
-
insulin-regulated
-
fleck
- myotubularins
-
trpml1
-
k127nsgk1
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.7.1.150
-
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RECOMMENDED NAME
GeneOntology No.
1-phosphatidylinositol-3-phosphate 5-kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho-group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
ATP:1-phosphatidyl-1D-myo-inositol-3-phosphate 5-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
190606-24-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
enzyme inhibition reduces contraction- and AICAriboside (5-amino-4-imidazolecarboxamide riboside)-stimulated glucose uptake. PIKfyve knockdown in C2C12 myotubes reduced AICAriboside-stimulated glucose transport
malfunction
the vacuolation phenotype in cultured Vps34 (EC 2.7.1.137)-deficient podocytes is caused by the absence of a substrate for the Vps34 downstream effector PtdIns 3-phosphate 5-kinase, which phosphorylates Vps34-generated 1-phosphatidyl-1D-myo-inositol 3-phosphate to produce + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate. PtdIns 3-phosphate 5-kinase perturbation and 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate reduction result in massive membrane vacuolation along the endosomal system. Genetic deletion of the enzyme in endocytically active proximal tubular cells results in the development of large cytoplasmic vacuoles caused by arrested endocytic traffic progression at a late-endosome stage, while deletion of the enzyme in glomerular podocytes does not significantly alter the endosomal morphology, even in age 18-month-old mice
malfunction
a loss of enzyme function causes the release of late endosomal proteins, Ara7, and SNX1 from the endosome membrane. Downregulation of FAB1A/B or YM201636 inhibitor treatment affects the auxin distribution and and alteration of PIN2 localization in root cells. FAB1 knockdown causes relocation of the basal polarity of PIN2 in young root cortical cells
physiological function
in Xenopus oocytes expressing mammalian excitatory amino acid transporter EAAT4, glutamate induces a current which is significantly enhanced by coexpression of isoform PIKfyve and glucocorticoid inducible kinase SGK1. This glutamate-induced current is significantly larger than the current in Xenopus oocytes expressing EAAT4 together with either kinase alone. Coexpression of the inactive SGK1 mutant K127N does not significantly alter glutamate-induced current in EAAT4-expressing Xenopus oocytes and abolishes the stimulation of glutamate-induced current by coexpression of isoform PIKfyve. The stimulating effect of PIKfyve is abrogated by mutation S318A in the SGK consensus sequence of PIKfyve. Coexpression of PIKfyve S318A mutant significantly blunts the stimulating effect of SGK1 on EAAT4 activity
physiological function
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PIKFYVE knockdown produces a 36% reduction in phosphatidylinositol 3,5-bisphosphate and a 13% increase in phosphatidylinositol 3-phosphate. PIKFYVE and class II phosphatidylinositol 3-kinase PI3K-C2alpha are necessary for activation of the kinase complex mechanistic target of rapamycin mTORC1 and its translocation to the plasma membrane in 3T3-L1 adipocytes. The mTORC1 component Raptor directly interacts with phosphatidylinositol 3,5-bisphosphate
physiological function
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the enzyme activity is required for the stimulation of skeletal muscle glucose uptake by contraction/AMPK activation. In opossum kidney cells, wild-type, but not S307A mutant, PIKfyve is recruited to endosomal vesicles in response to AMPK activation
physiological function
the enzyme activity is implicated in be involved in contraction/AMPK (AMP-activated protein kinase)-stimulated glucose uptake in skeletal muscle rather than insulin-stimulated glucose uptake. The enzyme is an AMPK substrate whose phosphorylation at Ser307 promotes PIKfyve translocation to endosomes for PtdIns(3,5)P2 synthesis to facilitate GLUT4 (glucose transporter 4) translocation
physiological function
the enzyme mediates endosome maturation to establish endosome-cortical microtubule interaction in Arabidopsis thaliana. The enzyme and its product, 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate, are essential for the maturation process of endosomes to mediate cortical microtubule association of endosomes, thereby controlling proper PIN-FORMED protein trafficking in young cortical and stele cells of root. The enzyme and its product mediate the late endosome maturation by recruiting endosomal effector molecules, Ara7 and SNX1, onto endosomes to establish endosome-cortical microtubule interaction
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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 + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ATP + 1-phosphatidyl-1D-myo-inositol
ADP + 1-phosphatidyl-1D-myo-inositol 5-phosphate
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recombinant enzyme
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-
?
ATP + 1-phosphatidyl-1D-myo-inositol
ADP + 1-phosphatidyl-1D-myo-inositol 5-phosphate
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recombinant enzyme
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-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
the main function of PPK-3 is to mediate membrane retrieval from matured lysosomes through regulation of PtdIns(3,5)P2. Complete loss of ppk-3 function induces developmental defects characterized by embryonic lethality, whereas partial loss of function leads to growth retardation. At the cellular level, ppk-3 mutants display a striking enlargement of vacuoles positive for lysosome-associated membrane protein 1 in different tissues
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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Fab1 phosphatidylinositol 3-phosphate 5-kinase controls trafficking but not silencing of endocytosed receptors. Drosophila fab1 mutants contain undetectable phosphatidylinositol 3,5-bisphosphate levels, show profound increases in cell and organ size, and die at the pupal stage
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, interleukins, UV radiation, and autophosphorylation, overview
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
preferred substrate
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-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
stress-activated enzyme
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
essential for vacuole function
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
generation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate is regulated by Vac7 protein, whereas turnover of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate is mediated in part by the Sac1 polyphosphoinositide phosphatase family member Fig4
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
reaction is essential for retrograde trafficking between the vacuole/lysosome and the late endosome and also for trafficking of some proteins into the vacuole via multivesicular bodies, enzyme synthesis is regulated by vac14 and vac7, 2 upstream activators, physiological roles of the enzyme and regulation mechnaism, overview
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, overview, enzymes hydrolyzing the product are counteracting, overview
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-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
Fab1p and AP-1 are required for trafficking of endogenously ubiquitylated cargoes to the vacuole lumen
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
-
-
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
phosphatidylinositol(3,5)bisphosphate is essential for cellular responses to various stresses and for the mating pheromone signalling under starvation conditions
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
reaction is essential for retrograde trafficking between the vacuole/lysosome and the late endosome and also for trafficking of some proteins into the vacuole via multivesicular bodies, enzyme synthesis is regulated by vac14 and vac7, 2 upstream activators, physiological roles of the enzyme and regulation mechnaism, overview
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, overview
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
recombinant enzyme
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
recombinant enzyme
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
recombinant enzyme
-
-
?
additional information
?
-
TLC measurement of phospholipids in wild-type and FAB1A-GFP-expressing plants, overview
-
-
-
additional information
?
-
-
PIKfyve participates in the SGK1-dependent regulation of the Na+, glucose cotransporter SGLT1 (SLC5A1)
-
-
-
additional information
?
-
-
substrate specificity in descending order: 1-phosphatidyl-1D-myo-inositol 3-phosphate, 1-phosphatidyl-1D-myo-inositol 4-phosphate, and 1-phosphatidyl-1D-myo-inositol, the enzyme also shows lipid kinase activity
-
-
-
additional information
?
-
physiological roles of the catalyzed reaction, overview
-
-
-
additional information
?
-
substrate specificity, the enzyme also shows lipid kinase activity
-
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-
additional information
?
-
-
Fab1p activators, Vac7p and Vac14p, independently regulate Fab1p activity. A maximal increase in the levels of PI3,5P2 requires both Vac7p and the Vac14p–Fig4p complex
-
-
-
additional information
?
-
-
physiological roles of the catalyzed reaction, overview
-
-
-
additional information
?
-
-
substrate specificity in descending order: 1-phosphatidyl-1D-myo-inositol 3-phosphate, 1-phosphatidyl-1D-myo-inositol 4-phosphate, and 1-phosphatidyl-1D-myo-inositol
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
Q9LUM0
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
the main function of PPK-3 is to mediate membrane retrieval from matured lysosomes through regulation of PtdIns(3,5)P2. Complete loss of ppk-3 function induces developmental defects characterized by embryonic lethality, whereas partial loss of function leads to growth retardation. At the cellular level, ppk-3 mutants display a striking enlargement of vacuoles positive for lysosome-associated membrane protein 1 in different tissues
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
Fab1 phosphatidylinositol 3-phosphate 5-kinase controls trafficking but not silencing of endocytosed receptors. Drosophila fab1 mutants contain undetectable phosphatidylinositol 3,5-bisphosphate levels, show profound increases in cell and organ size, and die at the pupal stage
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
Q9Z1T6
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, interleukins, UV radiation, and autophosphorylation, overview
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
D3ZYT8
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
stress-activated enzyme
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
essential for vacuole function
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
generation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate is regulated by Vac7 protein, whereas turnover of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate is mediated in part by the Sac1 polyphosphoinositide phosphatase family member Fig4
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
reaction is essential for retrograde trafficking between the vacuole/lysosome and the late endosome and also for trafficking of some proteins into the vacuole via multivesicular bodies, enzyme synthesis is regulated by vac14 and vac7, 2 upstream activators, physiological roles of the enzyme and regulation mechnaism, overview
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
P34756
regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, overview, enzymes hydrolyzing the product are counteracting, overview
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
Fab1p and AP-1 are required for trafficking of endogenously ubiquitylated cargoes to the vacuole lumen
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
phosphatidylinositol(3,5)bisphosphate is essential for cellular responses to various stresses and for the mating pheromone signalling under starvation conditions
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
reaction is essential for retrograde trafficking between the vacuole/lysosome and the late endosome and also for trafficking of some proteins into the vacuole via multivesicular bodies, enzyme synthesis is regulated by vac14 and vac7, 2 upstream activators, physiological roles of the enzyme and regulation mechnaism, overview
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, overview
-
-
?
additional information
?
-
Q9LUM0
TLC measurement of phospholipids in wild-type and FAB1A-GFP-expressing plants, overview
-
-
-
additional information
?
-
-
PIKfyve participates in the SGK1-dependent regulation of the Na+, glucose cotransporter SGLT1 (SLC5A1)
-
-
-
additional information
?
-
P34756
physiological roles of the catalyzed reaction, overview
-
-
-
additional information
?
-
-
Fab1p activators, Vac7p and Vac14p, independently regulate Fab1p activity. A maximal increase in the levels of PI3,5P2 requires both Vac7p and the Vac14p–Fig4p complex
-
-
-
additional information
?
-
-
physiological roles of the catalyzed reaction, overview
-
-
-
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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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme synthesis is stimulated by a hyperosmotic shock
-
additional information
-
enzyme synthesis is stimulated by a hyperosmotic shock and UV radiation
-
additional information
-
enzyme synthesis is stimulated by a hyperosmotic shock
-
additional information
-
enzyme synthesis is stimulated by a hyperosmotic shock
-
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the enzyme is increased in contracting versus resting muscles
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
enzyme is not localized in the Golgi apparatus, recycling endosomes, or lysosomes
-
the enzyme predominantly localizes on the Sorting Nexin1 (SNX1)-residing late endosomes, the SNX1-positive endosomes
localizes mainly to early endosomes. PIKfyve is distributed in microdomains
-
PIKfyve is predominantly associated with the early endosome, from where it regulates retrograde membrane trafficking to the trans-Golgi-network
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the PIPkin type III family enzyme consists of 4 typical domains: the FYVE RING Zn-finger domain, the TCP-I/chaperone-like domain, the PIPkin domain, and the cysteine-rich domain, the the FYVE RING Zn-finger domain is missing in 2 homologues from Arabidopsis thaliana, overview
additional information
-
the PIPkin type III family enzyme consists of 4 typical domains: the FYVE RING Zn-finger domain, the TCP-I/chaperone-like domain, the PIPkin domain, and the cysteine-rich domain
additional information
-
the PIPkin type III family enzyme consists of 4 typical domains: the FYVE RING Zn-finger domain, the TCP-I/chaperone-like domain, the PIPkin domain, and the cysteine-rich domain
additional information
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the PIPkin type III family enzyme consists of 4 typical domains: the FYVE RING Zn-finger domain, the TCP-I/chaperone-like domain, the PIPkin domain, and the cysteine-rich domain, the fly enzyme contains additionally a DEP domain
additional information
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the PIPkin type III family enzyme consists of 4 typical domains: the FYVE RING Zn-finger domain, the TCP-I/chaperone-like domain, the PIPkin domain, and the cysteine-rich domain, the human enzyme contains additionally a DEP domain
additional information
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the PIPkin type III family enzyme consists of 4 typical domains: the FYVE RING Zn-finger domain, the TCP-I/chaperone-like domain, the PIPkin domain, and the cysteine-rich domain, the mouse enzyme contains additionally a DEP domain
additional information
-
the PIPkin type III family enzyme consists of 4 typical domains: the FYVE RING Zn-finger domain, the TCP-I/chaperone-like domain, the PIPkin domain, and the cysteine-rich domain
additional information
the PIPkin type III family enzyme consists of 4 typical domains: the FYVE RING Zn-finger domain, the TCP-I/chaperone-like domain, the PIPkin domain, and the cysteine-rich domain
additional information
-
the PIPkin type III family enzyme consists of 4 typical domains: the FYVE RING Zn-finger domain, the TCP-I/chaperone-like domain, the PIPkin domain, and the cysteine-rich domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
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AMP-activated protein kinase stimulates the enzyme by phosphorylation at Ser307 both in vitro and in intact cells
phosphoprotein
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the enzyme downregulates its own activity by autophosphorylation
phosphoprotein
AMP-activated protein kinase stimulates the enzyme by phosphorylation at Ser307 both in vitro and in intact cells
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene FAB1, DNA sequence determination and analysis, functional expression as fusion protein
gene PIKfyve, recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana plants
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S318A
in Xenopus oocytes expressing mammalian excitatory amino acid transporter EAAT4, glutamate induces a current which is significantly enhanced by coexpression of isoform PIKfyve and glucocorticoid inducible kinase SGK1. The stimulating effect of PIKfyve is abrogated by mutation S318A in the SGK consensus sequence of PIKfyve. Coexpression of PIKfyve S318A mutant significantly blunts the stimulating effect of SGK1 on EAAT4 activity
D2134R
site-directed mutagenesis, in vivo abrogation of lipid kinase activity of the enzyme
K2059M
site-directed mutagenesis, in vitro abrogation of lipid kinase activity of the enzyme
additional information
additional information
FAB1 null mutants possess no phosphatidylinositol 3,5-bisphosphate and shows vacuolar defects, expression of murine enzyme PIKfyve, but of the enzyme from Schizosaccharomyces pombe, can revert the vacuolar defects in vivo, while the enzyme from Schizosaccharomyces pombe can restore catalytic activity in response to hyperosmotic stress
additional information
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enzyme defect leads to enlarged vacuoles that do not acidify correctly, the defect can be complemented by enzyme overexpression, mutants grow poorly at elevated temperature
additional information
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enzyme defect leads to enlarged vacuoles that do not acidify correctly, the defect can be complemented by enzyme overexpression, mutants grow poorly at elevated temperature
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.150)
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