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

BRENDA support

Literature summary extracted from

  • Cooke, F.T.
    Phosphatidylinositol 3,5-bisphosphate: metabolism and function (2002), Arch. Biochem. Biophys., 407, 143-151.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.150 additional information enzyme synthesis is stimulated by a hyperosmotic shock Homo sapiens
2.7.1.150 additional information enzyme synthesis is stimulated by a hyperosmotic shock Schizosaccharomyces pombe
2.7.1.150 additional information enzyme synthesis is stimulated by a hyperosmotic shock Saccharomyces cerevisiae
2.7.1.150 additional information enzyme synthesis is stimulated by a hyperosmotic shock and UV radiation Mus musculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.150 gene FAB1, DNA sequence determination and analysis, functional expression as fusion protein Saccharomyces cerevisiae
2.7.1.150 overexpression of the enzmye fused to EGFP in COS-7 cells Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.150 D2134R site-directed mutagenesis, in vivo abrogation of lipid kinase activity of the enzyme Saccharomyces cerevisiae
2.7.1.150 K2059M site-directed mutagenesis, in vitro abrogation of lipid kinase activity of the enzyme Saccharomyces cerevisiae
2.7.1.150 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 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.150 additional information enzyme is not localized in the Golgi apparatus, recycling endosomes, or lysosomes Mus musculus
-
-
2.7.1.150 vacuole
-
 Saccharomyces cerevisiae 5773
-
2.7.1.150 vesicle
-
 Mus musculus 31982
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.150 257000
-
-
 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate Drosophila melanogaster
-
 ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate Homo sapiens
-
 ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate Arabidopsis thaliana
-
 ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate Caenorhabditis elegans
-
 ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate Candida albicans
-
 ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate Oryza sativa
-
 ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate Mus musculus regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, interleukins, UV radiation, and autophosphorylation, overview ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate Schizosaccharomyces pombe regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, overview ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate Saccharomyces cerevisiae regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, overview, enzymes hydrolyzing the product are counteracting, overview ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 additional information Schizosaccharomyces pombe physiological roles of the catalyzed reaction, overview ?
-
 ?
2.7.1.150 additional information Saccharomyces cerevisiae physiological roles of the catalyzed reaction, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.150 Arabidopsis thaliana
-
-
-
2.7.1.150 Caenorhabditis elegans
-
-
-
2.7.1.150 Candida albicans
-
-
-
2.7.1.150 Drosophila melanogaster
-
-
-
2.7.1.150 Homo sapiens
-
-
-
2.7.1.150 Mus musculus
-
-
-
2.7.1.150 Oryza sativa
-
-
-
2.7.1.150 Saccharomyces cerevisiae P34756 gene FAB1
-
2.7.1.150 Schizosaccharomyces pombe
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.1.150 phosphoprotein the enzyme downregulates its own activity by autophosphorylation Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.150 adipocyte
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol recombinant enzyme Mus musculus ADP + 1-phosphatidyl-1D-myo-inositol 5-phosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol recombinant enzyme Schizosaccharomyces pombe ADP + 1-phosphatidyl-1D-myo-inositol 5-phosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 Drosophila melanogaster ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 Mus musculus ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 Homo sapiens ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 Arabidopsis thaliana ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 Schizosaccharomyces pombe ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 Caenorhabditis elegans ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 Candida albicans ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 Oryza sativa ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate preferred substrate Saccharomyces cerevisiae ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, interleukins, UV radiation, and autophosphorylation, overview Mus musculus ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, overview Schizosaccharomyces pombe ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, overview, enzymes hydrolyzing the product are counteracting, overview Saccharomyces cerevisiae ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate recombinant enzyme Mus musculus ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate recombinant enzyme Schizosaccharomyces pombe ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
 ?
2.7.1.150 ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate recombinant enzyme Saccharomyces cerevisiae ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
 ?
2.7.1.150 additional information physiological roles of the catalyzed reaction, overview Schizosaccharomyces pombe ?
-
 ?
2.7.1.150 additional information physiological roles of the catalyzed reaction, overview Saccharomyces cerevisiae ?
-
 ?
2.7.1.150 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 Schizosaccharomyces pombe ?
-
 ?
2.7.1.150 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 Mus musculus ?
-
 ?
2.7.1.150 additional information substrate specificity, the enzyme also shows lipid kinase activity Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.150 More 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 Schizosaccharomyces pombe
2.7.1.150 More 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 Caenorhabditis elegans
2.7.1.150 More 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 Candida albicans
2.7.1.150 More 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 Oryza sativa
2.7.1.150 More 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 Saccharomyces cerevisiae
2.7.1.150 More 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 Drosophila melanogaster
2.7.1.150 More 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 Homo sapiens
2.7.1.150 More 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 Mus musculus
2.7.1.150 More 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 Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
2.7.1.150 Fab1p
-
 Schizosaccharomyces pombe
2.7.1.150 Fab1p
-
 Saccharomyces cerevisiae
2.7.1.150 More the enzyme belongs to the type III PIPkin family Drosophila melanogaster
2.7.1.150 More the enzyme belongs to the type III PIPkin family Mus musculus
2.7.1.150 More the enzyme belongs to the type III PIPkin family Homo sapiens
2.7.1.150 More the enzyme belongs to the type III PIPkin family Arabidopsis thaliana
2.7.1.150 More the enzyme belongs to the type III PIPkin family Schizosaccharomyces pombe
2.7.1.150 More the enzyme belongs to the type III PIPkin family Caenorhabditis elegans
2.7.1.150 More the enzyme belongs to the type III PIPkin family Candida albicans
2.7.1.150 More the enzyme belongs to the type III PIPkin family Oryza sativa
2.7.1.150 More the enzyme belongs to the type III PIPkin family Saccharomyces cerevisiae
2.7.1.150 phosphatidylinositol 5-OH kinase
-
 Drosophila melanogaster
2.7.1.150 phosphatidylinositol 5-OH kinase
-
 Mus musculus
2.7.1.150 phosphatidylinositol 5-OH kinase
-
 Homo sapiens
2.7.1.150 phosphatidylinositol 5-OH kinase
-
 Arabidopsis thaliana
2.7.1.150 phosphatidylinositol 5-OH kinase
-
 Schizosaccharomyces pombe
2.7.1.150 phosphatidylinositol 5-OH kinase
-
 Caenorhabditis elegans
2.7.1.150 phosphatidylinositol 5-OH kinase
-
 Candida albicans
2.7.1.150 phosphatidylinositol 5-OH kinase
-
 Oryza sativa
2.7.1.150 phosphatidylinositol 5-OH kinase
-
 Saccharomyces cerevisiae
2.7.1.150 PIKfyve
-
 Mus musculus
2.7.1.150 PtdIns3P 5-OH kinase
-
 Drosophila melanogaster
2.7.1.150 PtdIns3P 5-OH kinase
-
 Mus musculus
2.7.1.150 PtdIns3P 5-OH kinase
-
 Homo sapiens
2.7.1.150 PtdIns3P 5-OH kinase
-
 Arabidopsis thaliana
2.7.1.150 PtdIns3P 5-OH kinase
-
 Schizosaccharomyces pombe
2.7.1.150 PtdIns3P 5-OH kinase
-
 Caenorhabditis elegans
2.7.1.150 PtdIns3P 5-OH kinase
-
 Candida albicans
2.7.1.150 PtdIns3P 5-OH kinase
-
 Oryza sativa
2.7.1.150 PtdIns3P 5-OH kinase
-
 Saccharomyces cerevisiae