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Literature summary for 2.7.1.150 extracted from
- Phosphatidylinositol 3,5-bisphosphate: metabolism and function (2002), Arch. Biochem. Biophys., 407, 143-151.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | enzyme synthesis is stimulated by a hyperosmotic shock | Homo sapiens | |
| additional information | enzyme synthesis is stimulated by a hyperosmotic shock | Schizosaccharomyces pombe | |
| additional information | enzyme synthesis is stimulated by a hyperosmotic shock | Saccharomyces cerevisiae | |
| additional information | enzyme synthesis is stimulated by a hyperosmotic shock and UV radiation | Mus musculus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene FAB1, DNA sequence determination and analysis, functional expression as fusion protein | Saccharomyces cerevisiae |
| overexpression of the enzmye fused to EGFP in COS-7 cells | Mus musculus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D2134R | site-directed mutagenesis, in vivo abrogation of lipid kinase activity of the enzyme | Saccharomyces cerevisiae |
| K2059M | site-directed mutagenesis, in vitro abrogation of lipid kinase activity of the enzyme | Saccharomyces cerevisiae |
| 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
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | enzyme is not localized in the Golgi apparatus, recycling endosomes, or lysosomes | Mus musculus | - |
- |
| vacuole | - |
Saccharomyces cerevisiae | 5773 | - |
| vesicle | - |
Mus musculus | 31982 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 257000 | - |
- |
Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | Drosophila melanogaster | - |
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? |  |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | Homo sapiens | - |
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | Arabidopsis thaliana | - |
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | Caenorhabditis elegans | - |
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | Candida albicans | - |
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | Oryza sativa | - |
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| additional information | Schizosaccharomyces pombe | physiological roles of the catalyzed reaction, overview | ? | - |
? | |
| additional information | Saccharomyces cerevisiae | physiological roles of the catalyzed reaction, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
| Caenorhabditis elegans | - |
- |
- |
| Candida albicans | - |
- |
- |
| Drosophila melanogaster | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
- |
- |
| Oryza sativa | - |
- |
- |
| Saccharomyces cerevisiae | P34756 | gene FAB1 | - |
| Schizosaccharomyces pombe | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | the enzyme downregulates its own activity by autophosphorylation | Mus musculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| adipocyte | - |
Mus musculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 1-phosphatidyl-1D-myo-inositol | recombinant enzyme | Mus musculus | ADP + 1-phosphatidyl-1D-myo-inositol 5-phosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol | recombinant enzyme | Schizosaccharomyces pombe | ADP + 1-phosphatidyl-1D-myo-inositol 5-phosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
Drosophila melanogaster | ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
Mus musculus | ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
Homo sapiens | ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
Arabidopsis thaliana | ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
Schizosaccharomyces pombe | ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
Caenorhabditis elegans | ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
Candida albicans | ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
Oryza sativa | ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | preferred substrate | Saccharomyces cerevisiae | ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate | recombinant enzyme | Mus musculus | ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate | recombinant enzyme | Schizosaccharomyces pombe | ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate | recombinant enzyme | Saccharomyces cerevisiae | ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate | - |
? | |
| additional information | physiological roles of the catalyzed reaction, overview | Schizosaccharomyces pombe | ? | - |
? | |
| additional information | physiological roles of the catalyzed reaction, overview | Saccharomyces cerevisiae | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| additional information | substrate specificity, the enzyme also shows lipid kinase activity | Saccharomyces cerevisiae | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| Fab1p | - |
Schizosaccharomyces pombe |
| Fab1p | - |
Saccharomyces cerevisiae |
| More | the enzyme belongs to the type III PIPkin family | Drosophila melanogaster |
| More | the enzyme belongs to the type III PIPkin family | Mus musculus |
| More | the enzyme belongs to the type III PIPkin family | Homo sapiens |
| More | the enzyme belongs to the type III PIPkin family | Arabidopsis thaliana |
| More | the enzyme belongs to the type III PIPkin family | Schizosaccharomyces pombe |
| More | the enzyme belongs to the type III PIPkin family | Caenorhabditis elegans |
| More | the enzyme belongs to the type III PIPkin family | Candida albicans |
| More | the enzyme belongs to the type III PIPkin family | Oryza sativa |
| More | the enzyme belongs to the type III PIPkin family | Saccharomyces cerevisiae |
| phosphatidylinositol 5-OH kinase | - |
Drosophila melanogaster |
| phosphatidylinositol 5-OH kinase | - |
Mus musculus |
| phosphatidylinositol 5-OH kinase | - |
Homo sapiens |
| phosphatidylinositol 5-OH kinase | - |
Arabidopsis thaliana |
| phosphatidylinositol 5-OH kinase | - |
Schizosaccharomyces pombe |
| phosphatidylinositol 5-OH kinase | - |
Caenorhabditis elegans |
| phosphatidylinositol 5-OH kinase | - |
Candida albicans |
| phosphatidylinositol 5-OH kinase | - |
Oryza sativa |
| phosphatidylinositol 5-OH kinase | - |
Saccharomyces cerevisiae |
| PIKfyve | - |
Mus musculus |
| PtdIns3P 5-OH kinase | - |
Drosophila melanogaster |
| PtdIns3P 5-OH kinase | - |
Mus musculus |
| PtdIns3P 5-OH kinase | - |
Homo sapiens |
| PtdIns3P 5-OH kinase | - |
Arabidopsis thaliana |
| PtdIns3P 5-OH kinase | - |
Schizosaccharomyces pombe |
| PtdIns3P 5-OH kinase | - |
Caenorhabditis elegans |
| PtdIns3P 5-OH kinase | - |
Candida albicans |
| PtdIns3P 5-OH kinase | - |
Oryza sativa |
| PtdIns3P 5-OH kinase | - |
Saccharomyces cerevisiae |
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