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Literature summary for 2.7.1.68 extracted from
- Dibasic amino acid residues at the carboxy-terminal end of kinase homology domain participate in the plasma membrane localization and function of phosphatidylinositol 5-kinase gamma (2004), Biochem. Biophys. Res. Commun., 319, 456-463.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| phosphatidic acid | activation | Mus musculus |  |
| small GTPase ARF/phosphatidic acid | regulation of isozyme gamma | Mus musculus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| functional complementation of a yeast Mss4-1 mutant strain YOC808 by the wild-type isozyme gamma and the deletion mutants localizing to the plasma membrane, while the deletion mutants localized to the cytosol cannot support yeast cell growth, expression of wild-type and mutant type I HA-tagged or EGFP-tagged isozymes gamma in Neuro 2A cells and in COS-1 cells | Mus musculus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of N-terminal deletion mutants DELTA68, DELTA 72, and DELTA74 are still localized to the plasma membrane, while the N-terminal deletion mutants DELTA82, DELTA 97 are mislocated to the cytosol, construction of C-terminal deletion mutant DELTA446 is still localized to the plasma membrane, while the N-terminal deletion mutant DELTA444 is mislocated to the cytosol, mutant fusion protein DELTA68-DELTA444 localizes to the plasma membrane | Mus musculus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| plasma membrane | type I isozyme gamma, the highly conserved central kinase domain KHD is necessary and sufficient for plasma membrane localization, with the C-termnal Arg-Lys dibasic sequence being responsible for plasma membrane targeting | Mus musculus | 5886 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Mus musculus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate | Mus musculus | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate is an important lipid in several cellular processes e.g. in actin cytoskeleton regulation and membrane trafficking | ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
type I enzymes, isozyme gamma | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate | - |
Mus musculus | ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate is an important lipid in several cellular processes e.g. in actin cytoskeleton regulation and membrane trafficking | Mus musculus | ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| phosphatidylinositol 5-kinase gamma | - |
Mus musculus |
| PIP5Kgamma | - |
Mus musculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Mus musculus | |
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Release 2023.1 (January 2023)
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