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Literature summary extracted from

  • Hinchliffe, K.A.; Irvine, R.F.
    Regulation of type II PIP kinase by PKD phosphorylation (2006), Cell. Signal., 18, 1906-1913.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.149 ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate Sus scrofa type II PIP kinases are physiological targets for protein kinase D phosphorylation. This modification is likely to regulate inositol lipid turnover by inhibition of these lipid kinases ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.149 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.1.149 phosphoprotein phosphorylation of T376 in living cells Sus scrofa

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.149
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.149 blood platelet
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.149 ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate
-
 Sus scrofa ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
 ?
2.7.1.149 ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate type II PIP kinases are physiological targets for protein kinase D phosphorylation. This modification is likely to regulate inositol lipid turnover by inhibition of these lipid kinases Sus scrofa ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
 ?