Description

IPR000756 is a Diacylglycerol kinase, accessory domain.

<p>Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The DAG kinase domain is assumed to be an accessory domain. Upon cell stimulation, DAG kinase converts DAG into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. It catalyses the reaction: ATP + 1,2-diacylglycerol = ADP + 1,2-diacylglycerol 3-phosphate. The enzyme is stimulated by calcium and phosphatidylserine and phosphorylated by protein kinase C. This domain is always associated with [interpro:IPR001206].</p> <p>Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [[cite:PUB00005115]]:</p> <ul> <li>Serine/threonine-protein kinases</li> <li>Tyrosine-protein kinases</li> <li>Dual specificity protein kinases (e.g. MEK -phosphorylates both Thr and Tyr on target proteins)</li> </ul> <p>Protein kinase function is evolutionarily conserved from Escherichia coli to human [[cite:PUB00020114]]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [[cite:PUB00015362]]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [[cite:PUB00034898]], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [[cite:PUB00034899]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 21

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: