Aliases for DGKQ Gene
External Ids for DGKQ Gene
Previous Symbols for DGKQ Gene
The protein encoded by this gene contains three cysteine-rich domains, a proline-rich region, and a pleckstrin homology domain with an overlapping Ras-associating domain. It is localized in the speckle domains of the nucleus, and mediates the regeneration of phosphatidylinositol (PI) from diacylglycerol in the PI-cycle during cell signal transduction. [provided by RefSeq, Jul 2008]
GeneCards Summary for DGKQ Gene
DGKQ (Diacylglycerol Kinase, Theta 110kDa) is a Protein Coding gene. Among its related pathways are Signaling by GPCR and Signaling by GPCR. GO annotations related to this gene include kinase binding and NAD+ kinase activity. An important paralog of this gene is DGKI.
UniProtKB/Swiss-Prot for DGKQ Gene
Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). May regulate the activity of protein kinase C by controlling the balance between these two signaling lipids. Activated in the nucleus in response to alpha-thrombin and nerve growth factor (By similarity). May be involved in cAMP-induced activation of NR5A1 and subsequent steroidogenic gene transcription by delivering PA as ligand for NR5A1. Acts synergistically with NR5A1 on CYP17 transcriptional activity.
Diacylglycerol kinases (DGKs) are a group of ten enzymes (DGKalpha, DGKbeta, DGKgamma, DGKdelta, DGKepsilon, DGKzeta, DGKeta, DGKtheta, DGKiota and DGKkappa) that metabolize 1,2,diacylglycerol (DAG) to produce phosphatidic acid (PA). They all contain a conserved C-terminal catalytic domain, two cysteine-rich Zn2+-finger motifs that bind DAG and an ATP-binding site, whilst the regulatory domain varies. DGKs are widely distributed throughout mammalian tissues and different isozymes have different subcellular localizations; some are cytosolic (for example DGKalpha), some are membrane-bound (for example DGKgamma is associated with the Golgi membrane) and some are nuclear (for example DGKzeta. DGKs have diverse biological roles as they participate in signal transduction by modulating levels of DAG in a variety of cellular responses to extracellular stimuli.