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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | This entry represents the first protein kinase C conserved region 1 (C1 domain) of DAG kinase beta and similar proteins from vertebrates and arthropods. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn2-binding sites.Diacylglycerol (DAG) kinase ( ) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase beta, also called 90 kDa diacylglycerol kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca2 and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DAG kinase beta contains two copies of the C1 domain, which bind DAG and phorbol esters [ , , , , , ]. This enzyme is specifically expressed in brain and regulates neuron-specific morphological changes including neurite branching and neurite spine formation [].Diacylglycerol kinase 1 (DGK1), the DAG kinase beta orthologue from Drosophila melanogaster, is also included in this entry. Upon cell stimulation DGK1 converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. It may have a role in the development of the embryonic nervous system and the function of the adult nervous system and muscle, regulating signal transduction in neurons [ , ]. | Name | Diacylglycerol kinase beta-like, first protein kinase C conserved region 1 |
| Short Name | C1_DGKbeta-like_rpt1 | Type | Domain |
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