Aliases for DYRK3 Gene
- Dual Specificity Tyrosine Phosphorylation Regulated Kinase 3 2 3 5
- Regulatory Erythroid Kinase 2 3 4
- Dual Specificity Tyrosine-(Y)-Phosphorylation Regulated Kinase 3 2 3
- Dual-Specificity Tyrosine-(Y)-Phosphorylation Regulated Kinase 5 2 3
- Protein Kinase Dyrk3 2 3
- REDK 3 4
- Dual-Specificity Tyrosine-(Y)-Phosphorylation Regulated Kinase 3 2
External Ids for DYRK3 Gene
Previous GeneCards Identifiers for DYRK3 Gene
This gene product belongs to the DYRK family of dual-specificity protein kinases that catalyze autophosphorylation on serine/threonine and tyrosine residues. The members of this family share structural similarity, however, differ in their substrate specificity, suggesting their involvement in different cellular functions. The encoded protein has been shown to autophosphorylate on tyrosine residue and catalyze phosphorylation of histones H3 and H2B in vitro. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]
GeneCards Summary for DYRK3 Gene
DYRK3 (Dual Specificity Tyrosine Phosphorylation Regulated Kinase 3) is a Protein Coding gene. Gene Ontology (GO) annotations related to this gene include transferase activity, transferring phosphorus-containing groups and protein tyrosine kinase activity. An important paralog of this gene is DYRK2.
UniProtKB/Swiss-Prot for DYRK3 Gene
Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Negative regulator of EPO-dependent erythropoiesis, may place an upper limit on red cell production during stress erythropoiesis. Inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells (PubMed:10779429). May act by regulating CREB/CRE signaling (By similarity). Stabilizes and prevents stress granule disassembly thereby regulating mTORC1 signaling during cellular stress. During stressful conditions, DYRK3 partitions to the stress granule from the cytosol, as well as mTORC1 components, which prevents mTORC1 signaling. When stress signals are gone, the kinase activity of DYRK3 is required for the dissolution of stress granule and mTORC1 relocation to the cytosol, and promotes the phosphorylation of the mTORC1 inhibitor, AKT1S1, allowing full reactivation of mTORC1 signaling (PubMed:23415227). Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits TP53 activity and apoptosis (PubMed:20167603).