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DAK is a member of the family of dihydroxyacetone kinases, which have a protein structure distinct from other kinases.
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The peptide fragment (m/z 520.3) of DAK is a promising biomarker to guide timing of antiviral treatment and to avoid liver biopsy in compensated chronic hepatitis B patients.
analysis of human triokinase/FMN (zeige FMN1 Proteine) cyclase reveals that kinase activity requires intact homodimers, but cyclase requires only a truncated, single domain subunit
Evidence supports that a single protein sustains both FMN (zeige FMN1 Proteine) cyclase and ATP-dependent Dha kinase activities, probably in a single active center
DAK, the physiological suppressor of cytoplasmic viral RNA sensor MDA5 (zeige IFIH1 Proteine), specifically inhibits MDA5 (zeige IFIH1 Proteine)- but not RNA helicase RIG-I (zeige DDX58 Proteine)-mediated innate antiviral signaling.
This gene is a member of the family of dihydroxyacetone kinases, which have a protein structure distinct from other kinases. The product of this gene phosphorylates dihydroxyacetone, and also catalyzes the formation of riboflavin 4',5'-phosphate (aka cyclin FMN) from FAD. Several alternatively spliced transcript variants have been identified, but the full-length nature of only one has been determined.
, deoxycytidine kinase-like
, dihydroxyacetone kinase 2
, bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)
, ATP-dependent dihydroxyacetone kinase
, DHA kinase
, Dha kinase/FMN cyclase
, FAD-AMP lyase cyclic FMN forming
, FAD-AMP lyase cyclizing
, glycerone kinase
, dihydroxyacetone kinase 2 homolog
, triokinase/FMN cyclase