DAK (gene)

Triokinase/FMN cyclase
Identifiers
Symbols	TKFC ; DAK; NET45
External IDs	OMIM: 615844 MGI: 2385084 HomoloGene: 56710 GeneCards: TKFC Gene
EC number	2.7.1.28, 2.7.1.29, 4.6.1.15
Gene ontology Molecular function • glycerone kinase activity • protein binding • ATP binding • FAD-AMP lyase (cyclizing) activity • metal ion binding • triokinase activity Cellular component • nucleus • cytosol • extracellular exosome Biological process • carbohydrate metabolic process • fructose metabolic process • glycerol metabolic process • negative regulation of MDA-5 signaling pathway • cellular carbohydrate metabolic process • small molecule metabolic process • innate immune response • regulation of innate immune response • carbohydrate phosphorylation • fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	26007	225913
Ensembl	ENSG00000149476	ENSMUSG00000034371
UniProt	Q3LXA3	Q8VC30
RefSeq (mRNA)	NM_015533	NM_145496
RefSeq (protein)	NP_056348	NP_663471
Location (UCSC)	Chr 11: 61.33 – 61.35 Mb	Chr 19: 10.59 – 10.6 Mb
PubMed search

Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing) is an enzyme that in humans is encoded by the DAK gene.^[1]

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 cyclic FMN) from FAD. Several alternatively spliced transcript variants have been identified, but the full-length nature of only one has been determined.^[1]

References

1. "Entrez Gene: DAK dihydroxyacetone kinase 2 homolog (S. cerevisiae)".

Further reading

• Diao F, Li S, Tian Y, et al. (2007). "Negative regulation of MDA5- but not RIG-I-mediated innate antiviral signaling by the dihydroxyacetone kinase". Proc. Natl. Acad. Sci. U.S.A. 104 (28): 11706–11711. doi:10.1073/pnas.0700544104. PMC 1913852. PMID 17600090.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Cabezas A, Costas MJ, Pinto RM, et al. (2006). "Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases". Biochem. Biophys. Res. Commun. 338 (4): 1682–1689. doi:10.1016/j.bbrc.2005.10.142. PMID 16289032.
• Cheek S, Ginalski K, Zhang H, Grishin NV (2006). "A comprehensive update of the sequence and structure classification of kinases". BMC Struct. Biol. 5: 6. doi:10.1186/1472-6807-5-6. PMC 1079889. PMID 15771780.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–45. doi:10.1038/ng1285. PMID 14702039.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Cabezas A, Pinto RM, Fraiz F, et al. (2001). "Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion". Biochemistry 40 (45): 13710–13722. doi:10.1021/bi0157159. PMID 11695920.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.