DAK (gene)

Dihydroxyacetone kinase 2 homolog (S. cerevisiae)
Identifiers
Symbols	DAK; DKFZp586B1621; MGC5621; NET45
External IDs	MGI: 2385084 HomoloGene: 56710 GeneCards: DAK Gene
Gene Ontology Molecular function • nucleotide binding • glycerone kinase activity • ATP binding • transferase activity • lyase activity • FAD-AMP lyase (cyclizing) activity • metal ion binding Cellular component • cytosol Biological process • glycerol metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	26007	225913
Ensembl	ENSG00000149476	ENSMUSG00000034371
UniProt	Q3LXA3	Q3UTZ4
RefSeq (mRNA)	NM_015533	NM_145496.1
RefSeq (protein)	NP_056348	NP_663471.1
Location (UCSC)	Chr 11: 61.1 – 61.12 Mb	Chr 19: 10.66 – 10.68 Mb
PubMed search	[1]	[2]

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. ^ ^{a b} "Entrez Gene: DAK dihydroxyacetone kinase 2 homolog (S. cerevisiae)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26007. 

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1913852. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1079889. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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.