DAK (gene)

From Wikipedia, the free encyclopedia

Dihydroxyacetone kinase 2 homolog (S. cerevisiae)

Identifiers

DAK; DKFZP586B1621; MGC5621

External IDs

Gene ontology
Molecular Function:	• nucleotide binding • glycerone kinase activity • ATP binding • transferase activity • lyase activity
Biological Process:	• glycerol metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_015533 (mRNA)
NP_056348 (protein)

NM_145496 (mRNA)
NP_663471 (protein)

Location

Chr 11: 60.86 - 60.87 Mb

Chr 19: 10.66 - 10.67 Mb

Pubmed search

[1]

[2]

Dihydroxyacetone kinase 2 homolog (S. cerevisiae), also known as DAK, is a human 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 cyclin FMN) from FAD. Several alternatively spliced transcript variants have been identified, but the full-length nature of only one has been determined.^[1]

[edit] References

^ ^a ^b Entrez Gene: DAK dihydroxyacetone kinase 2 homolog (S. cerevisiae).

[edit] 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): 11706-11. doi:10.1073/pnas.0700544104. 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. 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): 1682-9. 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. 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): 2121-7. doi:10.1101/gr.2596504. 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): 40-5. 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): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
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): 149-56. 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): 171-4. PMID 8125298.