DAK (gene)

TKFC
Identifiers
Aliases	TKFC , NET45, DAK, triokinase and FMN cyclase, TKFCD
External IDs	OMIM: 615844; MGI: 2385084; HomoloGene: 56710; GeneCards: TKFC; OMA:TKFC - orthologs
Gene location (Human) Chr. Chromosome 11 (human) [1] Band 11q12.2 Start 61,333,220 bp [1] End 61,353,295 bp [1]
Gene location (Mouse) Chr. Chromosome 19 (mouse) [2] Band 19|19 A Start 10,565,155 bp [2] End 10,583,018 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right adrenal cortex left adrenal cortex right lobe of liver right uterine tube right testis left testis body of pancreas duodenum right lobe of thyroid gland mucosa of transverse colon Top expressed in spermatocyte right kidney yolk sac proximal tubule duodenum jejunum spermatid seminiferous tubule human kidney liver More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding metal ion binding kinase activity protein binding glycerone kinase activity catalytic activity lyase activity triokinase activity FAD-AMP lyase (cyclizing) activity ATP binding Cellular component cytosol extracellular exosome nucleus Biological process negative regulation of MDA-5 signaling pathway regulation of innate immune response phosphorylation fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate carbohydrate phosphorylation cellular carbohydrate metabolic process metabolism innate immune response glycerol metabolic process glycerol catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 26007 225913 Ensembl ENSG00000149476 ENSMUSG00000034371 UniProt Q3LXA3 Q8VC30 RefSeq (mRNA) NM_015533 NM_001351976 NM_001351977 NM_001351978 NM_001351979 NM_001351980 NM_145496 RefSeq (protein) NP_056348 NP_001338905 NP_001338906 NP_001338907 NP_001338908 NP_001338909 NP_663471 Location (UCSC) Chr 11: 61.33 – 61.35 Mb Chr 19: 10.57 – 10.58 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Triokinase/FMN cyclase is an enzyme that in humans is encoded by the DAK gene. ^[5]

Function

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. ^[5]

References

1. GRCh38: Ensembl release 89: ENSG00000149476 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000034371 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: DAK dihydroxyacetone kinase 2 homolog (S. cerevisiae)".

Further reading

• Diao F, Li S, Tian Y, Zhang M, Xu LG, Zhang Y, Wang RP, Chen D, Zhai Z, Zhong B, Tien P, Shu HB (July 2007). "Negative regulation of MDA5- but not RIG-I-mediated innate antiviral signaling by the dihydroxyacetone kinase". Proceedings of the National Academy of Sciences of the United States of America. 104 (28): 11706–11. Bibcode:2007PNAS..10411706D. doi: 10.1073/pnas.0700544104 . PMC   1913852 . PMID   17600090.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC   1356129 . PMID   16344560.
• Cabezas A, Costas MJ, Pinto RM, Couto A, Cameselle JC (December 2005). "Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases". Biochemical and Biophysical Research Communications. 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 Structural Biology. 5: 6. doi: 10.1186/1472-6807-5-6 . PMC   1079889 . PMID   15771780.
• Cabezas A, Pinto RM, Fraiz F, Canales J, González-Santiago S, Cameselle JC (November 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): 13710–22. doi:10.1021/bi0157159. PMID   11695920.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.