Deoxycytidine kinase

From Wikipedia, the free encyclopedia


Deoxycytidine kinase
PDB rendering based on 1p5z.
Available structures: 1p5z, 1p60, 1p61, 1p62, 2a2z, 2a30, 2a7q, 2no9, 2noa
Identifiers
Symbol(s) DCK; MGC117410; MGC138632
External IDs OMIM: 125450 MGI: 102726 HomoloGene: 616
EC number 2.7.1.74
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 1633 13178
Ensembl ENSG00000156136 ENSMUSG00000029366
Uniprot P27707 Q545E8
Refseq NM_000788 (mRNA)
NP_000779 (protein)		 XM_977104 (mRNA)
XP_982198 (protein)
Location Chr 4: 72.08 - 72.12 Mb Chr 5: 89.84 - 89.86 Mb
Pubmed search [1] [2]

Deoxycytidine kinase, also known as DCK, is a human gene.[1]

Deoxycytidine kinase is an enzyme which transfers phosphate to deoxycytidine.

Deoxycytidine kinase (DCK) is required for the phosphorylation of several deoxyribonucleosides and their nucleoside analogs. Deficiency of DCK is associated with resistance to antiviral and anticancer chemotherapeutic agents. Conversely, increased deoxycytidine kinase activity is associated with increased activation of these compounds to cytotoxic nucleoside triphosphate derivatives. DCK is clinically important because of its relationship to drug resistance and sensitivity.[1]

Contents

[edit] References

  1. ^ a b Entrez Gene: DCK deoxycytidine kinase.

[edit] Further reading

  • Arnér ES, Eriksson S (1996). "Mammalian deoxyribonucleoside kinases.". Pharmacol. Ther. 67 (2): 155–86. PMID 7494863. 
  • Chottiner EG, Shewach DS, Datta NS, et al. (1991). "Cloning and expression of human deoxycytidine kinase cDNA.". Proc. Natl. Acad. Sci. U.S.A. 88 (4): 1531–5. PMID 1996353. 
  • Eriksson S, Cederlund E, Bergman T, et al. (1991). "Characterization of human deoxycytidine kinase. Correlation with cDNA sequences.". FEBS Lett. 280 (2): 363–6. PMID 2013338. 
  • Yamada Y, Goto H, Ogasawara N (1984). "Purine nucleoside kinases in human T- and B-lymphoblasts.". Biochim. Biophys. Acta 761 (1): 34–40. PMID 6315069. 
  • Hurley MC, Palella TD, Fox IH (1984). "Human placental deoxyadenosine and deoxyguanosine phosphorylating activity.". J. Biol. Chem. 258 (24): 15021–7. PMID 6317685. 
  • Spasokoukotskaja T, Arnér ES, Brosjö O, et al. (1995). "Expression of deoxycytidine kinase and phosphorylation of 2-chlorodeoxyadenosine in human normal and tumour cells and tissues.". Eur. J. Cancer 31A (2): 202–8. PMID 7718326. 
  • Stegmann AP, Honders MW, Bolk MW, et al. (1993). "Assignment of the human deoxycytidine kinase (DCK) gene to chromosome 4 band q13.3-q21.1.". Genomics 17 (2): 528–9. doi:10.1006/geno.1993.1365. PMID 8406512. 
  • Song JJ, Walker S, Chen E, et al. (1993). "Genomic structure and chromosomal localization of the human deoxycytidine kinase gene.". Proc. Natl. Acad. Sci. U.S.A. 90 (2): 431–4. PMID 8421671. 
  • Johansson M, Brismar S, Karlsson A (1997). "Human deoxycytidine kinase is located in the cell nucleus.". Proc. Natl. Acad. Sci. U.S.A. 94 (22): 11941–5. PMID 9342341. 
  • Hatzis P, Al-Madhoon AS, Jüllig M, et al. (1998). "The intracellular localization of deoxycytidine kinase.". J. Biol. Chem. 273 (46): 30239–43. PMID 9804782. 
  • Saada A, Shaag A, Mandel H, et al. (2001). "Mutant mitochondrial thymidine kinase in mitochondrial DNA depletion myopathy.". Nat. Genet. 29 (3): 342–4. doi:10.1038/ng751. PMID 11687801. 
  • Veuger MJ, Heemskerk MH, Honders MW, et al. (2002). "Functional role of alternatively spliced deoxycytidine kinase in sensitivity to cytarabine of acute myeloid leukemic cells.". Blood 99 (4): 1373–80. PMID 11830489. 
  • Innoceta A, Galluzzi L, Ruzzo A, et al. (2002). "Molecular basis of 2',3'-dideoxycytidine-induced drug resistance in human cells.". Mol. Cell. Biochem. 231 (1-2): 173–7. PMID 11952160. 
  • 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. 
  • Krawiec K, Kierdaszuk B, Shugar D (2003). "Inorganic tripolyphosphate (PPP(i)) as a phosphate donor for human deoxyribonucleoside kinases.". Biochem. Biophys. Res. Commun. 301 (1): 192–7. PMID 12535661. 
  • van der Wilt CL, Kroep JR, Loves WJ, et al. (2003). "Expression of deoxycytidine kinase in leukaemic cells compared with solid tumour cell lines, liver metastases and normal liver.". Eur. J. Cancer 39 (5): 691–7. PMID 12628850. 
  • Ge Y, Jensen TL, Matherly LH, Taub JW (2004). "Physical and functional interactions between USF and Sp1 proteins regulate human deoxycytidine kinase promoter activity.". J. Biol. Chem. 278 (50): 49901–10. doi:10.1074/jbc.M305085200. PMID 14514691. 
  • Usova E, Maltseva T, Földesi A, et al. (2005). "Human deoxycytidine kinase as a deoxyribonucleoside phosphorylase.". J. Mol. Biol. 344 (5): 1347–58. doi:10.1016/j.jmb.2004.10.016. PMID 15561147. 
  • Mani RS, Usova EV, Eriksson S, Cass CE (2005). "Fluorescence studies of substrate binding to human recombinant deoxycytidine kinase.". Nucleosides Nucleotides Nucleic Acids 23 (8-9): 1343–6. PMID 15571255. 

[edit] See also

[edit] External links

 This transferase article is a stub. You can help Wikipedia by expanding it.
v • d • e
Transferases: Phosphotransferases/kinases (EC 2.7)
2.7.1 - OH acceptor
2.7.2 - COOH acceptor
2.7.3 - N acceptor
2.7.4 - PO4 acceptor
2.7.6 - P2O7
2.7.7 - nucleotidyl-
2.7.8 - other phos.
2.7.10-11 - protein