| First Author | Demontis S | Year | 1998 |
| Journal | Biochim Biophys Acta | Volume | 1443 |
| Issue | 3 | Pages | 323-33 |
| PubMed ID | 9878810 | Mgi Jnum | J:51973 |
| Mgi Id | MGI:1327520 | Doi | 10.1016/s0167-4781(98)00235-8 |
| Citation | Demontis S, et al. (1998) Isolation and characterization of the gene coding for human cytidine deaminase. Biochim Biophys Acta 1443(3):323-33 |
| abstractText | The human gene coding for cytidine deaminase (CD), the enzyme which catalyzes the deamination of cytidine and deoxycytidine to uridine and deoxyuridine, was isolated and structurally characterized. CD is a single copy gene with a length of 31 kb and consists of four exons. Exon-intron junctions do not bracket functional domains of the encoded protein as the boundary between exons 2 and 3 interrupts the catalytically important zinc-finger domain, which is well conserved along phylogenesis. 5'-RACE and RNase mapping experiments identify one major and multiple other minor transcription initiation sites, which are present in placenta as well as in the myeloid cell lines, HL-60 and U937. The 5'-flanking region of the gene contains an orientation- dependent functional promoter and is characterized by the presence of several potential sites for the binding of known transcriptional factors. |
