Abstract
Partial cDNAs coding for human protein S were isolated from a pUC9 human liver cDNA library. Together, the overlapping clones span a (partial) 5′-non-coding region, and the complete protein S coding and 3′-untranslated regions. The derived amino acid sequence deviates at five positions from two previously reported protein S sequences. Two of these differences (Phe instead of Leu at position - 16 and Tyr instead of Asp at position 222) are found in regions that are important for the post-translational modification of protein S, the γ-carboxylation of glutamic acid and the hydroxylation of asparagine, respectively.
| Original language | English |
|---|---|
| Pages (from-to) | 186-190 |
| Number of pages | 5 |
| Journal | FEBS letters |
| Volume | 222 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 28 Sept 1987 |
Keywords
- Carboxylation
- cDNA
- Hydroxylation
- Protein S