Table 3. Domains/motifs in matrix protein 1 are given. Domains and motifs in the M1 protein of A/Hatay/2004/ (H5N1) showing the site name, its position on the sequence and the domain directing the site.
| M1 | ||
|---|---|---|
| Site | Position | Domain |
| Casein kinase II phosphorylation site | 5 - 8 | TevE |
| (CK-2 is a protein serine/threonine kinase whose activity is independent of cyclic nucleotides and calcium. CK-2 phosphorylates many different proteins) | 37 - 40 | TdlE |
| Protein kinase C phosphorylation site | 70 - 72 | SeR |
| (In vivo, protein kinase C exhibits a preference for the phosphorylation of serine or threonine residues found close to a C-terminal basic residue) | 161 - 163 | ShR |
| 185 - 187 | TaK | |
| N-myristoylation site | 122 - 127 | GAlaSC |
| (Number of eukaryotic proteins are acylated by the covalent addition of myristate (a C14-saturated fatty acid) to their N-terminal residue via an amide linkage) | 129 - 134 | GLiyNR |
| 136 - 141 | GTvtTE | |
| 145 - 150 | GLvcAT | |
| 220 - 225 | GThpNS | |
| 228 - 233 | GLrdNL | |
| N-glycosylation site | 224 - 227 | NSSA |
| (Potential N-glycosylation sites are specific to the consensus sequence Asn-Xaa-Ser/Thr. Presence of the consensus tripeptide is not sufficient to conclude that an asparagine residue is glycosylated, due to the fact that the folding of the protein plays an important role in the regulation of N-glycosylation) | ||