Mutation detail:
| Mutation site | M502V |
| Virus | Measles virus |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | P |
| Gene ID | 1489805 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | K01711.1 |
| Drug/antibody/vaccine | AS-136A resistant |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Phosphoprotein |
| Uniprot protein ID | P35974 |
| Protein length | 507 amino acids |
| Protein description | P starts with a long disordered tail (304 amino acids) followed by a tetrameric domain of four long, parallel helices between residues 304 and 377. P of mumps forms a tetramer of the same length but with two anti-parallel dimers. At the C-terminus of P there is another folded domain (XD) which is linked to the tetramerization domain via the unfolded Ploop. Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis. |
Literature information:
| Pubmed ID | 19528268 |
| Clinical information | No |
| Disease | - |
| Published year | 2009 |
| Journal | Antimicrobial Agents and Chemotherapy |
| Title | Target analysis of the experimental measles therapeutic AS-136A |
| Author | Jeong-Joong Yoon,Stefanie A Krumm,J Maina Ndungu,Vanessa Hoffman,Bettina Bankamp |
| Evidence | Taken together, these data support the hypothesis that acquiring mutations in these L domains may reduce virus fitness. |