Mutation detail:
| Mutation site | H137R |
| Virus | Human rhinovirus |
Mutation level  |
Amino acid level |
| Gene/protein/region type | P2-A |
| Gene ID | 1493933 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | A |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | X02316.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | P2-A Polypeptide |
| Uniprot protein ID | P07210 |
| Protein length | 136 amino acids |
| Protein description | P2-A is the cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein.P2-A cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. P2-A inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores. P2-A counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly. |
Literature information:
| Pubmed ID | 8761474 |
| Clinical information | No |
| Disease | - |
| Published year | 1996 |
| Journal | Biochemical Journal |
| Title | Human rhinovirus 5A proteinase mutant and its second-site revertants |
| Author | M Luderer-Gmach,H D Liebig,W Sommergruber,T Voss,F Fessl |
| Evidence | activity was, however, partially restored by the following exchanges: Ser-27-->Pro, His-135-->Arg or His-139-->Arg. |