Mutation detail:
| Mutation site | N164D |
| Virus | Human rhinovirus |
Mutation level  |
Amino acid level |
| Gene/protein/region type | P3C |
| Gene ID | 1461213 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | B |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | NC_001490.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
hinder |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Protease 3C |
| Uniprot protein ID | P03303 |
| Protein length | 182 amino acids |
| Protein description | P3C major viral protease that mediates proteolytic processing of the polyprotein. Cleaves host EIF5B, contributing to host translation shutoff. Cleaves also host PABPC1, contributing to host translation shutoff. Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment. |
Literature information:
| Pubmed ID | 10224078 |
| Clinical information | No |
| Disease | - |
| Published year | 1999 |
| Journal | Journal Of Biological Chemistry |
| Title | Identification and characterization of human rhinovirus-14 3C protease deamidation isoform |
| Author | G A Cox,R B Johnson,J A Cook,M Wakulchik,M G Johnson |
| Evidence | Converting Asn-164 to Asp by site-directed mutagenesis resulted in a mutated 3C protease with extremely low activity, as seen with the pI 8.3 isoform, indicating a role of Asn-164 in substrate recognition and binding. |