Mutation detail:
Mutation site | A36T |
Virus | Influenzavirus A H1N1 |
Mutation level ![]() |
Amino acid Level |
Gene/protein/region type | PA |
Gene ID | 23308128 |
Country | - |
Mutation type ![]() |
nonsynonymous mutation |
Genotype/subtype/clade | - |
Sample ![]() |
cell line |
Variants | - |
Viral reference sequence | GQ166226.1 |
Drug/antibody/vaccine | - |
Transmissibility ![]() |
- |
Transmission mechanism | - |
Pathogenicity ![]() |
- |
Pathogenicity mechanism | - |
Immune escape mutation | - |
Immune escape mechanism | - |
RT-PCR primers probes | - |
Protein detail:
Protein name | Polymerase PA |
Uniprot protein ID | C3W5X6 |
Protein length | 716 amino acids |
Protein description | PA Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity. |
Literature information:
Pubmed ID | 22438920 |
Clinical information | No |
Disease | - |
Published year | 2012 |
Journal | PLOS ONE |
Title | |
Author | Wenfei Zhu,Yun Zhu,Kun Qin,Zaijiang Yu,Rongbao Gao |
Evidence | In summary, our results show that the amino acid 36T in PA and 357N in PB2 contribute to polymerase activity and viral replication of pH1N1 in mammalian cells. |