AVM v1, released 02-OCT-22

A manually curated database of aerosol-transmitted virus mutations, human diseases, and drugs

Mutation detail:


Mutation site R99A
Virus SARS-CoV
Mutation level Amino acid level
Gene/protein/region type ORF1ab(nsp1)
Gene ID 1489680
Country -
Mutation type nonsynonymous mutation
Genotype/subtype/clade -
Sample cell line
Variants -
Viral reference sequence AY278741.1
Drug/antibody/vaccine -
Transmissibility -
Transmission mechanism -
Pathogenicity -
Pathogenicity mechanism -
Immune escape mutation -
Immune escape mechanism -
RT-PCR primers probes -

Protein detail:


Protein name ORF1ab polyprotein
Uniprot protein ID P0C6X7
Protein length 7073 amino acids
Protein description The Orf1ab polyprotein contains the Orf1a polyprotein and 16 non-structural proteins. The Orf1ab polyprotein and its cleavage products carry out a wide range of activities associated with the viral replication, including ATP binding and breaking down of ADP and phosphate, cysteine-directed endopeptidase, leading to the formation of nonstructural proteins, such as exonuclease that produces ribose- 5-phosphate, methyltransferase for the synthesis of new nucleotides, RNA polymerase for the viral replication, RNA helicase for the removal of super twisting, as well as the regulation of the transcription through binding of zinc. However, the functions of the Orf1ab are the collective functions of the non-structural proteins encoded by the gene of Orf1ab

Literature information:


Pubmed ID 34624207
Clinical information No
Disease -
Published year 2021
Journal Cell Reports
Title The N-terminal domain of SARS-CoV-2 nsp1 plays key roles in suppression of cellular gene expression and preservation of viral gene expression
Author Aaron S. Mendez, Michael Ly, Angélica M. González-Sánchez, Ella Hartenian, Nicholas T. Ingolia
Evidence Remarkably, however, both the R124A/K125A and R99A mutants gained the ability to translationally repress CoV2L-nLuc (3-fold and 2.4-fold, respectively), although they remained impaired for the translational suppression of HBB-nLuc (Figure 5B).