Mutation detail:
| Mutation site | G214C |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | N |
| Gene ID | 43740575 |
| Country | Peru |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | NC_045512.2 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Nucleocapsid Phosphoprotein |
| Uniprot protein ID | P0DTC9 |
| Protein length | 419 amino acids |
| Protein description | The Nucleocapsid Phosphoprotein has a modular organization which can be divided into intrinsically disordered regions (IDRs) and conserved structural regions according to the sequence characteristics. The IDRs include three modules: N-arm, central Ser/Arg-rich flexible linker region (LKR), and C-tail, while the conserved structural regions including two modules: N-terminal domain (NTD) and C-terminal domain (CTD). In the primary structure, NTD and CTD are connected by LKR and are usually flanked by N-arm and C-tail. The nucleocapsid phosphoprotein is a structural protein that binds to, protects the viral RNA genome and is involved in packaging the RNA into virus particles. The N protein has been suggested as an antiviral drug target. |
Literature information:
| Pubmed ID | 34704780 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Microbiology spectrum |
| Title | The Emergence of Sars-CoV-2 Variant Lambda (C.37) in South America |
| Author | Pedro E Romero, Alejandra Davila-Barclay, Guillermo Salvatierra, Luis Gonzalez, Diego Cuicapuza |
| Evidence | C.37 contains a novel deletion (S: del 246 to 252, located at the N-terminal domain) plus seven nonsynonymous mutations in the Spike gene (G75V, T76I, D253N, L452Q, F490S, D614G, T859N) (Fig. 1C). Mutations L452Q and F490S both map to the Spike proteins receptor-binding domain (RBD). While L452Q is almost exclusive to C.37, L452R is present in variant of concern (VOC) delta (B.1.617.2) and variants of interest (VOI) epsilon (B.1.427/B.1.429) and kappa (B.1.617.1) and is associated with increased affinity for the ACE2 receptor (2). F490S has been associated with reduced in vitro susceptibility to antibody neutralization (3, 4). C.37 also displays the ORF1a del 3675 to 3677 deletion, found in VOCs alpha, beta, and gamma (5). |