Mutation detail:
| Mutation site | 28697G>T |
| Virus | SARS-CoV-2 |
Mutation level  |
Nucleotide level |
| Gene/protein/region type | N |
| Gene ID | 43740575 |
| Country | India |
| Mutation type |
- |
| 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 | 33705994 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | COMPUTERS IN BIOLOGY AND MEDICINE |
| Title | A hijack mechanism of Indian SARS-CoV-2 isolates for relapsing contemporary antiviral therapeutics |
| Author | R. Prathiviraj, S. Saranya, M. Bharathi, and P. Chellapandi |
| Evidence | Forty-one protein mutations were identified in 12 Indian SARS-CoV-2 isolates by analysis of genome variations across 460 genome sequences obtained from 30 geographic sites in India. Two unique mutations such as W6152R and N5928H found in exonuclease of Surat (GBRC275b) and Gandhinagar (GBRC239) isolates |