Glycosylation Sites
For glycosylation sites analysis, analysis of N-linked, O-linked, and C-linked glycosylation sites was done for all the HPV strains found on NCBI website.
For glycosylation sites analysis, analysis of N-linked, O-linked, and C-linked glycosylation sites was done for all the HPV strains found on NCBI website.
N-glycosylation is a type of post translational modification that plays a crucial role in viruses such as proteolytic process, protein trafficking, receptor binding, virus assembly, virulence, immune evasion, etc.
The most common N-linked glycosylation sites found in proteins are as follows:
> El : 31,53,272,314
> E2 : 21,83,84,133,134,219,252
> E6 : 80
> E7 : 5,29,71
> L1 : 216
> L2 : 143,149,159,160,208,209,394,397,419
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
Accession Id | Position | Motif | Score | Software Prediction |
|---|---|---|---|---|
In O-linked glycosylation sites, they have a function in various biological activities such as signal transduction, ligand recognition, virus/bacteria-host interactions etc.
The most common O-linked glycosylation sites in proteins are as follows:
> El : 168,167,166
> E2 : 207,247,264
> E4 : 47
> E6 : 6
> L2 : 133,134,156,212,213
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
Seqname | Protein | Source | Position | Score |
|---|---|---|---|---|
The function of the C-linked glycosylation sites is unknown, they may play a role in enzymatic activity and secretion. C-linked glycosylated sites in proteins are significant, but were unable to identify any potential glycosylation sites (any site cannot reach 0.5 threshold of the software).