Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| A | 0051260 | biological_process | protein homooligomerization |
Functional Information from PROSITE/UniProt
| site_id | PS00291 |
| Number of Residues | 16 |
| Details | PRION_1 Prion protein signature 1. AGAAAAGAVVGGLGGY |
| Chain | Residue | Details |
| A | ALA116-TYR131 | |
| site_id | PS00706 |
| Number of Residues | 19 |
| Details | PRION_2 Prion protein signature 2. EtDiKIMeRVVeQMCitQY |
| Chain | Residue | Details |
| A | GLU203-TYR221 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P04156","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"GPI-anchor amidated alanine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"33600485","evidenceCode":"ECO:0000269"}]} |
