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"}]} |