| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.-.- |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.-.-.- |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.25.- |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#comment | "A 20-S protein composed of 28 subunits arranged in four rings of seven."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#comment | "Belongs to peptidase family T1."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#comment | "Terminal apertures restrict access of substrates to the active sites."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#comment | "The molecule is barrel-shaped, and the active sites are on the inner surfaces."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#comment | "Inhibited by mercurial reagents and some inhibitors of serine endopeptidases."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#comment | "The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2000/01/rdf-schema#comment | "In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2004/02/skos/core#prefLabel | "proteasome endopeptidase complex"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7725107 |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9087403 |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8811196 |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9748229 |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2004/02/skos/core#altLabel | "proteasome"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2004/02/skos/core#altLabel | "macropain"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2004/02/skos/core#altLabel | "prosome"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2004/02/skos/core#altLabel | "Lens neutral proteinase"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2004/02/skos/core#altLabel | "ingensin"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2004/02/skos/core#altLabel | "multicatalytic endopeptidase complex"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://www.w3.org/2004/02/skos/core#altLabel | "multicatalytic proteinase (complex)"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.25.1 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/3.4.99.46 |