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The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a protein that inhibits the activation of the proteasome by the 11S and 19S regulators. Alternative transcript variants have been identified for this gene.
AW048666; BC012260; hPI31; PI31; proteasome (prosome, macropain) inhibitor subunit 1; proteasome (prosome, macropain) inhibitor subunit 1 (PI31); proteasome inhibitor PI31 subunit; proteasome inhibitor subunit 1; PSMB2; Psmf1; RP23 402M7.5; RP4 545L17.1; RP4-545L17.1
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