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Proteasome

large multisubunit complex which catalyzes protein degradation, found in eukaryotes, archaea and some bacteria

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Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionSep 11, 2026
Entity authorityQ14878333
Source-derived summary

Proteasomes are essential protein complexes responsible for the degradation of proteins by proteolysis, a chemical reaction that breaks peptide bonds. Enzymes that help such reactions are called proteases. Proteasomes are found inside all eukaryotes and archaea, and in some bacteria.

In eukaryotes, proteasomes are located both in the nucleus and in the cytoplasm. The proteasomal degradation pathway is essential for many cellular processes, including the cell cycle, the regulation of gene expression, and responses to oxidative stress. The importance of proteolytic degradation inside cells and the role of ubiquitin in proteolytic pathways was acknowledged in the award of the 2004 Nobel Prize in Chemistry to Aaron Ciechanover, Avram Hershko and Irwin Rose.

The core 20S proteasome (blue in the adjacent figure) is a cylindrical, compartmental protein complex of four stacked rings forming a central pore. Each ring is composed of seven individual proteins. The inner two rings are made of seven β subunits that contain three to seven protease active sites, within the central chamber of the complex. Access to these proteases is gated on the top of the 20S, and access is regulated by several large protein complexes, including the 19S Regulatory Particle forming the 26S Proteasome.

Editorial summary

This brief starts where responsible research should: with the source description of “Proteasome” as large multisubunit complex which catalyzes protein degradation, found in eukaryotes, archaea and some bacteria. Everything that follows is an evidence route, not borrowed authority.

Editorial reviewA dependable orientation record for establishing vocabulary, names and a first evidence trail. The current lead gives the account dated anchors—2004—that can be checked directly. The selected authority fields contribute no independent date. The account is most persuasive where Proteasome, large and multisubunit can be independently traced.
Editorial analysis

Why this record matters

The subject matters to the general reference register because the source frames it as large multisubunit complex which catalyzes protein degradation, found in eukaryotes, archaea and some bacteria. Its deeper value depends on whether names, dates, institutions and citations support that framing.

Evidence profile

Vocabulary and entity names are the principal evidence signals here, because they determine the precision of every later search. The source revision retrieved here is dated Sep 11, 2026. The linked authority identifier is Q14878333. None of the 0 selected statements returned an explicit reference. The first chronological checks are 2004.

Critical limits

The absence of detail may reflect summary conventions rather than a lack of surviving documentation. The lead is largely declarative, so disagreement and counter-evidence require a deliberate search beyond the opening account. Authority statements aid reconciliation but still require their own references, qualifiers and ranks to be checked.

How to read it

Use the entry as an orientation point, then follow its citations and revision history. Names, dates and institutional relationships should be checked against the original record.

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  • Search vocabulary
  • Locating named sources
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  2. Expand the search: follow Proteasome primary sources, Proteasome archive and Proteasome research across catalogues and specialist indexes.
  3. Test the account: compare the strongest cited source with the responsible institution’s current record and note any disagreement.

Questions for further research

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Source & attribution

This entry incorporates text from Proteasome” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.