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Psmb8 - proteasome 20S subunit beta 8 (Norway rat)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-17
Description
Predicted to enable endopeptidase activity. Predicted to be involved in fat cell differentiation; proteasome-mediated ubiquitin-dependent protein catabolic process; and regulation of endopeptidase activity. Predicted to act upstream of or within antigen processing and presentation. Predicted to be located in cytoplasm. Predicted to be part of proteasome core complex, beta-subunit complex and spermatoproteasome complex. Predicted to be active in cytosol and nucleus. Human ortholog(s) of this gene implicated in proteasome-associated autoinflammatory syndrome 1. Orthologous to human PSMB8 (proteasome 20S subunit beta 8).

1 Names and Identifiers

1.1 Synonyms

  • Lmp7
  • Ring10
  • proteasome subunit beta type-8
  • large multifunctional protease 7
  • low molecular mass polypeptide 7
  • macropain subunit C13
  • multicatalytic endopeptidase complex subunit C13
  • proteasome (prosome, macropain) subunit, beta type 8 (large multifunctional peptidase 7)
  • proteasome (prosome, macropain) subunit, beta type, 8
  • proteasome component C13
  • proteasome subunit beta 8
  • proteasome subunit beta type-8-like
  • proteasome subunit beta-5i

1.2 Other Identifiers

1.2.1 Ensembl ID

1.2.2 Alliance Gene ID

1.2.3 Bgee Gene ID

1.2.4 Enzyme Commission (EC) Number

1.2.5 RGD ID

1.2.6 VEuPathDB ID

1.2.7 Wikidata

3 Proteins

3.1 Protein Function

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. May participate in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (By similarity). Required for adipocyte differentiation (By similarity).

3.2 Protein 3D Structures

3.2.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

3.3 Protein Targets

4 Interactions and Pathways

4.1 Interactions

4.2 Pathways

5 Expression

6 Literature

6.1 Gene-Chemical Co-Occurrences in Literature

6.2 Gene-Gene Co-Occurrences in Literature

6.3 Gene-Disease Co-Occurrences in Literature

7 Patents

7.1 Gene-Chemical Co-Occurrences in Patents

7.2 Gene-Gene Co-Occurrences in Patents

7.3 Gene-Disease Co-Occurrences in Patents

8 Information Sources

  1. NCBI Gene
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. Alliance of Genome Resources
    LICENSE
    All annotations and data produced by Alliance members that are accessible from alliancegenome.org are distributed under a CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
    https://www.alliancegenome.org/privacy-warranty-licensing
  4. NCBI Gene Expression Omnibus (GEO)
  5. Rat Genome Database (RGD)
    LICENSE
    Creative Commons Attribution 4.0 International license (CC BY 4.0)
    https://creativecommons.org/licenses/by/4.0/
  6. STRING: functional protein association networks
  7. Swiss Institute of Bioinformatics Bgee
    LICENSE
    Creative Commons Zero license (CC0)
    https://www.bgee.org/about/
  8. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  9. VEuPathDB: The Eukaryotic Pathogen, Vector and Host Informatics Resource
    LICENSE
    All data on VEuPathDB websites are provided freely for public use.
    https://veupathdb.org/veupathdb/app/static-content/about.html
  10. Wikidata
  11. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
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