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Uba52 - ubiquitin A-52 residue ribosomal protein fusion product 1 (Norway rat)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-18
Description
Predicted to enable protein tag activity and ubiquitin protein ligase binding activity. Predicted to be a structural constituent of ribosome. Involved in response to insecticide. Part of cytosolic large ribosomal subunit. Orthologous to human UBA52 (ubiquitin A-52 residue ribosomal protein fusion product 1).

1 Names and Identifiers

1.1 Synonyms

  • Rps27a
  • Ubb
  • ubiquitin-ribosomal protein eL40 fusion protein
  • 60S ribosomal protein L40
  • CEP52
  • ubiquitin-60S ribosomal protein L40

1.2 Other Identifiers

1.2.1 Ensembl ID

1.2.2 Alliance Gene ID

1.2.3 Bgee Gene ID

1.2.4 RGD ID

1.2.5 Wikidata

3 Proteins

3.1 Protein Function

Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.

Component of the 60S subunit of the ribosome. Ribosomal protein L40 is essential for translation of a subset of cellular transcripts, and especially for cap-dependent translation of vesicular stomatitis virus mRNAs.

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 Consolidated References

6.2 Gene-Chemical Co-Occurrences in Literature

6.3 Gene-Gene Co-Occurrences in Literature

6.4 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. BioGRID
    LICENSE
    The MIT License (MIT); Copyright Mike Tyers Lab
    https://wiki.thebiogrid.org/doku.php/terms_and_conditions
  5. STRING: functional protein association networks
  6. NCBI Gene Expression Omnibus (GEO)
  7. Rat Genome Database (RGD)
    LICENSE
    Creative Commons Attribution 4.0 International license (CC BY 4.0)
    https://creativecommons.org/licenses/by/4.0/
  8. Swiss Institute of Bioinformatics Bgee
    LICENSE
    Creative Commons Zero license (CC0)
    https://www.bgee.org/about/
  9. 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
  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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