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Usp28 - ubiquitin specific peptidase 28 (Norway rat)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-18
Description
Predicted to enable cysteine-type deubiquitinase activity. Predicted to be involved in several processes, including intracellular signal transduction; protein deubiquitination involved in ubiquitin-dependent protein catabolic process; and response to ionizing radiation. Predicted to be located in nuclear body. Predicted to be part of protein-containing complex. Predicted to be active in cytosol and nucleus. Orthologous to human USP28 (ubiquitin specific peptidase 28).

1 Names and Identifiers

1.1 Synonyms

  • ubiquitin carboxyl-terminal hydrolase 28
  • deubiquitinating enzyme 28
  • ubiquitin specific protease 28
  • ubiquitin thioesterase 28
  • ubiquitin thiolesterase 28
  • ubiquitin-specific-processing protease 28

1.2 Other Identifiers

1.2.1 Ensembl ID

1.2.2 Alliance Gene ID

1.2.3 Enzyme Commission (EC) Number

1.2.4 RGD ID

1.2.5 Wikidata

3 Proteins

3.1 Protein Function

Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBXW7) complex. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells.

3.2 Protein Isoforms

Isoform
Isoform 1
UniProt ID
RefSeq Accession
Isoform
Isoform 2
UniProt ID
RefSeq Accession

3.3 Protein 3D Structures

3.3.1 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

3.4 Protein Targets

4 Interactions and Pathways

4.1 Interactions

4.2 Pathways

5 Biochemical Reactions

6 Expression

7 Literature

7.1 Gene-Chemical Co-Occurrences in Literature

7.2 Gene-Gene Co-Occurrences in Literature

7.3 Gene-Disease Co-Occurrences in Literature

8 Patents

8.1 Gene-Chemical Co-Occurrences in Patents

8.2 Gene-Gene Co-Occurrences in Patents

8.3 Gene-Disease Co-Occurrences in Patents

9 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. 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
  8. Wikidata
  9. 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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