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  2. Ubiquitin - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin

    Ubiquitin is a small (8.6 kDa) regulatory protein found in most tissues of eukaryotic organisms, i.e., it is found ubiquitously. It was discovered in 1975 [ 1 ] by Gideon Goldstein and further characterized throughout the late 1970s and 1980s. [ 2 ]

  3. Proteasome - Wikipedia

    en.wikipedia.org/wiki/Proteasome

    The ubiquitin protein itself is 76 amino acids long and was named due to its ubiquitous nature, as it has a highly conserved sequence and is found in all known eukaryotic organisms. [52] The genes encoding ubiquitin in eukaryotes are arranged in tandem repeats , possibly due to the heavy transcription demands on these genes to produce enough ...

  4. 40S ribosomal protein S27a - Wikipedia

    en.wikipedia.org/wiki/40S_ribosomal_protein_S27a

    40S ribosomal protein S27a is a protein that in humans is encoded by the RPS27A gene. [5] [6]Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein.

  5. Deubiquitinating enzyme - Wikipedia

    en.wikipedia.org/wiki/Deubiquitinating_enzyme

    A similar set of genes is found in other eukaryotes such as yeast. The UBA52 and RPS27A genes produce ubiquitin that is fused to ribosomal proteins and the UBB and UBC genes produce polyubiquitin (a chain of ubiquitin joined by their C-and N-termini). [14] [15] DUBs cleave the ubiquitin from these proteins, producing active single units of ...

  6. Ubiquitin D - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin_D

    Ubiquitin is a protein composed of 76 amino acids. In order for ubiquitin to bind to other proteins, it must go through an activation process by E1, an ATP-dependent ubiquitin activating enzyme. The carboxyl terminal (C-terminus) of ubiquitin is linked to the cysteine residue of the E1 protein by a high energy thioester linkage and activated.

  7. Ubiquitin-like protein - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin-like_protein

    Ubiquitin-like proteins (UBLs) are a family of small proteins involved in post-translational modification of other proteins in a cell, usually with a regulatory function. The UBL protein family derives its name from the first member of the class to be discovered, ubiquitin (Ub), best known for its role in regulating protein degradation through covalent modification of other proteins.

  8. Ubiquitin B - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin_B

    Ubiquitin is one of the most conserved proteins known in eukaryotic organisms. Ubiquitin is required for ATP-dependent, non-lysosomal intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation.

  9. Ubiquitin C - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin_C

    7316 22190 Ensembl ENSG00000150991 ENSMUSG00000008348 UniProt P0CG48 P0CG50 RefSeq (mRNA) NM_021009 NM_019639 RefSeq (protein) NP_066289 NP_062613 Location (UCSC) Chr 12: 124.91 – 124.92 Mb Chr 5: 125.46 – 125.47 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Polyubiquitin-C is a protein encoded by the UBC gene in humans. Polyubiquitin-C is one of the sources of ubiquitin, along ...