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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]
The human protein Mitochondrial E3 ubiquitin protein ligase 1 is ~40 kDa in size and composed of 352 amino acids. [7] [10] [11] The calculated theoretical pI of this protein is 7.28. [12] MUL1 contains Ring domains at both its N-terminal and C-terminal, which are both exposed to the cytosol. [6]
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.
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.
A ubiquitin ligase (also called an E3 ubiquitin ligase) is a protein that recruits an E2 ubiquitin-conjugating enzyme that has been loaded with ubiquitin, recognizes a protein substrate, and assists or directly catalyzes the transfer of ubiquitin from the E2 to the protein substrate. In simple and more general terms, the ligase enables movement ...
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.
Ubiquitin-protein ligase E3A (UBE3A) also known as E6AP ubiquitin-protein ligase (E6AP) is an enzyme that in humans is encoded by the UBE3A gene. This enzyme is involved in targeting proteins for degradation within cells. Protein degradation is a normal process that removes damaged or unnecessary proteins and helps maintain the normal functions ...
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 ...