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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.
Mdm2 also acts as an E3 ubiquitin ligase, targeting both itself and p53 for degradation by the proteasome (see also ubiquitin). Several lysine residues in p53 C-terminus have been identified as the sites of ubiquitination, and it has been shown that p53 protein levels are downregulated by Mdm2 in a proteasome-dependent manner. Mdm2 is capable ...
Ubiquitin is a small protein that exists in all eukaryotic cells. It performs its myriad functions through conjugation to a large range of target proteins. A variety of different modifications can occur. The ubiquitin protein itself consists of 76 amino acids and has a molecular mass of about 8.6 kDa.
Eating red meat twice a week may increase type 2 diabetes risk, according to new research. Here, nutritionists explain the link between red meat and diabetes.
7322 56550 Ensembl ENSG00000131508 ENSMUSG00000091896 UniProt P62837 P62838 RefSeq (mRNA) NM_003339 NM_181838 NM_019912 RefSeq (protein) NP_003330 NP_862821 NP_064296 Location (UCSC) Chr 5: 139.53 – 139.63 Mb Chr 18: 35.9 – 35.94 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Ubiquitin-conjugating enzyme E2 D2 is a protein that in humans is encoded by the UBE2D2 gene. Function ...
This covalent bond of ubiquitin or ubiquitin-like proteins to targeted proteins is a major mechanism for regulating protein function in eukaryotic organisms. [2] Many processes such as cell division , immune responses and embryonic development are also regulated by post-translational modification by ubiquitin and ubiquitin-like proteins.