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2. 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.

3. Ubiquitin - Wikipedia

   en.wikipedia.org/wiki/Ubiquitin

   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.

4. UBE2D2 - Wikipedia

   en.wikipedia.org/wiki/UBE2D2

   Modifying proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s; ubiquitin-conjugating enzymes, or E2s; and ubiquitin-protein ligases, or E3s.

5. Ubiquitin-activating enzyme - Wikipedia

   en.wikipedia.org/wiki/Ubiquitin-activating_enzyme

   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.

6. 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.

7. Deubiquitinating enzyme - Wikipedia

   en.wikipedia.org/wiki/Deubiquitinating_enzyme

   These modifications are a post translational modification (addition to a protein after it has been made) where single ubiquitin proteins or chains of ubiquitin are added to lysines of a substrate protein. These ubiquitin modifications are added to proteins by the ubiquitination machinery; ubiquitin-activating enzymes (E1s), ubiquitin ...

8. Ubiquitin-binding domain - Wikipedia

   en.wikipedia.org/wiki/Ubiquitin-binding_domain

   The NMR structure of a UBA domain, among the most common types of ubiquitin-binding domain, from the protein ubiquilin-1 (top, cyan) bound to ubiquitin (bottom, orange). ). Isoleucine 44, the center of a hydrophobic patch on the ubiquitin surface that interacts with a number of ubiquitin-binding domains, is highlighted i

9. Post-translational modification - Wikipedia

   en.wikipedia.org/wiki/Post-translational...

   Post-translational modifications can occur on the amino acid side chains or at the protein's C-or N-termini. [1] They can expand the chemical set of the 22 amino acids by changing an existing functional group or adding a new one such as phosphate.