Ubiquitin is a conserved polypeptide unit that plays an important role in the ubiquitin-proteasome pathway. Ubiquitin can be covalently attached to many cellular proteins via a ubiquitination process that targets the 26S proteasome-degrading protein. Three components are involved in the conjugation process of the ubiquitin target protein.
Ubiquitin/ UBB antibody is first activated by forming a thiol ester complex with the activating moiety E1; Activated ubiquitin is further transferred to the ubiquitin carrier protein E2, then from E2 to ubiquitin ligase E3 to finally deliver lysine target protein residues to epsilon-NH2.
The ubiquitin-proteasome pathway is involved in a variety of normal biological processes and disease-associated disorders. Several proteins such as IκB, p53, cdc25A and Bcl-2 have been shown to target the ubiquitin-proteasome process as part of the regulation of cell cycle development, differentiation, cellular stress response, and apoptosis.
Ubiquitin, a highly conserved protein that plays a key role in directing cellular proteins to degrade the 26S proteasome, is synthesized as a precursor protein consisting of a single polyubiquitin or ubiquitin chain fused to an unbound protein. This gene encodes a fusion protein consisting of ubiquitin at the N-terminus and ribosomal protein S27a at the C-terminus.
When expressed in yeast, the protein undergoes post-translational processing to produce free ubiquitin monomer and ribosomal protein S27a. The ribosomal protein S27a is part of the 40S subunit of the ribosome and belongs to the family of ribosomal proteins S27AE. It contains the earth zinc domain of C4 and is located in the cytoplasm.