Ubiquitin is a conserved protein that plays a significant role in targeting cellular protein for degradation by 26S proteasome. It is synthesized from a precursor protein composed of either a polyubiquitin chain or a single ubiquitin fused with an unrelated protein. This gene encodes a protein fusion consisting of ubiquitin (N terminus) and ribosomal proteins S27a (C terminus). 

The protein is expressed in yeast and post-translationally processed to generate ubiquitin monomer free of charge and ribosomal proteins S27a. The ribosomal protein S27a, a component the 40S subunit ribosome, is part of the S27AE family. It is found in the cytoplasm and contains C4-type zinc fingers domains. You can know more about ubiquitin antibodies via www.bosterbio.com/anti-ubiquitin-picoband-trade-antibody-pb9122-boster.html.

The genome contains pseudogenes that are derived from this gene. Like ribosomal proteins S27a and L40, ribosomal proteins L40 are also synthesized with ubiquitin. In the same way, ribosomal proteins S30 and S30 are synthesized with the ubiquitin-like fubi. Multiple variants of alternatively spliced transcripts have been identified that encode the same proteins.

Ubiquitin can be found in the nucleus, in the cytoplasm, and on the cell surface membranes. Ubiquitin, (Ub), and ubiquitin-like protein (Ubls) are examples. SUMO, Nedd), is a group of 15 proteins with a molecular mass of about 8 kD. These proteins are then conjugated by activating (E1) and conjugating (E2) enzymes to lysines from a target protein. 

The number of potential ubiquitin-ligases found in mammalian cells is more than that of the superfamily of PTM protein kinases. Ubiquitination targets proteins for proteasomal degradation. This function can be a general housekeeping function, clearing out miss-folded proteins from cells, or it could involve tightly controlled Spatio-temporal cell signaling events.