Ubiquitin
Ubiquitin is a small protein. It marks a target protein for degradation by attaching covalently to the target. Ubiquitinated protein is degraded by proteasome.
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Ubiquitin
a small protein (76 amino acids)
conserved throughout all the kingdoms of life; that is, virtually identical in sequence whether in bacteria, yeast, or mammals.
used by all these creatures to target proteins for destruction.
ubiquitination and SUMOylation
Various full-length, folded proteins can be attached at their C-termini to the sidechain ammonium groups of lysines of other proteins.
Ubiquitin (yoo-BIH-kwe-tin) A small protein that attaches to and marks other proteins for destruction by the proteasome.
The 26S proteasome is used for the digestion of ubiquitin-marked proteins. It is located on both sides of a cell's nuclear membrane and consists of a 20S core protease particle and two 19S regulatory particles.
Cullins directly interact with Roc1, a Ring finger protein, and the Cullin-Roc1 complex comprises the core module of a series of ubiquitin E3 ligases, which confer substrate specificity and therefore regulate the degradation process (Kamura et al.
A giant protein complex that recognizes and destroys proteins tagged for elimination by the small protein ubiquitin.
protoderm ...
PIC1-related is ~ 93% identical to PIC1 or sentrin, a gene that encodes a ubiquitin-homology domain protein. NABC1 encodes a novel cytoplasmic protein of unknown function. ZABC1 is especially interesting.
Proteasomes Large protein complexes that carry out routine degradation of ubiquitinated cellular proteins as well as of those from pathogens.
 See also: Protein, Proteins, Cell, Trans, Action
  
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