| Primary Identifier | IPR033205 | Type | Family |
| Short Name | COP9_CSN8 |
| description | The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].In the complex, CSN8, which is the smallest subunit, probably interacts directly with CSN3, CSN4 and CSN7 (CSN7A or CSN7B). It is necessary for assembly of the complex []. CSN8 plays an important role in maintaining the proper duration of the G1 phase of the cell cycle []. |
