| Primary Identifier | IPR037757 | Type | Family |
| Short Name | COPS7A |
| 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 mammals, the CSN7 subunit is encoded by two similar genes, CSN7A and CSN7B []. This entry irepresents the COP9 signalosome complex (CSN) subunit 7a (CSN7A). Either CSN7A or CSN7B can be a component of CSN. CSN7A binds to polyamine-modulated factor 1, and each competes with the other for binding to NF-E2 related factor-2 (Nrf-2). Binding to Nrf-2 regulates transcription of spermidine/spermine N(1)-acetyltransferase []. CSN7A also binds the Int-6 protein subunit of the eIF3 translation initiation factor []; and protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53, resulting in their degradation by the ubiquitin-26S proteasome system []. |
