COP9 signalosome complex subunit 3 (COPS3)
The protein contains 423 amino acids for an estimated molecular weight of 47873 Da.
Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
Cullin deneddylation
In utero embryonic development
Nucleotide-excision repair, DNA damage recognition
Post-translational protein modification
Protein deneddylation
Response to light stimulus
Signal transduction
Transcription-coupled nucleotide-excision repair
Ubiquitin-dependent protein catabolic process
Molecular Function
The reference OMIM entry for this protein is 604665
Cop9 signalosome, subunit 3; cops3
Sgn3
CLONING
To identify new components of the 26S proteasome, Seeger et al. (1998) obtained peptide sequences from a 45-kD protein. By micropeptide sequence analysis and probing of cDNA libraries, Seeger et al. (1998) isolated a cDNA encoding COPS3, which they termed SGN3, for subunit 3 of a novel 450-kD signalosome complex that also includes TRIP15 (604508), COPS5 (604850), GPS1 (601934), and 4 other subunits. Sequence analysis predicted that COPS3 is a 403-amino acid protein which contains regions with homology to the 26S proteasome S3 regulatory subunit. Autoradiographic analysis showed that the complex phosphorylates JUN (165160), IKBA (164008), and the C-terminal part of the p105 precursor of NFKB (164011). The 26S proteasome is not a phosphorylation target, although immunofluorescence microscopy demonstrated that the 450-kD complex has a cytosolic localization, concentrated around the nucleus.MAPPING
Elsea et al. (1999) reported the localization and partial characterization of SGN3. They mapped the SGN3 gene to 17p11.2 by somatic cell hybrid analysis. By analysis of genomic clones, they further localized the SGN3 gene to the distal end of the Smith-Magenis syndrome (SMS) critical region (182290), near marker D17S71. Although SMS patients were haploinsufficient for SGN3, analyses showed that the SGN3 protein was present at equivalent levels in patient and parental control cells, and that the COP9 signalosome complex was assembled and in normal quantities in transformed lymphoblastoid cell lines from patients. Elsea et al. (1999) concluded that SGN3 probably does not play a significant role with respect to SMS, although its involvement could not be ruled out since the importance of the COP9 signalosome in embryogenesis or differentiation was not well understood. ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 26, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 604665 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed