COP9 signalosome complex subunit 7a (COPS7A)
The protein contains 275 amino acids for an estimated molecular weight of 30277 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, JUN, I-kappa-B-alpha/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: March 4, 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.
- 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
COP9 signalosome assembly
Cullin deneddylation
Nucleotide-excision repair, DNA damage recognition
Post-translational protein modification
Protein deneddylation
Transcription-coupled nucleotide-excision repair
Viral process
Molecular Function
The reference OMIM entry for this protein is 616009
Cop9 signalosome, subunit 7a; cops7a
Csn7
DESCRIPTION
COPS7A is a subunit of the COP9 signalosome, which functions in intracellular signaling and transcriptional control. COPS7A also appears to have an independent role in transcriptional control (Wang et al., 2002).CLONING
Wei et al. (1998) purified COP9 complexes from pig spleen and mouse brain, liver, and spleen extracts. Sequencing revealed that the highly conserved 275-amino acid mammalian S7a subunit has a central proteasome (see 604449)-COP9-initiation factor-3 (see 602039) (PCI) domain and a C-terminal coiled-coil domain. PMF1 (609176) is a transcriptional cofactor of NRF2 (NFE2L2; 600492) involved in facilitating polyamine-inducible transcription of SSAT (SAT1; 313020). Wang et al. (2002) used PMF1 as bait in a yeast 2-hybrid screen of a placenta cDNA library and identified COPS7A, which they called CSN7. The deduced 275-amino acid protein shares 98.9% identity with mouse Csn7a. Northern blot analysis showed variable expression of an approximately 2-kb transcript in all human tissues examined, with highest expression in brain, heart, and skeletal muscle. In vitro transcription and translation resulted in a CSN7 protein with an apparent molecular mass of 31 kD by SDS-PAGE.GENE FUNCTION
NRF2 constitutively binds the polyamine responsive element (PRE) in the minimal SSAT promoter, but it needs a binding partner to activate SSAT transcription. Using electrophoretic mobility-shift and reporter gene assays, Wang et al. (2002) found that PMF1 and CSN7 competed for binding to NRF2 at the PRE to activate the SSAT reporter. Coexpression of CSN7 and PMF1 reduced the availability of CSN7 as a binding partner for NRF2 and reduced PRE transcriptional activity.MAPPING
Hartz (2014) mapped the COPS7A gene to chromosome 12p13.31 based on an alignment of the COPS7A sequence (GenBank GENBANK AB033603) with the genomic sequence (GRCh38). ... More on the omim web site
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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 616009 was added.