26S proteasome regulatory subunit 7 (PSMC2)
The protein contains 433 amino acids for an estimated molecular weight of 48634 Da.
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC2 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. (updated: Dec. 20, 2017)
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
Anaphase-promoting complex-dependent catabolic process
Antigen processing and presentation of exogenous peptide antigen via MHC class I
Antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent
Antigen processing and presentation of peptide antigen via MHC class I
Apoptotic process
Cellular nitrogen compound metabolic process
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
Fc-epsilon receptor signaling pathway
G1/S transition of mitotic cell cycle
Gene expression
Interleukin-1-mediated signaling pathway
MAPK cascade
Mitotic cell cycle
Negative regulation of apoptotic process
Negative regulation of canonical Wnt signaling pathway
Negative regulation of G2/M transition of mitotic cell cycle
Neutrophil degranulation
NIK/NF-kappaB signaling
Obsolete negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle
Obsolete positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition
Obsolete regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle
Osteoblast differentiation
Positive regulation of canonical Wnt signaling pathway
Positive regulation of RNA polymerase II transcription preinitiation complex assembly
Post-translational protein modification
Pre-replicative complex assembly
Proteasome-mediated ubiquitin-dependent protein catabolic process
Protein deubiquitination
Protein polyubiquitination
Regulation of apoptotic process
Regulation of cellular amino acid metabolic process
Regulation of hematopoietic stem cell differentiation
Regulation of mitotic cell cycle phase transition
Regulation of mRNA stability
Regulation of transcription from RNA polymerase II promoter in response to hypoxia
SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
Small molecule metabolic process
Stimulatory C-type lectin receptor signaling pathway
T cell receptor signaling pathway
Transmembrane transport
Tumor necrosis factor-mediated signaling pathway
Ubiquitin-dependent ERAD pathway
Ubiquitin-dependent protein catabolic process
Viral process
Wnt signaling pathway, planar cell polarity pathway
Cellular Component
Cytoplasm
Cytoplasmic ribonucleoprotein granule
Cytosol
Cytosolic proteasome complex
Dendritic spine
Extracellular region
Ficolin-1-rich granule lumen
Membrane
Nuclear proteasome complex
Nucleoplasm
Nucleus
P-body
Proteasome accessory complex
Proteasome complex
Proteasome regulatory particle, base subcomplex
Secretory granule lumen
The reference OMIM entry for this protein is 154365
Proteasome 26s subunit, atpase, 2; psmc2
Mammalian suppressor of sgv-1 of yeast; mss1
Protease 26s, subunit 7; s7
DESCRIPTION
The 26S proteasome (see PSMC1; 602706) is a multisubunit protease complex composed of a 20S core component and two 19S regulatory complexes. PSMC2 is 1 of 6 putative ATPases contained within the regulatory complex. PSMC2 was first identified as a possible cellular factor that cooperates with the human immunodeficiency virus-1 (HIV-1) protein Tat, a potent activator of virus gene expression.CLONING
By transcomplementation of a yeast sgv1-deficient mutant, Shibuya et al. (1992) isolated a human cDNA from a novel gene, MSS1. The MSS1 protein was found to share 42% sequence identity with the human TBP1 protein (PSMC3; 186852), which binds Tat in vitro and suppresses Tat-mediated transactivation in vivo (Nelbock et al., 1990). Shibuya et al. (1992) found that the levels of HIV activation by Tat correlated with endogenous levels of MSS1 mRNA. Furthermore, they provided evidence that expression of MSS1 enhances the Tat-mediated transactivation. The 1.5-kb MSS1 cDNA encodes a protein of 433 amino acids. To characterize components of the 26S proteasome, Dubiel et al. (1993) performed peptide sequence analysis on subunit 7 (S7). They determined that S7 is identical to MSS1. By SDS-PAGE, S7 has a molecular mass of 49 kD. By Western blot analysis of rat tissues, Yanagi et al. (2000) found that the level of PSMC2 expression varied among tissues but was ubiquitous. This was in contrast to the expression pattern of the 30-kD component of the proteasome 20S core, which showed similar levels of expression in all tissues. Immunolocalization of proteasome subunits in HeLa and HepG2 cells showed proteasome localization within nuclei, while immunolocalization of PSMC2 gave homogeneous staining of both cytoplasm and nucleoplasm. By glycerol gradient sedimentation, Yanagi et al. (2000) found PSMC2 purified from rat liver nuclear extracts associated with the proteasome and with protein complexes of lighter density, and it also existed as a monomer. They also found that several basal transcription factors for RNA polymerase II, including TATA box-binding protein (TBP; 600075), and the general transcription factors IIB (GFT2B; 189963), IIH (see GTF2H1; 189972), and IIF (see GTF2F1; 189968) coimmunoprecipitated with PSMC2 from rat liver lysosomes, suggesting dual functionality of PSMC2.MAPPING
Tanahashi et al. (1998) mapped the PSMC2 gene to 7q22.1-q22.3 by fluorescence in situ hybridization. ... More on the omim web site
Feb. 5, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
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
March 15, 2016: Protein entry updated
Automatic update: OMIM entry 154365 was added.