The protein contains 277 amino acids for an estimated molecular weight of 29965 Da.
Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a trypsin-like activity. (updated: Jan. 31, 2018)
Protein identification was indicated in the following studies:
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.
(right-click above to access to more options from the contextual menu)
Variant | Description |
---|---|
dbSNP:rs4574 |
The reference OMIM entry for this protein is 604030
The 20S (700-kD) proteasome, which contains multiple peptidase activities, is one component of the 26S (2000-kD) complex, which degrades ubiquitinated proteins. The 20S proteasome is composed of alpha and proteolytic beta subunits. See PSMB2 (602175). One important function of the proteasome in higher vertebrates is to generate the peptides presented on MHC-class 1 molecules to circulating lymphocytes. The cytokine gamma-interferon (IFNG; 147570), which stimulates antigen presentation, alters proteasome subunit composition and functional activity. Upon IFNG treatment, the beta subunits X (600306) and Y (600307) are replaced by subunits LMP7 (177046) and LMP2 (177045), respectively. The changes in peptidase activity are due to the incorporation of the LMP subunits (Coux et al. (1996)). Hisamatsu et al. (1996) determined that a third pair of proteasome subunits, Z and MECL1 (176847), are expressed reciprocally in response to IFNG treatment. Z is downregulated, while MECL1 is markedly induced, suggesting that Z can be replaced by MECL1 in the proteasomal complex. By screening a HepG2 cell line library with a probe based on the partial amino acid sequence of the Z protein, the authors isolated cDNAs encoding Z. Sequence analysis revealed that the predicted 277-amino acid Z protein is a beta subunit. Z shares 58% and 55% protein sequence identity with MECL1 and PUP1, a S. cerevisiae proteasomal subunit, respectively. Both Z and MECL1 are proteolytically processed to generate a mature protein with an N-terminal threonine residue that is required for activity. Coux et al. (1996) stated that the IFNG-induced beta subunits MECL1, LMP7, and LMP2, likely alter peptidase activity because they contain distinct active sites. Thus the proteasomes from IFNG-treated cells should generate more peptides with hydrophobic or basic C termini, like the vast majority of peptides presented on MHC class I molecules. Hisamatsu et al. (1996) proposed that 20S particles containing MECL1, LMP7, and LMP2 be designated immunoproteasomes to emphasize their role in immunologic processing of endogenous antigens. By fluorescence in situ hybridization, Hisamatsu et al. (1996) mapped the Z gene to 9q34.11-q34.12. ... More on the omim web site
Feb. 10, 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 16, 2016: Protein entry updated
Automatic update: OMIM entry 604030 was added.