Proteasome subunit beta type-11 (PSMB11)
The protein contains 300 amino acids for an estimated molecular weight of 32530 Da.
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome (By similarity). Plays a pivotal role in development of CD8-positive T cells (By similarity). (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
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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| Variant | Description |
|---|---|
| dbSNP:rs34457782 |
No binding partner found
Biological Process
Anaphase-promoting complex-dependent catabolic process
Antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent
CD8-positive, alpha-beta T cell differentiation
Fc-epsilon receptor signaling pathway
Interleukin-1-mediated signaling pathway
MAPK cascade
Negative regulation of canonical Wnt signaling pathway
Negative regulation of G2/M transition of mitotic cell cycle
NIK/NF-kappaB signaling
Positive regulation of canonical Wnt signaling pathway
Post-translational protein modification
Pre-replicative complex assembly
Proteasomal protein catabolic process
Proteasomal ubiquitin-independent protein catabolic process
Proteasome-mediated ubiquitin-dependent protein catabolic process
Protein deubiquitination
Protein polyubiquitination
Proteolysis
Proteolysis involved in cellular protein catabolic 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
Stimulatory C-type lectin receptor signaling pathway
T cell differentiation in thymus
T cell receptor signaling pathway
Transmembrane transport
Tumor necrosis factor-mediated signaling pathway
Wnt signaling pathway, planar cell polarity pathway
Cellular Component
Cytoplasm
Cytosol
Nucleus
Proteasome core complex
Proteasome core complex, beta-subunit complex
The reference OMIM entry for this protein is 611137
Proteasome subunit, beta-type, 11; psmb11
Proteasome subunit, beta-5 family, thymus-specific
Proteasome subunit beta-5t
DESCRIPTION
Proteasomes generate peptides that are presented by major histocompatibility complex (MHC) I molecules to other cells of the immune system. Proteolysis is conducted by 20S proteasomes, complexes of 28 subunits arranged as a cylinder in 4 heteroheptameric rings: alpha-1 to -7, beta-1 to -7, beta-1 to -7, and alpha-1 to -7. The catalytic subunits are beta-1 (PSMB6; 600307), beta-2 (PSMB7; 604030), and beta-5 (PSMB5; 600306). Three additional subunits, beta-1i (PSMB9; 177045), beta-2i (PSMB10; 176847), and beta-5i (PSMB8; 177046), are induced by gamma-interferon (IFNG; 147570) and are preferentially incorporated into proteasomes to make immunoproteasomes. PSMB11, or beta-5t, is a catalytic subunit expressed exclusively in cortical thymic epithelial cells (Murata et al., 2007).CLONING
By searching databases for proteasome-related genes, followed by PCR of HeLa cell genomic DNA, Murata et al. (2007) cloned human PSMB11, which they called beta-5t. The beta-5t protein was most homologous to beta-5 and beta-5i. Northern and Western blot analyses of mouse tissues showed that beta-5t was expressed exclusively in thymus. Immunohistochemical analysis detected beta-5t expression in mouse cortical thymic epithelial cells.GENE FUNCTION
Using immunoprecipitation analysis, Murata et al. (2007) found that about 20% of 20S proteasomes in mouse thymus contained beta-5t instead of beta-5 or beta-5i. Moreover, these beta-5t-containing proteasomes, or thymoproteasomes, preferentially incorporated beta-1i and beta-2i in place of beta-1 and beta-2, respectively.GENE STRUCTURE
Murata et al. (2007) determined that the PSMB11 gene contains 1 exon in both mice and humans.MAPPING
By genomic sequence analysis, Murata et al. (2007) mapped the PSMB11 gene to chromosome 14, adjacent to the PSMB5 gene on the opposite strand.ANIMAL MODEL
Murata et al. (2007) found that mice deficient in beta-5t had fewer Cd8 (see 186910) single-positive (SP) thymocytes, but normal numbers of Cd4 (186940) SP cells, compared with wildtype mice. They concluded that PSMB11 plays a pivotal role in development of CD8-positive T cells. ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 611137 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).