Proteasome subunit beta type-10 (PSMB10)
The protein contains 273 amino acids for an estimated molecular weight of 28936 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. This subunit is involved in antigen processing to generate class I binding peptides. (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.
- 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.
- 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
Cell morphogenesis
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
Humoral immune response
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
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
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 involved in cellular protein catabolic process
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 proliferation
T cell receptor signaling pathway
Transmembrane transport
Tumor necrosis factor-mediated signaling pathway
Viral process
Wnt signaling pathway, planar cell polarity pathway
The reference OMIM entry for this protein is 176847
Proteasome subunit, beta-type, 10; psmb10
Proteasome subunit mecl1
Proteasome subunit beta-2i
CLONING
CpG islands are useful landmarks in the genome for identifying genes. By database screening, Larsen et al. (1992) found that 57% of human genes are associated with CpG islands. Sites for rare cutting restriction enzymes are mainly found in CpG islands. Clustered sites for at least 2 such enzymes are good indicators of a CpG island, and an estimated 78% of island-associated genes can be located in this way. Guided by identification of an island in a 40-kb cosmid insert, Larsen et al. (1993) identified a cluster of 5 unrelated human genes on chromosome 16q22.1. One of the genes encodes a putative subunit of the proteasome complex, MECL1, an intracellular, multicatalytic proteinase (Goldberg and Rock, 1992). The derived protein sequence shares about 50% identity with a putative yeast proteasome subunit and is similar to the sequence of a peptide fragment from a rat proteasome subunit. Cruz et al. (1997) characterized a full-length mouse Lmp10 cDNA and found that Lmp10 encodes a protein of 273 amino acids with a calculated molecular mass of 29 kD. Northern blot analysis showed that mouse Lmp2 (PSMB9; 177045), Lmp7 (PSMB8; 177046), and Lmp10 were expressed in heart, liver, thymus, lung, and spleen, but not in brain, kidney, skeletal muscle, or testis.GENE FUNCTION
Cruz et al. (1997) found that mouse Lmp2, Lmp7, and Lmp10 were induced by gamma-interferon (IFNG; 147570).GENE STRUCTURE
Larsen et al. (1993) determined that the MECL1 gene has 8 exons, covers 2.3 kb, and is transcribed in the same direction as the LCAT gene (606967), from which it is separated by 3.1 kb.MAPPING
By sequence analysis, Larsen et al. (1993) mapped the PSMB10 gene to chromosome 16q22.1. Cruz et al. (1997) found that in mice the Psmb10 gene is present in single copy localized on chromosome 8 in a region of conserved synteny with human chromosome 16.ANIMAL MODEL
Basler et al. (2006) generated fertile and viable Mecl1 -/- mice. Flow cytometric analysis showed that these mice had reduced numbers of splenic Cd8 (see 186910)-positive T cells. The cytotoxic T lymphocyte (CTL) response to dominant epitopes of lymphocytic choriomeningitis virus (LCMV) was impaired in Mecl1 -/- mice. The defect was not attributable to alterations in antigen presentation, but Mecl1 -/- mice had reduced numbers of CTLs expressing the V-beta-10 segment of the T-cell receptor (see 186930), which was prominent in the wildtype anti-LCMV response. Basler et al. (2006) concluded that MECL1 has a role in determining the T-cell repertoire for an antiviral T-cell response. ... 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 176847 was added.