26S proteasome non-ATPase regulatory subunit 2 (PSMD2)
The protein contains 908 amino acids for an estimated molecular weight of 100200 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.', 'Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1. (updated: Nov. 22, 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.
- 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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| Variant | Description |
|---|---|
| dbSNP:rs11545172 | |
| dbSNP:rs11545169 | |
| dbSNP:rs17856236 |
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
Positive regulation of canonical Wnt signaling pathway
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 protein catabolic process
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
Viral process
Wnt signaling pathway, planar cell polarity pathway
Cellular Component
Cytosol
Extracellular exosome
Extracellular region
Ficolin-1-rich granule lumen
Membrane
Nucleoplasm
Nucleus
Proteasome accessory complex
Proteasome complex
Proteasome regulatory particle
Proteasome regulatory particle, base subcomplex
Proteasome storage granule
Secretory granule lumen
The reference OMIM entry for this protein is 606223
Proteasome 26s subunit, non-atpase, 2; psmd2
Proteasome 26s, subunit 2; s2
Tumor necrosis factor receptor-associated protein 2; trap2
Tnfr-associated protein 2
The 26S proteasome is a multisubunit protein complex involved in the degradation of constitutively short-lived proteins, regulatory proteins, and abnormal and malfolded proteins. It is composed of a 700-kD 20S proteasome catalytic core proteinase (e.g., PSMA3; 176843) and PA700 regulatory modules. The PA700 subunits are divided into a family of ATPases (e.g., PSMC6; 602708) and a family of non-ATPases (e.g., PSMD9; 603146).
CLONING
Using a yeast 2-hybrid screen of a HeLa cDNA library with the intracellular death domain of the p55 tumor necrosis factor receptor (TNFRSF1A; 191190) as bait, Boldin et al. (1995) isolated a cDNA encoding PSMD2, which they designated 55.11. Binding analysis indicated that the 900-amino acid 55.11 protein binds to C-terminally truncated p55 lacking the death domain. Northern blot analysis revealed expression of an approximately 3.0-kb transcript in HeLa, leukemic T-cell, and hepatic carcinoma cell lines. Recombinant 55.11 was expressed as an 84-kD protein. Sequence analysis predicted that 55.11 has a KEKE motif and shares homology with the yeast Sen3 protein, a component of the 26S proteasome regulatory complex. Boldin et al. (1995) proposed that given the rapidity with which TNF binding decreases after the inhibition of protein synthesis, TNFR has a short half-life consistent with proteasomal degradation of the molecule. By biochemical purification of a 97-kD PA700 subunit from bovine red cells, peptide sequence analysis, and database searching, Tsurumi et al. (1996) obtained a cDNA encoding PSMD2, which they termed p97. The deduced 908-amino acid protein contains a KEKE motif, a hydrophilic region rich in alternately positively charged (lys) and negatively charged (glu) amino acids. Northern blot analysis detected ubiquitous expression of a 3.0-kb transcript, with highest levels in heart and skeletal muscle. Complementation analysis indicated that PSMD2 is a functional homolog of Nas1 in yeast. Using a yeast 2-hybrid screen with the intracellular domain of TNFR1 as bait, Dunbar et al. (1997) cloned and characterized a partial cDNA encoding PSMD2, which they called TRAP2.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PSMD2 gene to chromosome 3 (TMAP RH65279). ... More on the omim web site
Dec. 9, 2018: Protein entry updated
Automatic update: model status changed
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 606223 was added.