26S proteasome regulatory subunit 8 (PSMC5)
The protein contains 406 amino acids for an estimated molecular weight of 45626 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. PSMC5 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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| Variant | Description |
|---|---|
| a colorectal cancer sample; somatic mutation | |
| dbSNP:rs11543211 |
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
Modulation of chemical synaptic transmission
Negative regulation of apoptotic process
Negative regulation of canonical Wnt signaling pathway
Negative regulation of G2/M transition of mitotic cell cycle
Negative regulation of programmed cell death
Negative regulation of transcription, DNA-templated
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
Positive regulation of inclusion body assembly
Positive regulation of RNA polymerase II transcription preinitiation complex assembly
Positive regulation of transcription, DNA-templated
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 by RNA polymerase II
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
Transcription by RNA polymerase II
Transmembrane transport
Tumor necrosis factor-mediated signaling pathway
Ubiquitin-dependent ERAD pathway
Viral process
Wnt signaling pathway, planar cell polarity pathway
Cellular Component
Blood microparticle
Cytoplasm
Cytoplasmic vesicle
Cytosol
Cytosolic proteasome complex
Extracellular exosome
Inclusion body
Membrane
Nuclear proteasome complex
Nucleoplasm
Nucleus
Postsynapse
Proteasome accessory complex
Proteasome complex
Proteasome regulatory particle
Proteasome regulatory particle, base subcomplex
The reference OMIM entry for this protein is 601681
Proteasome 26s subunit, atpase, 5; psmc5
Thyroid hormone receptor interactor 1; trip1
DESCRIPTION
PSMC5 is a member of the AAA (ATPases Associated with diverse cellular Activities) gene family (Hoyle et al., 1997).GENE FAMILY
Members of the AAA gene family are most similar throughout an approximately 230-amino acid ATPase domain (the AAA domain), and related genes have been described in organisms as distant as archaebacteria and eubacteria. All the known AAA proteins contain either 1 or 2 AAA domains, and the family can be subdivided into 2 groups on this basis. It appears that 2-domain AAA proteins (e.g., NSF, 601633) are associated with membrane functions. In eukaryotes, the 1-domain AAA proteins such as PSMC5 appear to be involved largely in the regulatory subunit of the 26S protease (summary by Hoyle et al., 1997).CLONING
Lee et al. (1995) used the yeast interaction trap, a version of the yeast 2-hybrid system, to identify proteins that specifically interact with the ligand-binding domain of rat thyroid hormone receptor-beta (THRB; 190160). They isolated HeLa cell cDNAs encoding several different thyroid hormone receptor (TR)-interacting proteins (TRIPs), including TRIP1 (PSMC5). TRIP1 strongly interacted with rat Thrb only in the presence of thyroid hormone. It also showed a ligand-dependent interaction with retinoid X receptor-alpha (RXRA; 180245), but did not interact with the glucocorticoid receptor (NR3C1; 138040) under any condition. The deduced 406-amino acid TRIP1 protein shares a high degree of sequence similarity with the yeast transcriptional coactivator SUG1. TRIP1 contains an AAA domain that is positioned toward the C terminus, which is typical in the AAA family. Lee et al. (1995) found that TRIP1 is ubiquitously expressed as an approximately 1.4-kb transcript.GENE FUNCTION
Lee et al. (1995) showed that TRIP1 can functionally substitute for Sug1 in yeast, and that both proteins interact in vitro with the TR and with the transcriptional activation domains of yeast GAL4 and herpes virus VP16.MAPPING
By PCR amplification of a partial sequence of PSMC5 in a panel of human monochromosomal cell hybrids, Hoyle et al. (1997) demonstrated that the PSMC5 gene is located on chromosome 17. By fluorescence in situ hybridization (FISH), they refined the localization to chromosome 17q24-q25. Tanahashi et al. (1998) mapped the PSMC5 gene to chromosome 17q23.1-q23.3 by FISH. ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 16, 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
Oct. 26, 2017: Protein entry updated
Automatic update: model status changed
March 15, 2016: Protein entry updated
Automatic update: OMIM entry 601681 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed