26S proteasome non-ATPase regulatory subunit 7 (PSMD7)

The protein contains 324 amino acids for an estimated molecular weight of 37025 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. (updated: Dec. 20, 2017)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. 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.
  3. 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.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. 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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 99%
Model score: 0

(right-click above to access to more options from the contextual menu)

Biological Process

Anaphase-promoting complex-dependent catabolic process GO Logo
Antigen processing and presentation of exogenous peptide antigen via MHC class I GO Logo
Antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent GO Logo
Antigen processing and presentation of peptide antigen via MHC class I GO Logo
Apoptotic process GO Logo
Cellular nitrogen compound metabolic process GO Logo
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest GO Logo
Fc-epsilon receptor signaling pathway GO Logo
G1/S transition of mitotic cell cycle GO Logo
Gene expression GO Logo
Interleukin-1-mediated signaling pathway GO Logo
MAPK cascade GO Logo
Mitotic cell cycle GO Logo
Negative regulation of apoptotic process GO Logo
Negative regulation of canonical Wnt signaling pathway GO Logo
Negative regulation of G2/M transition of mitotic cell cycle GO Logo
Neutrophil degranulation GO Logo
NIK/NF-kappaB signaling GO Logo
Obsolete negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle GO Logo
Obsolete positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition GO Logo
Obsolete regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle GO Logo
Positive regulation of canonical Wnt signaling pathway GO Logo
Post-translational protein modification GO Logo
Pre-replicative complex assembly GO Logo
Proteasome-mediated ubiquitin-dependent protein catabolic process GO Logo
Protein deubiquitination GO Logo
Protein polyubiquitination GO Logo
Regulation of apoptotic process GO Logo
Regulation of cellular amino acid metabolic process GO Logo
Regulation of hematopoietic stem cell differentiation GO Logo
Regulation of mitotic cell cycle phase transition GO Logo
Regulation of mRNA stability GO Logo
Regulation of transcription from RNA polymerase II promoter in response to hypoxia GO Logo
SCF-dependent proteasomal ubiquitin-dependent protein catabolic process GO Logo
Small molecule metabolic process GO Logo
Stimulatory C-type lectin receptor signaling pathway GO Logo
T cell receptor signaling pathway GO Logo
Transmembrane transport GO Logo
Tumor necrosis factor-mediated signaling pathway GO Logo
Viral process GO Logo
Wnt signaling pathway, planar cell polarity pathway GO Logo

The reference OMIM entry for this protein is 157970

Proteasome 26s subunit, non-atpase, 7; psmd7
Moloney leukemia virus 34 proviral integration site gene, mouse, homolog of; mov34
Rpn8

CLONING

Gridley et al. (1990) stated that the Mov34 mutation is a recessive embryonic lethal mutation caused by retroviral integration into the murine germline. This integration disrupts a transcription unit, designated Mov34, that appears to encode a novel protein. Gridley et al. (1990) found that the Mov34 transcript is conserved in evolution. A Drosophila homolog encodes a protein with 62% amino acid identity to the murine protein. Gridley et al. (1991) cloned a full-length cDNA encoding mouse Mov34. The deduced 321-amino acid protein has a calculated molecular mass of 36 kD.

MAPPING

Gridley et al. (1990) found that the Mov34 gene is located on mouse chromosome 8. By Southern analysis of rodent/human cell hybrids and by in situ hybridization, they mapped the human homolog of Mov34 to chromosome 16q23-q24. An evolutionarily conserved syntenic relationship exists between these 2 regions. Mouse chromosome 8 also contains 'oligosyndactyly' (os), another recessive lethal mutation. By genetic studies, Gridley et al. (1990) ruled out the possibility that os resides at the same locus as the Mov34 integration. ... More on the omim web site

Subscribe to this protein entry history

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 157970 was added.

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed