Proteasome inhibitor PI31 subunit (PSMF1)

The protein contains 271 amino acids for an estimated molecular weight of 29817 Da.

 

Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28. (updated: April 1, 2015)

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.

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: 59%
Model score: 40

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VariantDescription
dbSNP:rs1803415
dbSNP:rs2235587

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 endopeptidase activity GO Logo
Negative regulation of G2/M transition of mitotic cell cycle GO Logo
Negative regulation of proteasomal protein catabolic process 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
Ubiquitin-dependent protein catabolic process GO Logo
Viral process GO Logo
Wnt signaling pathway, planar cell polarity pathway GO Logo
Subscribe to this protein entry history

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

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