Proteins > Proteasome subunit beta type-11
Page last updated: 2024-08-07 12:27:56
Proteasome subunit beta type-11
A proteasome subunit beta type-11 that is encoded in the genome of human. [PRO:DNx, UniProtKB:A5LHX3]
Synonyms
EC 3.4.25.1;
Proteasome subunit beta-5t
Research
Bioassay Publications (17)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (17.65) | 29.6817 |
| 2010's | 7 (41.18) | 24.3611 |
| 2020's | 7 (41.18) | 2.80 |
Compounds (14)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| am 404 | Homo sapiens (human) | EC50 | 28.0000 | 1 | 1 |
Drugs with Other Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| chlorpromazine | Homo sapiens (human) | EC200 | 45.1250 | 4 | 4 |
Metabolism guided optimization of peptidomimetics as non-covalent proteasome inhibitors for cancer treatment.European journal of medicinal chemistry, , Apr-05, Volume: 233, 2022
Structure-Based Design of Selective LONP1 Inhibitors for Probing Journal of medicinal chemistry, , 04-22, Volume: 64, Issue:8, 2021
Covalent docking modelling-based discovery of tripeptidyl epoxyketone proteasome inhibitors composed of aliphatic-heterocycles.European journal of medicinal chemistry, , Feb-15, Volume: 164, 2019
Design, synthesis and biological evaluation of novel tripeptidyl epoxyketone derivatives constructed from β-amino acid as proteasome inhibitors.Bioorganic & medicinal chemistry, , Jun-01, Volume: 22, Issue:11, 2014
Structurally novel highly potent proteasome inhibitors created by the structure-based hybridization of nonpeptidic belactosin derivatives and peptide boronates.Journal of medicinal chemistry, , Mar-27, Volume: 57, Issue:6, 2014
Macrocyclic Immunoproteasome Inhibitors as a Potential Therapy for Alzheimer's Disease.Journal of medicinal chemistry, , 08-12, Volume: 64, Issue:15, 2021
Covalent docking modelling-based discovery of tripeptidyl epoxyketone proteasome inhibitors composed of aliphatic-heterocycles.European journal of medicinal chemistry, , Feb-15, Volume: 164, 2019
Reviewing Hit Discovery Literature for Difficult Targets: Glutathione Transferase Omega-1 as an Example.Journal of medicinal chemistry, , 09-13, Volume: 61, Issue:17, 2018
Design, synthesis and biological evaluation of novel tripeptidyl epoxyketone derivatives constructed from β-amino acid as proteasome inhibitors.Bioorganic & medicinal chemistry, , Jun-01, Volume: 22, Issue:11, 2014
Development of a new class of proteasome inhibitors with an epoxyketone warhead: Rational hybridization of non-peptidic belactosin derivatives and peptide epoxyketones.Bioorganic & medicinal chemistry, , Jun-15, Volume: 22, Issue:12, 2014
Structurally novel highly potent proteasome inhibitors created by the structure-based hybridization of nonpeptidic belactosin derivatives and peptide boronates.Journal of medicinal chemistry, , Mar-27, Volume: 57, Issue:6, 2014
Enables
This protein enables 4 target(s):
| Target | Category | Definition |
|---|
| threonine-type endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal peptide bonds in a polypeptide chain by a mechanism in which the hydroxyl group of a threonine residue at the active center acts as a nucleophile. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE, https://www.ebi.ac.uk/merops/about/glossary.shtml#ENDOPEPTIDASE] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| peptidase activity | molecular function | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. [GOC:jl, ISBN:0815332181] |
| endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. [http://merops.sanger.ac.uk/about/glossary.htm#ENDOPEPTIDASE] |
Located In
This protein is located in 1 target(s):
| Target | Category | Definition |
|---|
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
Active In
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|
| nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
Part Of
This protein is part of 1 target(s):
| Target | Category | Definition |
|---|
| proteasome core complex, beta-subunit complex | cellular component | The proteasome core subcomplex that constitutes the two inner rings of the proteasome core complex. An example of this component is found in Mus musculus. [GOC:jl, GOC:mtg_sensu, GOC:rb, PMID:10854779] |
Involved In
This protein is involved in 3 target(s):
| Target | Category | Definition |
|---|
| T cell differentiation in thymus | biological process | The process in which a precursor cell type acquires the specialized features of a T cell via a differentiation pathway dependent upon transit through the thymus. [GOC:add, ISBN:0781735149] |
| CD8-positive, alpha-beta T cell differentiation | biological process | The process in which a relatively unspecialized T cell acquires specialized features of a mature CD8-positive, alpha-beta T cell. [ISBN:0781735149] |
| proteasome-mediated ubiquitin-dependent protein catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. [GOC:go_curators] |