Proteins > Proteasome subunit beta type-7
Page last updated: 2024-08-07 17:23:05
Proteasome subunit beta type-7
A proteasome subunit beta type-7 that is encoded in the genome of human. [PRO:DNx]
Synonyms
EC 3.4.25.1;
Macropain chain Z;
Multicatalytic endopeptidase complex chain Z;
Proteasome subunit Z
Research
Bioassay Publications (18)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (16.67) | 29.6817 |
| 2010's | 7 (38.89) | 24.3611 |
| 2020's | 8 (44.44) | 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 Optimization and Discovery of M3258, a Specific Inhibitor of the Immunoproteasome Subunit LMP7 (β5i).Journal of medicinal chemistry, , 07-22, Volume: 64, Issue:14, 2021
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
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
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
Macrocyclic Immunoproteasome Inhibitors as a Potential Therapy for Alzheimer's Disease.Journal of medicinal chemistry, , 08-12, Volume: 64, Issue:15, 2021
Structure-Based Optimization and Discovery of M3258, a Specific Inhibitor of the Immunoproteasome Subunit LMP7 (β5i).Journal of medicinal chemistry, , 07-22, Volume: 64, Issue:14, 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
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
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
Enables
This protein enables 3 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] |
| 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 7 target(s):
| Target | Category | Definition |
|---|
| extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
| 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] |
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| 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] |
| nuclear body | cellular component | Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins. [GOC:ma, PMID:10330182] |
| secretory granule lumen | cellular component | The volume enclosed by the membrane of a secretory granule. [GOC:rph] |
| ficolin-1-rich granule lumen | cellular component | Any membrane-enclosed lumen that is part of a ficolin-1-rich granule. [GO_REF:0000064, GOC:TermGenie, PMID:23650620] |
Active In
This protein is active in 3 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] |
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
| 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 3 target(s):
| Target | Category | Definition |
|---|
| proteasome complex | cellular component | A large multisubunit complex which catalyzes protein degradation, found in eukaryotes, archaea and some bacteria. In eukaryotes, this complex consists of the barrel shaped proteasome core complex and one or two associated proteins or complexes that act in regulating entry into or exit from the core. [GOC:rb, Wikipedia:Proteasome] |
| proteasome core complex | cellular component | A multisubunit barrel shaped endoprotease complex, which is the core of the proteasome complex. [GOC:rb, PMID:10806206] |
| 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 1 target(s):
| Target | Category | Definition |
|---|
| 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] |