Proteins > Proteasome subunit beta type-9
Page last updated: 2024-08-07 13:10:06
Proteasome subunit beta type-9
A proteasome subunit beta type-9 that is encoded in the genome of human. [PRO:DNx]
Synonyms
EC 3.4.25.1;
Low molecular mass protein 2;
Macropain chain 7;
Multicatalytic endopeptidase complex chain 7;
Proteasome chain 7;
Proteasome subunit beta-1i;
Really interesting new gene 12 protein
Research
Bioassay Publications (28)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (10.71) | 29.6817 |
| 2010's | 15 (53.57) | 24.3611 |
| 2020's | 10 (35.71) | 2.80 |
Compounds (16)
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
Exploration of novel macrocyclic dipeptide N-benzyl amides as proteasome inhibitors.European journal of medicinal chemistry, , Feb-15, Volume: 164, 2019
Immunoproteasome-selective inhibitors: An overview of recent developments as potential drugs for hematologic malignancies and autoimmune diseases.European journal of medicinal chemistry, , Nov-15, Volume: 182, 2019
Covalent docking modelling-based discovery of tripeptidyl epoxyketone proteasome inhibitors composed of aliphatic-heterocycles.European journal of medicinal chemistry, , Feb-15, Volume: 164, 2019
Target Validation and Identification of Novel Boronate Inhibitors of the Plasmodium falciparum Proteasome.Journal of medicinal chemistry, , 11-21, Volume: 61, Issue:22, 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
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
Macrocyclic Immunoproteasome Inhibitors as a Potential Therapy for Alzheimer's Disease.Journal of medicinal chemistry, , 08-12, Volume: 64, Issue:15, 2021
Development of Novel Epoxyketone-Based Proteasome Inhibitors as a Strategy To Overcome Cancer Resistance to Carfilzomib and Bortezomib.Journal of medicinal chemistry, , 05-09, Volume: 62, Issue:9, 2019
Immunoproteasome-selective inhibitors: An overview of recent developments as potential drugs for hematologic malignancies and autoimmune diseases.European journal of medicinal chemistry, , Nov-15, Volume: 182, 2019
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 peptide epoxyketones as selective immunoproteasome inhibitors.European journal of medicinal chemistry, , Oct-05, Volume: 221, 2021
LMP2 Inhibitors as a Potential Treatment for Alzheimer's Disease.Journal of medicinal chemistry, , 04-09, Volume: 63, Issue:7, 2020
Required Immunoproteasome Subunit Inhibition Profile for Anti-Inflammatory Efficacy and Clinical Candidate KZR-616 ((2 S,3 R)- N-(( S)-3-(Cyclopent-1-en-1-yl)-1-(( R)-2-methyloxiran-2-yl)-1-oxopropan-2-yl)-3-hydroxy-3-(4-methoxyphenyl)-2-(( S)-2-(2-morphoJournal of medicinal chemistry, , 12-27, Volume: 61, Issue:24, 2018
Structure-based design of human immuno- and constitutive proteasomes inhibitors.European journal of medicinal chemistry, , Feb-10, Volume: 145, 2018
Discovery of Highly Selective Inhibitors of the Immunoproteasome Low Molecular Mass Polypeptide 2 (LMP2) Subunit.ACS medicinal chemistry letters, , Apr-13, Volume: 8, Issue:4, 2017
Structure-based design of β1i or β5i specific inhibitors of human immunoproteasomes.Journal of medicinal chemistry, , Jul-24, Volume: 57, Issue:14, 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 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 3 target(s):
| Target | Category | Definition |
|---|
| 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] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
Active In
This protein is active in 2 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] |
| 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] |
Part Of
This protein is part of 4 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] |
| spermatoproteasome complex | cellular component | A proteasome specifically found in mammalian testis. Contains the proteasome activator PA200 in the regulatory particle, and beta1i, beta2i, beta5i and/or alpha4s in the core (20S) subunit. Beta1i, beta2i and beta5i are inducible catalytic subunits, closely related to beta1, beta2 and beta5. Alpha4s is a sperm-specific 20S subunit, but unlike other alternative 20S subunits alpha4s lies in the outer alpha-ring and lacks catalytic activity. [GOC:sp, PMID:23706739] |
Involved In
This protein is involved in 3 target(s):
| Target | Category | Definition |
|---|
| immune system process | biological process | Any process involved in the development or functioning of the immune system, an organismal system for calibrated responses to potential internal or invasive threats. [GO_REF:0000022, GOC:add] |
| regulation of cysteine-type endopeptidase activity | biological process | Any process that modulates the frequency, rate or extent of cysteine-type endopeptidase activity. [GOC:obol, GOC:yaf] |
| 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] |