Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes.
Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes, ubiquitin, and protein substrates of proteasome.
Protein-protein interactions among human 20S proteasome subunits and proteassemblin.
A protein interaction framework for human mRNA degradation.
Mass spectrometric characterization of the affinity-purified human 26S proteasome complex.
Regulation of CD8+ T cell development by thymus-specific proteasomes.
The proteasome maturation protein POMP facilitates major steps of 20S proteasome formation at the endoplasmic reticulum.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Recognition and processing of ubiquitin-protein conjugates by the proteasome.
Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress.
Proteomic characterization of the human sperm nucleus.
Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis.
Proteasome activators, PA28γ and PA200, play indispensable roles in male fertility.
The inhibition mechanism of human 20S proteasomes enables next-generation inhibitor design.
Architecture of the human interactome defines protein communities and disease networks.
Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome.
Regulation of Proteasome Activity by (Post-)transcriptional Mechanisms.
Characterization of Fully Recombinant Human 20S and 20S-PA200 Proteasome Complexes.
Cryo-EM structures of the human PA200 and PA200-20S complex reveal regulation of proteasome gate opening and two PA200 apertures.
A reference map of the human binary protein interactome.
Role of oncogenic REGγ in cancer.
Proteasome in action: substrate degradation by the 26S proteasome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag.
AKIRIN2 controls the nuclear import of proteasomes in vertebrates.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Proteasome complexes experience profound structural and functional rearrangements throughout mammalian spermatogenesis.
Proteasome activator 28γ (PA28γ) allosterically activates trypsin-like proteolysis by binding to the α-ring of the 20S proteasome.
Structural insights into the human PA28-20S proteasome enabled by efficient tagging and purification of endogenous proteins.
An abundance of free regulatory (19S) proteasome particles regulates neuronal synapses.
Multimodal cell maps as a foundation for structural and functional genomics.
Structure and functions of the 20S and 26S proteasomes.
Ubiquitinated IkB is degraded
Proteasome proteolyzes ub-HIF-alpha
Proteasomal clevage of exogenous antigen (26S proteasome catalyst)
Ubiquitinated DVL is degraded by the proteasome
Degradation of multiubiquitinated Cdh1
Degradation of multiubiquitinated cell cycle proteins
Degradation of multiubiquitinated Securin
SCF-mediated degradation of Emi1
Degradation multiubiquitinated Cyclin A
Degradation of ubiquitinated CD4
Proteosome-mediated degradation of APOBEC3G
Degradation of ubiquitinated p27/p21 by the 26S proteasome
APC/C:Cdh1-mediated degradation of Skp2
Ubiquitinated and phosphorylated IKBA binds to and is degraded by the proteasome complex
Degradation of ubiquitinated beta catenin by the proteasome
Proteasome mediated degradation of COP1
26S proteosome degrades ODC holoenzyme complex
Ub-RibC-AXIN is degraded by the proteasome
AUF1:mRNA complex is degraded
PRICKLE1 is degraded by the proteasome
Ubiquitinated AXIN is degraded by the proteasome
Ubiquitinated DVL1 is degraded by the proteasome
Hh C-terminal fragments are degraded by the proteasome
processing defective Hh variants are degraded by the proteasome
26S proteasome processes K48PolyUb-K21,22-p-S32,36-IkBA:NF-kB complex to form NF-kB complex
26S proteasome processes p-7S-p100:RELB to form p52:RELB
GLI3 is partially degraded by the proteasome to yield the GLI3 repressor
GLI1 is degraded by the proteasome after ubiquitination by beta-TrCP
GLI1 is degraded by the proteasome after ubiquitination by ITCH
GLI2,3 are degraded by the proteasome
ub-GLI is degraded by the proteasome
NF1 is degraded by the proteasome
ADRM1:26S proteaseome binds UCHL5
ADRM1 binds 26S proteasome
Protesomal degradation of K48polyUb-TRAF3
26Sproteasome degrades K48polyUb-NIK
MAPK6 is degraded by the 26S proteasome
ADRM1:26S proteaseome binds USP14
Ubiquitinated geminin is degraded by the proteasome
Ubiquitinated Orc1 is degraded by the proteasome
Ubiquitinated Cdc6 is degraded by the proteasome
Proteolytic degradation of ubiquitinated-Cdc25A
Proteasome mediated degradation of Cyclin D1
Proteasome degrades polyubiquitinated PTEN
GTSE1 facilitates proteasome-mediated degradation of TP53
Proteasome degrades AURKA ubiquitinated by SCF-FBXL7
Proteasome-mediated degradation of PolyUb-FBXL7
misfolded CFTR is degraded by the 26S proteasome
CFTR F508del is degraded by the 26S proteasome
26S proteasome degrades Ub-NFE2L2
26S proteasome degrades PolyUb-RUNX2
Polyubiquitinated RUNX3 is degraded by the proteasome
NEDD8 and UBD bind NUB1 and the 26S proteasome
26S- and NUB1-mediated degradation of NEDD8, UBD and their conjugates
26S proteasome degrades TP73 polyubiquitinated by ITCH
26S proteasome degrades HIFalpha
ub UBXN7 is degraded by the 26S proteasome
Ub,pS335,S338,T NFE2L2 is degraded
Proteasome-dependent degradation of ubiquitinated CDH1
Proteasomal cleavage of substrate
Formation of the inner ring of the 20S core particle of the 26S proteasome
Formation of the preholoproteasome
Maturation of the canonical 20S core particle
Formation of the 26S proteasome
Formation of the PA28-alpha-beta-20S proteasome
Formation of the PA28gamma-20S proteasome
Antigen processing: Ub, ATP-independent proteasomal degradation
Proteasomal cleavage of intracellular substrate (PA28-alpha-beta-20S proteasome catalyst)
Ubiquitinated CD274 is degraded by the 26S proteasome
SPOP-mediated degradation of CD274 by 26S Proteosome
Proteasomal degradation of polyUb-p-S195-CD274
Proteolysis of K48polyUb-K,p-S-PER1,2,3
The proteasome degrades the K48-polyubiquitinated alanine-tailed nascent peptide
Proteasome mediated degradation of PAK-2p34
Gli2is degraded by the proteasome
Proteasome degrades SAX-3 ubiquitinated by EBAX-1
Proteasome degrades ubiquitinated mouse NICD4
Molecular architecture and assembly of the eukaryotic proteasome.
Human 20S proteasome activity towards fluorogenic peptides of various chain lengths.
Molecular basis of bortezomib resistance: proteasome subunit beta5 (PSMB5) gene mutation and overexpression of PSMB5 protein.
Point mutation of the proteasome beta5 subunit gene is an important mechanism of bortezomib resistance in bortezomib-selected variants of Jurkat T cell lymphoblastic lymphoma/leukemia line.
Falcon deep research on PSMB5 (Edison Scientific Literature)
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PSMB5 encodes the constitutive catalytic beta5 subunit of the 20S proteasome core particle, one of the three catalytically active beta subunits (beta1, beta2, beta5) and part of the 26S proteasome; it provides the chymotrypsin-like (CT-L) activity.
"The target gene PSMB5 (proteasome 20S subunit beta 5) encodes the constitutive catalytic β5 subunit of the 20S proteasome core particle (CP), which forms the proteolytic core of the 26S proteasome. In the standard/constitutive proteasome, β5 is one of three catalytically active β-subunits (β1, β2, β5) and is responsible for the chymotrypsin-like (CT-L) activity."
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The CT-L activity of beta5 preferentially cleaves peptide bonds after hydrophobic residues.
"β5 (PSMB5) is assigned the CT-L activity, which preferentially cleaves peptide bonds after hydrophobic residues."
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Catalysis uses an N-terminal threonine (Thr1) nucleophile mechanism typical of Ntn hydrolases; Thr1 attacks the scissile peptide bond to form an acyl-enzyme intermediate that is then hydrolyzed.
"Proteasome catalytic β subunits operate via an N-terminal nucleophile mechanism centered on the N-terminal threonine (Thr1). Mechanistically, Thr1 attacks the scissile peptide bond carbonyl to form an acyl-enzyme intermediate, which is subsequently hydrolyzed to release products and regenerate the catalytic threonine."
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Catalytic beta subunits are made with N-terminal propeptides removed by autolysis between a glycine and a threonine residue, exposing the mature Thr1; beta5 propeptide also contributes to 20S assembly.
"Catalytic β subunits are synthesized with N-terminal propeptides that are removed by autolysis after correct assembly. The propeptides are described as being autolyzed between a glycine residue and a threonine residue, yielding the mature catalytic subunit with Thr1 at the N-terminus; β5 propeptides also contribute to proteasome assembly."
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The beta5 active sites are buried inside the central catalytic chamber of the barrel-shaped 20S core (alpha-beta-beta-alpha arrangement); the 26S proteasome degrades ubiquitin-tagged cytosolic proteins with access controlled by regulatory caps and gates.
"The active sites are located on the inner surface of the 20S core, sequestered in the central catalytic chamber; access is controlled by α-ring gating and by association with regulatory particles such as the 19S cap (forming the 26S proteasome)."
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Proteasome proteolysis contributes to MHC class I antigen presentation; proteasome subtype composition shifts cleavage preferences and the peptide repertoire loaded onto MHC I.
"proteasome proteolysis contributes to MHC class I antigen presentation by generating peptides that can be transported into the ER and loaded onto MHC I. Proteasome subtype composition (standard vs immunoproteasome and intermediates) shifts cleavage preferences."
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PSMB5/beta5 is the dominant catalytic drug target; clinically successful proteasome inhibitors (bortezomib, carfilzomib, ixazomib) largely exploit the beta5/CT-L site, and resistance includes beta5 active-site mutations (A49T, A50V, C52F) and non-mutational rewiring such as PSMB5 upregulation and compensatory autophagy.
"Clinically successful proteasome inhibitors largely exploit the β5/CT-L site... PI resistance can also arise through PSMB5 upregulation/subunit replacement and compensatory autophagy."