3.4.25.1: proteasome endopeptidase complex
This is an abbreviated version!
For detailed information about proteasome endopeptidase complex, go to the full flat file.
Word Map on EC 3.4.25.1
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3.4.25.1
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bortezomib
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myeloma
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polyubiquitinated
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neurodegenerative
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misfolded
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lysosomal
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histone
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chymotrypsin-like
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ligases
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leukemia
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relapsed
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nf-kappab
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immunomodulatory
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parkinsonism
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lymphoma
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deacetylase
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ubiquitin-dependent
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alzheimer
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cyclins
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hematologic
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caspase
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histocompatibility
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proteostasis
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ubiquitin-like
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dexamethasone
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hsp90
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deubiquitinating
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ubiquitin-conjugating
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calpains
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autologous
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inclusions
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incurable
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cyclin-dependent
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short-lived
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mantle
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trypsin-like
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progression-free
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thalidomide
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ubiquitin-mediated
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polyglutamine
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ikappab
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mcl-1
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multisubunit
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mdm2
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ikappabalpha
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parkin
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rituximab
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alpha-synuclein
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single-agent
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p27kip1
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synthesis
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medicine
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degradation
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analysis
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drug development
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biotechnology
- 3.4.25.1
- bortezomib
- myeloma
-
polyubiquitinated
- neurodegenerative
-
misfolded
- lysosomal
- histone
-
chymotrypsin-like
- ligases
- leukemia
-
relapsed
- nf-kappab
-
immunomodulatory
- parkinsonism
- lymphoma
- deacetylase
-
ubiquitin-dependent
- alzheimer
- cyclins
- hematologic
-
caspase
-
histocompatibility
-
proteostasis
-
ubiquitin-like
- dexamethasone
- hsp90
-
deubiquitinating
-
ubiquitin-conjugating
- calpains
-
autologous
- inclusions
-
incurable
-
cyclin-dependent
-
short-lived
-
mantle
-
trypsin-like
-
progression-free
- thalidomide
-
ubiquitin-mediated
-
polyglutamine
- ikappab
- mcl-1
-
multisubunit
- mdm2
- ikappabalpha
- parkin
- rituximab
- alpha-synuclein
-
single-agent
- p27kip1
- synthesis
- medicine
- degradation
- analysis
- drug development
- biotechnology
Reaction
cleavage of peptide bonds with very broad specificity =
Synonyms
20 S proteasome, 206 proteasome, 20S CP, 20S protease core, 20S proteasome, 26 S proteasome, 26S protease, 26S proteasome, 26S proteasome complex, 27 kDa prosomal protein, 30 kDa prosomal protein, beta1-PF1404, c20S, Component Y8, constitutive proteasome 20S, EC 3.4.22.21, EC 3.4.24.5, EC 3.4.99.46, GPRO-28, HsBPROS26, HSN3, i20S, immunoproteasome 20S, ingensin, KIPase, large multicatalytic protease, macropain, multi-subunit protease complex, multicatalytic endopeptidase complex, Multicatalytic endopeptidase complex C7, multicatalytic protease, multicatalytic proteinase, p27K, PROS-27, PROS-30, PROS-Dm25, PROS-Dm28.1, PROS-Dm29, PROS-Dm35, Pros26.4, prosome, proteasome, proteasome 19S, proteasome 20S, Proteasome component C13, Proteasome component C2, Proteasome component C3, Proteasome component C5, Proteasome component C8, Proteasome component C9, Proteasome component DD4, Proteasome component DD5, Proteasome component pts1, proteasome subunit alpha-type 7-like, PSMA5, Psma8, RING12 protein, RN3, Scl1, SCL1 suppressor protein, SFRICE_003436, T20S, TAS-F22/FAFP98, TAS-G64, TCPR29, tricorn protease, tricorn proteinase, XC3
ECTree
3.4.25.1 proteasome endopeptidase complexAdvanced search results
results (
results (Subunits
Subunits on EC 3.4.25.1 - proteasome endopeptidase complex
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
heteromer
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the 20S proteasomes are cylinder-shaped heteromeric dimers with a subunit configuration of alpha7, beta7, beta7, alpha7
heterooctacosamer
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14 * 27400 + 14 * 21800, surface induced dissociation mass spectrometry
multimer
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7 * ? (20S alpha-type subunits) + 10 * ? (20S beta-type subnits) + 16 * ? (19S ATPase subunits) + 14 * ? (19S non-ATPase subunits)
octadecamer
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
oligomer
14 * alpha + 14 * beta, the similarity of the derived amino acid sequences of 233 (alpha subunit) and 211 (beta subunit) residues, respectively, indicates that they arose from a common ancestral gene. The alpha-subunits have regulatory and targeting functions, while the beta-subunits carry the active sites
polymer
tetradecamer
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
additional information
polymer
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alpha, beta, 14 * 24000 + 14 * 22000, SDS-PAGE, alpha7,beta7,beta7,alpha7 in the 20S proteasome
polymer
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alpha, beta, 14 * 24000 + 14 * 22000, SDS-PAGE, alpha7,beta7,beta7,alpha7 in the 20S proteasome
additional information
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AE3 encodes the 26S proteasome lid subunit RPN8a that plays a role in specifying leaf adaxial identity
additional information
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the 26 S proteasome is composed of two subparticles, the 20S core protease that compartmentalizes the protease active sites and the 19S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. The 2.5-MDa core protease-regulatory particle complex is actually a heterogeneous set of particles assembled with paralogous pairs for most subunits, mass spectrometric analysis of the complex, overview
additional information
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the 26 S proteasome is composed of two subparticles, the 20S core protease that compartmentalizes the protease active sites and the 19S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. The 2.5-MDa core protease-regulatory particle complex is actually a heterogeneous set of particles assembled with paralogous pairs for most subunits, mass spectrometric analysis of the complex, overview
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additional information
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thre proteasomal subunits are identified as alpha6/Pre5, alpha3/Y13 and alpha5/Pup2 by internal sequencing of tryptic fragments. A fourth subunit is identified as alpha7/Prs1 by immunorecognition with a monoclonal antibody specific for C8
additional information
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the tobacco mosaic virus-induced RNP7 subunit may be involved in programmed cell death
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings
additional information
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in the catalytic core, the 20S proteasome, the beta1, beta2 and beta5 subunits show peptidylglutamyl peptide hydrolyzing, trypsin-like and chymotrypsin-like activities, respectively. By INF-gamma and TNFalpha stimulus, these subunits are replaced by their counterparts LMP2, MECL-1 and LMP7, defined inducible subunits, thus originating the immunoproteasome
additional information
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in the 20S proteasome, the 20S core particle is composed of 28 subunits arranged in four stacked heptameric rings, alpha7beta7beta7alpha7, forming a symmetrical barrel-shaped structure. Determination of the subunits in proteasomal analysis, method optimization, overview
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The eukaryotic alpha and beta rings are each composed of seven distinct homologous subunits, which form a pseudo 7fold symmetrical structure of alpha1-7beta1-7beta1-7alpha1-7, with proteolytic active sites located at the N-termini of three subunits, beta1, beta2 and beta5, of each beta-ring. Another form of proteasome, called immunoproteasome, in which three beta-subunits of the normal 20S, beta1, beta2, beta5 are replaced by three IFN-gamma induced beta-subunits, beta1i, beta2i, beta5i. ATPase induced gate opening in the 20S CP
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The archaeal alpha and beta rings are each composed of seven identical subunits, thus the archaeal 20S CP has true D7-symmetry
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings
additional information
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around 15 subunits from 20000-115000, SDS-PAGE
additional information
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x * 31000, x * 29000, x * 25000, x * 24000, tricine-SDS-PAGE
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The eukaryotic alpha and beta rings are each composed of seven distinct homologous subunits, which form a pseudo 7fold symmetrical structure of alpha17beta17beta17alpha17, with proteolytic active sites located at the N-termini of three subunits, beta1, beta2 and beta5, of each beta-ring
additional information
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on 1-D SDS-PAGE five to seven bands of molecular weight range 20 to 30 kDa that prove to be entirely proteasome subunits, when the constituents are separated by 2-D SDS-PAGE, an unexpectedly large number of subunits is observed with at least 46 spots present versus an absolute minimum of 14 possible for a 20S core
additional information
presence of 7 alpha-type and 7 beta-type subunits in the 20S complex
additional information
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presence of 7 alpha-type and 7 beta-type subunits in the 20S complex
additional information
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a ladder of 22200-33500 Da bands detected on SDS-PAGE
additional information
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alpha, beta x * 27000 + x * 25000, SDS-PAGE
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The archaeal alpha and beta rings are each composed of seven identical subunits, thus the archaeal 20S CP has true D7-symmetry
