| + |
PSMD3 | form complex 
binding
|
26S Proteasome |
0.89 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263353 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMD2 | form complex
binding
|
26S Proteasome |
0.887 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263344 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ADRM1 | form complex
binding
|
26S Proteasome |
0.823 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263342 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAC1-PAC2 proteasomal chaperone complex | up-regulates quantity by stabilization 
binding
|
26S Proteasome |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281319 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18786393 |
The 26S proteasome mediates ubiquitin-dependent proteolysis in eukaryotic cells. A number of studies including very recent ones have revealed that assembly of its 20S catalytic core particle is an ordered process that involves several conserved proteasome assembly chaperones (PACs). Two heterodimeric chaperones, PAC1-PAC2 and PAC3-PAC4, promote the assembly of rings composed of seven alpha subunits. Subsequently, beta subunits join to form half-proteasome precursor complexes containing all but one of the 14 subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
26S Proteasome | down-regulates quantity 
destabilization
|
CTNNB1 |
0.404 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270947 |
|
|
Mus musculus |
C57MG Cell |
| pmid |
sentence |
| 9233789 |
Here we show that the ubiquitin-dependent proteolysis system is involved in the regulation of beta-catenin turnover. beta-catenin, but not E-cadherin, p120(cas) or alpha-catenin, becomes stabilized when proteasome-mediated proteolysis is inhibited and this leads to the accumulation of multi-ubiquitinated forms of beta-catenin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270340 |
|
|
Mus musculus |
C57MG Cell |
| pmid |
sentence |
| 9233789 |
Here we show that the ubiquitin-dependent proteolysis system is involved in the regulation of beta-catenin turnover. beta-catenin, but not E-cadherin, p120(cas) or alpha-catenin, becomes stabilized when proteasome-mediated proteolysis is inhibited and this leads to the accumulation of multi-ubiquitinated forms of beta-catenin. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
PSMC3 | form complex
binding
|
26S Proteasome |
0.871 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263369 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMD7 | form complex
binding
|
26S Proteasome |
0.902 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263349 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMD4 | form complex
binding
|
26S Proteasome |
0.898 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263347 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMB6 | form complex
binding
|
26S Proteasome |
0.844 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263361 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMD13 | form complex
binding
|
26S Proteasome |
0.881 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263348 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMC2 | form complex
binding
|
26S Proteasome |
0.872 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263374 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMD12 | form complex
binding
|
26S Proteasome |
0.914 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263352 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMA2 | form complex
binding
|
26S Proteasome |
0.845 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263367 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMB5 | form complex
binding
|
26S Proteasome |
0.852 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263357 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMB3 | form complex
binding
|
26S Proteasome |
0.859 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263359 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSME1 | up-regulates activity
binding
|
26S Proteasome |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275867 |
|
|
|
|
| pmid |
sentence |
| 35932807 |
While PA28alpha beta is responsible for promoting peptidase activity of proteasome to facilitate MHC-I antigen processing, but unable to promote protein degradation, PA28gamma is well-known to not only promote peptidase activity but also proteolytic activity of proteasome. |
|
| Publications: |
1 |
| + |
PSMA5 | form complex
binding
|
26S Proteasome |
0.863 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263364 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates activity
ubiquitination
|
26S Proteasome |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270946 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28559284 |
Through quantitative proteomics and reporter assays, we found that the UBE3AT485A protein ubiquitinates multiple proteasome subunits, reduces proteasome subunit abundance and activity, stabilizes nuclear β-catenin, and stimulates canonical Wnt signaling more effectively than wild-type UBE3A |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270339 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28559284 |
Through quantitative proteomics and reporter assays, we found that the UBE3AT485A protein ubiquitinates multiple proteasome subunits, reduces proteasome subunit abundance and activity, stabilizes nuclear β-catenin, and stimulates canonical Wnt signaling more effectively than wild-type UBE3A |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PSME2 | up-regulates activity
binding
|
26S Proteasome |
0.62 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275868 |
|
|
|
|
| pmid |
sentence |
| 35932807 |
While PA28alpha beta is responsible for promoting peptidase activity of proteasome to facilitate MHC-I antigen processing, but unable to promote protein degradation, PA28gamma is well-known to not only promote peptidase activity but also proteolytic activity of proteasome. |
|
| Publications: |
1 |
| + |
PSMD8 | form complex
binding
|
26S Proteasome |
0.911 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263345 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAC3-PAC4 proteasomal chaperone complex | up-regulates quantity by stabilization
binding
|
26S Proteasome |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281320 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18786393 |
The 26S proteasome mediates ubiquitin-dependent proteolysis in eukaryotic cells. A number of studies including very recent ones have revealed that assembly of its 20S catalytic core particle is an ordered process that involves several conserved proteasome assembly chaperones (PACs). Two heterodimeric chaperones, PAC1-PAC2 and PAC3-PAC4, promote the assembly of rings composed of seven alpha subunits. Subsequently, beta subunits join to form half-proteasome precursor complexes containing all but one of the 14 subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMC5 | form complex
binding
|
26S Proteasome |
0.876 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263372 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
26S Proteasome | down-regulates quantity
cleavage
|
Ubiquitinated-Viral_Protein |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267769 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15571818 |
The proteasome system is the central proteolytic system of the eukaryotic cell [1] and plays an important role in the generation of MHC-class I peptides. The enzyme complex responsible for the selectivity of intracellular protein degradation is the 26S proteasome that degrades poly-ubiquitinated substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SEM1 | form complex
binding
|
26S Proteasome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263343 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMB4 | form complex
binding
|
26S Proteasome |
0.884 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263355 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COP9 signalosome variant 2 | up-regulates activity
binding
|
26S Proteasome |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270794 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26497135 |
The COP9 signalosome (CSN) and the proteasomal LID are conserved macromolecular complexes composed of at least eight subunits with molecular weights of approximately 350 kDa. CSN and LID are part of the ubiquitin–proteasome pathway and cleave isopeptide linkages of lysine side chains on target proteins. CSN cleaves the isopeptide bond of ubiquitin-like protein Nedd8 from cullins, whereas the LID cleaves ubiquitin from target proteins sentenced for degradation. The evolutionary conserved ubiquitin proteasome pathway (UPP) mediates degradation of intracellular proteins in all eukaryotes. This essential process requires three protein complexes: E3 ubiquitin ligases as e.g., cullin-RING ligases (CRLs), CSN and the 26S proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMD6 | form complex
binding
|
26S Proteasome |
0.885 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263350 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMA7 | form complex
binding
|
26S Proteasome |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263365 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMA3 | form complex
binding
|
26S Proteasome |
0.845 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263362 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMA1 | form complex
binding
|
26S Proteasome |
0.853 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263363 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMC1 | form complex
binding
|
26S Proteasome |
0.865 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263373 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMB7 | form complex
binding
|
26S Proteasome |
0.854 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263360 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMA6 | form complex
binding
|
26S Proteasome |
0.824 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263368 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMD11 | form complex
binding
|
26S Proteasome |
0.898 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263351 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMA4 | form complex
binding
|
26S Proteasome |
0.833 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263366 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMC6 | form complex
binding
|
26S Proteasome |
0.849 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263370 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMB1 | form complex
binding
|
26S Proteasome |
0.862 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263356 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMD1 | form complex
binding
|
26S Proteasome |
0.901 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263354 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMB2 | form complex
binding
|
26S Proteasome |
0.886 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263358 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMD14 | form complex
binding
|
26S Proteasome |
0.893 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263346 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMF1 | down-regulates activity
binding
|
26S Proteasome |
0.517 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263341 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23622245 |
We identify the ADP-ribosyltransferase tankyrase (TNKS) and the 19S assembly chaperones dp27 and dS5b as direct binding partners of the proteasome regulator PI31. TNKS-mediated ADP-ribosylation of PI31 drastically reduces its affinity for 20S proteasome alpha subunits to relieve 20S repression by PI31. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMC4 | form complex
binding
|
26S Proteasome |
0.87 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263371 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
26S Proteasome | up-regulates quantity
cleavage
|
oligopeptide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267768 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15571818 |
The proteasome system is the central proteolytic system of the eukaryotic cell [1] and plays an important role in the generation of MHC-class I peptides. The enzyme complex responsible for the selectivity of intracellular protein degradation is the 26S proteasome that degrades poly-ubiquitinated substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSME3 | up-regulates activity
binding
|
26S Proteasome |
0.635 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275869 |
|
|
|
|
| pmid |
sentence |
| 35932807 |
While PA28alpha beta is responsible for promoting peptidase activity of proteasome to facilitate MHC-I antigen processing, but unable to promote protein degradation, PA28gamma is well-known to not only promote peptidase activity but also proteolytic activity of proteasome. |
|
| Publications: |
1 |
| + |
COP9 signalosome variant 1 | up-regulates activity
binding
|
26S Proteasome |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270795 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26497135 |
The COP9 signalosome (CSN) and the proteasomal LID are conserved macromolecular complexes composed of at least eight subunits with molecular weights of approximately 350 kDa. CSN and LID are part of the ubiquitin–proteasome pathway and cleave isopeptide linkages of lysine side chains on target proteins. CSN cleaves the isopeptide bond of ubiquitin-like protein Nedd8 from cullins, whereas the LID cleaves ubiquitin from target proteins sentenced for degradation. The evolutionary conserved ubiquitin proteasome pathway (UPP) mediates degradation of intracellular proteins in all eukaryotes. This essential process requires three protein complexes: E3 ubiquitin ligases as e.g., cullin-RING ligases (CRLs), CSN and the 26S proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
26S Proteasome | up-regulates 
|
Protein_degradation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263375 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29636472 |
The proteasome is a sophisticated ATP-dependent molecular machine responsible for protein degradation in all known eukaryotic cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ubiquitinated-Viral_Protein | up-regulates activity
binding
|
26S Proteasome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267767 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15571818 |
The proteasome system is the central proteolytic system of the eukaryotic cell [1] and plays an important role in the generation of MHC-class I peptides. The enzyme complex responsible for the selectivity of intracellular protein degradation is the 26S proteasome that degrades poly-ubiquitinated substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
26S Proteasome
CPX-5993