EC Number   |
Natural Substrates |
|---|
   3.4.25.1 | dihydrofolate reductase + H2O |
directly hydrolyzed by the 20S complex, without any previous ubiquitination. The degradation is increased under oxidative conditions. The folate metabolism may be impaired by an increased degradation of dihydrofolate reductase, mediated by the 20S proteasome |
| 3.4.25.1 | more |
proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites |
| 3.4.25.1 | more |
the chymotrypsin-like and trypsin-like activities, but not the peptidylglutamyl peptide hydrolyzing activity plays a key role in oocyte maturation |
| 3.4.25.1 | more |
the tobacco mosaic virus-induced RNP7 subunit may be involved in programmed cell death |
| 3.4.25.1 | more |
proteasome status in KG1a and U937 cells, overview |
| 3.4.25.1 | more |
the proteasome is a cylindrical, multicatalytic proteolytic machine with three peptidase activities, chymotryptic, tryptic and postglutamyl peptide hydrolytic |
| 3.4.25.1 | more |
three major proteolytic activities of the proteasome can be distinguished as trypsin-like, chymotrypsin-like, and peptidyl-glutamyl peptide hydrolase activities, which cleave peptide bonds on the carboxyl side of basic, hydrophobic, and acidic amino acid residues, respectively. The catalytic core of the 20S proteasome is a Thr residue, responsible for the catalytic cleavage of substrates through nucleophilic attack |
| 3.4.25.1 | more |
mass spectrometric analysis of proteasome interactions. Several proteasome-interacting proteins unique to synaptic 26S proteasomes, i.e. 14-3-3gamma, TAX1BP1, drebrin, SNAP-25, may modulate proteolysis in a synapse-specific manner. Three E3s, i.e. KCMF1, HUWE1, and UBE3A, and five DUBs, i.e. USP5, USP7, USP13, USP14, and UCH37, in association with synaptic proteasomes, which may help proteasomes function more efficiently, help determine specificity for certain types of conjugates, or insure the rapid elimination of ubiquitin chains released from the substrate |
| 3.4.25.1 | more |
several other proteins associate with the Arabidopsis thaliana proteasome, including the PBAC2 assembly chaperonin, the associated DSS1/Sem1/RPN15 protein, the deubiquitylating enzyme UBP16, and the alternative activator PA200, genetic analysis of PA200 in Arabidopsis, overview |
| 3.4.25.1 | PS1/gamma-secretase complex component + H2O |
gamma-secretase components are PS1, nicastrin, Pen-2, and Aph-1. Degradation of the complex components involves the proteasome, but regulation of their activity involves the PI3K/Akt pathway, overview. PS1/gamma-secretase is involved in the activation of phosphatidylinositol-3 kinase/Akt pathway, and is responsible for the intramembranous cleavage of various type-I membrane proteins. PS1/gamma-secretase is also deeply involved in the production of amyloid beta protein |
