| IED ID | IndEnz0002012982 |
| Enzyme Type ID | protease012982 |
| Protein Name |
Proteasome subunit beta type-5 EC 3.4.25.1 Macropain epsilon chain Multicatalytic endopeptidase complex epsilon chain Proteasome chain 6 Proteasome epsilon chain Proteasome subunit X |
| Gene Name | Psmb5 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MALASVLQRPMPVNQHGFFGLGGGADLLDLGPGSPGDGLSLAAPSWGVPEEPRIEMLHGTTTLAFKFLHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGTAFSVGSGSVYAYGVMDRGYSYDLKVEEAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHDKYSSVSVP |
| Enzyme Length | 264 |
| Uniprot Accession Number | O55234 |
| Absorption | |
| Active Site | ACT_SITE 60; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P28074 |
| Activity Regulation | |
| Binding Site | BINDING 108; /note=Bortezomib; via amide nitrogen; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; Evidence={ECO:0000250|UniProtKB:P28074}; |
| DNA Binding | |
| EC Number | 3.4.25.1 |
| Enzyme Function | FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity. {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:19183883, ECO:0000269|PubMed:22341445}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (13); Binding site (1); Chain (1); Helix (5); Propeptide (1); Sequence conflict (2); Turn (1) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Hydrolase;Nucleus;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen |
| Interact With | |
| Induction | INDUCTION: Up-regulated in embryonic fibroblasts and neuroblastoma cells by antioxidants through the Nrf2-ARE pathway (at protein level). Up-regulated by the antioxidant dithiolethione (D3T) in liver, small intestine and brain (at protein level). Down-regulated under lithium treatment. {ECO:0000269|PubMed:14612418, ECO:0000269|PubMed:16723119, ECO:0000269|PubMed:17521679, ECO:0000269|PubMed:18349697}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28074}. Nucleus {ECO:0000250|UniProtKB:P28074}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3UNB; 3UNE; |
| Mapped Pubmed ID | 11217851; 12466851; 14610273; 15198663; 16615898; 16857963; 17540904; 19455133; 20498273; 21267068; 21455682; 21565611; 22768135; 23029399; 23706739; 26116868; 26496610; 27768902; 29950673; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,532 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |