Search Results
Overview
| Uniprot ID | Q99436 |
|---|---|
| Protein Name | Proteasome subunit beta type-7 |
| Gene Name | PSMB7 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 249 | LGRYRCEKGTTAVLT |
| 72 | EGMVVADKNCSKIHF |
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, PSMB7 displays a trypsin-like activity
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:1904813 | ficolin-1-rich granule lumen |
| Cellular Component | GO:0016604 | nuclear body |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0000502 | proteasome complex |
| Cellular Component | GO:0005839 | proteasome core complex |
| Cellular Component | GO:0019774 | proteasome core complex, beta-subunit complex |
| Cellular Component | GO:0034515 | proteasome storage granule |
| Cellular Component | GO:0034774 | secretory granule lumen |
| Cellular Component | GO:0008021 | synaptic vesicle |
| Molecular Function | GO:0004175 | endopeptidase activity |
| Molecular Function | GO:0004298 | threonine-type endopeptidase activity |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0071357 | cellular response to type I interferon |
| Biological Process | GO:0006974 | DNA damage response |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0030317 | flagellated sperm motility |
| Biological Process | GO:0051321 | meiotic cell cycle |
| Biological Process | GO:0010498 | proteasomal protein catabolic process |
| Biological Process | GO:0010499 | proteasomal ubiquitin-independent protein catabolic process |
| Biological Process | GO:0043161 | proteasome-mediated ubiquitin-dependent protein catabolic process |
| Biological Process | GO:2000045 | regulation of G1/S transition of mitotic cell cycle |
| Biological Process | GO:0061136 | regulation of proteasomal protein catabolic process |
| Biological Process | GO:0006979 | response to oxidative stress |
| Biological Process | GO:0007283 | spermatogenesis |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.