Search Results
Overview
| Uniprot ID | P35998 |
|---|---|
| Protein Name | 26S proteasome regulatory subunit 7 |
| Gene Name | PSMC2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 100 | LQVARCTKIINADSE |
| 116 | PKYIINVKQFAKFVV |
| 402 | FAIRARRKIATEKDF |
| 422 | KVIKSYAKFSATPRY |
Function
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC2 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0036464 | cytoplasmic ribonucleoprotein granule |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:1904813 | ficolin-1-rich granule lumen |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0000932 | P-body |
| Cellular Component | GO:0022624 | proteasome accessory complex |
| Cellular Component | GO:0000502 | proteasome complex |
| Cellular Component | GO:0008540 | proteasome regulatory particle, base subcomplex |
| Cellular Component | GO:0034774 | secretory granule lumen |
| Cellular Component | GO:0008021 | synaptic vesicle |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0036402 | proteasome-activating activity |
| Biological Process | GO:0071357 | cellular response to type I interferon |
| Biological Process | GO:0001649 | osteoblast differentiation |
| Biological Process | GO:1901800 | positive regulation of proteasomal protein catabolic process |
| Biological Process | GO:0010498 | proteasomal protein catabolic process |
| Biological Process | GO:0043161 | proteasome-mediated ubiquitin-dependent protein catabolic process |
| Biological Process | GO:0061136 | regulation of proteasomal protein catabolic process |
| Biological Process | GO:0006979 | response to oxidative stress |
| Biological Process | GO:0006511 | ubiquitin-dependent protein catabolic process |
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] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[4] 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.