Search Results
Overview
| Uniprot ID | P62195 |
|---|---|
| Protein Name | 26S proteasome regulatory subunit 8 |
| Gene Name | PSMC5 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 125 | NDSYTLHKILPNKVD |
| 55 | QRNELNAKVRLLREE |
| 88 | DKKKVLVKVHPEGKF |
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. PSMC5 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:0072562 | blood microparticle |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0031410 | cytoplasmic vesicle |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0031597 | cytosolic proteasome complex |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0016234 | inclusion body |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0031595 | nuclear proteasome complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| 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:0008021 | synaptic vesicle |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0140297 | DNA-binding transcription factor binding |
| Molecular Function | GO:0140296 | general transcription initiation factor binding |
| Molecular Function | GO:0036402 | proteasome-activating activity |
| Molecular Function | GO:0017025 | TBP-class protein binding |
| Molecular Function | GO:0031531 | thyrotropin-releasing hormone receptor binding |
| Molecular Function | GO:0008134 | transcription factor binding |
| Biological Process | GO:0071357 | cellular response to type I interferon |
| Biological Process | GO:0043069 | negative regulation of programmed cell death |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0090261 | positive regulation of inclusion body assembly |
| 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:0006357 | regulation of transcription by RNA polymerase II |
| Biological Process | GO:0006979 | response to oxidative stress |
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.