Search Results
Overview
| Uniprot ID | P55036 |
|---|---|
| Protein Name | 26S proteasome non-ATPase regulatory subunit 4 |
| Gene Name | PSMD4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 365 | SLASQATKDGKKDKK |
| 40 | VNIVCHSKTRSNPEN |
| 74 | DTGRILSKLHTVQPK |
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. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. Displays a preferred selectivity for longer polyubiquitin chains
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005634 | nucleus |
| 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:0042802 | identical protein binding |
| Molecular Function | GO:0060090 | molecular adaptor activity |
| Molecular Function | GO:0031593 | polyubiquitin modification-dependent protein binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0071357 | cellular response to type I interferon |
| 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 |
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] 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.