Search Results
Overview
| Uniprot ID | Q16401 |
|---|---|
| Protein Name | 26S proteasome non-ATPase regulatory subunit 5 |
| Gene Name | PSMD5 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 147 | SVAKAAIKSLSRISL |
| 358 | KNAPVELKIRCLDAI |
Function
Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0022624 | proteasome accessory complex |
| Cellular Component | GO:0000502 | proteasome complex |
| Biological Process | GO:0070682 | proteasome regulatory particle assembly |
Reference
[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[2] 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.