Search Results
Overview
| Uniprot ID | P25788 |
|---|---|
| Protein Name | Proteasome subunit alpha type-3 |
| Gene Name | PSMA3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 110 | FGYNIPLKHLADRVA |
| 183 | EIEKLQMKEMTCRDI |
| 206 | YIVHDEVKDKAFELE |
| 208 | VHDEVKDKAFELELS |
| 43 | TAIGIRCKDGVVFGV |
| 57 | VEKLVLSKLYEEGSN |
| 65 | LYEEGSNKRLFNVDR |
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). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005839 | proteasome core complex |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0000502 | proteasome complex |
| Cellular Component | GO:0019773 | proteasome core complex, alpha-subunit complex |
| Cellular Component | GO:0034515 | proteasome storage granule |
| Cellular Component | GO:0008021 | synaptic vesicle |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0043374 | CD8-positive, alpha-beta T cell differentiation |
| Biological Process | GO:0160165 | CD8-positive, alpha-beta T cell homeostasis |
| 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:0002376 | immune system process |
| Biological Process | GO:0051321 | meiotic cell cycle |
| Biological Process | GO:0045590 | negative regulation of regulatory T cell differentiation |
| Biological Process | GO:0032743 | positive regulation of interleukin-2 production |
| Biological Process | GO:0032760 | positive regulation of tumor necrosis factor production |
| Biological Process | GO:0032729 | positive regulation of type II interferon production |
| 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:0034341 | response to type II interferon |
| Biological Process | GO:0007283 | spermatogenesis |
| Biological Process | GO:0045063 | T-helper 1 cell differentiation |
| Biological Process | GO:0072539 | T-helper 17 cell differentiation |
| Biological Process | GO:0045061 | thymic T cell selection |
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] 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.
[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[4] 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.
[5] 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.