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Overview

Uniprot IDP25787
Protein NameProteasome subunit alpha type-2
Gene NamePSMA2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
50 GVVLATEKKQKSILY
53 LATEKKQKSILYDER

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)

Protein Sequence

10 MAERGYSFSL 20 TTFSPSGKLV 30 QIEYALAAVA 40 GGAPSVGIKA 50 ANGVVLATEK 60 KQKSILYDER 70 SVHKVEPITK 80 HIGLVYSGMG 90 PDYRVLVHRA 100 RKLAQQYYLV 110 YQEPIPTAQL 120 VQRVASVMQE 130 YTQSGGVRPF 140 GVSLLICGWN 150 EGRPYLFQSD 160 PSGAYFAWKA 170 TAMGKNYVNG 180 KTFLEKRYNE 190 DLELEDAIHT 200 AILTLKESFE 210 GQMTEDNIEV 220 GICNEAGFRR 230 LTPTEVKDYL AAIA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
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:0009615 response to virus
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
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0000932 P-body
Cellular Component GO:0000502 proteasome complex
Cellular Component GO:0005839 proteasome core complex
Cellular Component GO:0019773 proteasome core complex, alpha-subunit complex
Cellular Component GO:0034515 proteasome storage granule
Cellular Component GO:0034774 secretory granule lumen
Cellular Component GO:0008021 synaptic vesicle
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

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] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.