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Overview

Uniprot IDP08865
Protein NameSmall ribosomal subunit protein uS2
Gene NameRPSA
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
166 IAIPCNNKGAHSVGL
220 EEQAAAEKAVTKEEF
42 EQYIYKRKSDGIYII
52 GIYIINLKRTWEKLL
57 NLKRTWEKLLLAARA
89 TGQRAVLKFAAATGA

Function

Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA

Protein Sequence

10 MSGALDVLQM 20 KEEDVLKFLA 30 AGTHLGGTNL 40 DFQMEQYIYK 50 RKSDGIYIIN 60 LKRTWEKLLL 70 AARAIVAIEN 80 PADVSVISSR 90 NTGQRAVLKF 100 AAATGATPIA 110 GRFTPGTFTN 120 QIQAAFREPR 130 LLVVTDPRAD 140 HQPLTEASYV 150 NLPTIALCNT 160 DSPLRYVDIA 170 IPCNNKGAHS 180 VGLMWWMLAR 190 EVLRMRGTIS 200 REHPWEVMPD 210 LYFYRDPEEI 220 EKEEQAAAEK 230 AVTKEEFQGE 240 WTAPAPEFTA 250 TQPEVADWSE 260 GVQVPSVPIQ 270 QFPTEDWSAQ 280 PATEDWSAAP 290 TAQATEWVGA TTDWS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0022626 cytosolic ribosome
Cellular Component GO:0022627 cytosolic small ribosomal subunit
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0043236 laminin binding
Molecular Function GO:0005055 laminin receptor activity
Molecular Function GO:0043022 ribosome binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003735 structural constituent of ribosome
Molecular Function GO:0001618 virus receptor activity
Biological Process GO:0140374 antiviral innate immune response
Biological Process GO:0002181 cytoplasmic translation
Biological Process GO:0000028 ribosomal small subunit assembly
Biological Process GO:0006412 translation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] 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.

[5] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[6] 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.

[7] 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.

[8] 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.