Search Results

Overview

Uniprot IDP61247
Protein NameSmall ribosomal subunit protein eS1
Gene NameRPS3A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
144 LFCVGFTKKRNNQIR
145 FCVGFTKKRNNQIRK
152 KRNNQIRKTSYAQHQ
167 QVRQIRKKMMEIMTR
182 EVQTNDLKEVVNKLI
187 DLKEVVNKLIPDSIG
20 GKKGAKKKVVDPFSK
222 VKMLKKPKFELGKLM
240 GEGSSSGKATGDETG
249 TGDETGAKVERADGY
27 KVVDPFSKKDWYDVK
28 VVDPFSKKDWYDVKA
46 FNIRNIGKTLVTRTQ
56 VTRTQGTKIASDGLK
63 KIASDGLKGRVFEVS
85 EVAFRKFKLITEDVQ
94 ITEDVQGKNCLTNFH

Function

Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). May play a role during erythropoiesis through regulation of transcription factor DDIT3 (By similarity)

Protein Sequence

10 MAVGKNKRLT 20 KGGKKGAKKK 30 VVDPFSKKDW 40 YDVKAPAMFN 50 IRNIGKTLVT 60 RTQGTKIASD 70 GLKGRVFEVS 80 LADLQNDEVA 90 FRKFKLITED 100 VQGKNCLTNF 110 HGMDLTRDKM 120 CSMVKKWQTM 130 IEAHVDVKTT 140 DGYLLRLFCV 150 GFTKKRNNQI 160 RKTSYAQHQQ 170 VRQIRKKMME 180 IMTREVQTND 190 LKEVVNKLIP 200 DSIGKDIEKA 210 CQSIYPLHDV 220 FVRKVKMLKK 230 PKFELGKLME 240 LHGEGSSSGK 250 ATGDETGAKV 260 ERADGYEPPV QESV

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:0005783 endoplasmic reticulum
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0032040 small-subunit processome
Molecular Function GO:0048027 mRNA 5'-UTR binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003735 structural constituent of ribosome
Biological Process GO:0030154 cell differentiation
Biological Process GO:0002181 cytoplasmic translation
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0042274 ribosomal small subunit biogenesis
Biological Process GO:0006412 translation
Biological Process GO:0006413 translational initiation

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] 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.

[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.