Search Results

Overview

Uniprot IDP39023
Protein NameLarge ribosomal subunit protein uL3
Gene NameRPL3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
103 PRGLRTFKTVFAEHI
115 EHISDECKRRFYKNW
120 ECKRRFYKNWHKSKK
144 WQDEDGKKQLEKDFS
155 KDFSSMKKYCQVIRV
177 LLPLRQKKAHLMEIQ
229 VTKGKGYKGVTSRWH
250 KTHRGLRKVACIGAW
286 EINKKIYKIGQGYLI
294 IGQGYLIKDGKLIKN
300 IKDGKLIKNNASTDY
349 KRVLTLRKSLLVQTK
356 KSLLVQTKRRALEKI
362 TKRRALEKIDLKFID
366 ALEKIDLKFIDTTSK
373 KFIDTTSKFGHGRFQ
385 RFQTMEEKKAFMGPL
393 KAFMGPLKKDRIAKE
394 AFMGPLKKDRIAKEE
399 LKKDRIAKEEGA***
66 EVDRPGSKVNKKEVV

Function

Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547, PubMed:35674491). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547)

Protein Sequence

10 MSHRKFSAPR 20 HGSLGFLPRK 30 RSSRHRGKVK 40 SFPKDDPSKP 50 VHLTAFLGYK 60 AGMTHIVREV 70 DRPGSKVNKK 80 EVVEAVTIVE 90 TPPMVVVGIV 100 GYVETPRGLR 110 TFKTVFAEHI 120 SDECKRRFYK 130 NWHKSKKKAF 140 TKYCKKWQDE 150 DGKKQLEKDF 160 SSMKKYCQVI 170 RVIAHTQMRL 180 LPLRQKKAHL 190 MEIQVNGGTV 200 AEKLDWARER 210 LEQQVPVNQV 220 FGQDEMIDVI 230 GVTKGKGYKG 240 VTSRWHTKKL 250 PRKTHRGLRK 260 VACIGAWHPA 270 RVAFSVARAG 280 QKGYHHRTEI 290 NKKIYKIGQG 300 YLIKDGKLIK 310 NNASTDYDLS 320 DKSINPLGGF 330 VHYGEVTNDF 340 VMLKGCVVGT 350 KKRVLTLRKS 360 LLVQTKRRAL 370 EKIDLKFIDT 380 TSKFGHGRFQ 390 TMEEKKAFMG 400 PLKKDRIAKE EGA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0022625 cytosolic large ribosomal subunit
Cellular Component GO:0022626 cytosolic ribosome
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003735 structural constituent of ribosome
Biological Process GO:0002181 cytoplasmic translation
Biological Process GO:0007283 spermatogenesis
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] 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] 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.

[6] 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.

[7] 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.

[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.