Search Results

Overview

Uniprot IDP36578
Protein NameLarge ribosomal subunit protein uL4
Gene NameRPL4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
120 RRVNTTQKRYAICSA
14 LISVYSEKGESSGKN
165 VEGYKKTKEAVLLLK
172 KEAVLLLKKLKAWND
173 EAVLLLKKLKAWNDI
175 VLLLKKLKAWNDIKK
181 LKAWNDIKKVYASQR
182 KAWNDIKKVYASQRM
20 EKGESSGKNVTLPAV
239 VSKLNILKLAPGGHV
259 WTESAFRKLDELYGT
274 WRKAASLKSNYNLPM
283 NYNLPMHKMINTDLS
294 TDLSRILKSPEIQRA
353 NHKLRVDKAAAAAAA
364 AAAALQAKSDEKAAV
368 LQAKSDEKAAVAGKK
405 GKKAAATKKPAPEKK
416 PEKKPAEKKPTTEEK

Function

Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell

Protein Sequence

10 MACARPLISV 20 YSEKGESSGK 30 NVTLPAVFKA 40 PIRPDIVNFV 50 HTNLRKNNRQ 60 PYAVSELAGH 70 QTSAESWGTG 80 RAVARIPRVR 90 GGGTHRSGQG 100 AFGNMCRGGR 110 MFAPTKTWRR 120 WHRRVNTTQK 130 RYAICSALAA 140 SALPALVMSK 150 GHRIEEVPEL 160 PLVVEDKVEG 170 YKKTKEAVLL 180 LKKLKAWNDI 190 KKVYASQRMR 200 AGKGKMRNRR 210 RIQRRGPCII 220 YNEDNGIIKA 230 FRNIPGITLL 240 NVSKLNILKL 250 APGGHVGRFC 260 IWTESAFRKL 270 DELYGTWRKA 280 ASLKSNYNLP 290 MHKMINTDLS 300 RILKSPEIQR 310 ALRAPRKKIH 320 RRVLKKNPLK 330 NLRIMLKLNP 340 YAKTMRRNTI 350 LRQARNHKLR 360 VDKAAAAAAA 370 LQAKSDEKAA 380 VAGKKPVVGK 390 KGKKAAVGVK 400 KQKKPLVGKK 410 AAATKKPAPE 420 KKPAEKKPTT EEKKPAA

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:0016020 membrane
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0005791 rough endoplasmic reticulum
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003735 structural constituent of ribosome
Biological Process GO:0002181 cytoplasmic translation
Biological Process GO:1901740 negative regulation of myoblast fusion
Biological Process GO:0007283 spermatogenesis
Biological Process GO:0006941 striated muscle contraction
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] 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.