Search Results

Overview

Uniprot IDP18124
Protein NameLarge ribosomal subunit protein uL30
Gene NameRPL7
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
107 GVSPKVRKVLQLLRL
124 IFNGTFVKLNKASIN
156 SVNELIYKRGYGKIN
19 PAVPETLKKKRRNFA
223 PRGGMKKKTTHFVEG
53 RRKLIYEKAKHYHKE
7 *MEGVEEKKKEVPAV
77 RMARMARKAGNFYVP
9 EGVEEKKKEVPAVPE

Function

Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547). Binds to G-rich structures in 28S rRNA and in mRNAs (PubMed:12962325). Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs (PubMed:12962325)

Protein Sequence

10 MEGVEEKKKE 20 VPAVPETLKK 30 KRRNFAELKI 40 KRLRKKFAQK 50 MLRKARRKLI 60 YEKAKHYHKE 70 YRQMYRTEIR 80 MARMARKAGN 90 FYVPAEPKLA 100 FVIRIRGING 110 VSPKVRKVLQ 120 LLRLRQIFNG 130 TFVKLNKASI 140 NMLRIVEPYI 150 AWGYPNLKSV 160 NELIYKRGYG 170 KINKKRIALT 180 DNALIARSLG 190 KYGIICMEDL 200 IHEIYTVGKR 210 FKEANNFLWP 220 FKLSSPRGGM 230 KKKTTHFVEG 240 GDAGNREDQI NRLIRRMN

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:0005925 focal adhesion
Cellular Component GO:0016020 membrane
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005634 nucleus
Cellular Component GO:0014069 postsynaptic density
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003735 structural constituent of ribosome
Biological Process GO:0002181 cytoplasmic translation
Biological Process GO:0000463 maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Biological Process GO:1901740 negative regulation of myoblast fusion
Biological Process GO:0042273 ribosomal large subunit biogenesis
Biological Process GO:0006364 rRNA processing
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] 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.

[4] 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.

[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.