Search Results

Overview

Uniprot IDP62424
Protein NameLarge ribosomal subunit protein eL8
Gene NameRPL7A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
11 GKKAKGKKVAPAPAV
125 AEKKAAGKGDVPTKR
150 VTTLVENKKAQLVVI
151 TTLVENKKAQLVVIA
197 LGRLVHRKTCTTVAF
20 APAPAVVKKQEAKKV
21 PAPAVVKKQEAKKVV
212 TQVNSEDKGALAKLV
245 GGNVLGPKSVARIAK
26 VKKQEAKKVVNPLFE
264 KAKELATKLG*****
34 VVNPLFEKRPKNFGI
37 PLFEKRPKNFGIGQD
48 IGQDIQPKRDLTRFV
97 QTATQLLKLAHKYRP

Function

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

Protein Sequence

10 MPKGKKAKGK 20 KVAPAPAVVK 30 KQEAKKVVNP 40 LFEKRPKNFG 50 IGQDIQPKRD 60 LTRFVKWPRY 70 IRLQRQRAIL 80 YKRLKVPPAI 90 NQFTQALDRQ 100 TATQLLKLAH 110 KYRPETKQEK 120 KQRLLARAEK 130 KAAGKGDVPT 140 KRPPVLRAGV 150 NTVTTLVENK 160 KAQLVVIAHD 170 VDPIELVVFL 180 PALCRKMGVP 190 YCIIKGKARL 200 GRLVHRKTCT 210 TVAFTQVNSE 220 DKGALAKLVE 230 AIRTNYNDRY 240 DEIRRHWGGN 250 VLGPKSVARI 260 AKLEKAKAKE LATKLG

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:0005840 ribosome
Cellular Component GO:0045202 synapse
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003735 structural constituent of ribosome
Biological Process GO:0002181 cytoplasmic translation
Biological Process GO:0000470 maturation of LSU-rRNA
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] 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] 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.

[5] 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.

[6] 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.