Search Results

Overview

Uniprot IDP62917
Protein NameLarge ribosomal subunit protein uL2
Gene NameRPL8
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
10 RVIRGQRKGAGSVFR
144 ISHNPETKKTRVKLP
145 SHNPETKKTRVKLPS
149 ETKKTRVKLPSGSKK
156 KLPSGSKKVISSANR
181 RIDKPILKAGRAYHK
250 TGRLRGTKTVQEKEN
42 AERHGYIKGIVKDII
46 GYIKGIVKDIIHDPG
92 GQFVYCGKKAQLNIG

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 MGRVIRGQRK 20 GAGSVFRAHV 30 KHRKGAARLR 40 AVDFAERHGY 50 IKGIVKDIIH 60 DPGRGAPLAK 70 VVFRDPYRFK 80 KRTELFIAAE 90 GIHTGQFVYC 100 GKKAQLNIGN 110 VLPVGTMPEG 120 TIVCCLEEKP 130 GDRGKLARAS 140 GNYATVISHN 150 PETKKTRVKL 160 PSGSKKVISS 170 ANRAVVGVVA 180 GGGRIDKPIL 190 KAGRAYHKYK 200 AKRNCWPRVR 210 GVAMNPVEHP 220 FGGGNHQHIG 230 KPSTIRRDAP 240 AGRKVGLIAA 250 RRTGRLRGTK TVQEKEN

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:0005783 endoplasmic reticulum
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0016020 membrane
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0098794 postsynapse
Cellular Component GO:0014069 postsynaptic density
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0019843 rRNA 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 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.

[5] 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.