Search Results

Overview

Uniprot IDQ02878
Protein NameLarge ribosomal subunit protein eL6
Gene NameRPL6
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
12 KVEKPDTKEKKPEAK
131 KLLSHGKKPFSQHVR
14 EKPDTKEKKPEAKKV
15 KPDTKEKKPEAKKVD
192 PLRRTHQKFVIATST
207 KIDISNVKIPKHLTD
210 ISNVKIPKHLTDAYF
218 HLTDAYFKKKKLRKP
219 LTDAYFKKKKLRKPR
239 IFDTEKEKYEITEQR
26 KKVDAGGKVKKGNLK
260 VDSQILPKIKAIPQL
262 SQILPKIKAIPQLQG
5 ***MAGEKVEKPDTK
87 VEKKKKEKVLATVTK
94 KVLATVTKPVGGDKN

Function

Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:25901680, PubMed:25957688, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:25901680, PubMed:25957688, PubMed:32669547)

Protein Sequence

10 MAGEKVEKPD 20 TKEKKPEAKK 30 VDAGGKVKKG 40 NLKAKKPKKG 50 KPHCSRNPVL 60 VRGIGRYSRS 70 AMYSRKAMYK 80 RKYSAAKSKV 90 EKKKKEKVLA 100 TVTKPVGGDK 110 NGGTRVVKLR 120 KMPRYYPTED 130 VPRKLLSHGK 140 KPFSQHVRKL 150 RASITPGTIL 160 IILTGRHRGK 170 RVVFLKQLAS 180 GLLLVTGPLV 190 LNRVPLRRTH 200 QKFVIATSTK 210 IDISNVKIPK 220 HLTDAYFKKK 230 KLRKPRHQEG 240 EIFDTEKEKY 250 EITEQRKIDQ 260 KAVDSQILPK 270 IKAIPQLQGY 280 LRSVFALTNG IYPHKLVF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0036464 cytoplasmic ribonucleoprotein granule
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:0005634 nucleus
Cellular Component GO:0014069 postsynaptic density
Cellular Component GO:0005791 rough endoplasmic reticulum
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0003677 DNA binding
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:0006355 regulation of DNA-templated transcription
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] 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.