Search Results

Overview

Uniprot IDO76021
Protein NameRibosomal L1 domain-containing protein 1
Gene NameRSL1D1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
100 EDICLFTKDEPNSTP
311 KKRQQARKTASVLSK
331 ESGDTTVKKPESKKE
356 GRGKAQVKATNESED
373 PQLVPIGKKTPANEK
374 QLVPIGKKTPANEKV
38 LDKEQVRKAVDALLT
380 KKTPANEKVEIQKHA
385 NEKVEIQKHATGKKS
391 QKHATGKKSPAKSPN
395 TGKKSPAKSPNPSTP
408 TPRGKKRKALPASET
426 AESETPGKSPEKKPK
448 EKSPSLGKKDARQTP
449 KSPSLGKKDARQTPK
461 TPKKPEAKFFTTPSK
468 KFFTTPSKSVRKASH
472 TPSKSVRKASHTPKK
478 RKASHTPKKWPKKPK
48 DALLTHCKSRKNNYG

Function

Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage

Protein Sequence

10 MEDSASASLS 20 SAAATGTSTS 30 TPAAPTARKQ 40 LDKEQVRKAV 50 DALLTHCKSR 60 KNNYGLLLNE 70 NESLFLMVVL 80 WKIPSKELRV 90 RLTLPHSIRS 100 DSEDICLFTK 110 DEPNSTPEKT 120 EQFYRKLLNK 130 HGIKTVSQII 140 SLQTLKKEYK 150 SYEAKLRLLS 160 SFDFFLTDAR 170 IRRLLPSLIG 180 RHFYQRKKVP 190 VSVNLLSKNL 200 SREINDCIGG 210 TVLNISKSGS 220 CSAIRIGHVG 230 MQIEHIIENI 240 VAVTKGLSEK 250 LPEKWESVKL 260 LFVKTEKSAA 270 LPIFSSFVSN 280 WDEATKRSLL 290 NKKKKEARRK 300 RRERNFEKQK 310 ERKKKRQQAR 320 KTASVLSKDD 330 VAPESGDTTV 340 KKPESKKEQT 350 PEHGKKKRGR 360 GKAQVKATNE 370 SEDEIPQLVP 380 IGKKTPANEK 390 VEIQKHATGK 400 KSPAKSPNPS 410 TPRGKKRKAL 420 PASETPKAAE 430 SETPGKSPEK 440 KPKIKEEAVK 450 EKSPSLGKKD 460 ARQTPKKPEA 470 KFFTTPSKSV 480 RKASHTPKKW 490 PKKPKVPQST

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016020 membrane
Cellular Component GO:0005730 nucleolus
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0003730 mRNA 3'-UTR binding
Molecular Function GO:0048027 mRNA 5'-UTR binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0001649 osteoblast differentiation
Biological Process GO:0042981 regulation of apoptotic process
Biological Process GO:2000772 regulation of cellular senescence
Biological Process GO:0032880 regulation of protein localization

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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] 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.

[7] 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.

[8] 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.