Search Results

Overview

Uniprot IDO43159
Protein NameRibosomal RNA-processing protein 8
Gene NameRRP8
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
135 EDEKRKRKCQKHAPI
138 KRKRKCQKHAPINSA
201 NKRRCKNKFQPPQVP
78 RKKKCPKKASFASAS
90 SASAEVGKKGKKKCQ
91 ASAEVGKKGKKKCQK

Function

Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown

Protein Sequence

10 MFEEPEWAEA 20 APVAAGLGPV 30 ISRPPPAASS 40 QNKGSKRRQL 50 LATLRALEAA 60 SLSQHPPSLC 70 ISDSEEEEEE 80 RKKKCPKKAS 90 FASASAEVGK 100 KGKKKCQKQG 110 PPCSDSEEEV 120 ERKKKCHKQA 130 LVGSDSAEDE 140 KRKRKCQKHA 150 PINSAQHLDN 160 VDQTGPKAWK 170 GSTTNDPPKQ 180 SPGSTSPKPP 190 HTLSRKQWRN 200 RQKNKRRCKN 210 KFQPPQVPDQ 220 APAEAPTEKT 230 EVSPVPRTDS 240 HEARAGALRA 250 RMAQRLDGAR 260 FRYLNEQLYS 270 GPSSAAQRLF 280 QEDPEAFLLY 290 HRGFQSQVKK 300 WPLQPVDRIA 310 RDLRQRPASL 320 VVADFGCGDC 330 RLASSIRNPV 340 HCFDLASLDP 350 RVTVCDMAQV 360 PLEDESVDVA 370 VFCLSLMGTN 380 IRDFLEEANR 390 VLKPGGLLKV 400 AEVSSRFEDV 410 RTFLRAVTKL 420 GFKIVSKDLT 430 NSHFFLFDFQ 440 KTGPPLVGPK 450 AQLSGLQLQP CLYKRR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005677 chromatin silencing complex
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0033553 rDNA heterochromatin
Molecular Function GO:0062072 histone H3K9me2/3 reader activity
Molecular Function GO:0008168 methyltransferase activity
Molecular Function GO:0003723 RNA binding
Biological Process GO:0042149 cellular response to glucose starvation
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0097009 energy homeostasis
Biological Process GO:0072332 intrinsic apoptotic signaling pathway by p53 class mediator
Biological Process GO:0032259 methylation
Biological Process GO:0045786 negative regulation of cell cycle
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0000183 rDNA heterochromatin formation
Biological Process GO:1903450 regulation of G1 to G0 transition
Biological Process GO:0046015 regulation of transcription by glucose
Biological Process GO:0006364 rRNA processing

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] 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.