Search Results

Overview

Uniprot IDP46087
Protein Name28S rRNA (cytosine(4447)-C(5))-methyltransferase
Gene NameNOP2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
22 GRKARKQKGAETELV
41 AVSDENSKRLSSRAR
638 KTKQQLQKQQHPKKA
649 PKKASFQKLNGISKG
655 QKLNGISKGADSELS
669 STVPSVTKTQASSSF
685 DSSQPAGKAEGIREP
704 KLKQRSPKLQSSKKV
71 TNKSPEAKPLPGKLP
735 PAVLSPSKTQATLKP
757 GRAKGVEKQQLPEQP
76 EAKPLPGKLPKGISA
767 LPEQPFEKAAFQKQN
772 FEKAAFQKQNDTPKG
79 PLPGKLPKGISAGAV
91 GAVQTAGKKGPQSLF
92 AVQTAGKKGPQSLFN

Function

S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 4447 in 28S rRNA (PubMed:26196125). Required for efficient rRNA processing and 60S ribosomal subunit biogenesis (PubMed:24120868, PubMed:36161484). Regulates pre-rRNA processing through non-catalytic complex formation with box C/D snoRNAs and facilitates the recruitment of U3 and U8 snoRNAs to pre-90S ribosomal particles and their stable assembly into snoRNP complexes (PubMed:36161484). May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation (PubMed:24120868)

Protein Sequence

10 MGRKLDPTKE 20 KRGPGRKARK 30 QKGAETELVR 40 FLPAVSDENS 50 KRLSSRARKR 60 AAKRRLGSVE 70 APKTNKSPEA 80 KPLPGKLPKG 90 ISAGAVQTAG 100 KKGPQSLFNA 110 PRGKKRPAPG 120 SDEEEEEEDS 130 EEDGMVNHGD 140 LWGSEDDADT 150 VDDYGADSNS 160 EDEEEGEALL 170 PIERAARKQK 180 AREAAAGIQW 190 SEEETEDEEE 200 EKEVTPESGP 210 PKVEEADGGL 220 QINVDEEPFV 230 LPPAGEMEQD 240 AQAPDLQRVH 250 KRIQDIVGIL 260 RDFGAQREEG 270 RSRSEYLNRL 280 KKDLAIYYSY 290 GDFLLGKLMD 300 LFPLSELVEF 310 LEANEVPRPV 320 TLRTNTLKTR 330 RRDLAQALIN 340 RGVNLDPLGK 350 WSKTGLVVYD 360 SSVPIGATPE 370 YLAGHYMLQG 380 ASSMLPVMAL 390 APQEHERILD 400 MCCAPGGKTS 410 YMAQLMKNTG 420 VILANDANAE 430 RLKSVVGNLH 440 RLGVTNTIIS 450 HYDGRQFPKV 460 VGGFDRVLLD 470 APCSGTGVIS 480 KDPAVKTNKD 490 EKDILRCAHL 500 QKELLLSAID 510 SVNATSKTGG 520 YLVYCTCSIT 530 VEENEWVVDY 540 ALKKRNVRLV 550 PTGLDFGQEG 560 FTRFRERRFH 570 PSLRSTRRFY 580 PHTHNMDGFF 590 IAKFKKFSNS 600 IPQSQTGNSE 610 TATPTNVDLP 620 QVIPKSENSS 630 QPAKKAKGAA 640 KTKQQLQKQQ 650 HPKKASFQKL 660 NGISKGADSE 670 LSTVPSVTKT 680 QASSSFQDSS 690 QPAGKAEGIR 700 EPKVTGKLKQ 710 RSPKLQSSKK 720 VAFLRQNAPP 730 KGTDTQTPAV 740 LSPSKTQATL 750 KPKDHHQPLG 760 RAKGVEKQQL 770 PEQPFEKAAF 780 QKQNDTPKGP 790 QPPTVSPIRS 800 SRPPPAKRKK 810 SQSRGNSQLL LS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0009383 rRNA (cytosine-C5-)-methyltransferase activity
Biological Process GO:0000470 maturation of LSU-rRNA
Biological Process GO:0008284 positive regulation of cell population proliferation
Biological Process GO:1901796 regulation of signal transduction by p53 class mediator
Biological Process GO:0000027 ribosomal large subunit assembly
Biological Process GO:0042273 ribosomal large subunit biogenesis
Biological Process GO:0070475 rRNA base methylation
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] 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.

[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.