Search Results

Overview

Uniprot IDO00567
Protein NameNucleolar protein 56
Gene NameNOP56
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
158 SYSRAKVKFNVNRVD
242 TMDGAKAKAILDASR
375 ISRYLANKCSIASRI
510 FSKPKKKKSFSKEEL
533 AGSTSIPKRKKSTPK
536 TSIPKRKKSTPKEET
540 KRKKSTPKEETVNDP
561 SGSKKKRKFSKEEPV
564 KKKRKFSKEEPVSSG
578 GPEEAVGKSSSKKKK
589 KKKKKFHKASQED**

Function

Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs (PubMed:12777385, PubMed:15574333). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) complexes that function in methylation of multiple sites on ribosomal RNAs (rRNAs) and messenger RNAs (mRNAs) (PubMed:12777385, PubMed:39570315)

Protein Sequence

10 MVLLHVLFEH 20 AVGYALLALK 30 EVEEISLLQP 40 QVEESVLNLG 50 KFHSIVRLVA 60 FCPFASSQVA 70 LENANAVSEG 80 VVHEDLRLLL 90 ETHLPSKKKK 100 VLLGVGDPKI 110 GAAIQEELGY 120 NCQTGGVIAE 130 ILRGVRLHFH 140 NLVKGLTDLS 150 ACKAQLGLGH 160 SYSRAKVKFN 170 VNRVDNMIIQ 180 SISLLDQLDK 190 DINTFSMRVR 200 EWYGYHFPEL 210 VKIINDNATY 220 CRLAQFIGNR 230 RELNEDKLEK 240 LEELTMDGAK 250 AKAILDASRS 260 SMGMDISAID 270 LINIESFSSR 280 VVSLSEYRQS 290 LHTYLRSKMS 300 QVAPSLSALI 310 GEAVGARLIA 320 HAGSLTNLAK 330 YPASTVQILG 340 AEKALFRALK 350 TRGNTPKYGL 360 IFHSTFIGRA 370 AAKNKGRISR 380 YLANKCSIAS 390 RIDCFSEVPT 400 SVFGEKLREQ 410 VEERLSFYET 420 GEIPRKNLDV 430 MKEAMVQAEE 440 AAAEITRKLE 450 KQEKKRLKKE 460 KKRLAALALA 470 SSENSSSTPE 480 ECEEMSEKPK 490 KKKKQKPQEV 500 PQENGMEDPS 510 ISFSKPKKKK 520 SFSKEELMSS 530 DLEETAGSTS 540 IPKRKKSTPK 550 EETVNDPEEA 560 GHRSGSKKKR 570 KFSKEEPVSS 580 GPEEAVGKSS 590 SKKKKKFHKA SQED

Gene Ontology

Classification GO ID Description
Cellular Component GO:0031428 box C/D methylation guide snoRNP complex
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0001650 fibrillar center
Cellular Component GO:0016020 membrane
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0070761 pre-snoRNP complex
Cellular Component GO:0032040 small-subunit processome
Cellular Component GO:0005732 sno(s)RNA-containing ribonucleoprotein complex
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:1990226 histone methyltransferase binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0030515 snoRNA binding
Biological Process GO:0030490 maturation of SSU-rRNA
Biological Process GO:0016556 mRNA modification
Biological Process GO:0030182 neuron differentiation
Biological Process GO:0042274 ribosomal small subunit biogenesis
Biological Process GO:0000451 rRNA 2'-O-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] 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.

[4] 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.

[5] 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.

[6] 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.