Search Results

Overview

Uniprot IDQ9Y2X3
Protein NameNucleolar protein 58
Gene NameNOP58
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
101 LGGVIKEKLNLSCIH
411 RKISGTGKALAKTEK
415 GTGKALAKTEKYEHK
422 KTEKYEHKSEVKTYD
441 STLPTCSKKRKIEQV
442 TLPTCSKKRKIEQVD
444 PTCSKKRKIEQVDKE
485 EEEETSVKKKKKRGK
486 EEETSVKKKKKRGKK

Function

Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs (PubMed:15574333, PubMed:17636026, PubMed:19620283, PubMed:34516797). 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:39570315)

Protein Sequence

10 MLVLFETSVG 20 YAIFKVLNEK 30 KLQEVDSLWK 40 EFETPEKANK 50 IVKLKHFEKF 60 QDTAEALAAF 70 TALMEGKINK 80 QLKKVLKKIV 90 KEAHEPLAVA 100 DAKLGGVIKE 110 KLNLSCIHSP 120 VVNELMRGIR 130 SQMDGLIPGV 140 EPREMAAMCL 150 GLAHSLSRYR 160 LKFSADKVDT 170 MIVQAISLLD 180 DLDKELNNYI 190 MRCREWYGWH 200 FPELGKIISD 210 NLTYCKCLQK 220 VGDRKNYASA 230 KLSELLPEEV 240 EAEVKAAAEI 250 SMGTEVSEED 260 ICNILHLCTQ 270 VIEISEYRTQ 280 LYEYLQNRMM 290 AIAPNVTVMV 300 GELVGARLIA 310 HAGSLLNLAK 320 HAASTVQILG 330 AEKALFRALK 340 SRRDTPKYGL 350 IYHASLVGQT 360 SPKHKGKISR 370 MLAAKTVLAI 380 RYDAFGEDSS 390 SAMGVENRAK 400 LEARLRTLED 410 RGIRKISGTG 420 KALAKTEKYE 430 HKSEVKTYDP 440 SGDSTLPTCS 450 KKRKIEQVDK 460 EDEITEKKAK 470 KAKIKVKVEE 480 EEEEKVAEEE 490 ETSVKKKKKR 500 GKKKHIKEEP 510 LSEEEPCTST 520 AIASPEKKKK KKKKRENED

Gene Ontology

Classification GO ID Description
Cellular Component GO:0031428 box C/D methylation guide snoRNP complex
Cellular Component GO:0015030 Cajal body
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:0051117 ATPase binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0030515 snoRNA binding
Molecular Function GO:0001094 TFIID-class transcription factor complex 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
Biological Process GO:0048254 snoRNA 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] 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] 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.