Search Results

Overview

Uniprot IDQ9H0A0
Protein NameRNA cytidine acetyltransferase
Gene NameNAT10
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
447 VSTTAENKTTTTARL
989 NASIISLKSDKKRKL
992 IISLKSDKKRKLEAK
999 KKRKLEAKQEPKQSK

Function

RNA cytidine acetyltransferase that catalyzes the formation of N(4)-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs (PubMed:25411247, PubMed:25653167, PubMed:30449621, PubMed:35679869). Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed:30449621, PubMed:35679869). mRNA ac4C modification is frequently present within wobble cytidine sites and promotes translation efficiency (PubMed:30449621). Mediates the formation of ac4C at position 1842 in 18S rRNA (PubMed:25411247). May also catalyze the formation of ac4C at position 1337 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25411247, PubMed:25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMPD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167). In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). The relevance of the protein lysine acetyltransferase activity is however unsure in vivo (PubMed:30449621). Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization (PubMed:14592445, PubMed:18082603). Involved in the regulation of centrosome duplication by acetylating CENATAC during mitosis, promoting SASS6 proteasome degradation (PubMed:31722219). 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)

Protein Sequence

10 MHRKKVDNRI 20 RILIENGVAE 30 RQRSLFVVVG 40 DRGKDQVVIL 50 HHMLSKATVK 60 ARPSVLWCYK 70 KELGFSSHRK 80 KRMRQLQKKI 90 KNGTLNIKQD 100 DPFELFIAAT 110 NIRYCYYNET 120 HKILGNTFGM 130 CVLQDFEALT 140 PNLLARTVET 150 VEGGGLVVIL 160 LRTMNSLKQL 170 YTVTMDVHSR 180 YRTEAHQDVV 190 GRFNERFILS 200 LASCKKCLVI 210 DDQLNILPIS 220 SHVATMEALP 230 PQTPDESLGP 240 SDLELRELKE 250 SLQDTQPVGV 260 LVDCCKTLDQ 270 AKAVLKFIEG 280 ISEKTLRSTV 290 ALTAARGRGK 300 SAALGLAIAG 310 AVAFGYSNIF 320 VTSPSPDNLH 330 TLFEFVFKGF 340 DALQYQEHLD 350 YEIIQSLNPE 360 FNKAVIRVNV 370 FREHRQTIQY 380 IHPADAVKLG 390 QAELVVIDEA 400 AAIPLPLVKS 410 LLGPYLVFMA 420 STINGYEGTG 430 RSLSLKLIQQ 440 LRQQSAQSQV 450 STTAENKTTT 460 TARLASARTL 470 YEVSLQESIR 480 YAPGDAVEKW 490 LNDLLCLDCL 500 NITRIVSGCP 510 LPEACELYYV 520 NRDTLFCYHK 530 ASEVFLQRLM 540 ALYVASHYKN 550 SPNDLQMLSD 560 APAHHLFCLL 570 PPVPPTQNAL 580 PEVLAVIQVC 590 LEGEISRQSI 600 LNSLSRGKKA 610 SGDLIPWTVS 620 EQFQDPDFGG 630 LSGGRVVRIA 640 VHPDYQGMGY 650 GSRALQLLQM 660 YYEGRFPCLE 670 EKVLETPQEI 680 HTVSSEAVSL 690 LEEVITPRKD 700 LPPLLLKLNE 710 RPAERLDYLG 720 VSYGLTPRLL 730 KFWKRAGFVP 740 VYLRQTPNDL 750 TGEHSCIMLK 760 TLTDEDEADQ 770 GGWLAAFWKD 780 FRRRFLALLS 790 YQFSTFSPSL 800 ALNIIQNRNM 810 GKPAQPALSR 820 EELEALFLPY 830 DLKRLEMYSR 840 NMVDYHLIMD 850 MIPAISRIYF 860 LNQLGDLALS 870 AAQSALLLGI 880 GLQHKSVDQL 890 EKEIELPSGQ 900 LMGLFNRIIR 910 KVVKLFNEVQ 920 EKAIEEQMVA 930 AKDVVMEPTM 940 KTLSDDLDEA 950 AKEFQEKHKK 960 EVGKLKSMDL 970 SEYIIRGDDE 980 EWNEVLNKAG 990 PNASIISLKS 1000 DKKRKLEAKQ 1010 EPKQSKKLKN 1020 RETKNKKDMK LKRKK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0016020 membrane
Cellular Component GO:0030496 midbody
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032040 small-subunit processome
Cellular Component GO:0005697 telomerase holoenzyme complex
Molecular Function GO:1990883 18S rRNA cytidine N-acetyltransferase activity
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0070182 DNA polymerase binding
Molecular Function GO:0106162 mRNA N-acetyltransferase activity
Molecular Function GO:0008080 N-acetyltransferase activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0000049 tRNA binding
Molecular Function GO:0051392 tRNA cytidine N4-acetyltransferase activity
Biological Process GO:0030490 maturation of SSU-rRNA
Biological Process GO:0032211 negative regulation of telomere maintenance via telomerase
Biological Process GO:0045727 positive regulation of translation
Biological Process GO:0006473 protein acetylation
Biological Process GO:0010824 regulation of centrosome duplication
Biological Process GO:0006417 regulation of translation
Biological Process GO:0042274 ribosomal small subunit biogenesis
Biological Process GO:1904812 rRNA acetylation involved in maturation of SSU-rRNA
Biological Process GO:0000154 rRNA modification
Biological Process GO:0051391 tRNA acetylation
Biological Process GO:0002101 tRNA wobble cytosine modification

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] 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.

[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] 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.