NAT10
entrez
55226
canonical
uniprot
Q9H0A0
canonical
ensembl
ENSG00000135372
resolver
ensp
ENSP00000257829
resolver
ensp
ENSP00000433011
resolver
genesymbol
NAT10
resolver
genesymbol_syn
ALP
resolver
genesymbol_syn
KIAA1709
resolver
hgnc
HGNC:29830
resolver
uniprot
B4DFD5
resolver
uniprot
E7ESU4
resolver
uniprot
E9PMN9
resolver
uniprot
Q86WK5
resolver
uniprot
Q9C0F4
resolver
uniprot
Q9HA61
resolver
uniprot
Q9NVF2
resolver
uniprot_entry
NAT10_HUMAN
resolver
uniprot_sec
B4DFD5
resolver
uniprot_sec
E7ESU4
resolver
uniprot_sec
E9PMN9
resolver
uniprot_sec
Q86WK5
resolver
uniprot_sec
Q9C0F4
resolver
uniprot_sec
Q9HA61
resolver
uniprot_sec
Q9NVF2
resolver
activity_regulation
ACTIVITY REGULATION: Specifically inhibited by remodelin (4-[2-(2-cyclopentylidenehydrazinyl)-4-thiazolyl]-benzonitrile, monohydrobromide), a hydrobromide salt molecule (PubMed:24786082). Remodelin can improve nuclear architecture, chromatin organization and fitness of cells from patients suffering from Hutchinson-Gilford progeria syndrome (HGPS); molecular mechanisms explaining the relation between NAT10 activity and nuclear architecture are however unclear (PubMed:24786082). {ECO:0000269|PubMed:24786082}.
uniprot
proteins
amino_acid_sequence
MHRKKVDNRIRILIENGVAERQRSLFVVVGDRGKDQVVILHHMLSKATVKARPSVLWCYKKELGFSSHRKKRMRQLQKKIKNGTLNIKQDDPFELFIAATNIRYCYYNETHKILGNTFGMCVLQDFEALTPNLLARTVETVEGGGLVVILLRTMNSLKQLYTVTMDVHSRYRTEAHQDVVGRFNERFILSLASCKKCLVIDDQLNILPISSHVATMEALPPQTPDESLGPSDLELRELKESLQDTQPVGVLVDCCKTLDQAKAVLKFIEGISEKTLRSTVALTAARGRGKSAALGLAIAGAVAFGYSNIFVTSPSPDNLHTLFEFVFKGFDALQYQEHLDYEIIQSLNPEFNKAVIRVNVFREHRQTIQYIHPADAVKLGQAELVVIDEAAAIPLPLVKSLLGPYLVFMASTINGYEGTGRSLSLKLIQQLRQQSAQSQVSTTAENKTTTTARLASARTLYEVSLQESIRYAPGDAVEKWLNDLLCLDCLNITRIVSGCPLPEACELYYVNRDTLFCYHKASEVFLQRLMALYVASHYKNSPNDLQMLSDAPAHHLFCLLPPVPPTQNALPEVLAVIQVCLEGEISRQSILNSLSRGKKASGDLIPWTVSEQFQDPDFGGLSGGRVVRIAVHPDYQGMGYGSRALQLLQMYYEGRFPCLEEKVLETPQEIHTVSSEAVSLLEEVITPRKDLPPLLLKLNERPAERLDYLGVSYGLTPRLLKFWKRAGFVPVYLRQTPNDLTGEHSCIMLKTLTDEDEADQGGWLAAFWKDFRRRFLALLSYQFSTFSPSLALNIIQNRNMGKPAQPALSREELEALFLPYDLKRLEMYSRNMVDYHLIMDMIPAISRIYFLNQLGDLALSAAQSALLLGIGLQHKSVDQLEKEIELPSGQLMGLFNRIIRKVVKLFNEVQEKAIEEQMVAAKDVVMEPTMKTLSDDLDEAAKEFQEKHKKEVGKLKSMDLSEYIIRGDDEEWNEVLNKAGPNASIISLKSDKKRKLEAKQEPKQSKKLKNRETKNKKDMKLKRKK
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:P53914, ECO:0000269|PubMed:14592445, ECO:0000269|PubMed:17631499, ECO:0000269|PubMed:18082603, ECO:0000269|PubMed:19303003, ECO:0000269|PubMed:25411247, ECO:0000269|PubMed:25653167, ECO:0000269|PubMed:26882543, ECO:0000269|PubMed:27993683, ECO:0000269|PubMed:30165671, ECO:0000269|PubMed:30449621, ECO:0000269|PubMed:31722219, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:35679869}.
uniprot
proteins
mass_dalton
115730
uniprot
proteins
mutagenesis
MUTAGEN 426; /note="K->R: Abolished acetylation."; /evidence="ECO:0000269|PubMed:27993683"; MUTAGEN 641; /note="G->E: Abolished acetyltransferase activity, probably caused by impaired acetyl-CoA binding."; /evidence="ECO:0000269|PubMed:24786082
uniprot
proteins
post_translational_modification
PTM: Acetylation at Lys-426 is required to activation of rRNA transcription (PubMed:27993683). May be autoacetylated; however ability to autoacetylate in vivo requires additional evidence (PubMed:27993683). {ECO:0000269|PubMed:27993683}.
uniprot
proteins
protein_family
NAT10 subfamily
uniprot
proteins
protein_family
RNA cytidine acetyltransferase family
uniprot
proteins
pubmed
11214970
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
12429849
uniprot
proteins
pubmed
14592445
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17180247
uniprot
proteins
pubmed
17631499
uniprot
proteins
pubmed
18082603
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19303003
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24786082
uniprot
proteins
pubmed
25411247
uniprot
proteins
pubmed
25653167
uniprot
proteins
pubmed
26882543
uniprot
proteins
pubmed
27993683
uniprot
proteins
pubmed
30165671
uniprot
proteins
pubmed
30449621
uniprot
proteins
pubmed
31722219
uniprot
proteins
pubmed
34516797
uniprot
proteins
pubmed
35679869
uniprot
proteins
sequence_length
1025
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:14592445, ECO:0000269|PubMed:19303003, ECO:0000269|PubMed:24786082, ECO:0000269|PubMed:25653167, ECO:0000269|PubMed:30165671, ECO:0000269|PubMed:34516797}. Midbody {ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000269|PubMed:19303003}. Note=Nucleolar in interphase and redistributes to the perichromosomal layer and to the midbody during telophase. {ECO:0000269|PubMed:19303003}.
uniprot
proteins