Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q9H0A0 (NAT10_HUMAN)

Entry version 175 (03 Jul 2019)
Sequence version 2 (30 Nov 2010)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

RNA cytidine acetyltransferase

Gene

NAT10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

RNA cytidine acetyltransferase that catalyzes the formation of N4-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs (PubMed:25411247, PubMed:25653167, PubMed:30449621). Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed:30449621). 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).By similarity10 Publications

Caution

A number of papers have reported some protein lysine acetyltransferase activity in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). However, most experiments have been performed in vitro using a protein construct lacking the RNA-binding region at the terminus (PubMed:14592445, PubMed:17631499, PubMed:19303003). Recent evidence suggests that NAT10 mainly acts as a RNA cytidine acetyltransferase in vivo (PubMed:30449621).7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei470ATPUniRule annotation1
Binding sitei725Acetyl-CoAUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi287 – 296ATPUniRule annotation10

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processrRNA processing, tRNA processing
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-6790901 rRNA modification in the nucleus and cytosol

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
RNA cytidine acetyltransferase1 PublicationUniRule annotation (EC:2.3.1.-UniRule annotation2 Publications)
Alternative name(s):
18S rRNA cytosine acetyltransferase1 PublicationUniRule annotation
N-acetyltransferase 10UniRule annotation
N-acetyltransferase-like protein1 Publication
Short name:
hALP1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NAT10UniRule annotation
Synonyms:ALP2 Publications, KIAA17091 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:29830 NAT10

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		609221 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9H0A0

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi426K → R: Abolished acetylation. 1 Publication1
Mutagenesisi641G → E: Abolished acetyltransferase activity, probably caused by impaired acetyl-CoA binding. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		55226

Open Targets

More...OpenTargetsi		ENSG00000135372

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA143485555

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4105935

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		NAT10

Domain mapping of disease mutations (DMDM)

More...DMDMi		313104140

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002158831 – 1025RNA cytidine acetyltransferaseAdd BLAST1025

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei426N6-acetyllysineCombined sources1 Publication1
Modified residuei716PhosphothreonineCombined sources1
Modified residuei934PhosphoserineCombined sources1
Modified residuei984PhosphoserineCombined sources1
Modified residuei987PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylation at Lys-426 is required to activation of rRNA transcription (PubMed:27993683). May be autoacetylated; however ability to autoacetylate in vivo requires additional evidences (PubMed:27993683).1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9H0A0

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9H0A0

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9H0A0

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9H0A0

PeptideAtlas

More...PeptideAtlasi		Q9H0A0

PRoteomics IDEntifications database

More...PRIDEi		Q9H0A0

ProteomicsDB human proteome resource

More...ProteomicsDBi		80229

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		Q9H0A0

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9H0A0

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q9H0A0

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q9H0A0

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Transcriptionally activated by genotoxic agents; possible role in DNA damage and induction of cellular resistance to genotoxic agents.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000135372 Expressed in 222 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9H0A0 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9H0A0 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB035546
HPA057576
HPA071628

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with THUMPD1 (PubMed:25653167).

Interacts with SUN1 (via N-terminus) (PubMed:17631499).

Interacts with TERT (PubMed:18082603).

UniRule annotation3 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		120521, 105 interactors

Protein interaction database and analysis system

More...IntActi		Q9H0A0, 57 interactors

Molecular INTeraction database

More...MINTi		Q9H0A0

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000257829

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9H0A0

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini558 – 753N-acetyltransferaseUniRule annotationAdd BLAST196

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni629 – 631Acetyl-CoA bindingUniRule annotation3
Regioni636 – 642Acetyl-CoA bindingUniRule annotation7
Regioni702 – 1025Required for localization to the nucleolus and midbody1 PublicationAdd BLAST324

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RNA cytidine acetyltransferase family. NAT10 subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2036 Eukaryota
COG1444 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000009140

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000210833

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9H0A0

KEGG Orthology (KO)

More...KOi		K14521

Identification of Orthologs from Complete Genome Data

More...OMAi		FWKRASF

Database of Orthologous Groups

More...OrthoDBi		296129at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9H0A0

TreeFam database of animal gene trees

More...TreeFami		TF300601

Family and domain databases

HAMAP database of protein families

More...HAMAPi		MF_03211 RNA_acetyltr_Nat10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR016181 Acyl_CoA_acyltransferase
IPR000182 GNAT_dom
IPR007807 Helicase_dom
IPR033688 NAT10
IPR032672 TmcA/NAT10/Kre33
IPR013562 TmcA_N
IPR027992 tRNA_bind_dom

The PANTHER Classification System

More...PANTHERi		PTHR10925 PTHR10925, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08351 DUF1726, 1 hit
PF13718 GNAT_acetyltr_2, 1 hit
PF05127 Helicase_RecD, 1 hit
PF13725 tRNA_bind_2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55729 SSF55729, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51186 GNAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9H0A0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MHRKKVDNRI RILIENGVAE RQRSLFVVVG DRGKDQVVIL HHMLSKATVK 
        60         70         80         90        100
ARPSVLWCYK KELGFSSHRK KRMRQLQKKI KNGTLNIKQD DPFELFIAAT 
       110        120        130        140        150
NIRYCYYNET HKILGNTFGM CVLQDFEALT PNLLARTVET VEGGGLVVIL 
       160        170        180        190        200
LRTMNSLKQL YTVTMDVHSR YRTEAHQDVV GRFNERFILS LASCKKCLVI 
       210        220        230        240        250
DDQLNILPIS SHVATMEALP PQTPDESLGP SDLELRELKE SLQDTQPVGV 
       260        270        280        290        300
LVDCCKTLDQ AKAVLKFIEG ISEKTLRSTV ALTAARGRGK SAALGLAIAG 
       310        320        330        340        350
AVAFGYSNIF VTSPSPDNLH TLFEFVFKGF DALQYQEHLD YEIIQSLNPE 
       360        370        380        390        400
FNKAVIRVNV FREHRQTIQY IHPADAVKLG QAELVVIDEA AAIPLPLVKS 
       410        420        430        440        450
LLGPYLVFMA STINGYEGTG RSLSLKLIQQ LRQQSAQSQV STTAENKTTT 
       460        470        480        490        500
TARLASARTL YEVSLQESIR YAPGDAVEKW LNDLLCLDCL NITRIVSGCP 
       510        520        530        540        550
LPEACELYYV NRDTLFCYHK ASEVFLQRLM ALYVASHYKN SPNDLQMLSD 
       560        570        580        590        600
APAHHLFCLL PPVPPTQNAL PEVLAVIQVC LEGEISRQSI LNSLSRGKKA 
       610        620        630        640        650
SGDLIPWTVS EQFQDPDFGG LSGGRVVRIA VHPDYQGMGY GSRALQLLQM 
       660        670        680        690        700
YYEGRFPCLE EKVLETPQEI HTVSSEAVSL LEEVITPRKD LPPLLLKLNE 
       710        720        730        740        750
RPAERLDYLG VSYGLTPRLL KFWKRAGFVP VYLRQTPNDL TGEHSCIMLK 
       760        770        780        790        800
TLTDEDEADQ GGWLAAFWKD FRRRFLALLS YQFSTFSPSL ALNIIQNRNM 
       810        820        830        840        850
GKPAQPALSR EELEALFLPY DLKRLEMYSR NMVDYHLIMD MIPAISRIYF 
       860        870        880        890        900
LNQLGDLALS AAQSALLLGI GLQHKSVDQL EKEIELPSGQ LMGLFNRIIR 
       910        920        930        940        950
KVVKLFNEVQ EKAIEEQMVA AKDVVMEPTM KTLSDDLDEA AKEFQEKHKK 
       960        970        980        990       1000
EVGKLKSMDL SEYIIRGDDE EWNEVLNKAG PNASIISLKS DKKRKLEAKQ 
      1010       1020 
EPKQSKKLKN RETKNKKDMK LKRKK
Length:1,025
Mass (Da):115,730
Last modified:November 30, 2010 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i88734933A46EB0EE
GO
Isoform 2 (identifier: Q9H0A0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Show »
Length:953
Mass (Da):107,297
Checksum:iFC718FD5410FEAAA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WV29A0A087WV29_HUMAN
RNA cytidine acetyltransferase
NAT10
834Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PMU0E9PMU0_HUMAN
RNA cytidine acetyltransferase
NAT10
288Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PJN6E9PJN6_HUMAN
RNA cytidine acetyltransferase
NAT10
145Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAO49126 differs from that shown. Reason: Frameshift at position 981.Curated
The sequence BAB21800 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti26F → L in BAA91800 (PubMed:14702039).Curated1
Sequence conflicti162T → A in AAO49126 (PubMed:14592445).Curated1
Sequence conflicti315S → C in BAB13995 (PubMed:14702039).Curated1
Sequence conflicti405Y → C in BAG57396 (PubMed:14702039).Curated1
Sequence conflicti879Q → R in BAB13995 (PubMed:14702039).Curated1
Sequence conflicti971E → G in BAG57396 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_059858461Y → HCombined sources5 PublicationsCorresponds to variant dbSNP:rs2957516Ensembl.1
Natural variantiVAR_061894983A → T. Corresponds to variant dbSNP:rs36006049Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0540181 – 72Missing in isoform 2. 1 PublicationAdd BLAST72

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AB051496 mRNA Translation: BAB21800.1 Different initiation.
AL136882 mRNA Translation: CAB66816.1
AK001636 mRNA Translation: BAA91800.1
AK022241 mRNA Translation: BAB13995.1
AK294044 mRNA Translation: BAG57396.1
AC090469 Genomic DNA No translation available.
BC035558 mRNA Translation: AAH35558.1
AF489535 mRNA Translation: AAO49126.1 Frameshift.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS44568.1 [Q9H0A0-2]
CCDS7889.1 [Q9H0A0-1]

NCBI Reference Sequences

More...RefSeqi		NP_001137502.1, NM_001144030.1
NP_078938.2, NM_024662.2 [Q9H0A0-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000257829; ENSP00000257829; ENSG00000135372 [Q9H0A0-1]
ENST00000531159; ENSP00000433011; ENSG00000135372 [Q9H0A0-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		55226

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:55226

UCSC genome browser

More...UCSCi		uc001mvk.4 human [Q9H0A0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051496 mRNA Translation: BAB21800.1 Different initiation.
AL136882 mRNA Translation: CAB66816.1
AK001636 mRNA Translation: BAA91800.1
AK022241 mRNA Translation: BAB13995.1
AK294044 mRNA Translation: BAG57396.1
AC090469 Genomic DNA No translation available.
BC035558 mRNA Translation: AAH35558.1
AF489535 mRNA Translation: AAO49126.1 Frameshift.
CCDSiCCDS44568.1 [Q9H0A0-2]
CCDS7889.1 [Q9H0A0-1]
RefSeqiNP_001137502.1, NM_001144030.1
NP_078938.2, NM_024662.2 [Q9H0A0-1]

3D structure databases

SMRiQ9H0A0
ModBaseiSearch...

Protein-protein interaction databases

BioGridi120521, 105 interactors
IntActiQ9H0A0, 57 interactors
MINTiQ9H0A0
STRINGi9606.ENSP00000257829

Chemistry databases

ChEMBLiCHEMBL4105935

PTM databases

iPTMnetiQ9H0A0
PhosphoSitePlusiQ9H0A0
SwissPalmiQ9H0A0

Polymorphism and mutation databases

BioMutaiNAT10
DMDMi313104140

2D gel databases

SWISS-2DPAGEiQ9H0A0

Proteomic databases

EPDiQ9H0A0
jPOSTiQ9H0A0
MaxQBiQ9H0A0
PaxDbiQ9H0A0
PeptideAtlasiQ9H0A0
PRIDEiQ9H0A0
ProteomicsDBi80229

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		55226
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257829; ENSP00000257829; ENSG00000135372 [Q9H0A0-1]
ENST00000531159; ENSP00000433011; ENSG00000135372 [Q9H0A0-2]
GeneIDi55226
KEGGihsa:55226
UCSCiuc001mvk.4 human [Q9H0A0-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		55226
DisGeNETi55226

GeneCards: human genes, protein and diseases

More...GeneCardsi		NAT10
HGNCiHGNC:29830 NAT10
HPAiCAB035546
HPA057576
HPA071628
MIMi609221 gene
neXtProtiNX_Q9H0A0
OpenTargetsiENSG00000135372
PharmGKBiPA143485555

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2036 Eukaryota
COG1444 LUCA
GeneTreeiENSGT00390000009140
HOGENOMiHOG000210833
InParanoidiQ9H0A0
KOiK14521
OMAiFWKRASF
OrthoDBi296129at2759
PhylomeDBiQ9H0A0
TreeFamiTF300601

Enzyme and pathway databases

ReactomeiR-HSA-6790901 rRNA modification in the nucleus and cytosol

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		NAT10 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		NAT10

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		55226

Protein Ontology

More...PROi		PR:Q9H0A0

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000135372 Expressed in 222 organ(s), highest expression level in testis
ExpressionAtlasiQ9H0A0 baseline and differential
GenevisibleiQ9H0A0 HS

Family and domain databases

HAMAPiMF_03211 RNA_acetyltr_Nat10, 1 hit
InterProiView protein in InterPro
IPR016181 Acyl_CoA_acyltransferase
IPR000182 GNAT_dom
IPR007807 Helicase_dom
IPR033688 NAT10
IPR032672 TmcA/NAT10/Kre33
IPR013562 TmcA_N
IPR027992 tRNA_bind_dom
PANTHERiPTHR10925 PTHR10925, 1 hit
PfamiView protein in Pfam
PF08351 DUF1726, 1 hit
PF13718 GNAT_acetyltr_2, 1 hit
PF05127 Helicase_RecD, 1 hit
PF13725 tRNA_bind_2, 1 hit
SUPFAMiSSF55729 SSF55729, 1 hit
PROSITEiView protein in PROSITE
PS51186 GNAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNAT10_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9H0A0
Secondary accession number(s): B4DFD5
, E7ESU4, E9PMN9, Q86WK5, Q9C0F4, Q9HA61, Q9NVF2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 30, 2010
Last modified: July 3, 2019
This is version 175 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again