Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9H0A0 (NAT10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetyltransferase 10

EC=2.3.1.-
Gene names
Name:NAT10
Synonyms:ALP, KIAA1709
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has protein acetyltransferase activity in vitro. Can acetylate both histones and microtubules. Histone acetylation may regulate transcription and mitotic chromosome de-condensation. 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. Acetylates alpha-tubulin, which may affect microtubule stability and cell division. Ref.6 Ref.8 Ref.9 Ref.12

Subunit structure

Interacts with SUN1 (via N-terminus). Also interacts with TERT. Ref.8 Ref.9

Subcellular location

Nucleusnucleolus. Note: Nucleolar in interphase and redistributes to the perichromosomal layer and to the midbody during telophase. Ref.6 Ref.7 Ref.12

Induction

Transcriptionally activated by genotoxic agents; possible role in DNA damage and induction of cellular resistance to genotoxic agents. Ref.10

Sequence similarities

Belongs to the UPF0202 family.

Contains 1 N-acetyltransferase domain.

Sequence caution

The sequence AAO49126.1 differs from that shown. Reason: Frameshift at position 981.

The sequence BAB21800.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

N-acetyltransferase activity

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LYARQ9NX581EBI-876527,EBI-713507

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H0A0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9H0A0-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10251025N-acetyltransferase 10
PRO_0000215883

Regions

Domain558 – 753196N-acetyltransferase
Nucleotide binding284 – 2918ATP Potential
Region702 – 1025324Required for localization to the nucleolus and midbody
Compositional bias989 – 102537Lys-rich

Amino acid modifications

Modified residue4261N6-acetyllysine Ref.13
Modified residue9341Phosphoserine Ref.11
Modified residue9841Phosphoserine Ref.11
Modified residue9871Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 7272Missing in isoform 2.
VSP_054018
Natural variant4611Y → H. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.14
Corresponds to variant rs2957516 [ dbSNP | Ensembl ].
VAR_059858
Natural variant9831A → T.
Corresponds to variant rs36006049 [ dbSNP | Ensembl ].
VAR_061894

Experimental info

Sequence conflict261F → L in BAA91800. Ref.3
Sequence conflict1621T → A in AAO49126. Ref.6
Sequence conflict3151S → C in BAB13995. Ref.3
Sequence conflict4051Y → C in BAG57396. Ref.3
Sequence conflict8791Q → R in BAB13995. Ref.3
Sequence conflict9711E → G in BAG57396. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 88734933A46EB0EE

FASTA1,025115,730
        10         20         30         40         50         60 
MHRKKVDNRI RILIENGVAE RQRSLFVVVG DRGKDQVVIL HHMLSKATVK ARPSVLWCYK 

        70         80         90        100        110        120 
KELGFSSHRK KRMRQLQKKI KNGTLNIKQD DPFELFIAAT NIRYCYYNET HKILGNTFGM 

       130        140        150        160        170        180 
CVLQDFEALT PNLLARTVET VEGGGLVVIL LRTMNSLKQL YTVTMDVHSR YRTEAHQDVV 

       190        200        210        220        230        240 
GRFNERFILS LASCKKCLVI DDQLNILPIS SHVATMEALP PQTPDESLGP SDLELRELKE 

       250        260        270        280        290        300 
SLQDTQPVGV LVDCCKTLDQ AKAVLKFIEG ISEKTLRSTV ALTAARGRGK SAALGLAIAG 

       310        320        330        340        350        360 
AVAFGYSNIF VTSPSPDNLH TLFEFVFKGF DALQYQEHLD YEIIQSLNPE FNKAVIRVNV 

       370        380        390        400        410        420 
FREHRQTIQY IHPADAVKLG QAELVVIDEA AAIPLPLVKS LLGPYLVFMA STINGYEGTG 

       430        440        450        460        470        480 
RSLSLKLIQQ LRQQSAQSQV STTAENKTTT TARLASARTL YEVSLQESIR YAPGDAVEKW 

       490        500        510        520        530        540 
LNDLLCLDCL NITRIVSGCP LPEACELYYV NRDTLFCYHK ASEVFLQRLM ALYVASHYKN 

       550        560        570        580        590        600 
SPNDLQMLSD APAHHLFCLL PPVPPTQNAL PEVLAVIQVC LEGEISRQSI LNSLSRGKKA 

       610        620        630        640        650        660 
SGDLIPWTVS EQFQDPDFGG LSGGRVVRIA VHPDYQGMGY GSRALQLLQM YYEGRFPCLE 

       670        680        690        700        710        720 
EKVLETPQEI HTVSSEAVSL LEEVITPRKD LPPLLLKLNE RPAERLDYLG VSYGLTPRLL 

       730        740        750        760        770        780 
KFWKRAGFVP VYLRQTPNDL TGEHSCIMLK TLTDEDEADQ GGWLAAFWKD FRRRFLALLS 

       790        800        810        820        830        840 
YQFSTFSPSL ALNIIQNRNM GKPAQPALSR EELEALFLPY DLKRLEMYSR NMVDYHLIMD 

       850        860        870        880        890        900 
MIPAISRIYF LNQLGDLALS AAQSALLLGI GLQHKSVDQL EKEIELPSGQ LMGLFNRIIR 

       910        920        930        940        950        960 
KVVKLFNEVQ EKAIEEQMVA AKDVVMEPTM KTLSDDLDEA AKEFQEKHKK EVGKLKSMDL 

       970        980        990       1000       1010       1020 
SEYIIRGDDE EWNEVLNKAG PNASIISLKS DKKRKLEAKQ EPKQSKKLKN RETKNKKDMK 


LKRKK 

« Hide

Isoform 2 [UniParc].

Checksum: FC718FD5410FEAAA
Show »

FASTA953107,297

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-461.
Tissue: Brain.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-461.
Tissue: Testis.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT HIS-461.
Tissue: Cerebellum and Mammary gland.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-461.
Tissue: Brain.
[6]"Molecular cloning of a novel human gene encoding histone acetyltransferase-like protein involved in transcriptional activation of hTERT."
Lv J., Liu H., Wang Q., Tang Z., Hou L., Zhang B.
Biochem. Biophys. Res. Commun. 311:506-513(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 154-1025, FUNCTION, SUBCELLULAR LOCATION, VARIANT HIS-461.
Tissue: Cervix carcinoma.
[7]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Histone acetyltransferase hALP and nuclear membrane protein hsSUN1 function in de-condensation of mitotic chromosomes."
Chi Y.-H., Haller K., Peloponese J.-M. Jr., Jeang K.-T.
J. Biol. Chem. 282:27447-27458(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SUN1.
[9]"Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation."
Fu D., Collins K.
Mol. Cell 28:773-785(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TERT.
[10]"DNA damage induces N-acetyltransferase NAT10 gene expression through transcriptional activation."
Liu H., Ling Y., Gong Y., Sun Y., Hou L., Zhang B.
Mol. Cell. Biochem. 300:249-258(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY GENOTOXIC AGENTS.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-934; SER-984 AND SER-987, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"NAT10, a nucleolar protein, localizes to the midbody and regulates cytokinesis and acetylation of microtubules."
Shen Q., Zheng X., McNutt M.A., Guang L., Sun Y., Wang J., Gong Y., Hou L., Zhang B.
Exp. Cell Res. 315:1653-1667(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001137502.1. NM_001144030.1.
NP_078938.2. NM_024662.2.
XP_005253056.1. XM_005252999.1.
UniGeneHs.577281.

3D structure databases

ProteinModelPortalQ9H0A0.
SMRQ9H0A0. Positions 623-651.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120521. 20 interactions.
IntActQ9H0A0. 10 interactions.
MINTMINT-2817086.
STRING9606.ENSP00000257829.

PTM databases

PhosphoSiteQ9H0A0.

Polymorphism databases

DMDM313104140.

2D gel databases

SWISS-2DPAGEQ9H0A0.

Proteomic databases

PaxDbQ9H0A0.
PRIDEQ9H0A0.

Protocols and materials databases

DNASU55226.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257829; ENSP00000257829; ENSG00000135372.
ENST00000531159; ENSP00000433011; ENSG00000135372.
GeneID55226.
KEGGhsa:55226.
UCSCuc001mvk.3. human.

Organism-specific databases

CTD55226.
GeneCardsGC11P034084.
HGNCHGNC:29830. NAT10.
HPACAB035546.
MIM609221. gene.
neXtProtNX_Q9H0A0.
PharmGKBPA143485555.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1444.
HOGENOMHOG000210833.
HOVERGENHBG052206.
InParanoidQ9H0A0.
KOK14521.
OMAKFLQQMV.
OrthoDBEOG7QK0B5.
PhylomeDBQ9H0A0.
TreeFamTF300601.

Gene expression databases

ArrayExpressQ9H0A0.
BgeeQ9H0A0.
CleanExHS_NAT10.
GenevestigatorQ9H0A0.

Family and domain databases

Gene3D3.40.630.30. 2 hits.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR013562. DUF1726.
IPR000182. GNAT_dom.
IPR007807. Helicase_dom.
IPR027992. tRNA_bind_dom.
[Graphical view]
PfamPF08351. DUF1726. 1 hit.
PF13718. GNAT_acetyltr_2. 1 hit.
PF05127. Helicase_RecD. 1 hit.
PF13725. tRNA_bind_2. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNAT10. human.
GeneWikiNAT10.
GenomeRNAi55226.
NextBio59220.
PROQ9H0A0.
SOURCESearch...

Entry information

Entry nameNAT10_HUMAN
AccessionPrimary (citable) accession number: Q9H0A0
Secondary accession number(s): B4DFD5 expand/collapse secondary AC list , E7ESU4, E9PMN9, Q86WK5, Q9C0F4, Q9HA61, Q9NVF2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM