Q9H0A0 (NAT10_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 114.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: N-acetyltransferase 10 EC=2.3.1.- | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1025 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 | Nucleus › nucleolus. 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 component | Nucleus |
| Coding sequence diversity | Polymorphism |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Acyltransferase Transferase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusNon-traceable author statement Ref.1. Source: UniProtKB |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-acetyltransferase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| LYAR | Q9NX58 | 1 | EBI-876527,EBI-713507 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1025 | 1025 | N-acetyltransferase 10 | PRO_0000215883 | |||||
Regions | |||||||||
| Domain | 558 – 753 | 196 | N-acetyltransferase | ||||||
| Nucleotide binding | 284 – 291 | 8 | ATP Potential | ||||||
| Region | 702 – 1025 | 324 | Required for localization to the nucleolus and midbody | ||||||
| Compositional bias | 989 – 1025 | 37 | Lys-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 426 | 1 | N6-acetyllysine Ref.13 | ||||||
| Modified residue | 934 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 984 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 987 | 1 | Phosphoserine Ref.11 | ||||||
Natural variations | |||||||||
| Natural variant | 461 | 1 | Y → H. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.14 Corresponds to variant rs2957516 [ dbSNP | Ensembl ]. | VAR_059858 | |||||
| Natural variant | 983 | 1 | A → T. Corresponds to variant rs36006049 [ dbSNP | Ensembl ]. | VAR_061894 | |||||
Experimental info | |||||||||
| Sequence conflict | 26 | 1 | F → L in BAA91800. Ref.3 | ||||||
| Sequence conflict | 162 | 1 | T → A in AAO49126. Ref.6 | ||||||
| Sequence conflict | 315 | 1 | S → C in BAB13995. Ref.3 | ||||||
| Sequence conflict | 879 | 1 | Q → R in BAB13995. Ref.3 | ||||||
Sequences
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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], 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. Poustka A.Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], 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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-461. Tissue: 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. 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], 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], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. |
| [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, MASS SPECTROMETRY. |
| + | 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. AC090469 Genomic DNA. No translation available. BC035558 mRNA. Translation: AAH35558.1. AF489535 mRNA. Translation: AAO49126.1. Frameshift. |
| IPI | IPI00300127. |
| RefSeq | NP_001137502.1. NM_001144030.1. NP_078938.2. NM_024662.2. |
| UniGene | Hs.577281. |
3D structure databases | |
| ProteinModelPortal | Q9H0A0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9H0A0. 6 interactions. |
| MINT | MINT-2817086. |
| STRING | 9606.ENSP00000257829. |
PTM databases | |
| PhosphoSite | Q9H0A0. |
2D gel databases | |
| SWISS-2DPAGE | Q9H0A0. |
Proteomic databases | |
| PaxDb | Q9H0A0. |
| PRIDE | Q9H0A0. |
Protocols and materials databases | |
| DNASU | 55226. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000257829; ENSP00000257829; ENSG00000135372. |
| GeneID | 55226. |
| KEGG | hsa:55226. |
| UCSC | uc001mvk.3. human. |
Organism-specific databases | |
| CTD | 55226. |
| GeneCards | GC11P034084. |
| HGNC | HGNC:29830. NAT10. |
| HPA | CAB035546. |
| MIM | 609221. gene. |
| neXtProt | NX_Q9H0A0. |
| PharmGKB | PA143485555. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | COG1444. |
| HOGENOM | HOG000210833. |
| HOVERGEN | HBG052206. |
| InParanoid | Q9H0A0. |
| KO | K14521. |
| OMA | LSAFWKD. |
| OrthoDB | EOG4H9XJS. |
| PhylomeDB | Q9H0A0. |
Gene expression databases | |
| ArrayExpress | Q9H0A0. |
| Bgee | Q9H0A0. |
| CleanEx | HS_NAT10. |
| Genevestigator | Q9H0A0. |
| GermOnline | ENSG00000135372. Homo sapiens. |
Family and domain databases | |
| Gene3D | 3.40.630.30. 2 hits. |
| InterPro | IPR016181. Acyl_CoA_acyltransferase. IPR013562. DUF1726. IPR000182. GNAT_dom. IPR007807. Helicase_dom. [Graphical view] |
| Pfam | PF08351. DUF1726. 1 hit. PF05127. Helicase_RecD. 1 hit. [Graphical view] |
| SUPFAM | SSF55729. Acyl_CoA_acyltransferase. 1 hit. |
| PROSITE | PS51186. GNAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | NAT10. human. |
| GenomeRNAi | 55226. |
| NextBio | 59220. |
| SOURCE | Search... |
Entry information
| Entry name | NAT10_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9H0A0 Secondary accession number(s): Q86WK5 Q9NVF2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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 |
| Human chromosome 11 Human chromosome 11: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
