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Q9H7X0 (NAA60_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-alpha-acetyltransferase 60

EC=2.3.1.48
EC=2.3.1.88
Alternative name(s):
Histone acetyltransferase type B protein 4
Short name=HAT4
N-acetyltransferase 15
NatF catalytic subunit
Gene names
Name:NAA60
Synonyms:HAT4, NAT15
ORF Names:UNQ2771/PRO7155
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length242 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone acetyltransferase localized in the Golgi apparatus that mediates acetylation of free histone H4, thereby facilitating nucleosome assembly. Has a preference for free histone H4 'Lys-20'(H4K20ac), 'Lys-79'(H4K79ac) and 'Lys-91' (H4K91ac). Also displays alpha (N-terminal) acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. Ref.8 Ref.9

Catalytic activity

Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA. Ref.8

Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.8

Subcellular location

Golgi apparatus membrane Ref.8.

Induction

Isoform 2 is imprinted. Promoter methylation of the paternal allele may restrict expression to the maternal allele in placenta and leukocytes. Isoform 1 is biallelically expressed. Ref.7

Post-translational modification

Acetylated: autoacetylation is required for optimal acetyltransferase activity. Ref.8

Sequence similarities

Belongs to the acetyltransferase family. NAA60 subfamily.

Contains 1 N-acetyltransferase domain.

Alternative products

This entry describes 5 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H7X0-1)

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: Q9H7X0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MTEVVPSSAL...KHLCGDWFPI → MFPRRRTERR...ASLSWEKSSR
Note: In placenta and leukocytes, expressed from the maternal allele, due to imprinting of the paternal allele.
Isoform 3 (identifier: Q9H7X0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 4 (identifier: Q9H7X0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     113-242: GSLLLESLKD...KSGIEYSRTM → ESTARPTACS...SVFCKELPAI
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 5 (identifier: Q9H7X0-5)

The sequence of this isoform differs from the canonical sequence as follows:
     113-242: GSLLLESLKD...KSGIEYSRTM → EPHGLHPAPG...PPAEPAFLSI
Note: Produced by alternative splicing. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 242242N-alpha-acetyltransferase 60
PRO_0000321566

Regions

Domain13 – 182170N-acetyltransferase

Amino acid modifications

Modified residue791N6-acetyllysine; by autocatalysis Ref.8
Modified residue1051N6-acetyllysine; by autocatalysis Ref.8
Modified residue1091N6-acetyllysine; by autocatalysis Probable
Modified residue1211N6-acetyllysine; by autocatalysis Probable
Modified residue1561N6-acetyllysine; by autocatalysis Ref.8

Natural variations

Alternative sequence1 – 6565Missing in isoform 3.
VSP_044122
Alternative sequence1 – 3636MTEVV…DWFPI → MFPRRRTERRLGDTGTRKKI AYRKAVPGGRKCGASLSWEK SSR in isoform 2.
VSP_044123
Alternative sequence113 – 242130GSLLL…YSRTM → ESTARPTACSAASCHGRASL PRVASSTAGPCDVGWAAATR PHPSAARRARLPVHLTPSVF CKELPAI in isoform 4.
VSP_044124
Alternative sequence113 – 242130GSLLL…YSRTM → EPHGLHPAPGLCTSQPEPLL HSAQSLPPGPQPALQLPAMV GHLFQEWHRVQPDHVMSAGQ PPPGPTLRPPAEPAFLSI in isoform 5.
VSP_044125
Natural variant2181H → Q.
Corresponds to variant rs34464545 [ dbSNP | Ensembl ].
VAR_060995

Experimental info

Mutagenesis791K → R: Decreased histone acetyltransferase activity; when associated with R-105, R-109, R-121 and R-156. Ref.8
Mutagenesis1051K → R: Decreased histone acetyltransferase activity; when associated with R-79, R-109, R-121 and R-156. Ref.8
Mutagenesis1091K → R: Decreased histone acetyltransferase activity; when associated with R-79, R-105, R-121 and R-156. Ref.8
Mutagenesis1111G → A: Abolishes histone acetyltransferase activity. Ref.8
Mutagenesis1211K → R: Decreased histone acetyltransferase activity; when associated with R-79, R-105, R-109 and R-156. Ref.8
Mutagenesis1561K → R: Decreased histone acetyltransferase activity; when associated with R-79, R-105, R-109 and R-121. Ref.8
Sequence conflict871S → T in AAQ88907. Ref.1
Sequence conflict2421M → I in CAG33605. Ref.3
Isoform 5:
Sequence conflict1801R → Q in BAG60760. Ref.2

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: 11234F2C51DF55DE

FASTA24227,451
        10         20         30         40         50         60 
MTEVVPSSAL SEVSLRLLCH DDIDTVKHLC GDWFPIEYPD SWYRDITSNK KFFSLAATYR 

        70         80         90        100        110        120 
GAIVGMIVAE IKNRTKIHKE DGDILASNFS VDTQVAYILS LGVVKEFRKH GIGSLLLESL 

       130        140        150        160        170        180 
KDHISTTAQD HCKAIYLHVL TTNNTAINFY ENRDFKQHHY LPYYYSIRGV LKDGFTYVLY 

       190        200        210        220        230        240 
INGGHPPWTI LDYIQHLGSA LASLSPCSIP HRVYRQAHSL LCSFLPWSGI SSKSGIEYSR 


TM 

« Hide

Isoform 2 [UniParc].

Checksum: E049FDCDA8FD6ECC
Show »

FASTA24928,375
Isoform 3 [UniParc].

Checksum: 32C31E8C2E777D5D
Show »

FASTA17720,103
Isoform 4 [UniParc].

Checksum: 806EE0412C45F54C
Show »

FASTA17919,493
Isoform 5 [UniParc].

Checksum: C82D743C3A3F0776
Show »

FASTA19020,911

References

« Hide 'large scale' references
[1]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]"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; 2; 3; 4 AND 5).
Tissue: Fetal brain, Mesangial cell, Teratocarcinoma and Testis.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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).
Tissue: Brain.
[7]"Methylation screening of reciprocal genome-wide UPDs identifies novel human-specific imprinted genes."
Nakabayashi K., Trujillo A.M., Tayama C., Camprubi C., Yoshida W., Lapunzina P., Sanchez A., Soejima H., Aburatani H., Nagae G., Ogata T., Hata K., Monk D.
Hum. Mol. Genet. 20:3188-3197(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IMPRINTING, INDUCTION.
[8]"HAT4, a Golgi apparatus-anchored B-type histone acetyltransferase, acetylates free histone H4 and facilitates chromatin assembly."
Yang X., Yu W., Shi L., Sun L., Liang J., Yi X., Li Q., Zhang Y., Yang F., Han X., Zhang D., Yang J., Yao Z., Shang Y.
Mol. Cell 44:39-50(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACETYLATION AT LYS-79; LYS-105; LYS-109; LYS-121 AND LYS-156, MUTAGENESIS OF LYS-79; LYS-105; LYS-109; GLY-111; LYS-121 AND LYS-156.
[9]"NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation."
Van Damme P., Hole K., Pimenta-Marques A., Helsens K., Vandekerckhove J., Martinho R.G., Gevaert K., Arnesen T.
PLoS Genet. 7:E1002169-E1002169(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY358543 mRNA. Translation: AAQ88907.1.
AK024216 mRNA. Translation: BAB14853.1.
AK092005 mRNA. Translation: BAG52462.1.
AK297219 mRNA. Translation: BAG59702.1.
AK298566 mRNA. Translation: BAG60760.1.
AK302361 mRNA. Translation: BAG63686.1.
CR457324 mRNA. Translation: CAG33605.1.
AC004224 Genomic DNA. No translation available.
AC025283 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85358.1.
CH471112 Genomic DNA. Translation: EAW85359.1.
CH471112 Genomic DNA. Translation: EAW85360.1.
CH471112 Genomic DNA. Translation: EAW85361.1.
CH471112 Genomic DNA. Translation: EAW85362.1.
CH471112 Genomic DNA. Translation: EAW85363.1.
CH471112 Genomic DNA. Translation: EAW85364.1.
BC011267 mRNA. Translation: AAH11267.1.
CCDSCCDS45396.1. [Q9H7X0-1]
RefSeqNP_001077069.1. NM_001083600.1. [Q9H7X0-1]
NP_001077070.1. NM_001083601.1. [Q9H7X0-1]
NP_079121.1. NM_024845.2. [Q9H7X0-1]
XP_006721012.1. XM_006720949.1. [Q9H7X0-1]
XP_006721013.1. XM_006720950.1. [Q9H7X0-1]
XP_006721014.1. XM_006720951.1. [Q9H7X0-1]
XP_006721015.1. XM_006720952.1. [Q9H7X0-1]
UniGeneHs.513296.

3D structure databases

ProteinModelPortalQ9H7X0.
SMRQ9H7X0. Positions 12-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000385903.

PTM databases

PhosphoSiteQ9H7X0.

Polymorphism databases

DMDM74733721.

Proteomic databases

MaxQBQ9H7X0.
PaxDbQ9H7X0.
PRIDEQ9H7X0.

Protocols and materials databases

DNASU79903.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360862; ENSP00000354108; ENSG00000122390. [Q9H7X0-3]
ENST00000407558; ENSP00000385903; ENSG00000122390. [Q9H7X0-1]
ENST00000414063; ENSP00000393224; ENSG00000122390. [Q9H7X0-1]
ENST00000421765; ENSP00000405873; ENSG00000122390. [Q9H7X0-5]
ENST00000424546; ENSP00000401237; ENSG00000122390. [Q9H7X0-2]
ENST00000570819; ENSP00000460763; ENSG00000122390. [Q9H7X0-4]
ENST00000572584; ENSP00000459057; ENSG00000122390. [Q9H7X0-1]
ENST00000572942; ENSP00000461730; ENSG00000122390. [Q9H7X0-4]
ENST00000573580; ENSP00000459055; ENSG00000122390. [Q9H7X0-3]
ENST00000575076; ENSP00000458667; ENSG00000122390. [Q9H7X0-1]
GeneID79903.
KEGGhsa:79903.
UCSCuc002cvg.2. human. [Q9H7X0-1]
uc010uxb.1. human. [Q9H7X0-2]

Organism-specific databases

CTD79903.
GeneCardsGC16P003495.
H-InvDBHIX0012768.
HIX0173265.
HGNCHGNC:25875. NAA60.
HPAHPA040916.
MIM614246. gene.
neXtProtNX_Q9H7X0.
PharmGKBPA164723438.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276305.
HOGENOMHOG000280717.
HOVERGENHBG061680.
InParanoidQ9H7X0.
OMAMTERMAQ.
OrthoDBEOG7M0NT7.
PhylomeDBQ9H7X0.
TreeFamTF323980.

Gene expression databases

ArrayExpressQ9H7X0.
BgeeQ9H7X0.
CleanExHS_NAT15.
GenevestigatorQ9H7X0.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNAA60. human.
GenomeRNAi79903.
NextBio69755.
PROQ9H7X0.
SOURCESearch...

Entry information

Entry nameNAA60_HUMAN
AccessionPrimary (citable) accession number: Q9H7X0
Secondary accession number(s): B3KRQ0 expand/collapse secondary AC list , B4DLZ0, B4DPZ8, B4DYC4, D3DUC2, E7EQ65, Q6IA31, Q6UX26
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 96 of the entry and version 1 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

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 16

Human chromosome 16: entries, gene names and cross-references to MIM