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Q9DBU2 (NAA60_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
N-acetyltransferase 15
NatF catalytic subunit
Gene names
Name:Naa60
Synonyms:Nat15
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length242 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

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

Subcellular location

Golgi apparatus membrane By similarity.

Post-translational modification

Acetylated: autoacetylation is required for optimal acetyltransferase activity By similarity.

Sequence similarities

Belongs to the acetyltransferase family. NAA60 subfamily.

Contains 1 N-acetyltransferase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 242242N-alpha-acetyltransferase 60
PRO_0000321567

Regions

Domain13 – 182170N-acetyltransferase

Amino acid modifications

Modified residue791N6-acetyllysine; by autocatalysis By similarity
Modified residue1051N6-acetyllysine; by autocatalysis By similarity
Modified residue1091N6-acetyllysine; by autocatalysis By similarity
Modified residue1211N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DBU2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F2307B2007F13F84

FASTA24227,507
        10         20         30         40         50         60 
MTEVVPSSAL SEVSLRLLCH DDIDTVKHLC GDWFPIEYPD SWYRDITSNK KFFSLAATYR 

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

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

       190        200        210        220        230        240 
INGGHPPWTI LDYIQHLGSA LANLSPCSIP HRIYRQAHSL LCSFLPWSSI STKGGIEYSR 


TM 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Lung and Thymus.
[2]"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].
Strain: NMRI.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004750 mRNA. Translation: BAB23531.1.
AK088736 mRNA. Translation: BAC40538.1.
BC004837 mRNA. Translation: AAH04837.1.
CCDSCCDS37239.1.
RefSeqNP_001277618.1. NM_001290689.1.
NP_083366.1. NM_029090.3.
XP_006522742.1. XM_006522679.1.
XP_006522743.1. XM_006522680.1.
UniGeneMm.28403.

3D structure databases

ProteinModelPortalQ9DBU2.
SMRQ9DBU2. Positions 11-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000006138.

PTM databases

PhosphoSiteQ9DBU2.

Proteomic databases

PRIDEQ9DBU2.

Protocols and materials databases

DNASU74763.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006138; ENSMUSP00000006138; ENSMUSG00000005982.
ENSMUST00000115860; ENSMUSP00000111526; ENSMUSG00000005982.
ENSMUST00000150655; ENSMUSP00000135206; ENSMUSG00000005982.
GeneID74763.
KEGGmmu:74763.
UCSCuc007xyw.1. mouse.

Organism-specific databases

CTD79903.
MGIMGI:1922013. Naa60.

Phylogenomic databases

eggNOGNOG276305.
GeneTreeENSGT00390000008314.
HOGENOMHOG000280717.
HOVERGENHBG061680.
InParanoidQ9DBU2.
OMAPPWTILI.
TreeFamTF323980.

Gene expression databases

ArrayExpressQ9DBU2.
BgeeQ9DBU2.
GenevestigatorQ9DBU2.

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

NextBio341584.
PROQ9DBU2.
SOURCESearch...

Entry information

Entry nameNAA60_MOUSE
AccessionPrimary (citable) accession number: Q9DBU2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot