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Q9DBU2

- NAA60_MOUSE

UniProt

Q9DBU2 - NAA60_MOUSE

Protein

N-alpha-acetyltransferase 60

Gene

Naa60

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.
    Acetyl-CoA + [histone] = CoA + acetyl-[histone].

    GO - Molecular functioni

    1. H4 histone acetyltransferase activity Source: UniProtKB
    2. peptide alpha-N-acetyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. chromosome segregation Source: UniProtKB
    3. histone H4 acetylation Source: UniProtKB
    4. N-terminal peptidyl-methionine acetylation Source: UniProtKB
    5. nucleosome assembly Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Chromatin regulator, Transferase

    Keywords - Biological processi

    Chromosome partition

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Naa60
    Synonyms:Nat15
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:1922013. Naa60.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 242242N-alpha-acetyltransferase 60PRO_0000321567Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791N6-acetyllysine; by autocatalysisBy similarity
    Modified residuei105 – 1051N6-acetyllysine; by autocatalysisBy similarity
    Modified residuei109 – 1091N6-acetyllysine; by autocatalysisBy similarity
    Modified residuei121 – 1211N6-acetyllysine; by autocatalysisBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ9DBU2.

    PTM databases

    PhosphoSiteiQ9DBU2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9DBU2.
    BgeeiQ9DBU2.
    GenevestigatoriQ9DBU2.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000006138.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBU2.
    SMRiQ9DBU2. Positions 11-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 182170N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG276305.
    GeneTreeiENSGT00390000008314.
    HOGENOMiHOG000280717.
    HOVERGENiHBG061680.
    InParanoidiQ9DBU2.
    OMAiPPWTILI.
    TreeFamiTF323980.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view]
    PfamiPF00583. Acetyltransf_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9DBU2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEVVPSSAL SEVSLRLLCH DDIDTVKHLC GDWFPIEYPD SWYRDITSNK    50
    KFFSLAATYR GAIVGMIVAE IKNRTKIHKE DGDILASSFS VDTQVAYILS 100
    LGVVKEFRKH GIGSLLLESL KDHISTTAQD HCKAIYLHVL TTNNTAINFY 150
    ENRDFRQHHY LPYYYSIRGV LKDGFTYVLY INGGHPPWTI LDYIQHLGSA 200
    LANLSPCSIP HRIYRQAHSL LCSFLPWSSI STKGGIEYSR TM 242
    Length:242
    Mass (Da):27,507
    Last modified:June 1, 2001 - v1
    Checksum:iF2307B2007F13F84
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004750 mRNA. Translation: BAB23531.1.
    AK088736 mRNA. Translation: BAC40538.1.
    BC004837 mRNA. Translation: AAH04837.1.
    CCDSiCCDS37239.1.
    RefSeqiNP_001277618.1. NM_001290689.1.
    NP_083366.1. NM_029090.3.
    XP_006522742.1. XM_006522679.1.
    XP_006522743.1. XM_006522680.1.
    UniGeneiMm.28403.

    Genome annotation databases

    EnsembliENSMUST00000006138; ENSMUSP00000006138; ENSMUSG00000005982.
    ENSMUST00000115860; ENSMUSP00000111526; ENSMUSG00000005982.
    ENSMUST00000150655; ENSMUSP00000135206; ENSMUSG00000005982.
    GeneIDi74763.
    KEGGimmu:74763.
    UCSCiuc007xyw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004750 mRNA. Translation: BAB23531.1 .
    AK088736 mRNA. Translation: BAC40538.1 .
    BC004837 mRNA. Translation: AAH04837.1 .
    CCDSi CCDS37239.1.
    RefSeqi NP_001277618.1. NM_001290689.1.
    NP_083366.1. NM_029090.3.
    XP_006522742.1. XM_006522679.1.
    XP_006522743.1. XM_006522680.1.
    UniGenei Mm.28403.

    3D structure databases

    ProteinModelPortali Q9DBU2.
    SMRi Q9DBU2. Positions 11-181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000006138.

    PTM databases

    PhosphoSitei Q9DBU2.

    Proteomic databases

    PRIDEi Q9DBU2.

    Protocols and materials databases

    DNASUi 74763.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006138 ; ENSMUSP00000006138 ; ENSMUSG00000005982 .
    ENSMUST00000115860 ; ENSMUSP00000111526 ; ENSMUSG00000005982 .
    ENSMUST00000150655 ; ENSMUSP00000135206 ; ENSMUSG00000005982 .
    GeneIDi 74763.
    KEGGi mmu:74763.
    UCSCi uc007xyw.1. mouse.

    Organism-specific databases

    CTDi 79903.
    MGIi MGI:1922013. Naa60.

    Phylogenomic databases

    eggNOGi NOG276305.
    GeneTreei ENSGT00390000008314.
    HOGENOMi HOG000280717.
    HOVERGENi HBG061680.
    InParanoidi Q9DBU2.
    OMAi PPWTILI.
    TreeFami TF323980.

    Miscellaneous databases

    NextBioi 341584.
    PROi Q9DBU2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DBU2.
    Bgeei Q9DBU2.
    Genevestigatori Q9DBU2.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view ]
    Pfami PF00583. Acetyltransf_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    PROSITEi PS51186. GNAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiNAA60_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3