Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9QY36

- NAA10_MOUSE

UniProt

Q9QY36 - NAA10_MOUSE

Protein

N-alpha-acetyltransferase 10

Gene

Naa10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic subunit of the N-terminal acetyltransferase A (NatC) complex which displays alpha (N-terminal) acetyltransferase activity. Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation. Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration. Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development By similarity.By similarity

    Catalytic activityi

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

    GO - Molecular functioni

    1. N-acetyltransferase activity Source: MGI
    2. peptide alpha-N-acetyltransferase activity Source: UniProtKB-EC
    3. protein binding Source: MGI
    4. ribosome binding Source: Ensembl

    GO - Biological processi

    1. N-terminal protein amino acid acetylation Source: Ensembl

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-alpha-acetyltransferase 10 (EC:2.3.1.-, EC:2.3.1.88)
    Alternative name(s):
    N-terminal acetyltransferase complex ARD1 subunit homolog A
    NatA catalytic subunit Naa10
    Gene namesi
    Name:Naa10
    Synonyms:Ard1, Ard1a, Te2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1915255. Naa10.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 235235N-alpha-acetyltransferase 10PRO_0000074533Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei205 – 2051PhosphoserineBy similarity
    Modified residuei209 – 2091Phosphoserine; by IKKBBy similarity
    Modified residuei213 – 2131PhosphoserineBy similarity
    Modified residuei216 – 2161PhosphoserineBy similarity

    Post-translational modificationi

    Cleaved by caspases during apoptosis.By similarity
    Phosphorylation by IKBKB/IKKB at Ser-209 destabilises NAA10 and promotes its proteasome-mediated degradation.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9QY36.
    PaxDbiQ9QY36.
    PRIDEiQ9QY36.

    PTM databases

    PhosphoSiteiQ9QY36.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Developmental stagei

    Expressed throughout the developing brain from E11.5 through E17, continues to be expressed at P0, but then is down-regulated.1 Publication

    Gene expression databases

    ArrayExpressiQ9QY36.
    BgeeiQ9QY36.
    GenevestigatoriQ9QY36.

    Interactioni

    Subunit structurei

    Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 and NAA15 or NAA16. Interacts with the ribosome. Binds to MYLK. Associates with HYPK when in complex with NAA15 By similarity. Interacts with HIF1A and NAA50. Interacts (via its C-terminal domain) with TSC2, leading to its acetylation By similarity.By similarity

    Protein-protein interaction databases

    BioGridi207880. 8 interactions.
    IntActiQ9QY36. 7 interactions.
    STRINGi10090.ENSMUSP00000033763.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QY36.
    SMRiQ9QY36. Positions 1-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 152152N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 5858Interaction with NAA15By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0456.
    GeneTreeiENSGT00550000074803.
    HOGENOMiHOG000078523.
    HOVERGENiHBG050561.
    InParanoidiQ9QY36.
    KOiK00670.
    OrthoDBiEOG7T4MMM.
    PhylomeDBiQ9QY36.
    TreeFamiTF300078.

    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.

    Q9QY36-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG    50
    KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE 100
    NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD 150
    LTQMADELRR HLELKEKGKH MVLAALENKA ENKGNVLLSS GEACREEKGL 200
    AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS 235
    Length:235
    Mass (Da):26,520
    Last modified:May 1, 2000 - v1
    Checksum:iAD2991C519277F29
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014469 mRNA. Translation: BAB29373.1.
    AF133093 Genomic DNA. No translation available.
    CCDSiCCDS30217.1.
    RefSeqiNP_063923.1. NM_019870.3.
    UniGeneiMm.246654.

    Genome annotation databases

    EnsembliENSMUST00000033763; ENSMUSP00000033763; ENSMUSG00000031388.
    GeneIDi56292.
    KEGGimmu:56292.
    UCSCiuc009tng.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014469 mRNA. Translation: BAB29373.1 .
    AF133093 Genomic DNA. No translation available.
    CCDSi CCDS30217.1.
    RefSeqi NP_063923.1. NM_019870.3.
    UniGenei Mm.246654.

    3D structure databases

    ProteinModelPortali Q9QY36.
    SMRi Q9QY36. Positions 1-152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207880. 8 interactions.
    IntActi Q9QY36. 7 interactions.
    STRINGi 10090.ENSMUSP00000033763.

    PTM databases

    PhosphoSitei Q9QY36.

    Proteomic databases

    MaxQBi Q9QY36.
    PaxDbi Q9QY36.
    PRIDEi Q9QY36.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033763 ; ENSMUSP00000033763 ; ENSMUSG00000031388 .
    GeneIDi 56292.
    KEGGi mmu:56292.
    UCSCi uc009tng.2. mouse.

    Organism-specific databases

    CTDi 8260.
    MGIi MGI:1915255. Naa10.

    Phylogenomic databases

    eggNOGi COG0456.
    GeneTreei ENSGT00550000074803.
    HOGENOMi HOG000078523.
    HOVERGENi HBG050561.
    InParanoidi Q9QY36.
    KOi K00670.
    OrthoDBi EOG7T4MMM.
    PhylomeDBi Q9QY36.
    TreeFami TF300078.

    Miscellaneous databases

    NextBioi 312200.
    PROi Q9QY36.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QY36.
    Bgeei Q9QY36.
    Genevestigatori Q9QY36.

    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. "Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation."
      Jeong J.-W., Bae M.-K., Ahn M.-Y., Kim S.-H., Sohn T.-K., Bae M.-H., Yoo M.-A., Song E.-J., Lee K.-J., Kim K.-W.
      Cell 111:709-720(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HIF1A.
      Tissue: Embryo and T-cell.
    2. "An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development."
      Sugiura N., Adams S.M., Corriveau R.A.
      J. Biol. Chem. 278:40113-40120(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NAA15, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "Comparative sequence analysis of the mouse L1cam locus and the corresponding region of human Xq28."
      Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A., Rosenthal A.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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.
      Tissue: Embryonic liver.

    Entry informationi

    Entry nameiNAA10_MOUSE
    AccessioniPrimary (citable) accession number: Q9QY36
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 106 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