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P41227

- NAA10_HUMAN

UniProt

P41227 - NAA10_HUMAN

Protein

N-alpha-acetyltransferase 10

Gene

NAA10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. 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.4 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. N-acetyltransferase activity Source: ProtInc
    2. peptide alpha-N-acetyltransferase activity Source: UniProtKB-EC
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA packaging Source: ProtInc
    2. internal protein amino acid acetylation Source: ProtInc
    3. N-terminal protein amino acid acetylation Source: UniProtKB

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:18704. NAA10.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: According to PubMed:12464182 it is cytoplasmic. According to PubMed:15496142, it is nuclear and cytoplasmic. Also present in the free cytosolic and cytoskeleton-bound polysomes.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. intracellular Source: LIFEdb
    3. membrane Source: UniProtKB
    4. NatA complex Source: UniProt
    5. nucleolus Source: HPA
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    N-terminal acetyltransferase deficiency (NATD) [MIM:300855]: An enzymatic deficiency resulting in postnatal growth failure with severe delays and dysmorphic features. It is clinically characterized by wrinkled forehead, prominent eyes, widely opened anterior and posterior fontanels, downsloping palpebral fissures, thickened lids, large ears, flared nares, hypoplastic alae, short columella, protruding upper lip, and microretrognathia. There are also delayed closing of fontanels and broad great toes. Skin is characterized by redundancy or laxity with minimal subcutaneous fat, cutaneous capillary malformations, and very fine hair and eyebrows. Death results from cardiogenic shock following arrhythmia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371S → P in NATD; in vitro assays of protein function demonstrates 60 to 80% reduction in NAT activity of the mutant protein toward the in vivo substrate RPP30 protein; the activity toward the substrate HMGA1 protein is reduced by only 20%. 1 Publication
    VAR_066652
    Microphthalmia, syndromic, 1 (MCOPS1) [MIM:309800]: A rare syndrome defined by the canonical features of unilateral or bilateral microphthalmia or anophthalmia and defects in the skeletal and genitourinary systems. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. Anomalies of the digits, teeth, and ears are hallmarks of MCOPS1. Intellectual disability ranges from mild to severe, with self-mutilating behaviors and seizures in severely affected MCOPS1 individuals.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi209 – 2091S → A: Abolishes phosphorylation by IKKB and reduces cell growth. 1 Publication

    Keywords - Diseasei

    Disease mutation, Microphthalmia

    Organism-specific databases

    MIMi300855. phenotype.
    309800. phenotype.
    Orphaneti568. Microphthalmia, Lenz type.
    276432. Premature ageing appearance-developmental delay-cardiac arrhythmia syndrome.
    PharmGKBiPA38648.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 235235N-alpha-acetyltransferase 10PRO_0000074532Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei182 – 1821Phosphoserine3 Publications
    Modified residuei186 – 1861Phosphoserine1 Publication
    Modified residuei205 – 2051Phosphoserine3 Publications
    Modified residuei209 – 2091Phosphoserine; by IKKB1 Publication
    Modified residuei213 – 2131Phosphoserine1 Publication
    Modified residuei216 – 2161Phosphoserine1 Publication

    Post-translational modificationi

    Cleaved by caspases during apoptosis.
    Phosphorylation by IKBKB/IKKB at Ser-209 promotes its proteasome-mediated degradation.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP41227.
    PaxDbiP41227.
    PRIDEiP41227.

    PTM databases

    PhosphoSiteiP41227.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiP41227.
    BgeeiP41227.
    CleanExiHS_ARD1A.
    GenevestigatoriP41227.

    Organism-specific databases

    HPAiCAB006269.
    HPA030711.

    Interactioni

    Subunit structurei

    Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 and NAA15 or NAA16. Interacts with HIF1A (via its ODD domain); the interaction increases HIF1A protein stability during normoxia, an down-regulates it when induced by hypoxia. Interacts with NAA50 and with the ribosome. Binds to MYLK. Associates with HYPK when in complex with NAA15. Interacts (via its C-terminal domain) with TSC2, leading to its acetylation.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARHGEF6Q150523EBI-747693,EBI-1642523
    ARHGEF7Q141553EBI-747693,EBI-717515
    Arhgef7O550433EBI-747693,EBI-3649585From a different organism.
    NAA50Q9GZZ12EBI-747693,EBI-1052523

    Protein-protein interaction databases

    BioGridi113881. 20 interactions.
    IntActiP41227. 16 interactions.
    MINTiMINT-1499850.
    STRINGi9606.ENSP00000417763.

    Structurei

    3D structure databases

    ProteinModelPortaliP41227.
    SMRiP41227. 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 NAA15Add
    BLAST

    Sequence similaritiesi

    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0456.
    HOGENOMiHOG000078523.
    HOVERGENiHBG050561.
    InParanoidiP41227.
    KOiK00670.
    PhylomeDBiP41227.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P41227-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG    50
    KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE 100
    NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD 150
    LTQMADELRR HLELKEKGRH VVLGAIENKV ESKGNSPPSS GEACREEKGL 200
    AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS 235
    Length:235
    Mass (Da):26,459
    Last modified:February 1, 1995 - v1
    Checksum:i6393A907F5C2DDC4
    GO
    Isoform 2 (identifier: P41227-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         114-128: Missing.
         129-129: Q → R

    Show »
    Length:220
    Mass (Da):24,784
    Checksum:iFF22A79BB1ACA0BC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371S → P in NATD; in vitro assays of protein function demonstrates 60 to 80% reduction in NAT activity of the mutant protein toward the in vivo substrate RPP30 protein; the activity toward the substrate HMGA1 protein is reduced by only 20%. 1 Publication
    VAR_066652

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei114 – 12815Missing in isoform 2. CuratedVSP_046205Add
    BLAST
    Alternative sequencei129 – 1291Q → R in isoform 2. CuratedVSP_046206

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77588 mRNA. Translation: CAA54691.1.
    U52112 Genomic DNA. No translation available.
    CH471172 Genomic DNA. Translation: EAW72774.1.
    BC000308 mRNA. Translation: AAH00308.1.
    BC019312 mRNA. Translation: AAH19312.1.
    CCDSiCCDS14737.1. [P41227-1]
    CCDS59179.1. [P41227-2]
    PIRiI38333.
    RefSeqiNP_001243048.1. NM_001256119.1. [P41227-2]
    NP_003482.1. NM_003491.3. [P41227-1]
    UniGeneiHs.433291.

    Genome annotation databases

    EnsembliENST00000370009; ENSP00000359026; ENSG00000102030. [P41227-2]
    ENST00000464845; ENSP00000417763; ENSG00000102030. [P41227-1]
    GeneIDi8260.
    KEGGihsa:8260.
    UCSCiuc004fjm.2. human. [P41227-1]
    uc004fjn.2. human.

    Polymorphism databases

    DMDMi728880.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77588 mRNA. Translation: CAA54691.1 .
    U52112 Genomic DNA. No translation available.
    CH471172 Genomic DNA. Translation: EAW72774.1 .
    BC000308 mRNA. Translation: AAH00308.1 .
    BC019312 mRNA. Translation: AAH19312.1 .
    CCDSi CCDS14737.1. [P41227-1 ]
    CCDS59179.1. [P41227-2 ]
    PIRi I38333.
    RefSeqi NP_001243048.1. NM_001256119.1. [P41227-2 ]
    NP_003482.1. NM_003491.3. [P41227-1 ]
    UniGenei Hs.433291.

    3D structure databases

    ProteinModelPortali P41227.
    SMRi P41227. Positions 1-152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113881. 20 interactions.
    IntActi P41227. 16 interactions.
    MINTi MINT-1499850.
    STRINGi 9606.ENSP00000417763.

    PTM databases

    PhosphoSitei P41227.

    Polymorphism databases

    DMDMi 728880.

    Proteomic databases

    MaxQBi P41227.
    PaxDbi P41227.
    PRIDEi P41227.

    Protocols and materials databases

    DNASUi 8260.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370009 ; ENSP00000359026 ; ENSG00000102030 . [P41227-2 ]
    ENST00000464845 ; ENSP00000417763 ; ENSG00000102030 . [P41227-1 ]
    GeneIDi 8260.
    KEGGi hsa:8260.
    UCSCi uc004fjm.2. human. [P41227-1 ]
    uc004fjn.2. human.

    Organism-specific databases

    CTDi 8260.
    GeneCardsi GC0XM153194.
    HGNCi HGNC:18704. NAA10.
    HPAi CAB006269.
    HPA030711.
    MIMi 300013. gene.
    300855. phenotype.
    309800. phenotype.
    neXtProti NX_P41227.
    Orphaneti 568. Microphthalmia, Lenz type.
    276432. Premature ageing appearance-developmental delay-cardiac arrhythmia syndrome.
    PharmGKBi PA38648.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0456.
    HOGENOMi HOG000078523.
    HOVERGENi HBG050561.
    InParanoidi P41227.
    KOi K00670.
    PhylomeDBi P41227.
    TreeFami TF300078.

    Miscellaneous databases

    ChiTaRSi NAA10. human.
    GeneWikii ARD1A.
    GenomeRNAii 8260.
    NextBioi 31019.
    PROi P41227.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P41227.
    Bgeei P41227.
    CleanExi HS_ARD1A.
    Genevestigatori P41227.

    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. "Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae."
      Tribioli C., Mancini M., Plassart E., Bione S., Rivella S., Sala C., Torri G., Toniolo D.
      Hum. Mol. Genet. 3:1061-1068(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Identification and characterization of the human ARD1-NATH protein acetyltransferase complex."
      Arnesen T., Anderson D., Baldersheim C., Lanotte M., Varhaug J.E., Lillehaug J.R.
      Biochem. J. 386:433-443(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NAA15 AND RIBOSOMAL PROTEINS.
      Tissue: Thyroid carcinoma.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] (ISOFORM 1).
      Tissue: Lung.
    6. "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: INTERACTION WITH HIF1A, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex."
      Arnesen T., Anderson D., Torsvik J., Halseth H.B., Varhaug J.E., Lillehaug J.R.
      Gene 371:291-295(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NAA50.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "A novel human NatA Nalpha-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)."
      Arnesen T., Gromyko D., Kagabo D., Betts M.J., Starheim K.K., Varhaug J.E., Anderson D., Lillehaug J.R.
      BMC Biochem. 10:15-15(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NAA16.
    12. "A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates."
      Polevoda B., Arnesen T., Sherman F.
      BMC Proc. 3:S2-S2(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    13. "Phosphorylation of ARD1 by IKKbeta contributes to its destabilization and degradation."
      Kuo H.P., Lee D.F., Xia W., Lai C.C., Li L.Y., Hung M.C.
      Biochem. Biophys. Res. Commun. 389:156-161(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-209 BY IKBKB, MUTAGENESIS OF SER-209, INTERACTION WITH IKBKB.
    14. "Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase."
      Shin D.H., Chun Y.-S., Lee K.-H., Shin H.-W., Park J.-W.
      PLoS ONE 4:E7451-E7451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYLK.
    15. "The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation."
      Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H., Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.
      Mol. Cell. Biol. 30:1898-1909(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    16. Cited for: INTERACTION WITH TSC2, FUNCTION IN ACETYLATION OF TSC2.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-205; SER-213 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "A splice donor mutation in NAA10 results in the dysregulation of the retinoic acid signalling pathway and causes Lenz microphthalmia syndrome."
      Esmailpour T., Riazifar H., Liu L., Donkervoort S., Huang V.H., Madaan S., Shoucri B.M., Busch A., Wu J., Towbin A., Chadwick R.B., Sequeira A., Vawter M.P., Sun G., Johnston J.J., Biesecker L.G., Kawaguchi R., Sun H., Kimonis V., Huang T.
      J. Med. Genet. 51:185-196(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MCOPS1.
    21. Cited for: VARIANT NATD PRO-37, CHARACTERIZATION OF VARIANT NATD PRO-37.

    Entry informationi

    Entry nameiNAA10_HUMAN
    AccessioniPrimary (citable) accession number: P41227
    Secondary accession number(s): A6NM98
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3