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Q9QY36

- NAA10_MOUSE

UniProt

Q9QY36 - NAA10_MOUSE

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Protein

N-alpha-acetyltransferase 10

Gene

Naa10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. ribosome binding Source: Ensembl

GO - Biological processi

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

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. NatA complex Source: Ensembl
  3. nucleolus Source: Ensembl
Complete GO annotation...

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

BgeeiQ9QY36.
ExpressionAtlasiQ9QY36. baseline and differential.
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

        10         20         30         40         50
MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG
60 70 80 90 100
KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE
110 120 130 140 150
NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD
160 170 180 190 200
LTQMADELRR HLELKEKGKH MVLAALENKA ENKGNVLLSS GEACREEKGL
210 220 230
AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS
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

Bgeei Q9QY36.
ExpressionAtlasi Q9QY36. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 107 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