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Protein

N-alpha-acetyltransferase 10

Gene

Naa10

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

Functioni

Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity (PubMed:12888564). Acetylates amino termini that are devoid of initiator methionine (By similarity). The alpha (N-terminal) acetyltransferase activity may be important for vascular, hematopoietic and neuronal growth and development (By similarity). Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation (PubMed:12464182). Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration (By similarity). Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development (By similarity). Acetylates HSPA1A and HSPA1B at 'Lys-77' which enhances its chaperone activity and leads to preferential binding to co-chaperone HOPX (By similarity). Acts as a negative regulator of sister chromatid cohesion during mitosis (By similarity).By similarity2 Publications

Catalytic activityi

Acetyl-CoA + an N-terminal-glycyl-[protein] = an N-terminal-N(alpha)-acetyl-glycyl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-alanyl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-seryl-[protein] = an N-terminal-N(alpha)-acetyl-L-seryl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-valyl-[protein] = an N-terminal-N(alpha)-acetyl-L-valyl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-cysteinyl-[protein] = an N-terminal-N(alpha)-acetyl-L-cysteinyl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-threonyl-[protein] = an N-terminal-N(alpha)-acetyl-L-threonyl-[protein] + CoA.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
N-alpha-acetyltransferase 10 (EC:2.3.1.255By similarity)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1915255. Naa10.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000745331 – 235N-alpha-acetyltransferase 10Add BLAST235

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei136N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei205PhosphoserineBy similarity1
Modified residuei209Phosphoserine; by IKKBBy similarity1
Modified residuei213PhosphoserineBy similarity1
Modified residuei216PhosphoserineBy similarity1

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.
Autoacetylated at Lys-136 which stimulates its catalytic activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9QY36.
MaxQBiQ9QY36.
PaxDbiQ9QY36.
PRIDEiQ9QY36.

PTM databases

iPTMnetiQ9QY36.
PhosphoSitePlusiQ9QY36.

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

BgeeiENSMUSG00000031388.
ExpressionAtlasiQ9QY36. baseline and differential.
GenevisibleiQ9QY36. MM.

Interactioni

Subunit structurei

Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 and NAA15 or NAA16 (By similarity). Interacts with HIF1A (via its ODD domain); the interaction increases HIF1A protein stability during normoxia, an down-regulates it when induced by hypoxia (PubMed:12464182). Interacts with NAA50 and with the ribosome (By similarity). Binds to MYLK (By similarity). Associates with HYPK when in complex with NAA15 (By similarity). Interacts with NAA15 (PubMed:12888564). Interacts with NAA16 (By similarity). Interacts (via its C-terminal domain) with TSC2, leading to its acetylation (By similarity). Interacts with NAA16 (By similarity). Interacts with IKBKB (By similarity). Interacts with HSPA1A and HSPA1B leading to its acetylation (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi207880. 38 interactors.
IntActiQ9QY36. 37 interactors.
STRINGi10090.ENSMUSP00000033763.

Structurei

3D structure databases

ProteinModelPortaliQ9QY36.
SMRiQ9QY36.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 152N-acetyltransferasePROSITE-ProRule annotationAdd BLAST152

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 58Interaction with NAA15By similarityAdd BLAST58

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3235. Eukaryota.
COG0456. LUCA.
GeneTreeiENSGT00550000074803.
HOGENOMiHOG000078523.
HOVERGENiHBG050561.
InParanoidiQ9QY36.
KOiK20791.
OrthoDBiEOG091G0JI1.
PhylomeDBiQ9QY36.
TreeFamiTF300078.

Family and domain databases

InterProiView protein in InterPro
IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
PfamiView protein in Pfam
PF00583. Acetyltransf_1. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiView protein in PROSITE
PS51186. GNAT. 1 hit.

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:
EMBLi
GenBanki
DDBJi
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.

Similar proteinsi

Entry informationi

Entry nameiNAA10_MOUSE
AccessioniPrimary (citable) accession number: Q9QY36
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: May 1, 2000
Last modified: October 25, 2017
This is version 131 of the entry and version 1 of the sequence. See 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