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Protein

N-alpha-acetyltransferase 10

Gene

NAA10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity (PubMed:15496142, PubMed:19826488, PubMed:19420222, PubMed:20145209, PubMed:27708256, PubMed:25489052). Acetylates amino termini that are devoid of initiator methionine (PubMed:19420222). The alpha (N-terminal) acetyltransferase 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 (PubMed:12464182). Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration (PubMed:19826488). Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development (PubMed:20145209). Acetylates HSPA1A and HSPA1B at 'Lys-77' which enhances its chaperone activity and leads to preferential binding to co-chaperone HOPX (PubMed:27708256). Acts as a negative regulator of sister chromatid cohesion during mitosis (PubMed:27422821).8 Publications

Catalytic activityi

Acetyl-CoA + an N-terminal-glycyl-[protein] = an N-terminal-N(alpha)-acetyl-glycyl-[protein] + CoA.3 Publications
Acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-alanyl-[protein] + CoA.3 Publications
Acetyl-CoA + an N-terminal-L-seryl-[protein] = an N-terminal-N(alpha)-acetyl-L-seryl-[protein] + CoA.3 Publications
Acetyl-CoA + an N-terminal-L-valyl-[protein] = an N-terminal-N(alpha)-acetyl-L-valyl-[protein] + CoA.3 Publications
Acetyl-CoA + an N-terminal-L-cysteinyl-[protein] = an N-terminal-N(alpha)-acetyl-L-cysteinyl-[protein] + CoA.3 Publications
Acetyl-CoA + an N-terminal-L-threonyl-[protein] = an N-terminal-N(alpha)-acetyl-L-threonyl-[protein] + CoA.3 Publications

GO - Molecular functioni

  • N-acetyltransferase activity Source: ProtInc
  • peptide alpha-N-acetyltransferase activity Source: UniProtKB
  • peptide-glutamate-N-acetyltransferase activity Source: GO_Central
  • peptide-serine-N-acetyltransferase activity Source: GO_Central

GO - Biological processi

  • DNA packaging Source: ProtInc
  • internal protein amino acid acetylation Source: ProtInc
  • negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric Source: UniProtKB
  • N-terminal peptidyl-glutamic acid acetylation Source: GO_Central
  • N-terminal peptidyl-serine acetylation Source: GO_Central
  • N-terminal protein amino acid acetylation Source: UniProtKB
  • protein acetylation Source: UniProtKB

Keywordsi

Molecular functionAcyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS02336-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
N-alpha-acetyltransferase 10 (EC:2.3.1.2553 Publications)
Alternative name(s):
N-terminal acetyltransferase complex ARD1 subunit homolog A
Short name:
hARD11 Publication
NatA catalytic subunit Naa10
Gene namesi
Name:NAA10
Synonyms:ARD1, ARD1A, TE2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

EuPathDBiHostDB:ENSG00000102030.15
HGNCiHGNC:18704 NAA10
MIMi300013 gene
neXtProtiNX_P41227

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

Pathology & Biotechi

Involvement in diseasei

N-terminal acetyltransferase deficiency (NATD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:300855
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06665237S → P in NATD; reduced N-terminal acetyltransferase activity; impaired interaction with NAA15 and NAA50; does not affect cytoplasmic localization. 2 PublicationsCorresponds to variant dbSNP:rs387906701EnsemblClinVar.1
Natural variantiVAR_07520643Y → S in NATD; decreased protein stability; strong decrease in N-terminal acetylation activity in vitro. 1 PublicationCorresponds to variant dbSNP:rs863225427EnsemblClinVar.1
Microphthalmia, syndromic, 1 (MCOPS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:309800

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi136K → R: Loss of its ability to acetylate HSPA1A and HSPA1B. 1 Publication1
Mutagenesisi209S → A: Abolishes phosphorylation by IKKB and reduces cell growth. 1 Publication1

Keywords - Diseasei

Disease mutation, Microphthalmia

Organism-specific databases

DisGeNETi8260
MalaCardsiNAA10
MIMi300855 phenotype
309800 phenotype
OpenTargetsiENSG00000102030
Orphaneti568 Microphthalmia, Lenz type
276432 Premature aging appearance-developmental delay-cardiac arrhythmia syndrome
PharmGKBiPA38648

Polymorphism and mutation databases

BioMutaiNAA10
DMDMi728880

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000745321 – 235N-alpha-acetyltransferase 10Add BLAST235

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei136N6-acetyllysine; by autocatalysis1 Publication1
Modified residuei182PhosphoserineCombined sources1
Modified residuei186PhosphoserineCombined sources1
Modified residuei205PhosphoserineCombined sources1
Modified residuei209Phosphoserine; by IKKB1 Publication1
Modified residuei213PhosphoserineCombined sources1
Modified residuei216PhosphoserineCombined sources1

Post-translational modificationi

Cleaved by caspases during apoptosis.
Phosphorylation by IKBKB/IKKB at Ser-209 promotes its proteasome-mediated degradation.1 Publication
Autoacetylated at Lys-136 which stimulates its catalytic activity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP41227
MaxQBiP41227
PaxDbiP41227
PeptideAtlasiP41227
PRIDEiP41227
TopDownProteomicsiP41227-1 [P41227-1]

PTM databases

iPTMnetiP41227
PhosphoSitePlusiP41227

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000102030
CleanExiHS_ARD1A
ExpressionAtlasiP41227 baseline and differential
GenevisibleiP41227 HS

Organism-specific databases

HPAiCAB006269
HPA030711

Interactioni

Subunit structurei

Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 and NAA15 or NAA16 (PubMed:20154145). 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 (PubMed:16507339). Binds to MYLK (PubMed:19826488). Associates with HYPK when in complex with NAA15 (PubMed:15496142). Interacts with NAA15 (PubMed:15496142). Interacts with NAA16 (PubMed:19480662). Interacts (via its C-terminal domain) with TSC2, leading to its acetylation (PubMed:20145209). Interacts with NAA16 (PubMed:19480662). Interacts with IKBKB (PubMed:19716809). Interacts with HSPA1A and HSPA1B leading to its acetylation (PubMed:27708256).9 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi113881, 63 interactors
IntActiP41227, 50 interactors
MINTiP41227
STRINGi9606.ENSP00000417763

Structurei

3D structure databases

ProteinModelPortaliP41227
SMRiP41227
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 NAA151 PublicationAdd BLAST58

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3235 Eukaryota
COG0456 LUCA
GeneTreeiENSGT00550000074803
HOGENOMiHOG000078523
HOVERGENiHBG050561
InParanoidiP41227
KOiK20791
OrthoDBiEOG091G0JI1
PhylomeDBiP41227
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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

        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 HLELKEKGRH VVLGAIENKV ESKGNSPPSS GEACREEKGL
210 220 230
AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06665237S → P in NATD; reduced N-terminal acetyltransferase activity; impaired interaction with NAA15 and NAA50; does not affect cytoplasmic localization. 2 PublicationsCorresponds to variant dbSNP:rs387906701EnsemblClinVar.1
Natural variantiVAR_07520643Y → S in NATD; decreased protein stability; strong decrease in N-terminal acetylation activity in vitro. 1 PublicationCorresponds to variant dbSNP:rs863225427EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_046205114 – 128Missing in isoform 2. CuratedAdd BLAST15
Alternative sequenceiVSP_046206129Q → R in isoform 2. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3 human [P41227-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiNAA10_HUMAN
AccessioniPrimary (citable) accession number: P41227
Secondary accession number(s): A6NM98
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 23, 2018
This is version 175 of the entry and version 1 of the sequence. See 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

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