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Information on EC 2.3.1.255 - N-terminal amino-acid Nalpha-acetyltransferase NatA and Organism(s) Mus musculus and UniProt Accession Q9QY36

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IUBMB Comments
N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine.
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Mus musculus
UNIPROT: Q9QY36
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(3 overall reactions are displayed. Show all (6)>>)
+
an N-terminal-glycyl-[protein]
=
an N-terminal-Nalpha-acetyl-glycyl-[protein]
+
+
an N-terminal-L-alanyl-[protein]
=
an N-terminal-Nalpha-acetyl-L-alanyl-[protein]
+
+
an N-terminal-L-seryl-[protein]
=
an N-terminal-Nalpha-acetyl-L-seryl-[protein]
+
Synonyms
naa15, ard1b, hnaa10, daf-31, naa11, n-terminal acetyltransferase a, arrest-defective protein 1, mtrimi, ta0058, n-alpha-acetyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ARD1198
variant
ARD1225
variant
ARD1235
variant
N-alpha-acetyltransferase 10
-
arrest-defective protein 1
-
-
N-alpha-acetyltransferase 11
-
NAA10
-
-
-
-
NAA15
-
-
-
-
NAT1
-
NAT1 and its co-subunit ARD1 assemble to form a functional acetyltransferase
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-terminal-Gly/Ala/Ser/Val/Cys/Thr-[protein] Nalpha-acetyltransferase
N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [Runx2]
[Runx2]-N-terminal-N6-acetyl-L-lysine + CoA
show the reaction diagram
NAA10 acetylates Runx2 at Lys225
-
-
?
acetyl-CoA + an N-terminal-lysinyl-[androgen receptor]
an N-terminal-Nalpha-acetyl-lysinyl-[androgen receptor] + CoA
show the reaction diagram
-
ARD1 acetylates androgen receptor at lysine 618
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [Runx2]
[Runx2]-N-terminal-N6-acetyl-L-lysine + CoA
show the reaction diagram
NAA10 acetylates Runx2 at Lys225
-
-
?
acetyl-CoA + an N-terminal-lysinyl-[androgen receptor]
an N-terminal-Nalpha-acetyl-lysinyl-[androgen receptor] + CoA
show the reaction diagram
-
ARD1 acetylates androgen receptor at lysine 618
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
caudal half region, immortalized embryonic endothelial cells
Manually annotated by BRENDA team
immortalized embryonic endothelial cells
Manually annotated by BRENDA team
NAA10 expression decreases with the induction of differentiation in NB4 cells, but the level of NAA11 remains unchanged
Manually annotated by BRENDA team
Naa10 is expressed in premeiotic spermatogonia
Manually annotated by BRENDA team
NAA11, a homologue of NAA10, is predominantly expressed in mouse testis. NAA10 and NAA11 display opposite expression patterns during spermatogenesis
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
ARD1 variants have different effects on hypoxia-inducible factor-1alpha stability and acetylation
physiological function
physiological function
importance of NAA10 catalytic activity in mouse development. The potential role of NAA10 varies depending on transcriptional levels in different tissues and embryonic stages during development. Naa10 homologue Naa11 has a role in the cellular differentiation process while Naa10 has a role in the cellular proliferation process. The differential expression pattern of Naa10 and Naa11 suggests that Naa11 is complementary to Naa10 at least in the mice and that its biological role can be important in spermiogenesis or cellular processes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NAA10_MOUSE
235
0
26520
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
x * 35000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
silencing of mouse immortalized embryonic endothelial cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression increases during dendritic development
in mouse, the expression of Naa10 is downregulated during meiosis
in mouse, the expression of Naa11 is upregulated during meiosis
throughout brain development, NAT1 and ARD1 are down-regulated as neurons differentiate
-
throughout brain development, NAT1 and ARD1 are highly expressed in areas of cell division and migration
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sugiura, N.; Adams, S.M.; Corriveau, R.A.
An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development
J. Biol. Chem.
278
40113-40120
2003
Mus musculus
Manually annotated by BRENDA team
Ohkawa, N.; Sugisaki, S.; Tokunaga, E.; Fujitani, K.; Hayasaka, T.; Setou, M.; Inokuchi, K.
N-acetyltransferase ARD1-NAT1 regulates neuronal dendritic development
Genes Cells
13
1171-1183
2008
Mus musculus (Q9QY36)
Manually annotated by BRENDA team
Kim, S.H.; Park, J.A.; Kim, J.H.; Lee, J.W.; Seo, J.H.; Jung, B.K.; Chun, K.H.; Jeong, J.W.; Bae, M.K.; Kim, K.W.
Characterization of ARD1 variants in mammalian cells
Biochem. Biophys. Res. Commun.
340
422-427
2006
Homo sapiens (P41227), Mus musculus (Q9QY36)
Manually annotated by BRENDA team
Yoon, H.; Kim, H.L.; Chun, Y.S.; Shin, D.H.; Lee, K.H.; Shin, C.S.; Lee, D.Y.; Kim, H.H.; Lee, Z.H.; Ryoo, H.M.; Lee, M.N.; Oh, G.T.; Park, J.W.
NAA10 controls osteoblast differentiation and bone formation as a feedback regulator of Runx2
Nat. Commun.
5
5176
2014
Mus musculus (Q9QY36)
Manually annotated by BRENDA team
DePaolo, J.S.; Wang, Z.; Guo, J.; Zhang, G.; Qian, C.; Zhang, H.; Zabaleta, J.; Liu, W.
Acetylation of androgen receptor by ARD1 promotes dissociation from HSP90 complex and prostate tumorigenesis
Oncotarget
7
71417-71428
2016
Mus musculus
Manually annotated by BRENDA team
Lee, M.N.; Kweon, H.Y.; Oh, G.T.
N-alpha-acetyltransferase 10 (NAA10) in development the role of NAA10
Exp. Mol. Med.
50
1-11
2018
Arabidopsis thaliana (Q9FKI4), Caenorhabditis elegans (O61219), Caenorhabditis elegans DAF-31 (O61219), Danio rerio (Q7T3B8), Drosophila melanogaster (Q9VT75), Homo sapiens (P41227), Mus musculus (Q3UX61), Mus musculus (Q9QY36), Mus musculus C57Bl6/J (Q3UX61), Mus musculus C57Bl6/J (Q9QY36), Saccharomyces cerevisiae (P07347 AND P12945), Saccharomyces cerevisiae ATCC 204508 (P07347 AND P12945), Trypanosoma brucei (Q9NFL8)
Manually annotated by BRENDA team
Xu, H.; Han, Y.; Liu, B.; Li, R.
Unc-5 homolog B (UNC5B) is one of the key downstream targets of N-alpha-acetyltransferase 10 (Naa10)
Sci. Rep.
6
38508
2016
Homo sapiens (P41227), Mus musculus (Q9QY36), Mus musculus C57 (Q9QY36)
Manually annotated by BRENDA team