N-alpha-acetyltransferase 20

NAA20

Identifiers

NAA20, NAT3, NAT3P, NAT5, NAT5P, dJ1002M8.1, N(alpha)-acetyltransferase 20, NatB catalytic subunit, N-alpha-acetyltransferase 20, NatB catalytic subunit, MRT73

External IDs

OMIM: 610833; MGI: 1915127; GeneCards: NAA20

Enzyme activity
EC #	BRENDA	ExPASy	KEGG	MetaCyc
2.3.1.254	↗	↗	↗	↗

Gene location (Human)

Chr.	Chromosome 20 (human)

Band	20p11.23	Start	20,017,310 bp
Band	20p11.23	End	20,033,655 bp

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)

Band	2 G1\|2 71.28 cM	Start	145,744,019 bp
Band	2 G1\|2 71.28 cM	End	145,758,345 bp

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

islet of Langerhans

tibialis anterior muscle

mucosa of pharynx

gingival epithelium

oral cavity

skin of arm

body of pancreas

right testis

deltoid muscle

left testis

Top expressed in

heart

quadriceps femoris muscle

epiblast

embryo

neural tube

right kidney

mesencephalon

ventricular zone

lip

thymus

More reference expression data

n/a

Gene ontology
Molecular function	transferase activity acyltransferase activity peptide alpha-N-acetyltransferase activity
Cellular component	intracellular anatomical structure NatB complex cytosol nucleus cytoplasm
Biological process	N-terminal peptidyl-methionine acetylation
Sources:Amigo / QuickGO

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


51126


67877


ENSG00000173418


ENSMUSG00000002728


P61599


P61600

RefSeq (mRNA)


NM_181528 NM_016100 NM_181527


NM_001141965 NM_026425

RefSeq (protein)


NP_057184 NP_852668 NP_852669


NP_001135437 NP_080701

Location (UCSC)

Chr 20: 20.02 – 20.03 Mb

Chr 2: 145.74 – 145.76 Mb

PubMed search

View/Edit Human

View/Edit Mouse

N-alpha-acetyltransferase 20 is an enzyme that in humans is encoded by the NAA20 gene (previously NAT5). The NAA20 protein binds to NAA25 to form the NatB complex (N-acetyltransferase complex B) which acetylates certain methionine residues. It is the catalytic subunit.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000173418 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000002728 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Sugiura N, Adams SM, Corriveau RA (Oct 2003). "An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development". J Biol Chem. 278 (41): 40113–20. doi:10.1074/jbc.M301218200. PMID 12888564.
1 2 "Entrez Gene: NAT5 N-acetyltransferase 5".
↑ "N-alpha-acetyltransferase 20". uniprot.org. UniProt consortium. Retrieved 2026-09-09.

Further reading

Vitale N, Pacheco-Rodriguez G, Ferrans VJ, et al. (2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)". J. Biol. Chem. 275 (28): 21331–9. doi:10.1074/jbc.M909642199. PMID 10748148.
Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Polevoda B, Cardillo TS, Doyle TC, et al. (2003). "Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin". J. Biol. Chem. 278 (33): 30686–97. doi:10.1074/jbc.M304690200. PMID 12783868.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to Biology: A Functional Genomics Pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
Arnesen T, Anderson D, Torsvik J, et al. (2006). "Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex". Gene. 371 (2): 291–5. doi:10.1016/j.gene.2005.12.008. PMID 16507339.
Sánchez-Puig N, Fersht AR (2006). "Characterization of the native and fibrillar conformation of the human Nα-acetyltransferase ARD1". Protein Sci. 15 (8): 1968–76. doi:10.1110/ps.062264006. PMC 2242591. PMID 16823041.

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