P61599 (NAA20_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-alpha-acetyltransferase 20
EC=2.3.1.88

Alternative name(s):
N-acetyltransferase 5
N-terminal acetyltransferase B complex catalytic subunit NAA20
N-terminal acetyltransferase B complex catalytic subunit NAT5
Short name=NatB complex subunit NAT5
NatB catalytic subunit

Gene names

Name:	NAA20
Synonyms:	NAT5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	178 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp-Glu. May play a role in normal cell-cycle progression. Ref.7
Catalytic activity	Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.
Subunit structure	Component of the N-terminal acetyltransferase B (NatB) complex which is composed of NAA20 and NAA25 By similarity.
Subcellular location	Cytoplasm. Nucleus Ref.7.
Sequence similarities	Belongs to the acetyltransferase family. ARD1 subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptide alpha-N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 178	178	N-alpha-acetyltransferase 20		PRO_0000074534
Regions
	Domain	2 – 157	156	N-acetyltransferase
Experimental info
	Sequence conflict	47	1	E → V in CAB66576. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P61599 [UniParc]. Last modified May 24, 2004. Version 1. Checksum: C5CCEA50CD60E097	FASTA	178	20,368
	10 20 30 40 50 60 MTTLRAFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK 70 80 90 100 110 120 AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMELLEEIS ERKGGFFVDL FVRVSNQVAV 130 140 150 160 170 NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY DMRKALSRDT EKKSIIPLPH PVRPEDIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human N-terminal acetyltransferase complex ard1 subunit homologue, complete CDS." Liu T., Tao J., Zhang J., Li W., Ye M., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Pancreas.
[7]	"Identification of the human N(alpha)-acetyltransferase complex B (hNatB): a complex important for cell-cycle progression." Starheim K.K., Arnesen T., Gromyko D., Ryningen A., Varhaug J.E., Lillehaug J.R. Biochem. J. 415:325-331(2008) [PubMed: 18570629] [Abstract] Cited for: FUNCTION, INTERACTION WITH MDM20, SUBCELLULAR LOCATION.
[8]	"A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates." Polevoda B., Arnesen T., Sherman F. BMC Proc. 3:S2-S2(2009) [PubMed: 19660095] [Abstract] Cited for: NOMENCLATURE.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF085355 mRNA. Translation: AAD40190.1. AL136641 mRNA. Translation: CAB66576.1. AK311819 mRNA. Translation: BAG34761.1. AL049538, AL035454 Genomic DNA. Translation: CAI19341.1. AL035454, AL049538 Genomic DNA. Translation: CAI42118.1. CH471133 Genomic DNA. Translation: EAX10215.1. BC005181 mRNA. Translation: AAH05181.1. BC008446 mRNA. Translation: AAH08446.1.
IPI	IPI00007174.
RefSeq	NP_057184.1. NM_016100.4. NP_852669.1. NM_181528.3.
UniGene	Hs.368783. Hs.708298.
3D structure databases
ProteinModelPortal	P61599.
SMR	P61599. Positions 2-155.
ModBase	Search...
Protein-protein interaction databases
IntAct	P61599. 1 interaction.
STRING	P61599.
Polymorphism databases
DMDM	47606438.
Proteomic databases
PRIDE	P61599.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000334982; ENSP00000335636; ENSG00000173418.
GeneID	51126.
KEGG	hsa:51126.
UCSC	uc002wrp.1. human.
Organism-specific databases
CTD	51126.
GeneCards	GC20P019997.
HGNC	HGNC:15908. NAA20.
MIM	610833. gene.
neXtProt	NX_P61599.
PharmGKB	PA31449.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16217.
GeneTree	ENSGT00550000075046.
HOGENOM	HBG742014.
HOVERGEN	HBG107217.
InParanoid	P61599.
OMA	MTTLRPF.
OrthoDB	EOG42RD8C.
PhylomeDB	P61599.
Gene expression databases
ArrayExpress	P61599.
Bgee	P61599.
CleanEx	HS_NAT5.
Genevestigator	P61599.
GermOnline	ENSG00000173418. Homo sapiens.
Family and domain databases
InterPro	IPR000182. AcTrfase_GCN5-related_dom. IPR016181. Acyl_CoA_acyltransferase. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
KO	K00670.
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	53927.
SOURCE	Search...

Entry information

Entry name

NAA20_HUMAN

Accession

Primary (citable) accession number: P61599
Secondary accession number(s): B2R4G4 , Q5TFT7, Q9D7H8, Q9H0Y4, Q9NQH6, Q9Y6D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	December 14, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.