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P61599 (NAA20_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-alpha-acetyltransferase 20

EC=2.3.1.88
Alternative name(s):
Methionine N-acetyltransferase
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Protein existenceEvidence 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, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle functions are overrepresented in the pool of NatB substrates. Required for maintaining the structure and function of actomyosin fibers and for proper cellular migration. 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.

Subcellular location

Cytoplasm. Nucleus Ref.7.

Sequence similarities

Belongs to the acetyltransferase family. ARD1 subfamily.

Contains 1 N-acetyltransferase domain.

Sequence caution

The sequence BG548527 differs from that shown. Reason: Frameshift at position 111.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from direct assay. Source: LIFEdb

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptide alpha-N-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P61599-1)

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.
Isoform 2 (identifier: P61599-2)

The sequence of this isoform differs from the canonical sequence as follows:
     103-178: KGGFFVDLFV...PHPVRPEDIE → YEESTFQGY
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 178178N-alpha-acetyltransferase 20
PRO_0000074534

Regions

Domain2 – 157156N-acetyltransferase

Natural variations

Alternative sequence103 – 17876KGGFF…PEDIE → YEESTFQGY in isoform 2.
VSP_045644

Experimental info

Sequence conflict471E → V in CAB66576. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: C5CCEA50CD60E097

FASTA17820,368
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 55D80084800FB8E3
Show »

FASTA11112,746

References

« Hide '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] (ISOFORM 1).
[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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain, Lung 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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NAA25, 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] [Europe PMC] [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] [Europe PMC] [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.
AL035454, AL049538 Genomic DNA. Translation: CAX15127.1.
AL049538, AL035454 Genomic DNA. Translation: CAX15212.1.
CH471133 Genomic DNA. Translation: EAX10214.1.
CH471133 Genomic DNA. Translation: EAX10215.1.
BC005181 mRNA. Translation: AAH05181.1.
BC008446 mRNA. Translation: AAH08446.1.
BG548527 mRNA. No translation available.
RefSeqNP_057184.1. NM_016100.4.
NP_852669.1. NM_181528.3.
UniGeneHs.368783.
Hs.708298.

3D structure databases

ProteinModelPortalP61599.
SMRP61599. Positions 4-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119313. 10 interactions.
IntActP61599. 1 interaction.
MINTMINT-3022686.
STRING9606.ENSP00000335636.

PTM databases

PhosphoSiteP61599.

Polymorphism databases

DMDM47606438.

Proteomic databases

PaxDbP61599.
PRIDEP61599.

Protocols and materials databases

DNASU51126.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310450; ENSP00000311027; ENSG00000173418. [P61599-2]
ENST00000334982; ENSP00000335636; ENSG00000173418. [P61599-1]
GeneID51126.
KEGGhsa:51126.
UCSCuc002wrp.3. human. [P61599-1]
uc002wrq.3. human.

Organism-specific databases

CTD51126.
GeneCardsGC20P019997.
HGNCHGNC:15908. NAA20.
HPAHPA053117.
MIM610833. gene.
neXtProtNX_P61599.
PharmGKBPA31449.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0456.
HOVERGENHBG107217.
InParanoidP61599.
KOK17972.
OMAPWHAHIT.
OrthoDBEOG7PP57X.
PhylomeDBP61599.
TreeFamTF105829.

Gene expression databases

ArrayExpressP61599.
BgeeP61599.
CleanExHS_NAT5.
GenevestigatorP61599.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNAA20. human.
GeneWikiNAT5.
GenomeRNAi51126.
NextBio53927.
PROP61599.
SOURCESearch...

Entry information

Entry nameNAA20_HUMAN
AccessionPrimary (citable) accession number: P61599
Secondary accession number(s): A6NHA3 expand/collapse secondary AC list , B2R4G4, Q5TFT7, Q9D7H8, Q9H0Y4, Q9NQH6, Q9Y6D2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM