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Protein

N-alpha-acetyltransferase 20

Gene

NAA20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:NAA20
Synonyms:NAT5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15908. NAA20.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31449.

Polymorphism and mutation databases

BioMutaiNAA20.
DMDMi47606438.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 178178N-alpha-acetyltransferase 20PRO_0000074534Add
BLAST

Proteomic databases

MaxQBiP61599.
PaxDbiP61599.
PRIDEiP61599.

PTM databases

PhosphoSiteiP61599.

Expressioni

Gene expression databases

BgeeiP61599.
CleanExiHS_NAT5.
ExpressionAtlasiP61599. baseline and differential.
GenevestigatoriP61599.

Interactioni

Subunit structurei

Component of the N-terminal acetyltransferase B (NatB) complex which is composed of NAA20 and NAA25.

Protein-protein interaction databases

BioGridi119313. 9 interactions.
IntActiP61599. 1 interaction.
MINTiMINT-3022686.
STRINGi9606.ENSP00000335636.

Structurei

3D structure databases

ProteinModelPortaliP61599.
SMRiP61599. Positions 4-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 157156N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0456.
GeneTreeiENSGT00550000075046.
HOGENOMiHOG000078523.
HOVERGENiHBG107217.
InParanoidiP61599.
KOiK17972.
OMAiPWHAHIT.
OrthoDBiEOG7PP57X.
PhylomeDBiP61599.
TreeFamiTF105829.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P61599-1) [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
MTTLRAFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG
60 70 80 90 100
GELMGYIMGK AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMELLEEIS
110 120 130 140 150
ERKGGFFVDL FVRVSNQVAV NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY
160 170
DMRKALSRDT EKKSIIPLPH PVRPEDIE
Length:178
Mass (Da):20,368
Last modified:May 24, 2004 - v1
Checksum:iC5CCEA50CD60E097
GO
Isoform 2 (identifier: P61599-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     103-178: KGGFFVDLFV...PHPVRPEDIE → YEESTFQGY

Note: No experimental confirmation available.

Show »
Length:111
Mass (Da):12,746
Checksum:i55D80084800FB8E3
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471E → V in CAB66576 (PubMed:11230166).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei103 – 17876KGGFF…PEDIE → YEESTFQGY in isoform 2. 1 PublicationVSP_045644Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13141.1. [P61599-1]
CCDS13142.1. [P61599-2]
RefSeqiNP_057184.1. NM_016100.4. [P61599-1]
NP_852669.1. NM_181528.3. [P61599-2]
UniGeneiHs.368783.
Hs.708298.

Genome annotation databases

EnsembliENST00000310450; ENSP00000311027; ENSG00000173418. [P61599-2]
ENST00000334982; ENSP00000335636; ENSG00000173418. [P61599-1]
GeneIDi51126.
KEGGihsa:51126.
UCSCiuc002wrp.3. human. [P61599-1]
uc002wrq.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13141.1. [P61599-1]
CCDS13142.1. [P61599-2]
RefSeqiNP_057184.1. NM_016100.4. [P61599-1]
NP_852669.1. NM_181528.3. [P61599-2]
UniGeneiHs.368783.
Hs.708298.

3D structure databases

ProteinModelPortaliP61599.
SMRiP61599. Positions 4-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119313. 9 interactions.
IntActiP61599. 1 interaction.
MINTiMINT-3022686.
STRINGi9606.ENSP00000335636.

PTM databases

PhosphoSiteiP61599.

Polymorphism and mutation databases

BioMutaiNAA20.
DMDMi47606438.

Proteomic databases

MaxQBiP61599.
PaxDbiP61599.
PRIDEiP61599.

Protocols and materials databases

DNASUi51126.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310450; ENSP00000311027; ENSG00000173418. [P61599-2]
ENST00000334982; ENSP00000335636; ENSG00000173418. [P61599-1]
GeneIDi51126.
KEGGihsa:51126.
UCSCiuc002wrp.3. human. [P61599-1]
uc002wrq.3. human.

Organism-specific databases

CTDi51126.
GeneCardsiGC20P019997.
HGNCiHGNC:15908. NAA20.
MIMi610833. gene.
neXtProtiNX_P61599.
PharmGKBiPA31449.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0456.
GeneTreeiENSGT00550000075046.
HOGENOMiHOG000078523.
HOVERGENiHBG107217.
InParanoidiP61599.
KOiK17972.
OMAiPWHAHIT.
OrthoDBiEOG7PP57X.
PhylomeDBiP61599.
TreeFamiTF105829.

Miscellaneous databases

ChiTaRSiNAA20. human.
GeneWikiiNAT5.
GenomeRNAii51126.
NextBioi53927.
PROiP61599.
SOURCEiSearch...

Gene expression databases

BgeeiP61599.
CleanExiHS_NAT5.
ExpressionAtlasiP61599. baseline and differential.
GenevestigatoriP61599.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNAA20_HUMAN
AccessioniPrimary (citable) accession number: P61599
Secondary accession number(s): A6NHA3
, B2R4G4, Q5TFT7, Q9D7H8, Q9H0Y4, Q9NQH6, Q9Y6D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: April 29, 2015
This is version 105 of the entry and version 1 of the sequence. [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

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.