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N-alpha-acetyltransferase 20 (EC 2.3.1.254) (Methionine N-acetyltransferase) (N-acetyltransferase 5) (N-terminal acetyltransferase B complex catalytic subunit NAA20) (N-terminal acetyltransferase B complex catalytic subunit NAT5) (NatB complex subunit NAT5) (NatB catalytic subunit)

 NAA20_HUMAN             Reviewed;         178 AA.
P61599; A6NHA3; B2R4G4; Q5TFT7; Q9D7H8; Q9H0Y4; Q9NQH6; Q9Y6D2;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
24-MAY-2004, sequence version 1.
23-MAY-2018, entry version 132.
RecName: Full=N-alpha-acetyltransferase 20;
EC=2.3.1.254 {ECO:0000269|PubMed:18570629};
AltName: Full=Methionine N-acetyltransferase;
AltName: Full=N-acetyltransferase 5;
AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAA20;
AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAT5;
Short=NatB complex subunit NAT5;
AltName: Full=NatB catalytic subunit;
Name=NAA20; Synonyms=NAT5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Liu T., Tao J., Zhang J., Li W., Ye M., Zhou J., Wu J., Shen Y.,
Yu M., Chen S., Mao M., Chen Z.;
"Human N-terminal acetyltransferase complex ard1 subunit homologue,
complete CDS.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
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.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
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.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Lung, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH NAA25, AND SUBCELLULAR
LOCATION.
PubMed=18570629; DOI=10.1042/BJ20080658;
Starheim K.K., Arnesen T., Gromyko D., Ryningen A., Varhaug J.E.,
Lillehaug J.R.;
"Identification of the human N(alpha)-acetyltransferase complex B
(hNatB): a complex important for cell-cycle progression.";
Biochem. J. 415:325-331(2008).
[8]
NOMENCLATURE.
PubMed=19660095; DOI=10.1186/1753-6561-3-S6-S2;
Polevoda B., Arnesen T., Sherman F.;
"A synopsis of eukaryotic Nalpha-terminal acetyltransferases:
nomenclature, subunits and substrates.";
BMC Proc. 3:S2-S2(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
SUBCELLULAR LOCATION.
PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M.,
Stoeve S.I., Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C.,
Ljostveit S., Ziegler M., Niere M., Gevaert K., Arnesen T.;
"An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
termini of transmembrane proteins and maintains Golgi integrity.";
Cell Rep. 10:1362-1374(2015).
-!- 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.
{ECO:0000269|PubMed:18570629}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal L-methionyl-L-
asparaginyl-[protein] = an N-terminal N(alpha)-acetyl-L-methionyl-
L-asparginyl-[protein] + CoA. {ECO:0000269|PubMed:18570629}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal L-methionyl-L-
glutaminyl-[protein] = an N-terminal N(alpha)-acetyl-L-methionyl-
L-glutaminyl-[protein] + CoA. {ECO:0000269|PubMed:18570629}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal L-methionyl-L-
aspartyl-[protein] = an N-terminal N(alpha)-acetyl-L-methionyl-L-
aspartyl-[protein] + CoA. {ECO:0000269|PubMed:18570629}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal L-methionyl-L-
glutamyl-[protein] = an N-terminal N(alpha)-acetyl-L-methionyl-L-
glutamyl-[protein] + CoA. {ECO:0000269|PubMed:18570629}.
-!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB)
complex which is composed of NAA20 and NAA25.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18570629,
ECO:0000269|PubMed:25732826}. Nucleus
{ECO:0000269|PubMed:18570629, ECO:0000269|PubMed:25732826}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P61599-1; Sequence=Displayed;
Name=2;
IsoId=P61599-2; Sequence=VSP_045644;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the acetyltransferase family. ARD1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BG548527; Type=Frameshift; Positions=111; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF085355; AAD40190.1; -; mRNA.
EMBL; AL136641; CAB66576.1; -; mRNA.
EMBL; AK311819; BAG34761.1; -; mRNA.
EMBL; AL049538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL035454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471133; EAX10214.1; -; Genomic_DNA.
EMBL; CH471133; EAX10215.1; -; Genomic_DNA.
EMBL; BC005181; AAH05181.1; -; mRNA.
EMBL; BC008446; AAH08446.1; -; mRNA.
EMBL; BG548527; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS13141.1; -. [P61599-1]
CCDS; CCDS13142.1; -. [P61599-2]
RefSeq; NP_057184.1; NM_016100.4. [P61599-1]
RefSeq; NP_852669.1; NM_181528.3. [P61599-2]
UniGene; Hs.368783; -.
UniGene; Hs.708298; -.
ProteinModelPortal; P61599; -.
SMR; P61599; -.
BioGrid; 119313; 13.
IntAct; P61599; 1.
STRING; 9606.ENSP00000335636; -.
iPTMnet; P61599; -.
PhosphoSitePlus; P61599; -.
BioMuta; NAA20; -.
DMDM; 47606438; -.
EPD; P61599; -.
MaxQB; P61599; -.
PaxDb; P61599; -.
PeptideAtlas; P61599; -.
PRIDE; P61599; -.
TopDownProteomics; P61599-1; -. [P61599-1]
DNASU; 51126; -.
Ensembl; ENST00000310450; ENSP00000311027; ENSG00000173418. [P61599-2]
Ensembl; ENST00000334982; ENSP00000335636; ENSG00000173418. [P61599-1]
GeneID; 51126; -.
KEGG; hsa:51126; -.
UCSC; uc002wrp.4; human. [P61599-1]
CTD; 51126; -.
EuPathDB; HostDB:ENSG00000173418.11; -.
GeneCards; NAA20; -.
HGNC; HGNC:15908; NAA20.
HPA; HPA063344; -.
MIM; 610833; gene.
neXtProt; NX_P61599; -.
OpenTargets; ENSG00000173418; -.
PharmGKB; PA31449; -.
eggNOG; KOG3234; Eukaryota.
eggNOG; COG0456; LUCA.
GeneTree; ENSGT00550000075046; -.
HOGENOM; HOG000078523; -.
HOVERGEN; HBG107217; -.
InParanoid; P61599; -.
KO; K17972; -.
OMA; WTETYGI; -.
OrthoDB; EOG091G0NIY; -.
PhylomeDB; P61599; -.
TreeFam; TF105829; -.
BioCyc; MetaCyc:HS10662-MONOMER; -.
ChiTaRS; NAA20; human.
GeneWiki; NAT5; -.
GenomeRNAi; 51126; -.
PRO; PR:P61599; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000173418; -.
CleanEx; HS_NAT5; -.
ExpressionAtlas; P61599; baseline and differential.
Genevisible; P61599; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0031416; C:NatB complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central.
GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000182; GNAT_dom.
Pfam; PF00583; Acetyltransf_1; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome; Cytoplasm;
Nucleus; Reference proteome; Transferase.
CHAIN 1 178 N-alpha-acetyltransferase 20.
/FTId=PRO_0000074534.
DOMAIN 2 157 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
VAR_SEQ 103 178 KGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSASNG
EPDEDAYDMRKALSRDTEKKSIIPLPHPVRPEDIE -> YE
ESTFQGY (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045644.
CONFLICT 47 47 E -> V (in Ref. 2; CAB66576).
{ECO:0000305}.
SEQUENCE 178 AA; 20368 MW; C5CCEA50CD60E097 CRC64;
MTTLRAFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK
AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMELLEEIS ERKGGFFVDL FVRVSNQVAV
NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY DMRKALSRDT EKKSIIPLPH PVRPEDIE


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