NAA20_HUMAN
ID NAA20_HUMAN Reviewed; 178 AA.
AC P61599; A6NHA3; B2R4G4; Q5TFT7; Q9D7H8; Q9H0Y4; Q9NQH6; Q9Y6D2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=N-alpha-acetyltransferase 20;
DE EC=2.3.1.254 {ECO:0000269|PubMed:18570629};
DE AltName: Full=Methionine N-acetyltransferase;
DE AltName: Full=N-acetyltransferase 5;
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAA20;
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAT5;
DE Short=NatB complex subunit NAT5;
DE AltName: Full=NatB catalytic subunit;
GN Name=NAA20; Synonyms=NAT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu T., Tao J., Zhang J., Li W., Ye M., Zhou J., Wu J., Shen Y., Yu M.,
RA Chen S., Mao M., Chen Z.;
RT "Human N-terminal acetyltransferase complex ard1 subunit homologue,
RT complete CDS.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Lung, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH NAA25, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18570629; DOI=10.1042/bj20080658;
RA Starheim K.K., Arnesen T., Gromyko D., Ryningen A., Varhaug J.E.,
RA Lillehaug J.R.;
RT "Identification of the human N(alpha)-acetyltransferase complex B (hNatB):
RT a complex important for cell-cycle progression.";
RL Biochem. J. 415:325-331(2008).
RN [8]
RP NOMENCLATURE.
RX PubMed=19660095; DOI=10.1186/1753-6561-3-s6-s2;
RA Polevoda B., Arnesen T., Sherman F.;
RT "A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature,
RT subunits and substrates.";
RL BMC Proc. 3:S2-S2(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT termini of transmembrane proteins and maintains Golgi integrity.";
RL Cell Rep. 10:1362-1374(2015).
CC -!- FUNCTION: Catalytic subunit of the NatB complex which catalyzes
CC acetylation of the N-terminal methionine residues of peptides beginning
CC with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle
CC functions are overrepresented in the pool of NatB substrates. Required
CC for maintaining the structure and function of actomyosin fibers and for
CC proper cellular migration. {ECO:0000269|PubMed:18570629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-asparaginyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-asparaginyl-
CC [protein]; Xref=Rhea:RHEA:50484, Rhea:RHEA-COMP:12694, Rhea:RHEA-
CC COMP:12695, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133356, ChEBI:CHEBI:133358; EC=2.3.1.254;
CC Evidence={ECO:0000269|PubMed:18570629};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutaminyl-
CC [protein]; Xref=Rhea:RHEA:50492, Rhea:RHEA-COMP:12698, Rhea:RHEA-
CC COMP:12699, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133361, ChEBI:CHEBI:133362; EC=2.3.1.254;
CC Evidence={ECO:0000269|PubMed:18570629};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein];
CC Xref=Rhea:RHEA:50480, Rhea:RHEA-COMP:12692, Rhea:RHEA-COMP:12693,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133045, ChEBI:CHEBI:133063; EC=2.3.1.254;
CC Evidence={ECO:0000269|PubMed:18570629};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein];
CC Xref=Rhea:RHEA:50488, Rhea:RHEA-COMP:12696, Rhea:RHEA-COMP:12697,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133359, ChEBI:CHEBI:133360; EC=2.3.1.254;
CC Evidence={ECO:0000269|PubMed:18570629};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex
CC which is composed of NAA20 and NAA25.
CC -!- INTERACTION:
CC P61599; Q14CX7: NAA25; NbExp=2; IntAct=EBI-1055023, EBI-1048503;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18570629,
CC ECO:0000269|PubMed:25732826}. Nucleus {ECO:0000269|PubMed:18570629,
CC ECO:0000269|PubMed:25732826}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61599-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61599-2; Sequence=VSP_045644;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BG548527; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF085355; AAD40190.1; -; mRNA.
DR EMBL; AL136641; CAB66576.1; -; mRNA.
DR EMBL; AK311819; BAG34761.1; -; mRNA.
DR EMBL; AL049538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10214.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10215.1; -; Genomic_DNA.
DR EMBL; BC005181; AAH05181.1; -; mRNA.
DR EMBL; BC008446; AAH08446.1; -; mRNA.
DR EMBL; BG548527; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13141.1; -. [P61599-1]
DR CCDS; CCDS13142.1; -. [P61599-2]
DR RefSeq; NP_057184.1; NM_016100.4. [P61599-1]
DR RefSeq; NP_852669.1; NM_181528.3. [P61599-2]
DR PDB; 6VP9; EM; 3.46 A; A=1-163.
DR PDB; 7STX; EM; 3.14 A; A=1-178.
DR PDBsum; 6VP9; -.
DR PDBsum; 7STX; -.
DR AlphaFoldDB; P61599; -.
DR SMR; P61599; -.
DR BioGRID; 119313; 14.
DR ComplexPortal; CPX-6270; NatB N-alpha-acetyltransferase complex.
DR IntAct; P61599; 3.
DR STRING; 9606.ENSP00000335636; -.
DR GlyGen; P61599; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61599; -.
DR PhosphoSitePlus; P61599; -.
DR BioMuta; NAA20; -.
DR DMDM; 47606438; -.
DR EPD; P61599; -.
DR jPOST; P61599; -.
DR MassIVE; P61599; -.
DR MaxQB; P61599; -.
DR PaxDb; P61599; -.
DR PeptideAtlas; P61599; -.
DR PRIDE; P61599; -.
DR ProteomicsDB; 1184; -.
DR ProteomicsDB; 57323; -. [P61599-1]
DR TopDownProteomics; P61599-1; -. [P61599-1]
DR Antibodypedia; 24668; 137 antibodies from 26 providers.
DR DNASU; 51126; -.
DR Ensembl; ENST00000310450.8; ENSP00000311027.4; ENSG00000173418.12. [P61599-2]
DR Ensembl; ENST00000334982.9; ENSP00000335636.4; ENSG00000173418.12. [P61599-1]
DR GeneID; 51126; -.
DR KEGG; hsa:51126; -.
DR MANE-Select; ENST00000334982.9; ENSP00000335636.4; NM_016100.5; NP_057184.1.
DR UCSC; uc002wrp.4; human. [P61599-1]
DR CTD; 51126; -.
DR GeneCards; NAA20; -.
DR HGNC; HGNC:15908; NAA20.
DR HPA; ENSG00000173418; Low tissue specificity.
DR MIM; 610833; gene.
DR neXtProt; NX_P61599; -.
DR OpenTargets; ENSG00000173418; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA31449; -.
DR VEuPathDB; HostDB:ENSG00000173418; -.
DR eggNOG; KOG3234; Eukaryota.
DR GeneTree; ENSGT00550000075046; -.
DR HOGENOM; CLU_013985_7_1_1; -.
DR InParanoid; P61599; -.
DR OMA; SGEIMGY; -.
DR OrthoDB; 1355894at2759; -.
DR PhylomeDB; P61599; -.
DR TreeFam; TF105829; -.
DR BioCyc; MetaCyc:HS10662-MON; -.
DR BRENDA; 2.3.1.254; 2681.
DR PathwayCommons; P61599; -.
DR SignaLink; P61599; -.
DR SIGNOR; P61599; -.
DR BioGRID-ORCS; 51126; 624 hits in 1094 CRISPR screens.
DR ChiTaRS; NAA20; human.
DR GeneWiki; NAT5; -.
DR GenomeRNAi; 51126; -.
DR Pharos; P61599; Tbio.
DR PRO; PR:P61599; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P61599; protein.
DR Bgee; ENSG00000173418; Expressed in islet of Langerhans and 183 other tissues.
DR ExpressionAtlas; P61599; baseline and differential.
DR Genevisible; P61599; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031416; C:NatB complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IDA:ComplexPortal.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Cytoplasm; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..178
FT /note="N-alpha-acetyltransferase 20"
FT /id="PRO_0000074534"
FT DOMAIN 2..157
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT VAR_SEQ 103..178
FT /note="KGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSASNGEPDEDAYDMRK
FT ALSRDTEKKSIIPLPHPVRPEDIE -> YEESTFQGY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045644"
FT CONFLICT 47
FT /note="E -> V (in Ref. 2; CAB66576)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 88..102
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:7STX"
SQ 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
