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 27-MAR-2024, entry version 164. DE RecName: Full=N-alpha-acetyltransferase 20; DE EC=2.3.1.254 {ECO:0000269|PubMed:18570629, ECO:0000269|PubMed:34230638}; 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). RN [11] RP INVOLVEMENT IN MRT73, VARIANTS MRT73 VAL-54 AND VAL-80, CHARACTERIZATION OF RP VARIANTS MRT73 VAL-54 AND VAL-80, FUNCTION, CATALYTIC ACTIVITY, AND RP INTERACTION WITH NAA25. RX PubMed=34230638; DOI=10.1038/s41436-021-01264-0; RA Morrison J., Altuwaijri N.K., Broenstad K., Aksnes H., Alsaif H.S., RA Evans A., Hashem M., Wheeler P.G., Webb B.D., Alkuraya F.S., Arnesen T.; RT "Missense NAA20 variants impairing the NatB protein N-terminal RT acetyltransferase cause autosomal recessive developmental delay, RT intellectual disability, and microcephaly."; RL Genet. Med. 23:2213-2218(2021). RN [12] RP INTERACTION WITH NAA25, VARIANTS MRT73 PRO-4 AND 34-GLN--GLU-178 DEL, AND RP CHARACTERIZATION OF VARIANT MRT73 PRO-4. RX PubMed=37191084; DOI=10.1111/cge.14359; RA D'Onofrio G., Cuccurullo C., Larsen S.K., Severino M., D'Amico A., RA Broenstad K., AlOwain M., Morrison J.L., Wheeler P.G., Webb B.D., RA Alfalah A., Iacomino M., Uva P., Coppola A., Merla G., Salpietro V.D., RA Zara F., Striano P., Accogli A., Arnesen T., Bilo L.; RT "Novel biallelic variants expand the phenotype of NAA20-related syndrome."; RL Clin. Genet. 0:0-0(2023). 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 (PubMed:34230638). Proteins CC with cell cycle functions are overrepresented in the pool of NatB CC substrates. Required for maintaining the structure and function of CC actomyosin fibers and for proper cellular migration. CC {ECO:0000269|PubMed:18570629, ECO:0000269|PubMed:34230638}. 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, ECO:0000269|PubMed:34230638}; 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, ECO:0000269|PubMed:34230638}; 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, ECO:0000269|PubMed:34230638}; 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, ECO:0000269|PubMed:34230638}; CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex CC which is composed of NAA20 and NAA25. {ECO:0000269|PubMed:34230638, CC ECO:0000269|PubMed:37191084}. 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 -!- DISEASE: Intellectual developmental disorder, autosomal recessive 73 CC (MRT73) [MIM:619717]: A form of intellectual disability, a disorder CC characterized by significantly below average general intellectual CC functioning associated with impairments in adaptive behavior and CC manifested during the developmental period. MRT73 patients manifest CC global developmental delay with hypotonia and mildly delayed walking, CC impaired intellectual development with poor or absent speech, and CC mildly dysmorphic features. {ECO:0000269|PubMed:34230638, CC ECO:0000269|PubMed:37191084}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BG548527; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8G0L; EM; 3.39 A; A=1-178. DR PDBsum; 6VP9; -. DR PDBsum; 7STX; -. DR PDBsum; 8G0L; -. DR AlphaFoldDB; P61599; -. DR EMDB; EMD-21307; -. DR EMDB; EMD-25438; -. DR EMDB; EMD-29657; -. DR SMR; P61599; -. DR BioGRID; 119313; 21. 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; 9606-ENSP00000335636; -. DR PeptideAtlas; P61599; -. DR ProteomicsDB; 1184; -. DR ProteomicsDB; 57323; -. [P61599-1] DR Pumba; P61599; -. DR TopDownProteomics; P61599-1; -. [P61599-1] DR Antibodypedia; 24668; 149 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 AGR; HGNC:15908; -. DR CTD; 51126; -. DR GeneCards; NAA20; -. DR HGNC; HGNC:15908; NAA20. DR HPA; ENSG00000173418; Low tissue specificity. DR MalaCards; NAA20; -. DR MIM; 610833; gene. DR MIM; 619717; phenotype. 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; GHGENWH; -. DR OrthoDB; 5471170at2759; -. DR PhylomeDB; P61599; -. DR TreeFam; TF105829; -. DR BioCyc; MetaCyc:HS10662-MONOMER; -. DR BRENDA; 2.3.1.254; 2681. DR PathwayCommons; P61599; -. DR SignaLink; P61599; -. DR SIGNOR; P61599; -. DR BioGRID-ORCS; 51126; 657 hits in 1173 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 185 other cell types or tissues. DR ExpressionAtlas; P61599; baseline and differential. 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:0017190; P:N-terminal peptidyl-aspartic acid acetylation; IDA:UniProtKB. DR GO; GO:0018002; P:N-terminal peptidyl-glutamic acid acetylation; IDA:UniProtKB. DR GO; GO:0017192; P:N-terminal peptidyl-glutamine acetylation; IDA:UniProtKB. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:UniProtKB. DR CDD; cd04301; NAT_SF; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR PANTHER; PTHR45910; N-ALPHA-ACETYLTRANSFERASE 20; 1. DR PANTHER; PTHR45910:SF1; N-ALPHA-ACETYLTRANSFERASE 20; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR PROSITE; PS51186; GNAT; 1. DR Genevisible; P61599; HS. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Alternative splicing; Cytoplasm; KW Disease variant; Intellectual disability; Nucleus; Reference proteome; KW 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 VARIANT 4 FT /note="L -> P (in MRT73; decreases interaction with NAA25; FT may reduce protein capacity to acetylate Met-Glu N-terminal FT peptides; does not affect protein stability; FT dbSNP:rs752372862)" FT /evidence="ECO:0000269|PubMed:37191084" FT /id="VAR_088425" FT VARIANT 34..178 FT /note="Missing (in MRT73; dbSNP:rs755734957)" FT /evidence="ECO:0000269|PubMed:37191084" FT /id="VAR_088426" FT VARIANT 54 FT /note="M -> V (in MRT73; decreased complex formation with FT NAA25 and decreased N-acetylation catalytic activity in FT vitro for all 4 types of substrates; does not affect FT protein stability; dbSNP:rs2146464332)" FT /evidence="ECO:0000269|PubMed:34230638" FT /id="VAR_086809" FT VARIANT 80 FT /note="A -> V (in MRT73; strong decrease in N-acetylation FT catalytic activity in vitro for substrates Met-Glu, Met-Asn FT and Met-Gln, but not Met-Asp; does not affect protein FT stability; dbSNP:rs768029717)" FT /evidence="ECO:0000269|PubMed:34230638" FT /id="VAR_086810" 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 //