ID   NAA40_HUMAN             Reviewed;         237 AA.
AC   Q86UY6; B4DR03; B4DU10; Q5HYL5; Q9H897;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   28-JAN-2026, entry version 167.
DE   RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000303|PubMed:19660095, ECO:0000312|HGNC:HGNC:25845};
DE            EC=2.3.1.257 {ECO:0000269|PubMed:21935442, ECO:0000269|PubMed:25619998};
DE   AltName: Full=N-acetyltransferase 11;
DE   AltName: Full=N-alpha-acetyltransferase D {ECO:0000303|PubMed:25619998};
DE            Short=NatD {ECO:0000303|PubMed:25619998};
DE            Short=hNatD {ECO:0000303|PubMed:25619998};
DE   AltName: Full=Protein acetyltransferase 1 {ECO:0000303|PubMed:19695338};
GN   Name=NAA40 {ECO:0000303|PubMed:19660095, ECO:0000312|HGNC:HGNC:25845};
GN   Synonyms=NAT11, PATT1 {ECO:0000303|PubMed:19695338};
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Placenta, and Thyroid;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lymph;
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   [5]
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   [6]
RP   MUTAGENESIS OF TYR-136 AND GLU-139, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=19695338; DOI=10.1016/j.biocel.2009.08.009;
RA   Liu Z., Liu Y., Wang H., Ge X., Jin Q., Ding G., Hu Y., Zhou B., Chen Z.,
RA   Ge X., Zhang B., Man X., Zhai Q.;
RT   "Patt1, a novel protein acetyltransferase that is highly expressed in liver
RT   and downregulated in hepatocellular carcinoma, enhances apoptosis of
RT   hepatoma cells.";
RL   Int. J. Biochem. Cell Biol. 41:2528-2537(2009).
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=21935442; DOI=10.1371/journal.pone.0024713;
RA   Hole K., Van Damme P., Dalva M., Aksnes H., Glomnes N., Varhaug J.E.,
RA   Lillehaug J.R., Gevaert K., Arnesen T.;
RT   "The human N-alpha-acetyltransferase 40 (hNaa40p/hNatD) is conserved from
RT   yeast and N-terminally acetylates histones H2A and H4.";
RL   PLoS ONE 6:E24713-E24713(2011).
RN   [8]
RP   FUNCTION.
RX   PubMed=26666750; DOI=10.1007/s10495-015-1207-0;
RA   Pavlou D., Kirmizis A.;
RT   "Depletion of histone N-terminal-acetyltransferase Naa40 induces p53-
RT   independent apoptosis in colorectal cancer cells via the mitochondrial
RT   pathway.";
RL   Apoptosis 21:298-311(2016).
RN   [9]
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   [10]
RP   3D-STRUCTURE MODELING.
RX   PubMed=24248912; DOI=10.1007/s00894-013-2043-1;
RA   Jedrzejewski R.P., Kazmierkiewicz R.;
RT   "Structure of Patt1 human proapoptotic histone acetyltransferase.";
RL   J. Mol. Model. 19:5533-5538(2013).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 25-220 IN COMPLEX WITH ACETYL-COA
RP   AND SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-85;
RP   TRP-90; GLU-100; 127-ASP--GLU-129; TYR-136; CYS-137; TYR-138; GLU-139;
RP   THR-174 AND TYR-211.
RX   PubMed=25619998; DOI=10.1016/j.str.2014.10.025;
RA   Magin R.S., Liszczak G.P., Marmorstein R.;
RT   "The molecular basis for histone H4- and H2A-specific amino-terminal
RT   acetylation by NatD.";
RL   Structure 23:332-341(2015).
CC   -!- FUNCTION: N-alpha-acetyltransferase that specifically mediates the
CC       acetylation of the N-terminal residues of histones H4 and H2A
CC       (PubMed:21935442, PubMed:25619998). In contrast to other N-alpha-
CC       acetyltransferase, has a very specific selectivity for histones H4 and
CC       H2A N-terminus and specifically recognizes the 'Ser-Gly-Arg-Gly
CC       sequence' (PubMed:21935442, PubMed:25619998). Acts as a negative
CC       regulator of apoptosis (PubMed:26666750). May play a role in hepatic
CC       lipid metabolism (By similarity). {ECO:0000250|UniProtKB:Q8VE10,
CC       ECO:0000269|PubMed:21935442, ECO:0000269|PubMed:25619998,
CC       ECO:0000269|PubMed:26666750}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-seryl-[histone H4] + acetyl-CoA = N-terminal
CC         N(alpha)-acetyl-L-seryl-[histone H4] + CoA + H(+);
CC         Xref=Rhea:RHEA:50596, Rhea:RHEA-COMP:12740, Rhea:RHEA-COMP:12743,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.257;
CC         Evidence={ECO:0000269|PubMed:21935442, ECO:0000269|PubMed:25619998};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-seryl-[histone H2A] + acetyl-CoA = N-terminal
CC         N(alpha)-acetyl-L-seryl-[histone H2A] + CoA + H(+);
CC         Xref=Rhea:RHEA:50600, Rhea:RHEA-COMP:12742, Rhea:RHEA-COMP:12744,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.257;
CC         Evidence={ECO:0000269|PubMed:21935442, ECO:0000269|PubMed:25619998};
CC   -!- INTERACTION:
CC       Q86UY6; P20290-2: BTF3; NbExp=3; IntAct=EBI-16356946, EBI-1054703;
CC       Q86UY6-1; P62805: H4C9; NbExp=3; IntAct=EBI-16140302, EBI-302023;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25732826}. Nucleus
CC       {ECO:0000269|PubMed:25732826}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q86UY6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86UY6-3; Sequence=VSP_054274;
CC       Name=3;
CC         IsoId=Q86UY6-4; Sequence=VSP_054273;
CC   -!- TISSUE SPECIFICITY: Widely expressed; with the highest expression level
CC       in liver and the lowest expression in brain (at protein level).
CC       {ECO:0000269|PubMed:19695338}.
CC   -!- INDUCTION: Down-regulated in hepatocellular carcinoma tissues.
CC       {ECO:0000269|PubMed:19695338}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. NAA40 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI46006.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; AK023910; BAB14720.1; -; mRNA.
DR   EMBL; AK299041; BAG61115.1; -; mRNA.
DR   EMBL; AK300451; BAG62172.1; -; mRNA.
DR   EMBL; BX647309; CAI46006.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AP003780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC041617; AAH41617.1; -; mRNA.
DR   EMBL; BC052298; AAH52298.1; -; mRNA.
DR   CCDS; CCDS73311.1; -. [Q86UY6-3]
DR   CCDS; CCDS8053.1; -. [Q86UY6-1]
DR   RefSeq; NP_001287729.1; NM_001300800.1. [Q86UY6-3]
DR   RefSeq; NP_079047.2; NM_024771.4. [Q86UY6-1]
DR   PDB; 4U9V; X-ray; 1.78 A; B=25-220.
DR   PDB; 4U9W; X-ray; 2.49 A; A/B/C/D=17-220.
DR   PDB; 7KD7; X-ray; 1.44 A; A/D=17-220.
DR   PDB; 7KPU; X-ray; 1.43 A; A/D=17-220.
DR   PDBsum; 4U9V; -.
DR   PDBsum; 4U9W; -.
DR   PDBsum; 7KD7; -.
DR   PDBsum; 7KPU; -.
DR   AlphaFoldDB; Q86UY6; -.
DR   SMR; Q86UY6; -.
DR   BioGRID; 122921; 979.
DR   DIP; DIP-61383N; -.
DR   FunCoup; Q86UY6; 3527.
DR   IntAct; Q86UY6; 34.
DR   STRING; 9606.ENSP00000367024; -.
DR   BindingDB; Q86UY6; -.
DR   ChEMBL; CHEMBL4523373; -.
DR   GlyGen; Q86UY6; 1 site, 1 N-linked glycan (1 site).
DR   iPTMnet; Q86UY6; -.
DR   PhosphoSitePlus; Q86UY6; -.
DR   SwissPalm; Q86UY6; -.
DR   BioMuta; NAA40; -.
DR   DMDM; 74727506; -.
DR   jPOST; Q86UY6; -.
DR   MassIVE; Q86UY6; -.
DR   PaxDb; 9606-ENSP00000367024; -.
DR   PeptideAtlas; Q86UY6; -.
DR   ProteomicsDB; 4913; -.
DR   ProteomicsDB; 5140; -.
DR   ProteomicsDB; 69938; -. [Q86UY6-1]
DR   Pumba; Q86UY6; -.
DR   Antibodypedia; 43913; 73 antibodies from 23 providers.
DR   DNASU; 79829; -.
DR   Ensembl; ENST00000377793.9; ENSP00000367024.4; ENSG00000110583.14. [Q86UY6-1]
DR   Ensembl; ENST00000542163.1; ENSP00000442055.1; ENSG00000110583.14. [Q86UY6-3]
DR   GeneID; 79829; -.
DR   KEGG; hsa:79829; -.
DR   MANE-Select; ENST00000377793.9; ENSP00000367024.4; NM_024771.4; NP_079047.2.
DR   UCSC; uc009yoz.4; human. [Q86UY6-1]
DR   AGR; HGNC:25845; -.
DR   ClinPGx; PA165543497; -.
DR   CTD; 79829; -.
DR   DisGeNET; 79829; -.
DR   GeneCards; NAA40; -.
DR   HGNC; HGNC:25845; NAA40.
DR   HPA; ENSG00000110583; Low tissue specificity.
DR   MIM; 619999; gene.
DR   OpenTargets; ENSG00000110583; -.
DR   VEuPathDB; HostDB:ENSG00000110583; -.
DR   eggNOG; KOG2488; Eukaryota.
DR   GeneTree; ENSGT00390000014903; -.
DR   HOGENOM; CLU_051699_4_0_1; -.
DR   InParanoid; Q86UY6; -.
DR   OMA; AYLHYRF; -.
DR   OrthoDB; 424551at2759; -.
DR   PAN-GO; Q86UY6; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; Q86UY6; -.
DR   BioCyc; MetaCyc:ENSG00000110583-MONOMER; -.
DR   BRENDA; 2.3.1.257; 2681.
DR   PathwayCommons; Q86UY6; -.
DR   SignaLink; Q86UY6; -.
DR   Agora; ENSG00000110583; -.
DR   BioGRID-ORCS; 79829; 77 hits in 1159 CRISPR screens.
DR   ChiTaRS; NAA40; human.
DR   EvolutionaryTrace; Q86UY6; -.
DR   GenomeRNAi; 79829; -.
DR   Pharos; Q86UY6; Tbio.
DR   PRO; PR:Q86UY6; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q86UY6; protein.
DR   Bgee; ENSG00000110583; Expressed in buccal mucosa cell and 171 other cell types or tissues.
DR   ExpressionAtlas; Q86UY6; baseline and differential.
DR   GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043998; F:histone H2A acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:1990189; F:protein N-terminal-serine acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR   FunFam; 3.40.630.30:FF:000033; N-alpha-acetyltransferase 40 isoform X1; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR039949; NAA40.
DR   PANTHER; PTHR20531; N-ALPHA-ACETYLTRANSFERASE 40; 1.
DR   PANTHER; PTHR20531:SF1; N-ALPHA-ACETYLTRANSFERASE 40; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Alternative splicing; Cytoplasm;
KW   Lipoprotein; Myristate; Nucleus; Proteomics identification;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..237
FT                   /note="N-alpha-acetyltransferase 40"
FT                   /id="PRO_0000284897"
FT   DOMAIN          63..216
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:25619998,
FT                   ECO:0007744|PDB:4U9W"
FT   BINDING         127..129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:25619998,
FT                   ECO:0007744|PDB:4U9W"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:25619998,
FT                   ECO:0007744|PDB:4U9W"
FT   BINDING         140..142
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:25619998,
FT                   ECO:0007744|PDB:4U9V, ECO:0007744|PDB:4U9W"
FT   BINDING         148..153
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:25619998,
FT                   ECO:0007744|PDB:4U9V, ECO:0007744|PDB:4U9W"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:25619998,
FT                   ECO:0007744|PDB:4U9W"
FT   BINDING         179
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:25619998,
FT                   ECO:0007744|PDB:4U9V, ECO:0007744|PDB:4U9W"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:25619998,
FT                   ECO:0007744|PDB:4U9W"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:25619998,
FT                   ECO:0007744|PDB:4U9W"
FT   SITE            139
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000269|PubMed:25619998"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..51
FT                   /note="MGRKSSKAKEKKQKRLEERAAMDAVCAKVDAANRLGDPLEAFPVFKKYDRN
FT                   -> MPFVPKWTLPT (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054273"
FT   VAR_SEQ         1..21
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054274"
FT   MUTAGEN         85
FT                   /note="Y->A: Strongly reduced N-alpha-acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:25619998"
FT   MUTAGEN         90
FT                   /note="W->A: Strongly reduced N-alpha-acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:25619998"
FT   MUTAGEN         100
FT                   /note="E->A: 5 times reduced N-alpha-acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:25619998"
FT   MUTAGEN         127..129
FT                   /note="DVE->AVA: Strongly reduced N-alpha-acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:25619998"
FT   MUTAGEN         136
FT                   /note="Y->A: Strongly reduced N-alpha-acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:25619998"
FT   MUTAGEN         136
FT                   /note="Y->F: Slightly reduced N-alpha-acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:19695338,
FT                   ECO:0000269|PubMed:25619998"
FT   MUTAGEN         137
FT                   /note="C->A: Reduced N-alpha-acetyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:25619998"
FT   MUTAGEN         138
FT                   /note="Y->A: Strongly reduced N-alpha-acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:25619998"
FT   MUTAGEN         139
FT                   /note="E->Q: Abolished N-alpha-acetyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:19695338,
FT                   ECO:0000269|PubMed:25619998"
FT   MUTAGEN         174
FT                   /note="T->A: Does not affect N-alpha-acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:25619998"
FT   MUTAGEN         211
FT                   /note="Y->A: Does not affect N-alpha-acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:25619998"
FT   CONFLICT        233
FT                   /note="G -> S (in Ref. 1; BAB14720)"
FT                   /evidence="ECO:0000305"
FT   HELIX           19..33
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   TURN            38..41
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:4U9W"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   HELIX           67..87
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   HELIX           94..102
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   STRAND          107..113
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   STRAND          117..129
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   STRAND          132..142
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:7KD7"
FT   HELIX           151..165
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   STRAND          169..176
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   HELIX           180..187
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:7KPU"
FT   STRAND          211..217
FT                   /evidence="ECO:0007829|PDB:7KPU"
SQ   SEQUENCE   237 AA;  27194 MW;  AED75B559073FCE1 CRC64;
     MGRKSSKAKE KKQKRLEERA AMDAVCAKVD AANRLGDPLE AFPVFKKYDR NGLNVSIECK
     RVSGLEPATV DWAFDLTKTN MQTMYEQSEW GWKDREKREE MTDDRAWYLI AWENSSVPVA
     FSHFRFDVEC GDEVLYCYEV QLESKVRRKG LGKFLIQILQ LMANSTQMKK VMLTVFKHNH
     GAYQFFREAL QFEIDDSSPS MSGCCGEDCS YEILSRRTKF GDSHHSHAGG HCGGCCH
//