NAA40_HUMAN
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 03-AUG-2022, entry version 150.
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=acetyl-CoA + N-terminal L-seryl-[histone H4] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[histone H4]; Xref=Rhea:RHEA:50596,
CC Rhea:RHEA-COMP:12740, Rhea:RHEA-COMP:12743, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.257;
CC Evidence={ECO:0000269|PubMed:21935442, ECO:0000269|PubMed:25619998};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-seryl-[histone H2A];
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_024771.3. [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; 966.
DR DIP; DIP-61383N; -.
DR IntAct; Q86UY6; 15.
DR STRING; 9606.ENSP00000367024; -.
DR BindingDB; Q86UY6; -.
DR ChEMBL; CHEMBL4523373; -.
DR iPTMnet; Q86UY6; -.
DR PhosphoSitePlus; Q86UY6; -.
DR SwissPalm; Q86UY6; -.
DR BioMuta; NAA40; -.
DR DMDM; 74727506; -.
DR EPD; Q86UY6; -.
DR jPOST; Q86UY6; -.
DR MassIVE; Q86UY6; -.
DR MaxQB; Q86UY6; -.
DR PaxDb; Q86UY6; -.
DR PeptideAtlas; Q86UY6; -.
DR PRIDE; Q86UY6; -.
DR ProteomicsDB; 4913; -.
DR ProteomicsDB; 5140; -.
DR ProteomicsDB; 69938; -. [Q86UY6-1]
DR Antibodypedia; 43913; 79 antibodies from 24 providers.
DR DNASU; 79829; -.
DR Ensembl; ENST00000377793.9; ENSP00000367024.4; ENSG00000110583.13. [Q86UY6-1]
DR Ensembl; ENST00000542163.1; ENSP00000442055.1; ENSG00000110583.13. [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 CTD; 79829; -.
DR DisGeNET; 79829; -.
DR GeneCards; NAA40; -.
DR HGNC; HGNC:25845; NAA40.
DR HPA; ENSG00000110583; Low tissue specificity.
DR neXtProt; NX_Q86UY6; -.
DR OpenTargets; ENSG00000110583; -.
DR PharmGKB; PA165543497; -.
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; 1489686at2759; -.
DR PhylomeDB; Q86UY6; -.
DR TreeFam; TF315129; -.
DR BioCyc; MetaCyc:ENSG00000110583-MON; -.
DR BRENDA; 2.3.1.257; 2681.
DR PathwayCommons; Q86UY6; -.
DR SignaLink; Q86UY6; -.
DR BioGRID-ORCS; 79829; 62 hits in 1079 CRISPR screens.
DR ChiTaRS; NAA40; human.
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 169 other tissues.
DR ExpressionAtlas; Q86UY6; baseline and differential.
DR Genevisible; Q86UY6; HS.
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:H2A histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039949; NAA40.
DR PANTHER; PTHR20531; PTHR20531; 1.
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;
KW Lipoprotein; Myristate; Nucleus; 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
