ID NAA60_HUMAN Reviewed; 242 AA. AC Q9H7X0; B3KRQ0; B4DLZ0; B4DPZ8; B4DYC4; D3DUC2; E7EQ65; Q6IA31; Q6UX26; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 155. DE RecName: Full=N-alpha-acetyltransferase 60 {ECO:0000303|PubMed:25732826, ECO:0000312|HGNC:HGNC:25875}; DE Short=hNaa60 {ECO:0000303|PubMed:27320834, ECO:0000303|PubMed:27550639}; DE EC=2.3.1.259 {ECO:0000269|PubMed:25732826}; DE AltName: Full=Histone acetyltransferase type B protein 4 {ECO:0000303|PubMed:21981917}; DE Short=HAT4 {ECO:0000303|PubMed:21981917}; DE EC=2.3.1.48 {ECO:0000305|PubMed:21981917}; DE AltName: Full=N-acetyltransferase 15; DE AltName: Full=N-alpha-acetyltransferase F; DE Short=NatF; GN Name=NAA60 {ECO:0000303|PubMed:25732826, ECO:0000312|HGNC:HGNC:25875}; GN Synonyms=HAT4 {ECO:0000303|PubMed:21981917}, NAT15; GN ORFNames=UNQ2771/PRO7155; 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] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5). RC TISSUE=Fetal brain, Mesangial cell, Teratocarcinoma, and Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). 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] (ISOFORM 1). RC TISSUE=Brain; 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 IMPRINTING, AND INDUCTION. RX PubMed=21593219; DOI=10.1093/hmg/ddr224; RA Nakabayashi K., Trujillo A.M., Tayama C., Camprubi C., Yoshida W., RA Lapunzina P., Sanchez A., Soejima H., Aburatani H., Nagae G., Ogata T., RA Hata K., Monk D.; RT "Methylation screening of reciprocal genome-wide UPDs identifies novel RT human-specific imprinted genes."; RL Hum. Mol. Genet. 20:3188-3197(2011). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACETYLATION AT LYS-79; RP LYS-105; LYS-109; LYS-121 AND LYS-156, AND MUTAGENESIS OF LYS-79; LYS-105; RP LYS-109; GLY-111; LYS-121 AND LYS-156. RX PubMed=21981917; DOI=10.1016/j.molcel.2011.07.032; RA Yang X., Yu W., Shi L., Sun L., Liang J., Yi X., Li Q., Zhang Y., Yang F., RA Han X., Zhang D., Yang J., Yao Z., Shang Y.; RT "HAT4, a Golgi apparatus-anchored B-type histone acetyltransferase, RT acetylates free histone H4 and facilitates chromatin assembly."; RL Mol. Cell 44:39-50(2011). RN [9] RP FUNCTION. RX PubMed=21750686; DOI=10.1371/journal.pgen.1002169; RA Van Damme P., Hole K., Pimenta-Marques A., Helsens K., Vandekerckhove J., RA Martinho R.G., Gevaert K., Arnesen T.; RT "NatF contributes to an evolutionary shift in protein N-terminal RT acetylation and is important for normal chromosome segregation."; RL PLoS Genet. 7:E1002169-E1002169(2011). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, AND RP MUTAGENESIS OF CYS-19; CYS-30; CYS-132; CYS-207; 221-LEU-LEU-222 AND RP CYS-222. 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] {ECO:0000312|PDB:5HGZ, ECO:0000312|PDB:5HH0, ECO:0000312|PDB:5HH1} RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 4-242 IN COMPLEX WITH ACETYL-COA, RP FUNCTION, ACTIVE SITES, AND MUTAGENESIS OF PHE-34; GLU-37; TYR-38; LYS-79; RP GLU-80; ASP-81; ASP-83; TYR-97; HIS-138; ASN-143 AND TYR-165. RX PubMed=27550639; DOI=10.1038/srep31425; RA Chen J.Y., Liu L., Cao C.L., Li M.J., Tan K., Yang X., Yun C.H.; RT "Structure and function of human Naa60 (NatF), a Golgi-localized bi- RT functional acetyltransferase."; RL Sci. Rep. 6:31425-31425(2016). RN [12] {ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW} RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 3-184 IN COMPLEX WITH ACETYL-COA RP AND SUBSTRATE, FUNCTION, ACTIVE SITES, SUBUNIT, AND MUTAGENESIS OF PRO-35; RP ILE-36; TYR-38; ASP-81; ILE-84; TYR-97; HIS-138; LEU-140; TYR-164; TYR-165 RP AND ILE-167. RX PubMed=27320834; DOI=10.1016/j.str.2016.04.020; RA Stoeve S.I., Magin R.S., Foyn H., Haug B.E., Marmorstein R., Arnesen T.; RT "Crystal structure of the Golgi-associated human Nalpha-Acetyltransferase RT 60 Reveals the molecular determinants for substrate-specific acetylation."; RL Structure 24:1044-1056(2016). CC -!- FUNCTION: N-alpha-acetyltransferase that specifically mediates the CC acetylation of N-terminal residues of the transmembrane proteins, with CC a strong preference for N-termini facing the cytosol (PubMed:25732826). CC Displays N-terminal acetyltransferase activity towards a range of N- CC terminal sequences including those starting with Met-Lys, Met-Val, Met- CC Ala and Met-Met (PubMed:21750686, PubMed:25732826, PubMed:27550639, CC PubMed:27320834). Required for normal chromosomal segregation during CC anaphase (PubMed:21750686). May also show histone acetyltransferase CC activity; such results are however unclear in vivo and would require CC additional experimental evidences (PubMed:21981917). CC {ECO:0000269|PubMed:21750686, ECO:0000269|PubMed:25732826, CC ECO:0000269|PubMed:27320834, ECO:0000269|PubMed:27550639, CC ECO:0000305|PubMed:21981917}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + N-terminal L-methionyl-[transmembrane protein] = CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-[transmembrane CC protein]; Xref=Rhea:RHEA:50604, Rhea:RHEA-COMP:12745, Rhea:RHEA- CC COMP:12746, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:64731, ChEBI:CHEBI:133414; EC=2.3.1.259; CC Evidence={ECO:0000269|PubMed:25732826}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000305|PubMed:21981917}; CC -!- SUBUNIT: Monomer and homodimer; monomer in presence of substrate and CC homodimer in its absence (PubMed:27320834). CC {ECO:0000269|PubMed:27320834}. CC -!- INTERACTION: CC Q9H7X0; P55212: CASP6; NbExp=3; IntAct=EBI-12260336, EBI-718729; CC Q9H7X0; P13473-2: LAMP2; NbExp=3; IntAct=EBI-12260336, EBI-21591415; CC Q9H7X0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12260336, EBI-16439278; CC Q9H7X0; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-12260336, EBI-5280197; CC Q9H7X0; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-12260336, EBI-2623095; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:21981917, ECO:0000269|PubMed:25732826}; Peripheral CC membrane protein {ECO:0000269|PubMed:25732826}; Cytoplasmic side CC {ECO:0000269|PubMed:25732826}. Note=Probably forms an intramembrane CC hairpin-like structure in the membrane. {ECO:0000305|PubMed:25732826}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9H7X0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H7X0-2; Sequence=VSP_044123; CC Name=3; CC IsoId=Q9H7X0-3; Sequence=VSP_044122; CC Name=4; CC IsoId=Q9H7X0-4; Sequence=VSP_044124; CC Name=5; CC IsoId=Q9H7X0-5; Sequence=VSP_044125; CC -!- INDUCTION: Isoform 2: Imprinted (PubMed:21593219). Promoter methylation CC of the paternal allele may restrict expression to the maternal allele CC in placenta and leukocytes (PubMed:21593219). Isoform 1: Biallelically CC expressed (PubMed:21593219). {ECO:0000269|PubMed:21593219}. CC -!- PTM: Acetylated: autoacetylation is required for optimal CC acetyltransferase activity. {ECO:0000269|PubMed:21981917}. CC -!- MISCELLANEOUS: [Isoform 2]: In placenta and leukocytes, expressed from CC the maternal allele, due to imprinting of the paternal allele. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the acetyltransferase family. NAA60 subfamily. CC {ECO:0000305}. CC -!- CAUTION: According to a report, displays histone acetyltransferase CC activity while localized in the Golgi apparatus (PubMed:21981917). May CC mediate acetylation of free histone H4 and promote nucleosome assembly CC (PubMed:21981917). Such results are however unclear in vivo and recent CC reports strongly suggest that it acts as a N-alpha-acetyltransferase CC that specifically targets N-terminal residues of transmembrane proteins CC (PubMed:21750686, PubMed:25732826). {ECO:0000269|PubMed:21750686, CC ECO:0000269|PubMed:21981917, ECO:0000269|PubMed:25732826}. 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; AY358543; AAQ88907.1; -; mRNA. DR EMBL; AK024216; BAB14853.1; -; mRNA. DR EMBL; AK092005; BAG52462.1; -; mRNA. DR EMBL; AK297219; BAG59702.1; -; mRNA. DR EMBL; AK298566; BAG60760.1; -; mRNA. DR EMBL; AK302361; BAG63686.1; -; mRNA. DR EMBL; CR457324; CAG33605.1; -; mRNA. DR EMBL; AC004224; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC025283; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471112; EAW85358.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85359.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85360.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85361.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85362.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85363.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85364.1; -; Genomic_DNA. DR EMBL; BC011267; AAH11267.1; -; mRNA. DR CCDS; CCDS45396.1; -. [Q9H7X0-1] DR CCDS; CCDS81937.1; -. [Q9H7X0-2] DR CCDS; CCDS81938.1; -. [Q9H7X0-5] DR CCDS; CCDS81939.1; -. [Q9H7X0-4] DR CCDS; CCDS81941.1; -. [Q9H7X0-3] DR RefSeq; NP_001077069.1; NM_001083600.2. [Q9H7X0-1] DR RefSeq; NP_001077070.1; NM_001083601.2. [Q9H7X0-1] DR RefSeq; NP_001304022.1; NM_001317093.1. [Q9H7X0-2] DR RefSeq; NP_001304023.1; NM_001317094.1. DR RefSeq; NP_001304024.1; NM_001317095.1. [Q9H7X0-3] DR RefSeq; NP_001304025.1; NM_001317096.1. [Q9H7X0-5] DR RefSeq; NP_001304026.1; NM_001317097.1. [Q9H7X0-4] DR RefSeq; NP_001304027.1; NM_001317098.1. [Q9H7X0-4] DR RefSeq; NP_079121.1; NM_024845.3. [Q9H7X0-1] DR PDB; 5HGZ; X-ray; 1.38 A; A=4-242. DR PDB; 5HH0; X-ray; 1.60 A; A=4-199. DR PDB; 5HH1; X-ray; 1.80 A; A=4-199. DR PDB; 5ICV; X-ray; 1.53 A; A/B=5-184. DR PDB; 5ICW; X-ray; 1.95 A; A/B/C/D=3-184. DR PDBsum; 5HGZ; -. DR PDBsum; 5HH0; -. DR PDBsum; 5HH1; -. DR PDBsum; 5ICV; -. DR PDBsum; 5ICW; -. DR AlphaFoldDB; Q9H7X0; -. DR SMR; Q9H7X0; -. DR BioGRID; 122986; 47. DR DIP; DIP-62077N; -. DR IntAct; Q9H7X0; 6. DR MINT; Q9H7X0; -. DR STRING; 9606.ENSP00000401237; -. DR ChEMBL; CHEMBL4630856; -. DR iPTMnet; Q9H7X0; -. DR PhosphoSitePlus; Q9H7X0; -. DR SwissPalm; Q9H7X0; -. DR BioMuta; NAA60; -. DR DMDM; 74733721; -. DR EPD; Q9H7X0; -. DR jPOST; Q9H7X0; -. DR MassIVE; Q9H7X0; -. DR MaxQB; Q9H7X0; -. DR PaxDb; 9606-ENSP00000385903; -. DR PeptideAtlas; Q9H7X0; -. DR ProteomicsDB; 17514; -. DR ProteomicsDB; 5517; -. DR ProteomicsDB; 81152; -. [Q9H7X0-1] DR Pumba; Q9H7X0; -. DR Antibodypedia; 24137; 180 antibodies from 19 providers. DR DNASU; 79903; -. DR Ensembl; ENST00000360862.9; ENSP00000354108.5; ENSG00000122390.19. [Q9H7X0-3] DR Ensembl; ENST00000407558.9; ENSP00000385903.4; ENSG00000122390.19. [Q9H7X0-1] DR Ensembl; ENST00000414063.6; ENSP00000393224.2; ENSG00000122390.19. [Q9H7X0-1] DR Ensembl; ENST00000421765.7; ENSP00000405873.3; ENSG00000122390.19. [Q9H7X0-5] DR Ensembl; ENST00000424546.6; ENSP00000401237.2; ENSG00000122390.19. [Q9H7X0-2] DR Ensembl; ENST00000570819.5; ENSP00000460763.1; ENSG00000122390.19. [Q9H7X0-4] DR Ensembl; ENST00000572169.6; ENSP00000458928.2; ENSG00000122390.19. [Q9H7X0-1] DR Ensembl; ENST00000572584.2; ENSP00000459057.1; ENSG00000122390.19. [Q9H7X0-1] DR Ensembl; ENST00000572942.5; ENSP00000461730.1; ENSG00000122390.19. [Q9H7X0-4] DR Ensembl; ENST00000573580.5; ENSP00000459055.1; ENSG00000122390.19. [Q9H7X0-3] DR Ensembl; ENST00000575076.5; ENSP00000458667.1; ENSG00000122390.19. [Q9H7X0-1] DR Ensembl; ENST00000577013.6; ENSP00000458575.2; ENSG00000122390.19. [Q9H7X0-3] DR Ensembl; ENST00000649205.1; ENSP00000497988.1; ENSG00000122390.19. [Q9H7X0-1] DR Ensembl; ENST00000649360.1; ENSP00000497411.1; ENSG00000122390.19. [Q9H7X0-1] DR GeneID; 79903; -. DR KEGG; hsa:79903; -. DR MANE-Select; ENST00000407558.9; ENSP00000385903.4; NM_001083601.3; NP_001077070.1. DR UCSC; uc002cvg.3; human. [Q9H7X0-1] DR AGR; HGNC:25875; -. DR DisGeNET; 79903; -. DR GeneCards; NAA60; -. DR HGNC; HGNC:25875; NAA60. DR HPA; ENSG00000122390; Low tissue specificity. DR MIM; 614246; gene. DR neXtProt; NX_Q9H7X0; -. DR OpenTargets; ENSG00000122390; -. DR PharmGKB; PA164723438; -. DR VEuPathDB; HostDB:ENSG00000122390; -. DR eggNOG; KOG3138; Eukaryota. DR GeneTree; ENSGT00390000008314; -. DR HOGENOM; CLU_1427523_0_0_1; -. DR InParanoid; Q9H7X0; -. DR OMA; FDYIHHI; -. DR OrthoDB; 886671at2759; -. DR PhylomeDB; Q9H7X0; -. DR TreeFam; TF323980; -. DR BioCyc; MetaCyc:ENSG00000122390-MONOMER; -. DR BRENDA; 2.3.1.259; 2681. DR PathwayCommons; Q9H7X0; -. DR SignaLink; Q9H7X0; -. DR BioGRID-ORCS; 79903; 11 hits in 1166 CRISPR screens. DR ChiTaRS; NAA60; human. DR GenomeRNAi; 79903; -. DR Pharos; Q9H7X0; Tbio. DR PRO; PR:Q9H7X0; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9H7X0; Protein. DR Bgee; ENSG00000122390; Expressed in pancreatic ductal cell and 198 other cell types or tissues. DR ExpressionAtlas; Q9H7X0; baseline and differential. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central. DR GO; GO:0010485; F:histone H4 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB. DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB. DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IDA:UniProtKB. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:UniProtKB. DR GO; GO:0006334; P:nucleosome assembly; 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 InterPro; IPR045141; NAA60-like. DR PANTHER; PTHR14744; N-ALPHA-ACETYLTRANSFERASE 60; 1. DR PANTHER; PTHR14744:SF15; N-ALPHA-ACETYLTRANSFERASE 60; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR PROSITE; PS51186; GNAT; 1. DR Genevisible; Q9H7X0; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Alternative promoter usage; KW Alternative splicing; Chromatin regulator; Chromosome partition; KW Golgi apparatus; Membrane; Reference proteome; Transferase. FT CHAIN 1..242 FT /note="N-alpha-acetyltransferase 60" FT /id="PRO_0000321566" FT TOPO_DOM 1..192 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:25732826" FT INTRAMEM 193..236 FT /note="Helical" FT /evidence="ECO:0000305|PubMed:25732826" FT TOPO_DOM 237..242 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:25732826" FT DOMAIN 13..182 FT /note="N-acetyltransferase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532" FT REGION 162..173 FT /note="Required for homodimerization" FT /evidence="ECO:0000269|PubMed:27320834" FT ACT_SITE 97 FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639" FT ACT_SITE 138 FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639" FT BINDING 38 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW" FT BINDING 101..103 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639, ECO:0000312|PDB:5HGZ, FT ECO:0000312|PDB:5HH0, ECO:0000312|PDB:5HH1, FT ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW" FT BINDING 109..114 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639, ECO:0000312|PDB:5HGZ, FT ECO:0000312|PDB:5HH0, ECO:0000312|PDB:5HH1, FT ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW" FT BINDING 143 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639, ECO:0000312|PDB:5HGZ, FT ECO:0000312|PDB:5HH0, ECO:0000312|PDB:5HH1, FT ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW" FT BINDING 150..153 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639, ECO:0000312|PDB:5HGZ, FT ECO:0000312|PDB:5HH0, ECO:0000312|PDB:5HH1, FT ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW" FT BINDING 165 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW" FT SITE 34 FT /note="Required to position thioacetyl group" FT /evidence="ECO:0000269|PubMed:27550639" FT MOD_RES 79 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:21981917" FT MOD_RES 105 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:21981917" FT MOD_RES 109 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000305|PubMed:21981917" FT MOD_RES 121 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000305|PubMed:21981917" FT MOD_RES 156 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:21981917" FT VAR_SEQ 1..65 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044122" FT VAR_SEQ 1..36 FT /note="MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPI -> MFPRRRTERRLG FT DTGTRKKIAYRKAVPGGRKCGASLSWEKSSR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044123" FT VAR_SEQ 113..242 FT /note="GSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYY FT YSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCS FT FLPWSGISSKSGIEYSRTM -> ESTARPTACSAASCHGRASLPRVASSTAGPCDVGWA FT AATRPHPSAARRARLPVHLTPSVFCKELPAI (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044124" FT VAR_SEQ 113..242 FT /note="GSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYY FT YSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCS FT FLPWSGISSKSGIEYSRTM -> EPHGLHPAPGLCTSQPEPLLHSAQSLPPGPQPALQL FT PAMVGHLFQEWHRVQPDHVMSAGQPPPGPTLRPPAEPAFLSI (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044125" FT VARIANT 218 FT /note="H -> Q (in dbSNP:rs34464545)" FT /id="VAR_060995" FT MUTAGEN 19 FT /note="C->S: Does not affect localization to the Golgi FT apparatus; when associated with S-30; S-132; S-207 and FT S-222." FT /evidence="ECO:0000269|PubMed:25732826" FT MUTAGEN 30 FT /note="C->S: Does not affect localization to the Golgi FT apparatus; when associated with S-19; S-132; S-207 and FT S-222." FT /evidence="ECO:0000269|PubMed:25732826" FT MUTAGEN 34 FT /note="F->A: Abolished acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27550639" FT MUTAGEN 35 FT /note="P->A: Reduced acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27320834" FT MUTAGEN 36 FT /note="I->A: Reduced acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27320834" FT MUTAGEN 37 FT /note="E->A,F: Only slightly affects acetyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:27550639" FT MUTAGEN 38 FT /note="Y->A: Strongly reduced acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639" FT MUTAGEN 79 FT /note="K->A: Slightly reduced acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27550639" FT MUTAGEN 79 FT /note="K->R,Q: Increased acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27550639" FT MUTAGEN 79 FT /note="K->R: Decreased acetyltransferase activity; when FT associated with R-105, R-109, R-121 and R-156." FT /evidence="ECO:0000269|PubMed:21981917" FT MUTAGEN 80 FT /note="E->A: Slightly increased acetyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:27550639" FT MUTAGEN 81 FT /note="D->A: Slightly increased acetyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639" FT MUTAGEN 83 FT /note="D->A: Slightly increased acetyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:27550639" FT MUTAGEN 84 FT /note="I->A: Slightly altered acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27320834" FT MUTAGEN 97 FT /note="Y->A,F: Abolished acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639" FT MUTAGEN 105 FT /note="K->R: Decreased acetyltransferase activity; when FT associated with R-79, R-109, R-121 and R-156." FT /evidence="ECO:0000269|PubMed:21981917" FT MUTAGEN 109 FT /note="K->R: Decreased acetyltransferase activity; when FT associated with R-79, R-105, R-121 and R-156." FT /evidence="ECO:0000269|PubMed:21981917" FT MUTAGEN 111 FT /note="G->A: Abolishes acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:21981917" FT MUTAGEN 121 FT /note="K->R: Decreased acetyltransferase activity; when FT associated with R-79, R-105, R-109 and R-156." FT /evidence="ECO:0000269|PubMed:21981917" FT MUTAGEN 132 FT /note="C->S: Does not affect localization to the Golgi FT apparatus; when associated with S-19; S-30; S-207 and FT S-222." FT /evidence="ECO:0000269|PubMed:25732826" FT MUTAGEN 138 FT /note="H->A,F: Abolished acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639" FT MUTAGEN 140 FT /note="L->A: Decreased acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27320834" FT MUTAGEN 143 FT /note="N->A: Strongly reduced acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27550639" FT MUTAGEN 156 FT /note="K->R: Decreased histone acetyltransferase activity; FT when associated with R-79, R-105, R-109 and R-121." FT /evidence="ECO:0000269|PubMed:21981917" FT MUTAGEN 164 FT /note="Y->A,F: Slightly altered acetyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:27320834" FT MUTAGEN 165 FT /note="Y->A,F: Strongly reduced acetyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:27320834, FT ECO:0000269|PubMed:27550639" FT MUTAGEN 167 FT /note="I->A: Reduced acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:27320834" FT MUTAGEN 207 FT /note="C->S: Does not affect localization to the Golgi FT apparatus; when associated with S-19; S-30; S-132 and FT S-222." FT /evidence="ECO:0000269|PubMed:25732826" FT MUTAGEN 220..221 FT /note="LL->AA: Does not affect localization to the Golgi FT apparatus." FT /evidence="ECO:0000269|PubMed:25732826" FT MUTAGEN 222 FT /note="C->S: Does not affect localization to the Golgi FT apparatus; when associated with S-19; S-30; S-132 and FT S-207." FT /evidence="ECO:0000269|PubMed:25732826" FT CONFLICT 87 FT /note="S -> T (in Ref. 1; AAQ88907)" FT /evidence="ECO:0000305" FT CONFLICT 242 FT /note="M -> I (in Ref. 3; CAG33605)" FT /evidence="ECO:0000305" FT HELIX 3..9 FT /evidence="ECO:0007829|PDB:5HGZ" FT STRAND 12..17 FT /evidence="ECO:0007829|PDB:5HGZ" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:5HGZ" FT HELIX 23..33 FT /evidence="ECO:0007829|PDB:5HGZ" FT HELIX 40..48 FT /evidence="ECO:0007829|PDB:5HGZ" FT STRAND 52..59 FT /evidence="ECO:0007829|PDB:5HGZ" FT STRAND 62..73 FT /evidence="ECO:0007829|PDB:5HGZ" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:5HGZ" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:5HGZ" FT TURN 82..87 FT /evidence="ECO:0007829|PDB:5ICV" FT STRAND 94..103 FT /evidence="ECO:0007829|PDB:5HGZ" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:5HGZ" FT HELIX 112..128 FT /evidence="ECO:0007829|PDB:5HGZ" FT TURN 129..131 FT /evidence="ECO:0007829|PDB:5HGZ" FT STRAND 132..140 FT /evidence="ECO:0007829|PDB:5HGZ" FT HELIX 144..151 FT /evidence="ECO:0007829|PDB:5HGZ" FT TURN 152..154 FT /evidence="ECO:0007829|PDB:5HGZ" FT STRAND 156..167 FT /evidence="ECO:0007829|PDB:5HGZ" FT STRAND 170..180 FT /evidence="ECO:0007829|PDB:5HGZ" FT HELIX 190..201 FT /evidence="ECO:0007829|PDB:5HGZ" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:5HGZ" FT CONFLICT Q9H7X0-5:180 FT /note="R -> Q (in Ref. 2; BAG60760)" FT /evidence="ECO:0000305" SQ SEQUENCE 242 AA; 27451 MW; 11234F2C51DF55DE CRC64; MTEVVPSSAL SEVSLRLLCH DDIDTVKHLC GDWFPIEYPD SWYRDITSNK KFFSLAATYR GAIVGMIVAE IKNRTKIHKE DGDILASNFS VDTQVAYILS LGVVKEFRKH GIGSLLLESL KDHISTTAQD HCKAIYLHVL TTNNTAINFY ENRDFKQHHY LPYYYSIRGV LKDGFTYVLY INGGHPPWTI LDYIQHLGSA LASLSPCSIP HRVYRQAHSL LCSFLPWSGI SSKSGIEYSR TM //