NAA60_HUMAN
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 03-AUG-2022, entry version 146.
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}.
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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.ENSP00000385903; -.
DR ChEMBL; CHEMBL4630856; -.
DR iPTMnet; Q9H7X0; -.
DR PhosphoSitePlus; Q9H7X0; -.
DR BioMuta; NAA60; -.
DR DMDM; 74733721; -.
DR EPD; Q9H7X0; -.
DR jPOST; Q9H7X0; -.
DR MassIVE; Q9H7X0; -.
DR MaxQB; Q9H7X0; -.
DR PaxDb; Q9H7X0; -.
DR PeptideAtlas; Q9H7X0; -.
DR PRIDE; Q9H7X0; -.
DR ProteomicsDB; 17514; -.
DR ProteomicsDB; 5517; -.
DR ProteomicsDB; 81152; -. [Q9H7X0-1]
DR Antibodypedia; 24137; 158 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 CTD; 79903; -.
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; IYPTIAY; -.
DR OrthoDB; 1619974at2759; -.
DR PhylomeDB; Q9H7X0; -.
DR TreeFam; TF323980; -.
DR BioCyc; MetaCyc:ENSG00000122390-MON; -.
DR BRENDA; 2.3.1.259; 2681.
DR PathwayCommons; Q9H7X0; -.
DR SignaLink; Q9H7X0; -.
DR BioGRID-ORCS; 79903; 11 hits in 1078 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 196 other tissues.
DR ExpressionAtlas; Q9H7X0; baseline and differential.
DR Genevisible; Q9H7X0; HS.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
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:0043966; P:histone H3 acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IDA: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 InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR045141; NAA60-like.
DR PANTHER; PTHR14744; PTHR14744; 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; 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 S-
FT 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 S-
FT 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 S-
FT 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 S-
FT 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 S-
FT 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
