ID NAA15_HUMAN Reviewed; 866 AA. AC Q9BXJ9; D3DNY6; Q52LG9; Q8IWH4; Q8NEV2; Q9H8P6; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 198. DE RecName: Full=N-alpha-acetyltransferase 15, NatA auxiliary subunit; DE AltName: Full=Gastric cancer antigen Ga19; DE AltName: Full=N-terminal acetyltransferase; DE AltName: Full=NMDA receptor-regulated protein 1; DE AltName: Full=Protein tubedown-1; DE AltName: Full=Tbdn100; GN Name=NAA15; Synonyms=GA19, NARG1, NATH, TBDN100; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Gastric adenocarcinoma; RX PubMed=12087473; DOI=10.1038/sj.bjc.6600321; RA Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.; RT "Serological identification and expression analysis of gastric cancer- RT associated genes."; RL Br. J. Cancer 86:1824-1830(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS RP SPECTROMETRY, INTERACTION WITH XRCC6 AND XRCC5, AND FUNCTION. RC TISSUE=Heart, and Osteoblast; RX PubMed=12145306; DOI=10.1074/jbc.m206482200; RA Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S., Ornitz D.M., RA Towler D.A.; RT "Regulation of osteocalcin gene expression by a novel Ku antigen RT transcription factor complex."; RL J. Biol. Chem. 277:37280-37291(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Thyroid carcinoma; RX PubMed=12140756; DOI=10.1038/sj.onc.1205687; RA Fluge O., Bruland O., Akslen L.A., Varhaug J.E., Lillehaug J.R.; RT "NATH, a novel gene overexpressed in papillary thyroid carcinomas."; RL Oncogene 21:5056-5068(2002). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=12019451; RA He Y.G., Xie Y.F., Chen Y., Qian W., Lai J.H., Tan D.Y.; RT "Cloning and analysis of a novel gene encoding N-terminal acetyltransferase RT subunit."; RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:353-357(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Ovary; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and 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 [9] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=11687548; RA Gendron R.L., Good W.V., Adams L.C., Paradis H.; RT "Suppressed expression of tubedown-1 in retinal neovascularization of RT proliferative diabetic retinopathy."; RL Invest. Ophthalmol. Vis. Sci. 42:3000-3007(2001). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND RP INTERACTION WITH NAA10. RX PubMed=15496142; DOI=10.1042/bj20041071; RA Arnesen T., Anderson D., Baldersheim C., Lanotte M., Varhaug J.E., RA Lillehaug J.R.; RT "Identification and characterization of the human ARD1-NATH protein RT acetyltransferase complex."; RL Biochem. J. 386:433-443(2005). RN [11] RP INTERACTION WITH NAA11. RX PubMed=16638120; DOI=10.1186/1471-2091-7-13; RA Arnesen T., Betts M.J., Pendino F., Liberles D.A., Anderson D., Caro J., RA Kong X., Varhaug J.E., Lillehaug J.R.; RT "Characterization of hARD2, a processed hARD1 gene duplicate, encoding a RT human protein N-alpha-acetyltransferase."; RL BMC Biochem. 7:13-13(2006). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP INTERACTION WITH NAA50. RX PubMed=16507339; DOI=10.1016/j.gene.2005.12.008; RA Arnesen T., Anderson D., Torsvik J., Halseth H.B., Varhaug J.E., RA Lillehaug J.R.; RT "Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved RT component of the NatA protein N-alpha-acetyltransferase complex."; RL Gene 371:291-295(2006). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] 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 [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-262; LYS-735 AND LYS-756, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [19] RP FUNCTION, IDENTIFICATION IN THE N-TERMINAL ACETYLTRANSFERASE A COMPLEX, RP IDENTIFICATION IN THE N-TERMINAL ACETYLTRANSFERASE A/HYPK COMPLEX, AND RP INTERACTION WITH HYPK AND NAA10. RX PubMed=20154145; DOI=10.1128/mcb.01199-09; RA Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H., Betts M.J., RA Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.; RT "The chaperone-like protein HYPK acts together with NatA in cotranslational RT N-terminal acetylation and prevention of Huntingtin aggregation."; RL Mol. Cell. Biol. 30:1898-1909(2010). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-856, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-537; SER-588 AND RP SER-855, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [25] {ECO:0007744|PDB:6C95, ECO:0007744|PDB:6C9M} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH NAA10 AND HYPK, RP FUNCTION, IDENTIFICATION IN THE N-TERMINAL ACETYLTRANSFERASE A/HYPK RP COMPLEX, IDENTIFICATION IN THE N-TERMINAL ACETYLTRANSFERASE E COMPLEX, RP INTERACTION WITH NAA10; NAA50 AND HYPK, AND MUTAGENESIS OF TYR-834. RX PubMed=29754825; DOI=10.1016/j.str.2018.04.003; RA Gottlieb L., Marmorstein R.; RT "Structure of Human NatA and Its Regulation by the Huntingtin Interacting RT Protein HYPK."; RL Structure 26:925-935.e8(2018). RN [26] {ECO:0007744|PDB:6PPL, ECO:0007744|PDB:6PW9} RP STRUCTURE BY ELECTRON MICROSCOPY (3.02 ANGSTROMS), FUNCTION, IDENTIFICATION RP IN THE N-TERMINAL ACETYLTRANSFERASE A COMPLEX, IDENTIFICATION IN THE RP N-TERMINAL ACETYLTRANSFERASE A/HYPK COMPLEX, IDENTIFICATIONIN THE RP N-TERMINAL ACETYLTRANSFERASE E COMPLEX, IDENTIFICATION IN THE N-TERMINAL RP ACETYLTRANSFERASE E/HYPK COMPLEX, INTERACTION WITH NAA10; HYPK AND NAA50, RP AND MUTAGENESIS OF THR-406 AND LEU-814. RX PubMed=32042062; DOI=10.1038/s41467-020-14584-7; RA Deng S., McTiernan N., Wei X., Arnesen T., Marmorstein R.; RT "Molecular basis for N-terminal acetylation by human NatE and its RT modulation by HYPK."; RL Nat. Commun. 11:818-818(2020). RN [27] RP INVOLVEMENT IN MRD50, AND VARIANTS MRD50 52-LYS--ILE-866 DEL; ASN-112; RP 290-GLY--ILE-866 DEL; GLU-450; VAL-475; 565-TYR--ILE-866 DEL; RP 696-LYS--ILE-866 DEL; 782-ARG--ILE-866 DEL AND 797-ARG--ILE-866 DEL. RX PubMed=28191889; DOI=10.1038/ng.3792; RA Stessman H.A., Xiong B., Coe B.P., Wang T., Hoekzema K., Fenckova M., RA Kvarnung M., Gerdts J., Trinh S., Cosemans N., Vives L., Lin J., RA Turner T.N., Santen G., Ruivenkamp C., Kriek M., van Haeringen A., Aten E., RA Friend K., Liebelt J., Barnett C., Haan E., Shaw M., Gecz J., RA Anderlid B.M., Nordgren A., Lindstrand A., Schwartz C., Kooy R.F., RA Vandeweyer G., Helsmoortel C., Romano C., Alberti A., Vinci M., Avola E., RA Giusto S., Courchesne E., Pramparo T., Pierce K., Nalabolu S., Amaral D.G., RA Scheffer I.E., Delatycki M.B., Lockhart P.J., Hormozdiari F., Harich B., RA Castells-Nobau A., Xia K., Peeters H., Nordenskjoeld M., Schenck A., RA Bernier R.A., Eichler E.E.; RT "Targeted sequencing identifies 91 neurodevelopmental-disorder risk genes RT with autism and developmental-disability biases."; RL Nat. Genet. 49:515-526(2017). CC -!- FUNCTION: Auxillary subunit of N-terminal acetyltransferase complexes CC which display alpha (N-terminal) acetyltransferase (NAT) activity CC (PubMed:15496142, PubMed:20154145, PubMed:29754825, PubMed:32042062). CC The NAT activity may be important for vascular, hematopoietic and CC neuronal growth and development (PubMed:15496142). Required to control CC retinal neovascularization in adult ocular endothelial cells CC (PubMed:11687548). In complex with XRCC6 and XRCC5 (Ku80), up-regulates CC transcription from the osteocalcin promoter (PubMed:12145306). CC {ECO:0000269|PubMed:11687548, ECO:0000269|PubMed:12145306, CC ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:20154145, CC ECO:0000269|PubMed:29754825, ECO:0000269|PubMed:32042062}. CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A complex (also CC called the NatA complex) composed of NAA10 and NAA15 (PubMed:15496142, CC PubMed:20154145, PubMed:32042062). Within the complex interacts with CC NAA10 (PubMed:15496142, PubMed:20154145, PubMed:29754825, CC PubMed:32042062). Component of the N-terminal acetyltransferase A CC (NatA)/HYPK complex at least composed of NAA10, NAA15 and HYPK, which CC has N-terminal acetyltransferase activity (PubMed:20154145, CC PubMed:29754825, PubMed:32042062). In complex with NAA10, interacts CC with HYPK (PubMed:20154145, PubMed:29754825, PubMed:32042062). CC Component of the N-terminal acetyltransferase E (NatE) complex at least CC composed of NAA10, NAA15 and NAA50 (PubMed:29754825, PubMed:32042062). CC Within the complex interacts with NAA10; the interaction is required CC for binding to NAA50 (PubMed:29754825, PubMed:32042062). Interacts with CC NAAT50 (PubMed:16507339, PubMed:29754825, PubMed:32042062). The CC interaction of the NatA complex with NAA50 reduces the acetylation CC activity of the NatA complex (PubMed:32042062). Component of the N- CC terminal acetyltransferase E (NatE)/HYPK complex at least composed of CC NAA10, NAA15, NAA50 and HYPK (PubMed:32042062). In complex with NAA10 CC interacts with HYPK; the interaction with HYPK reduces the capacity of CC the NatA complex to interact with NAA50 (PubMed:20154145, CC PubMed:29754825, PubMed:32042062). Interacts with NAA11 CC (PubMed:16638120). Interacts with XRCC6 and XRCC5 (PubMed:12145306, CC PubMed:29754825, PubMed:16507339). {ECO:0000269|PubMed:12145306, CC ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:16507339, CC ECO:0000269|PubMed:16638120, ECO:0000269|PubMed:20154145, CC ECO:0000269|PubMed:29754825, ECO:0000269|PubMed:32042062}. CC -!- INTERACTION: CC Q9BXJ9; Q9NX55: HYPK; NbExp=5; IntAct=EBI-1042540, EBI-1048743; CC Q9BXJ9; P41227: NAA10; NbExp=7; IntAct=EBI-1042540, EBI-747693; CC Q9BXJ9; Q9GZZ1: NAA50; NbExp=3; IntAct=EBI-1042540, EBI-1052523; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic, CC nuclear in some cases. Present in the free cytosolic and cytoskeleton- CC bound polysomes, but not in the membrane-bound polysomes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long; CC IsoId=Q9BXJ9-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=Q9BXJ9-4; Sequence=VSP_012560, VSP_012561; CC -!- TISSUE SPECIFICITY: Expressed at high levels in testis and in ocular CC endothelial cells. Also found in brain (corpus callosum), heart, colon, CC bone marrow and at lower levels in most adult tissues, including CC thyroid, liver, pancreas, mammary and salivary glands, lung, ovary, CC urogenital system and upper gastrointestinal tract. Overexpressed in CC gastric cancer, in papillary thyroid carcinomas and in a Burkitt CC lymphoma cell line (Daudi). Specifically suppressed in abnormal CC proliferating blood vessels in eyes of patients with proliferative CC diabetic retinopathy. {ECO:0000269|PubMed:11687548, CC ECO:0000269|PubMed:12087473, ECO:0000269|PubMed:12140756}. CC -!- PTM: Cleaved by caspases during apoptosis, resulting in a stable 35 kDa CC fragment. CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 50, CC with behavioral abnormalities (MRD50) [MIM:617787]: A disorder CC characterized by significantly below average general intellectual CC functioning associated with impairments in adaptive behavior and CC manifested during the developmental period. CC {ECO:0000269|PubMed:28191889}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAH39818.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY039242; AAK68661.1; -; mRNA. DR EMBL; AY112670; AAM48746.1; -; mRNA. DR EMBL; AJ314788; CAC43228.1; -; mRNA. DR EMBL; AF327722; AAK15707.1; -; mRNA. DR EMBL; AK023402; BAB14562.1; -; mRNA. DR EMBL; AC097376; AAY40950.1; -; Genomic_DNA. DR EMBL; CH471056; EAX05119.1; -; Genomic_DNA. DR EMBL; BC039818; AAH39818.1; ALT_SEQ; mRNA. DR EMBL; BC093928; AAH93928.1; -; mRNA. DR EMBL; BC104806; AAI04807.1; -; mRNA. DR CCDS; CCDS43270.1; -. [Q9BXJ9-1] DR RefSeq; NP_476516.1; NM_057175.4. [Q9BXJ9-1] DR PDB; 6C95; X-ray; 3.15 A; A=1-866. DR PDB; 6C9M; X-ray; 2.80 A; A/C=1-866. DR PDB; 6PPL; EM; 3.02 A; B=1-866. DR PDB; 6PW9; EM; 4.03 A; B=1-866. DR PDBsum; 6C95; -. DR PDBsum; 6C9M; -. DR PDBsum; 6PPL; -. DR PDBsum; 6PW9; -. DR AlphaFoldDB; Q9BXJ9; -. DR EMDB; EMD-20442; -. DR EMDB; EMD-20501; -. DR SMR; Q9BXJ9; -. DR BioGRID; 123146; 170. DR ComplexPortal; CPX-6271; NatA N-alpha-acetyltransferase complex, NAA10-NAA15 variant. DR ComplexPortal; CPX-6273; NatA N-alpha-acetyltransferase complex, NAA11-NAA15 variant. DR CORUM; Q9BXJ9; -. DR IntAct; Q9BXJ9; 45. DR MINT; Q9BXJ9; -. DR STRING; 9606.ENSP00000296543; -. DR GlyCosmos; Q9BXJ9; 1 site, 1 glycan. DR GlyGen; Q9BXJ9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BXJ9; -. DR MetOSite; Q9BXJ9; -. DR PhosphoSitePlus; Q9BXJ9; -. DR SwissPalm; Q9BXJ9; -. DR BioMuta; NAA15; -. DR DMDM; 57012969; -. DR EPD; Q9BXJ9; -. DR jPOST; Q9BXJ9; -. DR MassIVE; Q9BXJ9; -. DR MaxQB; Q9BXJ9; -. DR PaxDb; 9606-ENSP00000296543; -. DR PeptideAtlas; Q9BXJ9; -. DR ProteomicsDB; 79443; -. [Q9BXJ9-1] DR ProteomicsDB; 79444; -. [Q9BXJ9-4] DR Pumba; Q9BXJ9; -. DR Antibodypedia; 7371; 271 antibodies from 29 providers. DR DNASU; 80155; -. DR Ensembl; ENST00000296543.10; ENSP00000296543.4; ENSG00000164134.14. [Q9BXJ9-1] DR GeneID; 80155; -. DR KEGG; hsa:80155; -. DR MANE-Select; ENST00000296543.10; ENSP00000296543.4; NM_057175.5; NP_476516.1. DR UCSC; uc003ihu.2; human. [Q9BXJ9-1] DR AGR; HGNC:30782; -. DR DisGeNET; 80155; -. DR GeneCards; NAA15; -. DR HGNC; HGNC:30782; NAA15. DR HPA; ENSG00000164134; Low tissue specificity. DR MalaCards; NAA15; -. DR MIM; 608000; gene. DR MIM; 617787; phenotype. DR neXtProt; NX_Q9BXJ9; -. DR OpenTargets; ENSG00000164134; -. DR PharmGKB; PA165664293; -. DR VEuPathDB; HostDB:ENSG00000164134; -. DR eggNOG; KOG1156; Eukaryota. DR GeneTree; ENSGT00950000183174; -. DR InParanoid; Q9BXJ9; -. DR OMA; MEMRADY; -. DR OrthoDB; 23236at2759; -. DR PhylomeDB; Q9BXJ9; -. DR TreeFam; TF106301; -. DR BioCyc; MetaCyc:ENSG00000164134-MONOMER; -. DR BRENDA; 2.3.1.255; 2681. DR BRENDA; 2.3.1.258; 2681. DR PathwayCommons; Q9BXJ9; -. DR SABIO-RK; Q9BXJ9; -. DR SignaLink; Q9BXJ9; -. DR SIGNOR; Q9BXJ9; -. DR BioGRID-ORCS; 80155; 764 hits in 1168 CRISPR screens. DR ChiTaRS; NAA15; human. DR GeneWiki; NARG1; -. DR GenomeRNAi; 80155; -. DR Pharos; Q9BXJ9; Tbio. DR PRO; PR:Q9BXJ9; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q9BXJ9; Protein. DR Bgee; ENSG00000164134; Expressed in calcaneal tendon and 198 other cell types or tissues. DR ExpressionAtlas; Q9BXJ9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0031415; C:NatA complex; IDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB. DR Gene3D; 1.25.40.1010; -; 1. DR Gene3D; 1.25.40.1040; -; 1. DR InterPro; IPR021183; NatA_aux_su. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR22767:SF6; N-ALPHA-ACETYLTRANSFERASE 15, NATA AUXILIARY SUBUNIT; 1. DR PANTHER; PTHR22767; N-TERMINAL ACETYLTRANSFERASE-RELATED; 1. DR Pfam; PF12569; NatA_aux_su; 1. DR Pfam; PF13181; TPR_8; 1. DR PIRSF; PIRSF000422; N-terminal-AcTrfase-A_aux_su; 1. DR SMART; SM00028; TPR; 6. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 2. DR Genevisible; Q9BXJ9; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Angiogenesis; Cytoplasm; KW Developmental protein; Differentiation; Disease variant; KW Intellectual disability; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; TPR repeat; Transcription; Transcription regulation. FT CHAIN 1..866 FT /note="N-alpha-acetyltransferase 15, NatA auxiliary FT subunit" FT /id="PRO_0000106294" FT REPEAT 46..79 FT /note="TPR 1" FT REPEAT 80..113 FT /note="TPR 2" FT REPEAT 148..184 FT /note="TPR 3" FT REPEAT 224..257 FT /note="TPR 4" FT REPEAT 374..407 FT /note="TPR 5" FT REPEAT 409..441 FT /note="TPR 6" FT REPEAT 485..518 FT /note="TPR 7" FT REPEAT 672..705 FT /note="TPR 8" FT REGION 500..866 FT /note="Interaction with HYPK" FT /evidence="ECO:0000269|PubMed:20154145" FT REGION 575..642 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 612..629 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000255" FT MOD_RES 262 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 302 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 537 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 588 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 735 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 756 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 855 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 856 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT VAR_SEQ 514..525 FT /note="HFIEITDDQFDF -> KSLMTSLTFIHTV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_012560" FT VAR_SEQ 526..866 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_012561" FT VARIANT 52..866 FT /note="Missing (in MRD50)" FT /evidence="ECO:0000269|PubMed:28191889" FT /id="VAR_080534" FT VARIANT 112 FT /note="D -> N (in MRD50; uncertain significance; FT dbSNP:rs889543097)" FT /evidence="ECO:0000269|PubMed:28191889" FT /id="VAR_080535" FT VARIANT 290..866 FT /note="Missing (in MRD50)" FT /evidence="ECO:0000269|PubMed:28191889" FT /id="VAR_080536" FT VARIANT 450 FT /note="K -> E (in MRD50; uncertain significance; FT dbSNP:rs1436993876)" FT /evidence="ECO:0000269|PubMed:28191889" FT /id="VAR_080537" FT VARIANT 475 FT /note="A -> V (in MRD50; uncertain significance; FT dbSNP:rs202204424)" FT /evidence="ECO:0000269|PubMed:28191889" FT /id="VAR_080538" FT VARIANT 565..866 FT /note="Missing (in MRD50)" FT /evidence="ECO:0000269|PubMed:28191889" FT /id="VAR_080539" FT VARIANT 696..866 FT /note="Missing (in MRD50)" FT /evidence="ECO:0000269|PubMed:28191889" FT /id="VAR_080540" FT VARIANT 782..866 FT /note="Missing (in MRD50)" FT /evidence="ECO:0000269|PubMed:28191889" FT /id="VAR_080541" FT VARIANT 797..866 FT /note="Missing (in MRD50)" FT /evidence="ECO:0000269|PubMed:28191889" FT /id="VAR_080542" FT MUTAGEN 406 FT /note="T->Y: Reduces binding to NAA50, but increases FT binding to HYPK. Reduces catalytic activity of the NatA FT complex while retaining the interaction with NAA10." FT /evidence="ECO:0000269|PubMed:32042062" FT MUTAGEN 814 FT /note="L->P: Reduces binding to HYPK, increases binding to FT NAA50. Increases catalytic activity of the NatA complex FT while retaining the interaction with NAA10." FT /evidence="ECO:0000269|PubMed:32042062" FT MUTAGEN 834 FT /note="Y->F,A: Reduces NatA complex stability and reduces FT catalytic activity." FT /evidence="ECO:0000269|PubMed:29754825" FT CONFLICT 425 FT /note="K -> R (in Ref. 2; AAM48746)" FT /evidence="ECO:0000305" FT HELIX 8..22 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 26..38 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 46..58 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 62..75 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 80..92 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 96..109 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 114..126 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 130..143 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:6C95" FT HELIX 148..161 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 164..180 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 186..202 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 206..216 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 223..236 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 240..253 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 258..268 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 273..286 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 292..295 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 297..300 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 304..320 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 325..329 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 330..334 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 336..355 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 356..360 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:6C95" FT HELIX 370..386 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 390..403 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 408..420 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 424..437 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:6C95" FT HELIX 442..454 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 458..465 FT /evidence="ECO:0007829|PDB:6C9M" FT TURN 466..468 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 475..481 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 485..497 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 501..520 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 521..524 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 525..532 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 535..546 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 547..550 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 552..570 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 644..648 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 653..667 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 672..684 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 688..701 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 706..721 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 724..726 FT /evidence="ECO:0007829|PDB:6PPL" FT HELIX 728..740 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 747..757 FT /evidence="ECO:0007829|PDB:6C9M" FT TURN 758..760 FT /evidence="ECO:0007829|PDB:6C95" FT HELIX 762..775 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 777..779 FT /evidence="ECO:0007829|PDB:6C95" FT HELIX 780..787 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 794..796 FT /evidence="ECO:0007829|PDB:6PPL" FT HELIX 799..810 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 812..814 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 818..829 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 836..838 FT /evidence="ECO:0007829|PDB:6C95" SQ SEQUENCE 866 AA; 101272 MW; 6B4BA23B99D99121 CRC64; MPAVSLPPKE NALFKRILRC YEHKQYRNGL KFCKQILSNP KFAEHGETLA MKGLTLNCLG KKEEAYELVR RGLRNDLKSH VCWHVYGLLQ RSDKKYDEAI KCYRNALKWD KDNLQILRDL SLLQIQMRDL EGYRETRYQL LQLRPAQRAS WIGYAIAYHL LEDYEMAAKI LEEFRKTQQT SPDKVDYEYS ELLLYQNQVL REAGLYREAL EHLCTYEKQI CDKLAVEETK GELLLQLCRL EDAADVYRGL QERNPENWAY YKGLEKALKP ANMLERLKIY EEAWTKYPRG LVPRRLPLNF LSGEKFKECL DKFLRMNFSK GCPPVFNTLR SLYKDKEKVA IIEELVVGYE TSLKSCRLFN PNDDGKEEPP TTLLWVQYYL AQHYDKIGQP SIALEYINTA IESTPTLIEL FLVKAKIYKH AGNIKEAARW MDEAQALDTA DRFINSKCAK YMLKANLIKE AEEMCSKFTR EGTSAVENLN EMQCMWFQTE CAQAYKAMNK FGEALKKCHE IERHFIEITD DQFDFHTYCM RKITLRSYVD LLKLEDVLRQ HPFYFKAARI AIEIYLKLHD NPLTDENKEH EADTANMSDK ELKKLRNKQR RAQKKAQIEE EKKNAEKEKQ QRNQKKKKDD DDEEIGGPKE ELIPEKLAKV ETPLEEAIKF LTPLKNLVKN KIETHLFAFE IYFRKEKFLL MLQSVKRAFA IDSSHPWLHE CMIRLFNTAV CESKDLSDTV RTVLKQEMNR LFGATNPKNF NETFLKRNSD SLPHRLSAAK MVYYLDPSSQ KRAIELATTL DESLTNRNLQ TCMEVLEALY DGSLGDCKEA AEIYRANCHK LFPYALAFMP PGYEEDMKIT VNGDSSAEAE ELANEI //