ID NAA10_HUMAN Reviewed; 235 AA. AC P41227; A6NM98; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 210. DE RecName: Full=N-alpha-acetyltransferase 10; DE EC=2.3.1.255 {ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:19420222, ECO:0000269|PubMed:25489052, ECO:0000269|PubMed:29754825}; DE AltName: Full=N-terminal acetyltransferase complex ARD1 subunit homolog A; DE Short=hARD1 {ECO:0000303|PubMed:19420222}; DE AltName: Full=NatA catalytic subunit Naa10; GN Name=NAA10; Synonyms=ARD1, ARD1A, TE2; 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). RX PubMed=7981673; DOI=10.1093/hmg/3.7.1061; RA Tribioli C., Mancini M., Plassart E., Bione S., Rivella S., Sala C., RA Torri G., Toniolo D.; RT "Isolation of new genes in distal Xq28: transcriptional map and RT identification of a human homologue of the ARD1 N-acetyl transferase of RT Saccharomyces cerevisiae."; RL Hum. Mol. Genet. 3:1061-1068(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS RP SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND RP INTERACTION WITH NAA15 AND RIBOSOMAL PROTEINS. RC TISSUE=Thyroid carcinoma; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [6] RP INTERACTION WITH HIF1A, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=12464182; DOI=10.1016/s0092-8674(02)01085-1; RA Jeong J.-W., Bae M.-K., Ahn M.-Y., Kim S.-H., Sohn T.-K., Bae M.-H., RA Yoo M.-A., Song E.-J., Lee K.-J., Kim K.-W.; RT "Regulation and destabilization of HIF-1alpha by ARD1-mediated RT acetylation."; RL Cell 111:709-720(2002). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY RP 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 [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-205, AND 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [11] RP INTERACTION WITH NAA16. RX PubMed=19480662; DOI=10.1186/1471-2091-10-15; RA Arnesen T., Gromyko D., Kagabo D., Betts M.J., Starheim K.K., Varhaug J.E., RA Anderson D., Lillehaug J.R.; RT "A novel human NatA Nalpha-terminal acetyltransferase complex: hNaa16p- RT hNaa10p (hNat2-hArd1)."; RL BMC Biochem. 10:15-15(2009). RN [12] 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 [13] RP PHOSPHORYLATION AT SER-209 BY IKBKB, MUTAGENESIS OF SER-209, AND RP INTERACTION WITH IKBKB. RX PubMed=19716809; DOI=10.1016/j.bbrc.2009.08.127; RA Kuo H.P., Lee D.F., Xia W., Lai C.C., Li L.Y., Hung M.C.; RT "Phosphorylation of ARD1 by IKKbeta contributes to its destabilization and RT degradation."; RL Biochem. Biophys. Res. Commun. 389:156-161(2009). RN [14] RP FUNCTION, AND INTERACTION WITH MYLK. RX PubMed=19826488; DOI=10.1371/journal.pone.0007451; RA Shin D.H., Chun Y.-S., Lee K.-H., Shin H.-W., Park J.-W.; RT "Arrest defective-1 controls tumor cell behavior by acetylating myosin RT light chain kinase."; RL PLoS ONE 4:E7451-E7451(2009). RN [15] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19420222; DOI=10.1073/pnas.0901931106; RA Arnesen T., Van Damme P., Polevoda B., Helsens K., Evjenth R., Colaert N., RA Varhaug J.E., Vandekerckhove J., Lillehaug J.R., Sherman F., Gevaert K.; RT "Proteomics analyses reveal the evolutionary conservation and divergence of RT N-terminal acetyltransferases from yeast and humans."; RL Proc. Natl. Acad. Sci. U.S.A. 106:8157-8162(2009). RN [16] 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 NAA15. 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-205; SER-213 AND RP SER-216, AND IDENTIFICATION BY 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 [18] RP INTERACTION WITH TSC2, AND FUNCTION IN ACETYLATION OF TSC2. RX PubMed=20145209; DOI=10.1126/scisignal.2000590; RA Kuo H.P., Lee D.F., Chen C.T., Liu M., Chou C.K., Lee H.J., Du Y., Xie X., RA Wei Y., Xia W., Weihua Z., Yang J.Y., Yen C.J., Huang T.H., Tan M., RA Xing G., Zhao Y., Lin C.H., Tsai S.F., Fidler I.J., Hung M.C.; RT "ARD1 stabilization of TSC2 suppresses tumorigenesis through the mTOR RT signaling pathway."; RL Sci. Signal. 3:RA9-RA9(2010). RN [19] 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-205, 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-186 AND SER-205, AND RP 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 [22] RP INVOLVEMENT IN MCOPS1. RX PubMed=24431331; DOI=10.1136/jmedgenet-2013-101660; RA Esmailpour T., Riazifar H., Liu L., Donkervoort S., Huang V.H., Madaan S., RA Shoucri B.M., Busch A., Wu J., Towbin A., Chadwick R.B., Sequeira A., RA Vawter M.P., Sun G., Johnston J.J., Biesecker L.G., Kawaguchi R., Sun H., RA Kimonis V., Huang T.; RT "A splice donor mutation in NAA10 results in the dysregulation of the RT retinoic acid signalling pathway and causes Lenz microphthalmia syndrome."; RL J. Med. Genet. 51:185-196(2014). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP SUBCELLULAR LOCATION. RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053; RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I., RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S., RA Ziegler M., Niere M., Gevaert K., Arnesen T.; RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N RT termini of transmembrane proteins and maintains Golgi integrity."; RL Cell Rep. 10:1362-1374(2015). RN [25] RP FUNCTION. RX PubMed=27422821; DOI=10.1074/jbc.m116.737585; RA Rong Z., Ouyang Z., Magin R.S., Marmorstein R., Yu H.; RT "Opposing functions of the N-terminal acetyltransferases Naa50 and NatA in RT sister-chromatid cohesion."; RL J. Biol. Chem. 291:19079-19091(2016). RN [26] RP FUNCTION, INTERACTION WITH HSPA1A AND HSPA1B, ACETYLATION AT LYS-136, AND RP MUTAGENESIS OF LYS-136. RX PubMed=27708256; DOI=10.1038/ncomms12882; RA Seo J.H., Park J.H., Lee E.J., Vo T.T., Choi H., Kim J.Y., Jang J.K., RA Wee H.J., Lee H.S., Jang S.H., Park Z.Y., Jeong J., Lee K.J., Seok S.H., RA Park J.Y., Lee B.J., Lee M.N., Oh G.T., Kim K.W.; RT "ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding RT and degradation."; RL Nat. Commun. 7:12882-12882(2016). RN [27] {ECO:0007744|PDB:6C95, ECO:0007744|PDB:6C9M} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-160 IN COMPLEX WITH NAA15 AND RP HYPK, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, RP IDENTIFICATION IN THE N-TERMINAL ACETYLTRANSFERASE A/HYPK COMPLEX, RP IDENTIFICATION IN THE N-TERMINAL ACETYLTRANSFERASE E COMPLEX, AND RP INTERACTION WITH NAA15. 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 [28] {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, AND INTERACTION WITH NAA15; HYPK AND RP NAA50. 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 [29] RP VARIANT NATD PRO-37, AND CHARACTERIZATION OF VARIANT NATD PRO-37. RX PubMed=21700266; DOI=10.1016/j.ajhg.2011.05.017; RA Rope A.F., Wang K., Evjenth R., Xing J., Johnston J.J., Swensen J.J., RA Johnson W.E., Moore B., Huff C.D., Bird L.M., Carey J.C., Opitz J.M., RA Stevens C.A., Jiang T., Schank C., Fain H.D., Robison R., Dalley B., RA Chin S., South S.T., Pysher T.J., Jorde L.B., Hakonarson H., RA Lillehaug J.R., Biesecker L.G., Yandell M., Arnesen T., Lyon G.J.; RT "Using VAAST to identify an X-linked disorder resulting in lethality in RT male infants due to N-terminal acetyltransferase deficiency."; RL Am. J. Hum. Genet. 89:28-43(2011). RN [30] RP VARIANT NATD PRO-37, CHARACTERIZATION OF VARIANT NATD PRO-37, FUNCTION, RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=25489052; DOI=10.1093/hmg/ddu611; RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A., RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H., RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.; RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt- RT acetylation defects."; RL Hum. Mol. Genet. 24:1956-1976(2015). RN [31] RP VARIANT NATD SER-43, AND CHARACTERIZATION OF VARIANT NATD SER-43. RX PubMed=26522270; DOI=10.1038/srep16022; RA Casey J.P., Stoeve S.I., McGorrian C., Galvin J., Blenski M., Dunne A., RA Ennis S., Brett F., King M.D., Arnesen T., Lynch S.A.; RT "NAA10 mutation causing a novel intellectual disability syndrome with Long RT QT due to N-terminal acetyltransferase impairment."; RL Sci. Rep. 5:16022-16022(2015). RN [32] RP VARIANT NATD HIS-83, AND CHARACTERIZATION OF VARIANT NATD HIS-83. RX PubMed=31174490; DOI=10.1186/s12881-019-0803-1; RG DDD study; RA Ree R., Geithus A.S., Toerring P.M., Soerensen K.P., Damkjaer M., RA Lynch S.A., Arnesen T.; RT "A novel NAA10 p.(R83H) variant with impaired acetyltransferase activity RT identified in two boys with ID and microcephaly."; RL BMC Med. Genet. 20:101-101(2019). CC -!- FUNCTION: Catalytic subunit of N-terminal acetyltransferase complexes CC which display alpha (N-terminal) acetyltransferase activity CC (PubMed:15496142, PubMed:19826488, PubMed:19420222, PubMed:20145209, CC PubMed:27708256, PubMed:25489052, PubMed:29754825, PubMed:20154145, CC PubMed:32042062). Acetylates amino termini that are devoid of initiator CC methionine (PubMed:19420222). The alpha (N-terminal) acetyltransferase CC activity may be important for vascular, hematopoietic and neuronal CC growth and development. Without NAA15, displays epsilon (internal) CC acetyltransferase activity towards HIF1A, thereby promoting its CC degradation (PubMed:12464182). Represses MYLK kinase activity by CC acetylation, and thus represses tumor cell migration (PubMed:19826488). CC Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and CC suppressing cancer development (PubMed:20145209). Acetylates HSPA1A and CC HSPA1B at 'Lys-77' which enhances its chaperone activity and leads to CC preferential binding to co-chaperone HOPX (PubMed:27708256). Acetylates CC HIST1H4A (PubMed:29754825). Acts as a negative regulator of sister CC chromatid cohesion during mitosis (PubMed:27422821). CC {ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:15496142, CC ECO:0000269|PubMed:19420222, ECO:0000269|PubMed:19826488, CC ECO:0000269|PubMed:20145209, ECO:0000269|PubMed:20154145, CC ECO:0000269|PubMed:25489052, ECO:0000269|PubMed:27422821, CC ECO:0000269|PubMed:27708256, ECO:0000269|PubMed:29754825, CC ECO:0000269|PubMed:32042062}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N- CC terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496, CC Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723, CC ChEBI:CHEBI:133369; EC=2.3.1.255; CC Evidence={ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:19420222, CC ECO:0000269|PubMed:25489052}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N- CC terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500, CC Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718, CC ChEBI:CHEBI:83683; EC=2.3.1.255; CC Evidence={ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:19420222, CC ECO:0000269|PubMed:25489052}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N- CC terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504, CC Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738, CC ChEBI:CHEBI:83690; EC=2.3.1.255; CC Evidence={ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:19420222, CC ECO:0000269|PubMed:25489052, ECO:0000269|PubMed:29754825}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N- CC terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508, CC Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741, CC ChEBI:CHEBI:133371; EC=2.3.1.255; CC Evidence={ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:19420222, CC ECO:0000269|PubMed:25489052}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) + CC N-terminal N(alpha)-acetyl-L-cysteinyl-[protein]; CC Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255; CC Evidence={ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:19420222, CC ECO:0000269|PubMed:25489052}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N- CC terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516, CC Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739, CC ChEBI:CHEBI:133375; EC=2.3.1.255; CC Evidence={ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:19420222, CC ECO:0000269|PubMed:25489052}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=27 uM for acetyl-CoA (at pH 8.0 and at 25 degrees Celsius) CC {ECO:0000269|PubMed:29754825}; CC KM=30 uM for histone H4 peptide (at pH 8.0 and at 25 degrees Celsius) CC {ECO:0000269|PubMed:29754825}; CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A complex (also CC called the NatA complex) composed of NAA10 and NAA15 (PubMed:20154145, CC PubMed:15496142, PubMed:32042062). Within the complex interacts with CC NAA15 (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 NAA15, 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 NAA15; the interaction is required CC for binding to NAAT50 (PubMed:29754825, PubMed:32042062). Interacts CC with NAAT50 (PubMed:16507339, PubMed:32042062). The interaction of the CC NatA complex with NAA50 reduces the acetylation activity of the NatA CC complex (PubMed:32042062). Component of the N-terminal CC acetyltransferase E (NatE)/HYPK complex at least composed of NAA10, CC NAA15, NAA50 and HYPK (PubMed:32042062). In complex with NAA15, CC interacts with HYPK; the interaction with HYPK reduces the capacity of CC the NatA complex to interact with NAA50 (PubMed:29754825, CC PubMed:32042062). Interacts with HIF1A (via its ODD domain); the CC interaction increases HIF1A protein stability during normoxia, an down- CC regulates it when induced by hypoxia (PubMed:12464182). Interacts with CC the ribosome (PubMed:16507339). Binds to MYLK (PubMed:19826488). CC Interacts with NAA16 (PubMed:19480662). Interacts (via its C-terminal CC domain) with TSC2, leading to its acetylation (PubMed:20145209). CC Interacts with IKBKB (PubMed:19716809). Interacts with HSPA1A and CC HSPA1B leading to its acetylation (PubMed:27708256). CC {ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:15496142, CC ECO:0000269|PubMed:16507339, ECO:0000269|PubMed:19716809, CC ECO:0000269|PubMed:19826488, ECO:0000269|PubMed:20145209, CC ECO:0000269|PubMed:20154145, ECO:0000269|PubMed:27708256, CC ECO:0000269|PubMed:29754825, ECO:0000269|PubMed:32042062}. CC -!- INTERACTION: CC P41227; Q8WYK0: ACOT12; NbExp=3; IntAct=EBI-747693, EBI-11954993; CC P41227; P05067: APP; NbExp=3; IntAct=EBI-747693, EBI-77613; CC P41227; Q15052: ARHGEF6; NbExp=3; IntAct=EBI-747693, EBI-1642523; CC P41227; Q14155: ARHGEF7; NbExp=3; IntAct=EBI-747693, EBI-717515; CC P41227; Q8WXS3-2: BAALC; NbExp=5; IntAct=EBI-747693, EBI-13079214; CC P41227; Q6W2J9-4: BCOR; NbExp=3; IntAct=EBI-747693, EBI-10208579; CC P41227; Q13137: CALCOCO2; NbExp=7; IntAct=EBI-747693, EBI-739580; CC P41227; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-747693, EBI-711501; CC P41227; Q6PII3: CCDC174; NbExp=3; IntAct=EBI-747693, EBI-747830; CC P41227; Q96FF9: CDCA5; NbExp=5; IntAct=EBI-747693, EBI-718805; CC P41227; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-747693, EBI-744115; CC P41227; P13569: CFTR; NbExp=5; IntAct=EBI-747693, EBI-349854; CC P41227; Q8IUR6: CREBRF; NbExp=3; IntAct=EBI-747693, EBI-1042699; CC P41227; Q96D03: DDIT4L; NbExp=4; IntAct=EBI-747693, EBI-742054; CC P41227; Q6P158: DHX57; NbExp=3; IntAct=EBI-747693, EBI-1051531; CC P41227; A2ABF9: EHMT2; NbExp=3; IntAct=EBI-747693, EBI-10174566; CC P41227; Q6UN15: FIP1L1; NbExp=3; IntAct=EBI-747693, EBI-1021914; CC P41227; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-747693, EBI-11959863; CC P41227; Q92845: KIFAP3; NbExp=7; IntAct=EBI-747693, EBI-954040; CC P41227; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-747693, EBI-10172150; CC P41227; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-747693, EBI-12012928; CC P41227; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-747693, EBI-10172290; CC P41227; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-747693, EBI-348259; CC P41227; O15151: MDM4; NbExp=3; IntAct=EBI-747693, EBI-398437; CC P41227; P50222: MEOX2; NbExp=3; IntAct=EBI-747693, EBI-748397; CC P41227; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-747693, EBI-16439278; CC P41227; Q9UHC7: MKRN1; NbExp=5; IntAct=EBI-747693, EBI-373524; CC P41227; P82912: MRPS11; NbExp=3; IntAct=EBI-747693, EBI-2371859; CC P41227; Q9BXJ9: NAA15; NbExp=7; IntAct=EBI-747693, EBI-1042540; CC P41227; Q6N069: NAA16; NbExp=2; IntAct=EBI-747693, EBI-2561139; CC P41227; Q9GZZ1: NAA50; NbExp=3; IntAct=EBI-747693, EBI-1052523; CC P41227; Q86UR1-2: NOXA1; NbExp=6; IntAct=EBI-747693, EBI-12025760; CC P41227; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-747693, EBI-1105124; CC P41227; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-747693, EBI-9640281; CC P41227; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-747693, EBI-9090282; CC P41227; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-747693, EBI-750734; CC P41227; Q9Y5P8: PPP2R3B; NbExp=3; IntAct=EBI-747693, EBI-2479826; CC P41227; Q96QF0: RAB3IP; NbExp=3; IntAct=EBI-747693, EBI-747844; CC P41227; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-747693, EBI-11984839; CC P41227; P63000: RAC1; NbExp=3; IntAct=EBI-747693, EBI-413628; CC P41227; Q9BYM8: RBCK1; NbExp=3; IntAct=EBI-747693, EBI-2340624; CC P41227; Q96D15: RCN3; NbExp=3; IntAct=EBI-747693, EBI-746283; CC P41227; O15034-2: RIMBP2; NbExp=3; IntAct=EBI-747693, EBI-12906594; CC P41227; Q13214-2: SEMA3B; NbExp=3; IntAct=EBI-747693, EBI-11017428; CC P41227; Q8WV41: SNX33; NbExp=3; IntAct=EBI-747693, EBI-2481535; CC P41227; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-747693, EBI-2212028; CC P41227; Q5H9L4: TAF7L; NbExp=3; IntAct=EBI-747693, EBI-6658013; CC P41227; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-747693, EBI-2559824; CC P41227; O43829: ZBTB14; NbExp=6; IntAct=EBI-747693, EBI-10176632; CC P41227; O95125: ZNF202; NbExp=3; IntAct=EBI-747693, EBI-751960; CC P41227; Q8N720: ZNF655; NbExp=3; IntAct=EBI-747693, EBI-625509; CC P41227; O55043: Arhgef7; Xeno; NbExp=3; IntAct=EBI-747693, EBI-3649585; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12464182, CC ECO:0000269|PubMed:25489052, ECO:0000269|PubMed:25732826}. Nucleus CC {ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:15496142, CC ECO:0000269|PubMed:25732826}. Note=Also present in the free cytosolic CC and cytoskeleton-bound polysomes. {ECO:0000269|PubMed:15496142}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P41227-1; Sequence=Displayed; CC Name=2; CC IsoId=P41227-2; Sequence=VSP_046205, VSP_046206; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12464182}. CC -!- PTM: Cleaved by caspases during apoptosis. CC -!- PTM: Phosphorylation by IKBKB/IKKB at Ser-209 promotes its proteasome- CC mediated degradation. {ECO:0000269|PubMed:19716809}. CC -!- PTM: Autoacetylated at Lys-136 which stimulates its catalytic activity. CC {ECO:0000269|PubMed:27708256}. CC -!- DISEASE: N-terminal acetyltransferase deficiency (NATD) [MIM:300855]: CC An enzymatic deficiency resulting in postnatal growth failure with CC severe delays and dysmorphic features. It is clinically characterized CC by wrinkled forehead, prominent eyes, widely opened anterior and CC posterior fontanels, downsloping palpebral fissures, thickened lids, CC large ears, flared nares, hypoplastic alae, short columella, protruding CC upper lip, and microretrognathia. There are also delayed closing of CC fontanels and broad great toes. Skin is characterized by redundancy or CC laxity with minimal subcutaneous fat, cutaneous capillary CC malformations, and very fine hair and eyebrows. Death results from CC cardiogenic shock following arrhythmia. {ECO:0000269|PubMed:21700266, CC ECO:0000269|PubMed:25489052, ECO:0000269|PubMed:26522270, CC ECO:0000269|PubMed:31174490}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Microphthalmia, syndromic, 1 (MCOPS1) [MIM:309800]: A rare CC syndrome defined by the canonical features of unilateral or bilateral CC microphthalmia or anophthalmia and defects in the skeletal and CC genitourinary systems. Microphthalmia is a disorder of eye formation, CC ranging from small size of a single eye to complete bilateral absence CC of ocular tissues (anophthalmia). In many cases, CC microphthalmia/anophthalmia occurs in association with syndromes that CC include non-ocular abnormalities. Anomalies of the digits, teeth, and CC ears are hallmarks of MCOPS1. Intellectual disability ranges from mild CC to severe, with self-mutilating behaviors and seizures in severely CC affected MCOPS1 individuals. {ECO:0000269|PubMed:24431331}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily. CC {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; X77588; CAA54691.1; -; mRNA. DR EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471172; EAW72774.1; -; Genomic_DNA. DR EMBL; BC000308; AAH00308.1; -; mRNA. DR EMBL; BC019312; AAH19312.1; -; mRNA. DR CCDS; CCDS14737.1; -. [P41227-1] DR CCDS; CCDS59179.1; -. [P41227-2] DR PIR; I38333; I38333. DR RefSeq; NP_001243048.1; NM_001256119.1. [P41227-2] DR RefSeq; NP_003482.1; NM_003491.3. [P41227-1] DR PDB; 6C95; X-ray; 3.15 A; B=1-160. DR PDB; 6C9M; X-ray; 2.80 A; B/D=1-160. DR PDB; 6PPL; EM; 3.02 A; C=1-235. DR PDB; 6PW9; EM; 4.03 A; C=1-235. DR PDBsum; 6C95; -. DR PDBsum; 6C9M; -. DR PDBsum; 6PPL; -. DR PDBsum; 6PW9; -. DR AlphaFoldDB; P41227; -. DR EMDB; EMD-20442; -. DR EMDB; EMD-20501; -. DR SMR; P41227; -. DR BioGRID; 113881; 189. DR ComplexPortal; CPX-6271; NatA N-alpha-acetyltransferase complex, NAA10-NAA15 variant. DR ComplexPortal; CPX-6272; NatA N-alpha-acetyltransferase complex, NAA10-NAA16 variant. DR IntAct; P41227; 86. DR MINT; P41227; -. DR STRING; 9606.ENSP00000417763; -. DR ChEMBL; CHEMBL4630819; -. DR GlyGen; P41227; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P41227; -. DR MetOSite; P41227; -. DR PhosphoSitePlus; P41227; -. DR SwissPalm; P41227; -. DR BioMuta; NAA10; -. DR DMDM; 728880; -. DR EPD; P41227; -. DR jPOST; P41227; -. DR MassIVE; P41227; -. DR MaxQB; P41227; -. DR PaxDb; 9606-ENSP00000417763; -. DR PeptideAtlas; P41227; -. DR ProteomicsDB; 1523; -. DR ProteomicsDB; 55435; -. [P41227-1] DR Pumba; P41227; -. DR TopDownProteomics; P41227-1; -. [P41227-1] DR Antibodypedia; 31057; 193 antibodies from 29 providers. DR DNASU; 8260; -. DR Ensembl; ENST00000370009.5; ENSP00000359026.1; ENSG00000102030.16. [P41227-2] DR Ensembl; ENST00000464845.6; ENSP00000417763.1; ENSG00000102030.16. [P41227-1] DR GeneID; 8260; -. DR KEGG; hsa:8260; -. DR MANE-Select; ENST00000464845.6; ENSP00000417763.1; NM_003491.4; NP_003482.1. DR UCSC; uc004fjm.3; human. [P41227-1] DR AGR; HGNC:18704; -. DR CTD; 8260; -. DR DisGeNET; 8260; -. DR GeneCards; NAA10; -. DR HGNC; HGNC:18704; NAA10. DR HPA; ENSG00000102030; Low tissue specificity. DR MalaCards; NAA10; -. DR MIM; 300013; gene. DR MIM; 300855; phenotype. DR MIM; 309800; phenotype. DR neXtProt; NX_P41227; -. DR OpenTargets; ENSG00000102030; -. DR Orphanet; 568; Microphthalmia, Lenz type. DR Orphanet; 276432; Ogden syndrome. DR PharmGKB; PA38648; -. DR VEuPathDB; HostDB:ENSG00000102030; -. DR eggNOG; KOG3235; Eukaryota. DR GeneTree; ENSGT00550000074803; -. DR HOGENOM; CLU_013985_7_0_1; -. DR InParanoid; P41227; -. DR OrthoDB; 275667at2759; -. DR PhylomeDB; P41227; -. DR TreeFam; TF300078; -. DR BioCyc; MetaCyc:HS02336-MONOMER; -. DR BRENDA; 2.3.1.255; 2681. DR BRENDA; 2.3.1.258; 2681. DR BRENDA; 2.3.1.48; 2681. DR PathwayCommons; P41227; -. DR SABIO-RK; P41227; -. DR SignaLink; P41227; -. DR SIGNOR; P41227; -. DR BioGRID-ORCS; 8260; 373 hits in 761 CRISPR screens. DR ChiTaRS; NAA10; human. DR GeneWiki; ARD1A; -. DR GenomeRNAi; 8260; -. DR Pharos; P41227; Tbio. DR PRO; PR:P41227; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P41227; Protein. DR Bgee; ENSG00000102030; Expressed in right hemisphere of cerebellum and 203 other cell types or tissues. DR ExpressionAtlas; P41227; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0031415; C:NatA complex; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0008080; F:N-acetyltransferase activity; TAS:ProtInc. DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:UniProtKB. DR GO; GO:1990190; F:peptide-glutamate-alpha-N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:1990189; F:peptide-serine-alpha-N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0051276; P:chromosome organization; TAS:ProtInc. DR GO; GO:0006475; P:internal protein amino acid acetylation; TAS:ProtInc. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:UniProtKB. DR GO; GO:2000719; P:negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric; IDA:UniProtKB. DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB. DR CDD; cd04301; NAT_SF; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR045047; Ard1-like. DR InterPro; IPR000182; GNAT_dom. DR PANTHER; PTHR23091:SF268; N-ALPHA-ACETYLTRANSFERASE 10; 1. DR PANTHER; PTHR23091; N-TERMINAL ACETYLTRANSFERASE; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR PROSITE; PS51186; GNAT; 1. DR Genevisible; P41227; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing; KW Cytoplasm; Disease variant; Microphthalmia; Nucleus; Phosphoprotein; KW Reference proteome; Transferase. FT CHAIN 1..235 FT /note="N-alpha-acetyltransferase 10" FT /id="PRO_0000074532" FT DOMAIN 1..152 FT /note="N-acetyltransferase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532" FT REGION 1..58 FT /note="Interaction with NAA15" FT /evidence="ECO:0000269|PubMed:15496142" FT REGION 178..235 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 196..227 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 136 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:27708256" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 186 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 209 FT /note="Phosphoserine; by IKKB" FT /evidence="ECO:0000269|PubMed:19716809" FT MOD_RES 213 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 216 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT VAR_SEQ 114..128 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_046205" FT VAR_SEQ 129 FT /note="Q -> R (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_046206" FT VARIANT 37 FT /note="S -> P (in NATD; reduced N-terminal FT acetyltransferase activity; impaired interaction with NAA15 FT and NAA50; does not affect cytoplasmic localization; FT dbSNP:rs387906701)" FT /evidence="ECO:0000269|PubMed:21700266, FT ECO:0000269|PubMed:25489052" FT /id="VAR_066652" FT VARIANT 43 FT /note="Y -> S (in NATD; decreased protein stability; strong FT decrease in N-terminal acetylation activity in vitro; FT dbSNP:rs863225427)" FT /evidence="ECO:0000269|PubMed:26522270" FT /id="VAR_075206" FT VARIANT 83 FT /note="R -> H (in NATD; reduced monomeric N-terminal FT acetyltransferase activity in vitro; dbSNP:rs1603290366)" FT /evidence="ECO:0000269|PubMed:31174490" FT /id="VAR_082604" FT MUTAGEN 136 FT /note="K->R: Loss of its ability to acetylate HSPA1A and FT HSPA1B." FT /evidence="ECO:0000269|PubMed:27708256" FT MUTAGEN 209 FT /note="S->A: Abolishes phosphorylation by IKKB and reduces FT cell growth." FT /evidence="ECO:0000269|PubMed:19716809" FT STRAND 2..5 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 8..10 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 11..21 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 28..35 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 52..60 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 70..77 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:6PPL" FT HELIX 86..102 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 105..112 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 116..124 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 129..134 FT /evidence="ECO:0007829|PDB:6C9M" FT STRAND 144..150 FT /evidence="ECO:0007829|PDB:6C9M" FT HELIX 152..159 FT /evidence="ECO:0007829|PDB:6C9M" SQ SEQUENCE 235 AA; 26459 MW; 6393A907F5C2DDC4 CRC64; MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGAIENKV ESKGNSPPSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS //