NAA10_HUMAN
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 03-AUG-2022, entry version 201.
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; 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}.
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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 SMR; P41227; -.
DR BioGRID; 113881; 148.
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; 84.
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; P41227; -.
DR PeptideAtlas; P41227; -.
DR PRIDE; P41227; -.
DR ProteomicsDB; 1523; -.
DR ProteomicsDB; 55435; -. [P41227-1]
DR TopDownProteomics; P41227-1; -. [P41227-1]
DR Antibodypedia; 31057; 175 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 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; 1489230at2759; -.
DR PhylomeDB; P41227; -.
DR TreeFam; TF300078; -.
DR BioCyc; MetaCyc:HS02336-MON; -.
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 SignaLink; P41227; -.
DR SIGNOR; P41227; -.
DR BioGRID-ORCS; 8260; 343 hits in 681 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 201 other tissues.
DR ExpressionAtlas; P41227; baseline and differential.
DR Genevisible; P41227; HS.
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-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990189; F:peptide-serine-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 InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 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 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
