Full text data of NAA15
NAA15
(GA19, NARG1, NATH, TBDN100)
[Confidence: low (only semi-automatic identification from reviews)]
N-alpha-acetyltransferase 15, NatA auxiliary subunit (Gastric cancer antigen Ga19; N-terminal acetyltransferase; NMDA receptor-regulated protein 1; Protein tubedown-1; Tbdn100)
N-alpha-acetyltransferase 15, NatA auxiliary subunit (Gastric cancer antigen Ga19; N-terminal acetyltransferase; NMDA receptor-regulated protein 1; Protein tubedown-1; Tbdn100)
UniProt
Q9BXJ9
ID NAA15_HUMAN Reviewed; 866 AA.
AC Q9BXJ9; D3DNY6; Q52LG9; Q8IWH4; Q8NEV2; Q9H8P6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 119.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Ornitz D.M., 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
RP TISSUE 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
RT acetyltransferase 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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,
RP AND 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 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [12]
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
RT conserved component of the NatA protein N-alpha-acetyltransferase
RT complex.";
RL Gene 371:291-295(2006).
RN [13]
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 [14]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
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:
RT nomenclature, subunits and substrates.";
RL BMC Proc. 3:S2-S2(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399 AND SER-403, AND
RP MASS SPECTROMETRY.
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-262; LYS-735 AND LYS-756,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [18]
RP INTERACTION WITH HYPK, AND SUBUNIT.
RX PubMed=20154145; DOI=10.1128/MCB.01199-09;
RA Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H.,
RA Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.;
RT "The chaperone-like protein HYPK acts together with NatA in
RT cotranslational N-terminal acetylation and prevention of Huntingtin
RT aggregation.";
RL Mol. Cell. Biol. 30:1898-1909(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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.,
RA Buerckstuemmer T., 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-856, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The NAA10-NAA15 complex displays alpha (N-terminal)
CC acetyltransferase activity that may be important for vascular,
CC hematopoietic and neuronal growth and development. Required to
CC control retinal neovascularization in adult ocular endothelial
CC cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates
CC transcription from the osteocalcin promoter.
CC -!- SUBUNIT: Interacts with NAA10, XRCC6, NAA50, XRCC5 and HYPK.
CC Associates with HYPK when in a complex with NAA10.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic,
CC nuclear in some cases. Present in the free cytosolic and
CC cytoskeleton-bound polysomes, but not in the membrane-bound
CC 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
CC ocular endothelial cells. Also found in brain (corpus callosum),
CC heart, colon, bone marrow and at lower levels in most adult
CC tissues, including thyroid, liver, pancreas, mammary and salivary
CC glands, lung, ovary, urogenital system and upper gastrointestinal
CC tract. Overexpressed in gastric cancer, in papillary thyroid
CC carcinomas and in a Burkitt lymphoma cell line (Daudi).
CC Specifically suppressed in abnormal proliferating blood vessels in
CC eyes of patients with proliferative diabetic retinopathy.
CC -!- PTM: Cleaved by caspases during apoptosis, resulting in a stable
CC 35 kDa fragment.
CC -!- SIMILARITY: Contains 8 TPR repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39818.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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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 RefSeq; NP_476516.1; NM_057175.3.
DR RefSeq; XP_005263294.1; XM_005263237.1.
DR UniGene; Hs.745047; -.
DR ProteinModelPortal; Q9BXJ9; -.
DR IntAct; Q9BXJ9; 5.
DR STRING; 9606.ENSP00000296543; -.
DR PhosphoSite; Q9BXJ9; -.
DR DMDM; 57012969; -.
DR PaxDb; Q9BXJ9; -.
DR PRIDE; Q9BXJ9; -.
DR Ensembl; ENST00000296543; ENSP00000296543; ENSG00000164134.
DR GeneID; 80155; -.
DR KEGG; hsa:80155; -.
DR UCSC; uc003ihu.1; human.
DR CTD; 80155; -.
DR GeneCards; GC04P140222; -.
DR HGNC; HGNC:30782; NAA15.
DR HPA; HPA023589; -.
DR MIM; 608000; gene.
DR neXtProt; NX_Q9BXJ9; -.
DR PharmGKB; PA165664293; -.
DR eggNOG; COG0457; -.
DR HOGENOM; HOG000191711; -.
DR HOVERGEN; HBG052576; -.
DR InParanoid; Q9BXJ9; -.
DR KO; K00670; -.
DR OMA; KIDTHLL; -.
DR OrthoDB; EOG747PKD; -.
DR PhylomeDB; Q9BXJ9; -.
DR BRENDA; 2.3.1.88; 2681.
DR ChiTaRS; NAA15; human.
DR GeneWiki; NARG1; -.
DR GenomeRNAi; 80155; -.
DR NextBio; 70453; -.
DR PRO; PR:Q9BXJ9; -.
DR ArrayExpress; Q9BXJ9; -.
DR Bgee; Q9BXJ9; -.
DR CleanEx; HS_NARG1; -.
DR Genevestigator; Q9BXJ9; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription factor complex; IDA:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:Ensembl.
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:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR021183; NatA_aux_su.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22767:SF2; PTHR22767:SF2; 1.
DR Pfam; PF12569; NARP1; 1.
DR Pfam; PF07719; TPR_2; 1.
DR PIRSF; PIRSF000422; N-terminal-AcTrfase-A_aux_su; 1.
DR SMART; SM00028; TPR; 4.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Angiogenesis; Complete proteome;
KW Cytoplasm; Developmental protein; Differentiation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1 866 N-alpha-acetyltransferase 15, NatA
FT auxiliary subunit.
FT /FTId=PRO_0000106294.
FT REPEAT 46 79 TPR 1.
FT REPEAT 80 113 TPR 2.
FT REPEAT 148 184 TPR 3.
FT REPEAT 224 257 TPR 4.
FT REPEAT 374 407 TPR 5.
FT REPEAT 409 441 TPR 6.
FT REPEAT 485 518 TPR 7.
FT REPEAT 672 705 TPR 8.
FT REGION 500 866 Interaction with HYPK.
FT MOTIF 612 629 Bipartite nuclear localization signal
FT (Potential).
FT COMPBIAS 629 632 Poly-Asp.
FT MOD_RES 262 262 N6-acetyllysine.
FT MOD_RES 399 399 Phosphothreonine.
FT MOD_RES 403 403 Phosphoserine.
FT MOD_RES 588 588 Phosphoserine.
FT MOD_RES 735 735 N6-acetyllysine.
FT MOD_RES 756 756 N6-acetyllysine.
FT MOD_RES 855 855 Phosphoserine (By similarity).
FT MOD_RES 856 856 Phosphoserine.
FT VAR_SEQ 514 525 HFIEITDDQFDF -> KSLMTSLTFIHTV (in isoform
FT 2).
FT /FTId=VSP_012560.
FT VAR_SEQ 526 866 Missing (in isoform 2).
FT /FTId=VSP_012561.
FT CONFLICT 425 425 K -> R (in Ref. 2; AAM48746).
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
//
ID NAA15_HUMAN Reviewed; 866 AA.
AC Q9BXJ9; D3DNY6; Q52LG9; Q8IWH4; Q8NEV2; Q9H8P6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 119.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Ornitz D.M., 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
RP TISSUE 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
RT acetyltransferase 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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,
RP AND 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 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [12]
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
RT conserved component of the NatA protein N-alpha-acetyltransferase
RT complex.";
RL Gene 371:291-295(2006).
RN [13]
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 [14]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
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:
RT nomenclature, subunits and substrates.";
RL BMC Proc. 3:S2-S2(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399 AND SER-403, AND
RP MASS SPECTROMETRY.
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-262; LYS-735 AND LYS-756,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [18]
RP INTERACTION WITH HYPK, AND SUBUNIT.
RX PubMed=20154145; DOI=10.1128/MCB.01199-09;
RA Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H.,
RA Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.;
RT "The chaperone-like protein HYPK acts together with NatA in
RT cotranslational N-terminal acetylation and prevention of Huntingtin
RT aggregation.";
RL Mol. Cell. Biol. 30:1898-1909(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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.,
RA Buerckstuemmer T., 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-856, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The NAA10-NAA15 complex displays alpha (N-terminal)
CC acetyltransferase activity that may be important for vascular,
CC hematopoietic and neuronal growth and development. Required to
CC control retinal neovascularization in adult ocular endothelial
CC cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates
CC transcription from the osteocalcin promoter.
CC -!- SUBUNIT: Interacts with NAA10, XRCC6, NAA50, XRCC5 and HYPK.
CC Associates with HYPK when in a complex with NAA10.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic,
CC nuclear in some cases. Present in the free cytosolic and
CC cytoskeleton-bound polysomes, but not in the membrane-bound
CC 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
CC ocular endothelial cells. Also found in brain (corpus callosum),
CC heart, colon, bone marrow and at lower levels in most adult
CC tissues, including thyroid, liver, pancreas, mammary and salivary
CC glands, lung, ovary, urogenital system and upper gastrointestinal
CC tract. Overexpressed in gastric cancer, in papillary thyroid
CC carcinomas and in a Burkitt lymphoma cell line (Daudi).
CC Specifically suppressed in abnormal proliferating blood vessels in
CC eyes of patients with proliferative diabetic retinopathy.
CC -!- PTM: Cleaved by caspases during apoptosis, resulting in a stable
CC 35 kDa fragment.
CC -!- SIMILARITY: Contains 8 TPR repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39818.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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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 RefSeq; NP_476516.1; NM_057175.3.
DR RefSeq; XP_005263294.1; XM_005263237.1.
DR UniGene; Hs.745047; -.
DR ProteinModelPortal; Q9BXJ9; -.
DR IntAct; Q9BXJ9; 5.
DR STRING; 9606.ENSP00000296543; -.
DR PhosphoSite; Q9BXJ9; -.
DR DMDM; 57012969; -.
DR PaxDb; Q9BXJ9; -.
DR PRIDE; Q9BXJ9; -.
DR Ensembl; ENST00000296543; ENSP00000296543; ENSG00000164134.
DR GeneID; 80155; -.
DR KEGG; hsa:80155; -.
DR UCSC; uc003ihu.1; human.
DR CTD; 80155; -.
DR GeneCards; GC04P140222; -.
DR HGNC; HGNC:30782; NAA15.
DR HPA; HPA023589; -.
DR MIM; 608000; gene.
DR neXtProt; NX_Q9BXJ9; -.
DR PharmGKB; PA165664293; -.
DR eggNOG; COG0457; -.
DR HOGENOM; HOG000191711; -.
DR HOVERGEN; HBG052576; -.
DR InParanoid; Q9BXJ9; -.
DR KO; K00670; -.
DR OMA; KIDTHLL; -.
DR OrthoDB; EOG747PKD; -.
DR PhylomeDB; Q9BXJ9; -.
DR BRENDA; 2.3.1.88; 2681.
DR ChiTaRS; NAA15; human.
DR GeneWiki; NARG1; -.
DR GenomeRNAi; 80155; -.
DR NextBio; 70453; -.
DR PRO; PR:Q9BXJ9; -.
DR ArrayExpress; Q9BXJ9; -.
DR Bgee; Q9BXJ9; -.
DR CleanEx; HS_NARG1; -.
DR Genevestigator; Q9BXJ9; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription factor complex; IDA:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:Ensembl.
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:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR021183; NatA_aux_su.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22767:SF2; PTHR22767:SF2; 1.
DR Pfam; PF12569; NARP1; 1.
DR Pfam; PF07719; TPR_2; 1.
DR PIRSF; PIRSF000422; N-terminal-AcTrfase-A_aux_su; 1.
DR SMART; SM00028; TPR; 4.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Angiogenesis; Complete proteome;
KW Cytoplasm; Developmental protein; Differentiation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1 866 N-alpha-acetyltransferase 15, NatA
FT auxiliary subunit.
FT /FTId=PRO_0000106294.
FT REPEAT 46 79 TPR 1.
FT REPEAT 80 113 TPR 2.
FT REPEAT 148 184 TPR 3.
FT REPEAT 224 257 TPR 4.
FT REPEAT 374 407 TPR 5.
FT REPEAT 409 441 TPR 6.
FT REPEAT 485 518 TPR 7.
FT REPEAT 672 705 TPR 8.
FT REGION 500 866 Interaction with HYPK.
FT MOTIF 612 629 Bipartite nuclear localization signal
FT (Potential).
FT COMPBIAS 629 632 Poly-Asp.
FT MOD_RES 262 262 N6-acetyllysine.
FT MOD_RES 399 399 Phosphothreonine.
FT MOD_RES 403 403 Phosphoserine.
FT MOD_RES 588 588 Phosphoserine.
FT MOD_RES 735 735 N6-acetyllysine.
FT MOD_RES 756 756 N6-acetyllysine.
FT MOD_RES 855 855 Phosphoserine (By similarity).
FT MOD_RES 856 856 Phosphoserine.
FT VAR_SEQ 514 525 HFIEITDDQFDF -> KSLMTSLTFIHTV (in isoform
FT 2).
FT /FTId=VSP_012560.
FT VAR_SEQ 526 866 Missing (in isoform 2).
FT /FTId=VSP_012561.
FT CONFLICT 425 425 K -> R (in Ref. 2; AAM48746).
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
//
MIM
608000
*RECORD*
*FIELD* NO
608000
*FIELD* TI
*608000 N-ALPHA-ACETYLTRANSFERASE 15, NatA AUXILIARY SUBUNIT; NAA15
;;NMDA RECEPTOR-REGULATED 1; NARG1;;
read moreNAT1, S. CEREVISIAE, HOMOLOG OF; NATH
*FIELD* TX
CLONING
By replica cDNA screening for genes upregulated in papillary thyroid
carcinomas, Fluge et al. (2002) cloned NARG1 (NAA15), which they called
NATH. The deduced 866-amino acid protein has a calculated molecular mass
of 101 kD. It contains 4 tetratricopeptide repeat domains in 2 tandems
and a putative bipartite nuclear localization signal. NATH shares
similarity with S. cerevisiae N-acetyltransferase-1 (NAT1; 108345) and
mouse Narg1 and Tbdn1. Northern blot analysis detected a major
transcript of 4.6 kb and a minor transcript of 5.8 kb in a papillary
carcinoma cell line and in an anaplastic thyroid carcinoma cell line.
Multitissue mRNA dot blot analysis showed low expression in most adult
tissues and specific brain regions examined. Highest expression was
detected in testis and a Burkitt lymphoma cell line. Expression of NATH
in COS-7 cells resulted in cytoplasmic staining.
By Northern blot analysis, Sugiura et al. (2001) found that expression
of mouse Narg1 was highest in testis and much lower in other tissues
examined. They cloned 2 alternatively spliced variants of mouse Narg1
from testis. The deduced proteins contained 865 and 815 amino acids. The
shorter protein has an N-terminal truncation.
GENE FUNCTION
By analyzing cDNA arrays, Sugiura et al. (2001) found the expression of
Narg1, Narg2 (610835), and Narg3 was upregulated in neonatal mice in
which the gene for the Nmda receptor (NMDAR1; GRIN1 138249) was deleted.
In situ hybridization of wildtype neonatal mouse brain showed that
Narg1, Narg2, and Narg3 were expressed at high levels in regions of
neuronal proliferation and migration, and their expression was
downregulated during early postnatal development. Northern blot analysis
detected low expression of these genes on embryonic day 13, high
expression on postnatal day 0, and very low expression thereafter.
By semiquantitative RT-PCR, Fluge et al. (2002) found NATH overexpressed
in papillary thyroid carcinomas, especially in clinically aggressive
tumors with histologic evidence of poorly differentiated or
undifferentiated areas. In situ hybridization detected NATH highly
expressed in tumor cells and only weakly expressed in adjacent
nonneoplastic thyroid follicular cells. Transfection of NATH into a
papillary carcinoma cell line or embryonic kidney cells did not alter
the cellular proliferation rate.
Using in vitro translated mouse proteins, Sugiura et al. (2003) showed
that Narg1 and Ard1 (ARD1A, NAA10; 300013) assembled to form a
functional acetyltransferase. Narg1 alone showed no activity.
Immunoprecipitation and Western blot analysis demonstrated that Narg1
and Ard1 coassembled in mammalian cells. By cotransfection of rat kidney
fibroblasts, they showed that Narg1 and Ard1 localized to the cytoplasm
in both overlapping and separate compartments. In situ hybridization
demonstrated that throughout mouse brain development Narg1 and Ard1 were
highly expressed in areas of cell division and migration and their
expression appeared to be downregulated as neurons differentiated. Narg1
and Ard1 were expressed in proliferation mouse embryonic carcinoma
cells. Treatment of these cells with retinoic acid initiated neuronal
differentiation and downregulation of Narg1 and Ard1 as a neuronal
marker gene was induced. Sugiura et al. (2003) concluded that NARG1 and
ARD1 plays a role in the generation and differentiation of neurons.
Asaumi et al. (2005) confirmed interaction of APP (104760) with ARD1A in
mammalian cells by coimmunoprecipitation studies. Using human ACTH as a
substrate, they showed that the ARD1/NARG1 complex has strong N-terminal
transferase activity. Immunoprecipitation and Western blotting
experiments showed that ARD1 and NARG1 formed a complex in HEK293 cells.
Because APP-binding proteins can modulate APP metabolism, they tested
the ability of ARD1 to modulate beta-amyloid-40 secretion and found that
coexpression of both ARD1 and NARG1 was required to suppress
beta-amyloid-40 generation from APP. APP endocytosis assay in HEK293
cells showed that ARD1 and NARG1 suppressed endocytosis of APP.
Using reciprocal immunoprecipitation followed by mass spectroscopic
analysis, Arnesen et al. (2005) showed that endogenous ARD1 and NATH
formed stable complexes in several human cell lines and that the complex
showed N-terminal acetylation activity. Mutation analysis and
examination of proteolytic fragments indicated that the interaction was
mediated through an N-terminal domain of ARD1 and the C-terminal end of
NATH. Immunoprecipitation analysis showed ARD1 and NATH associated with
several ribosomal proteins. ARD1 and NATH were also detected in isolated
polysomes; however, they were predominantly nonpolysomal. Endogenous
ARD1 was present in both the nuclei and cytoplasm in several human cell
lines, whereas NATH was predominantly in the cytoplasm, despite the
presence of a well-defined nuclear localization signal within the NATH
coiled-coil region. Both ARD1 and NATH were cleaved in a
caspase-dependent manner during apoptosis in stressed HeLa cells,
resulting in reduced acetylation activity.
GENE STRUCTURE
Fluge et al. (2002) determined that the NARG1 gene contains at least 24
exons and spans 90 kb.
MAPPING
By genomic sequence analysis, Fluge et al. (2002) mapped the NARG1 gene
to chromosome 4.
NOMENCLATURE
Sugiura et al. (2001) referred to NARG1 as mNat1 due to its homology
with yeast Nat1; this creates confusion with the NAT1 gene (108345).
*FIELD* RF
1. Arnesen, T.; Anderson, D.; Baldersheim, C.; Lanotte, M.; Varhaug,
J. E.; Lillehaug, J. R.: Identification and characterization of the
human ARD1-NATH protein acetyltransferase complex. Biochem. J. 386:
433-443, 2005.
2. Asaumi, M.; Iijima, K.; Sumioka, A.; Iijima-Ando, K.; Kirino, Y.;
Nakaya, T.; Suzuki, T.: Interaction of N-terminal acetyltransferase
with the cytoplasmic domain of beta-amyloid precursor protein and
its effect on A-beta secretion. J. Biochem. 137: 147-155, 2005.
3. Fluge, O.; Bruland, O.; Akslen, L. A.; Varhaug, J. E.; Lillehaug,
J. R.: NATH, a novel gene overexpressed in papillary thyroid carcinomas. Oncogene 21:
5056-5068, 2002.
4. Sugiura, N.; Adams, S. M.; Corriveau, R. A.: An evolutionarily
conserved N-terminal acetyltransferase complex associated with neuronal
development. J. Biol. Chem. 278: 40113-40120, 2003.
5. Sugiura, N.; Patel, R. G.; Corriveau, R. A.: N-methyl-D-aspartate
receptors regulate a group of transiently expressed genes in the developing
brain. J. Biol. Chem. 276: 14257-14263, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 3/6/2007
Stefanie A. Nelson - updated: 2/20/2007
*FIELD* CD
Patricia A. Hartz: 7/30/2003
*FIELD* ED
carol: 07/06/2011
wwang: 3/6/2007
wwang: 2/21/2007
wwang: 2/20/2007
terry: 7/20/2004
mgross: 7/30/2003
*RECORD*
*FIELD* NO
608000
*FIELD* TI
*608000 N-ALPHA-ACETYLTRANSFERASE 15, NatA AUXILIARY SUBUNIT; NAA15
;;NMDA RECEPTOR-REGULATED 1; NARG1;;
read moreNAT1, S. CEREVISIAE, HOMOLOG OF; NATH
*FIELD* TX
CLONING
By replica cDNA screening for genes upregulated in papillary thyroid
carcinomas, Fluge et al. (2002) cloned NARG1 (NAA15), which they called
NATH. The deduced 866-amino acid protein has a calculated molecular mass
of 101 kD. It contains 4 tetratricopeptide repeat domains in 2 tandems
and a putative bipartite nuclear localization signal. NATH shares
similarity with S. cerevisiae N-acetyltransferase-1 (NAT1; 108345) and
mouse Narg1 and Tbdn1. Northern blot analysis detected a major
transcript of 4.6 kb and a minor transcript of 5.8 kb in a papillary
carcinoma cell line and in an anaplastic thyroid carcinoma cell line.
Multitissue mRNA dot blot analysis showed low expression in most adult
tissues and specific brain regions examined. Highest expression was
detected in testis and a Burkitt lymphoma cell line. Expression of NATH
in COS-7 cells resulted in cytoplasmic staining.
By Northern blot analysis, Sugiura et al. (2001) found that expression
of mouse Narg1 was highest in testis and much lower in other tissues
examined. They cloned 2 alternatively spliced variants of mouse Narg1
from testis. The deduced proteins contained 865 and 815 amino acids. The
shorter protein has an N-terminal truncation.
GENE FUNCTION
By analyzing cDNA arrays, Sugiura et al. (2001) found the expression of
Narg1, Narg2 (610835), and Narg3 was upregulated in neonatal mice in
which the gene for the Nmda receptor (NMDAR1; GRIN1 138249) was deleted.
In situ hybridization of wildtype neonatal mouse brain showed that
Narg1, Narg2, and Narg3 were expressed at high levels in regions of
neuronal proliferation and migration, and their expression was
downregulated during early postnatal development. Northern blot analysis
detected low expression of these genes on embryonic day 13, high
expression on postnatal day 0, and very low expression thereafter.
By semiquantitative RT-PCR, Fluge et al. (2002) found NATH overexpressed
in papillary thyroid carcinomas, especially in clinically aggressive
tumors with histologic evidence of poorly differentiated or
undifferentiated areas. In situ hybridization detected NATH highly
expressed in tumor cells and only weakly expressed in adjacent
nonneoplastic thyroid follicular cells. Transfection of NATH into a
papillary carcinoma cell line or embryonic kidney cells did not alter
the cellular proliferation rate.
Using in vitro translated mouse proteins, Sugiura et al. (2003) showed
that Narg1 and Ard1 (ARD1A, NAA10; 300013) assembled to form a
functional acetyltransferase. Narg1 alone showed no activity.
Immunoprecipitation and Western blot analysis demonstrated that Narg1
and Ard1 coassembled in mammalian cells. By cotransfection of rat kidney
fibroblasts, they showed that Narg1 and Ard1 localized to the cytoplasm
in both overlapping and separate compartments. In situ hybridization
demonstrated that throughout mouse brain development Narg1 and Ard1 were
highly expressed in areas of cell division and migration and their
expression appeared to be downregulated as neurons differentiated. Narg1
and Ard1 were expressed in proliferation mouse embryonic carcinoma
cells. Treatment of these cells with retinoic acid initiated neuronal
differentiation and downregulation of Narg1 and Ard1 as a neuronal
marker gene was induced. Sugiura et al. (2003) concluded that NARG1 and
ARD1 plays a role in the generation and differentiation of neurons.
Asaumi et al. (2005) confirmed interaction of APP (104760) with ARD1A in
mammalian cells by coimmunoprecipitation studies. Using human ACTH as a
substrate, they showed that the ARD1/NARG1 complex has strong N-terminal
transferase activity. Immunoprecipitation and Western blotting
experiments showed that ARD1 and NARG1 formed a complex in HEK293 cells.
Because APP-binding proteins can modulate APP metabolism, they tested
the ability of ARD1 to modulate beta-amyloid-40 secretion and found that
coexpression of both ARD1 and NARG1 was required to suppress
beta-amyloid-40 generation from APP. APP endocytosis assay in HEK293
cells showed that ARD1 and NARG1 suppressed endocytosis of APP.
Using reciprocal immunoprecipitation followed by mass spectroscopic
analysis, Arnesen et al. (2005) showed that endogenous ARD1 and NATH
formed stable complexes in several human cell lines and that the complex
showed N-terminal acetylation activity. Mutation analysis and
examination of proteolytic fragments indicated that the interaction was
mediated through an N-terminal domain of ARD1 and the C-terminal end of
NATH. Immunoprecipitation analysis showed ARD1 and NATH associated with
several ribosomal proteins. ARD1 and NATH were also detected in isolated
polysomes; however, they were predominantly nonpolysomal. Endogenous
ARD1 was present in both the nuclei and cytoplasm in several human cell
lines, whereas NATH was predominantly in the cytoplasm, despite the
presence of a well-defined nuclear localization signal within the NATH
coiled-coil region. Both ARD1 and NATH were cleaved in a
caspase-dependent manner during apoptosis in stressed HeLa cells,
resulting in reduced acetylation activity.
GENE STRUCTURE
Fluge et al. (2002) determined that the NARG1 gene contains at least 24
exons and spans 90 kb.
MAPPING
By genomic sequence analysis, Fluge et al. (2002) mapped the NARG1 gene
to chromosome 4.
NOMENCLATURE
Sugiura et al. (2001) referred to NARG1 as mNat1 due to its homology
with yeast Nat1; this creates confusion with the NAT1 gene (108345).
*FIELD* RF
1. Arnesen, T.; Anderson, D.; Baldersheim, C.; Lanotte, M.; Varhaug,
J. E.; Lillehaug, J. R.: Identification and characterization of the
human ARD1-NATH protein acetyltransferase complex. Biochem. J. 386:
433-443, 2005.
2. Asaumi, M.; Iijima, K.; Sumioka, A.; Iijima-Ando, K.; Kirino, Y.;
Nakaya, T.; Suzuki, T.: Interaction of N-terminal acetyltransferase
with the cytoplasmic domain of beta-amyloid precursor protein and
its effect on A-beta secretion. J. Biochem. 137: 147-155, 2005.
3. Fluge, O.; Bruland, O.; Akslen, L. A.; Varhaug, J. E.; Lillehaug,
J. R.: NATH, a novel gene overexpressed in papillary thyroid carcinomas. Oncogene 21:
5056-5068, 2002.
4. Sugiura, N.; Adams, S. M.; Corriveau, R. A.: An evolutionarily
conserved N-terminal acetyltransferase complex associated with neuronal
development. J. Biol. Chem. 278: 40113-40120, 2003.
5. Sugiura, N.; Patel, R. G.; Corriveau, R. A.: N-methyl-D-aspartate
receptors regulate a group of transiently expressed genes in the developing
brain. J. Biol. Chem. 276: 14257-14263, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 3/6/2007
Stefanie A. Nelson - updated: 2/20/2007
*FIELD* CD
Patricia A. Hartz: 7/30/2003
*FIELD* ED
carol: 07/06/2011
wwang: 3/6/2007
wwang: 2/21/2007
wwang: 2/20/2007
terry: 7/20/2004
mgross: 7/30/2003