NTO1_YEAST
ID NTO1_YEAST Reviewed; 748 AA.
AC Q12311; D6W441;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=NuA3 HAT complex component NTO1;
GN Name=NTO1; OrderedLocusNames=YPR031W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP DOMAIN, AND PREDICTION OF FUNCTION.
RX PubMed=16412250; DOI=10.1186/1471-2164-7-6;
RA Perry J.;
RT "The Epc-N domain: a predicted protein-protein interaction domain found in
RT select chromatin associated proteins.";
RL BMC Genomics 7:6-6(2006).
RN [6]
RP FUNCTION OF THE NUA3 COMPLEX, IDENTIFICATION IN THE NUA3 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17157260; DOI=10.1016/j.molcel.2006.10.026;
RA Taverna S.D., Ilin S., Rogers R.S., Tanny J.C., Lavender H., Li H.,
RA Baker L., Boyle J., Blair L.P., Chait B.T., Patel D.J., Aitchison J.D.,
RA Tackett A.J., Allis C.D.;
RT "Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT
RT activity at K14 of H3 and transcription at a subset of targeted ORFs.";
RL Mol. Cell 24:785-796(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of the NuA3 histone acetyltransferase complex, that
CC acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes
CC requires methylated histone H3. In conjunction with the FACT complex,
CC NuA3 may be involved in transcriptional regulation.
CC {ECO:0000269|PubMed:17157260}.
CC -!- SUBUNIT: Component of the NuA3 complex, which consists of at least
CC NTO1, SAS3, TAF14, YNG1 and EAF6. {ECO:0000269|PubMed:17157260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: Residues 156 to 543 compose a region conserved in chromatin
CC associated proteins. {ECO:0000269|PubMed:16412250}.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49274; CAA89285.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95027.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11457.1; -; Genomic_DNA.
DR PIR; S54505; S54505.
DR RefSeq; NP_015356.1; NM_001184128.1.
DR AlphaFoldDB; Q12311; -.
DR SMR; Q12311; -.
DR BioGRID; 36209; 158.
DR ComplexPortal; CPX-1810; NuA3 histone acetyltransferase complex.
DR DIP; DIP-4956N; -.
DR IntAct; Q12311; 11.
DR MINT; Q12311; -.
DR STRING; 4932.YPR031W; -.
DR iPTMnet; Q12311; -.
DR MaxQB; Q12311; -.
DR PaxDb; Q12311; -.
DR PRIDE; Q12311; -.
DR DNASU; 856143; -.
DR EnsemblFungi; YPR031W_mRNA; YPR031W; YPR031W.
DR GeneID; 856143; -.
DR KEGG; sce:YPR031W; -.
DR SGD; S000006235; NTO1.
DR VEuPathDB; FungiDB:YPR031W; -.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000176097; -.
DR HOGENOM; CLU_002663_1_0_1; -.
DR InParanoid; Q12311; -.
DR OMA; YWSMKRE; -.
DR BioCyc; YEAST:G3O-34190-MON; -.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-6804758; Regulation of TP53 Activity through Acetylation.
DR PRO; PR:Q12311; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12311; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0033100; C:NuA3 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:1990467; C:NuA3a histone acetyltransferase complex; IDA:SGD.
DR GO; GO:1990468; C:NuA3b histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF10513; EPL1; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..748
FT /note="NuA3 HAT complex component NTO1"
FT /id="PRO_0000268692"
FT ZN_FING 263..313
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 317..350
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 374..439
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 748 AA; 86029 MW; 7D6796553BCFA06D CRC64;
MNRGSLDDGP KLREEKHFQD FYPDLNADTL LPFIVPLVET KDNSTDTDSD DISNRNNREI
GSVKSVQTKE LIFKGRVTTE PLVLKKNEVE FQKCKITTNE LKGKKNPYCV RFNESFISRY
YHINKVRNRK SYKQQQKEFD GVEAPYFTKF SSKEAPNITI STSTKSAIQK FASISPNLVN
FKPQYDMDEQ DELYLHYLNK RYFKDQMSHE IFEILMTTLE TEWFHIEKHI PSTNSLIARH
NILRDCKNYE LYGSDDGTGL SMDQACAVCL GTDSDNLNTI VFCDGCDIAV HQECYGIIFI
PEGKWLCRRC MISKNNFATC LMCPSHTGAF KQTDTGSWVH NICALWLPEL YFSNLHYMEP
IEGVQNVSVS RWKLNCYICK KKMGACIQCF QRNCFTAYHV TCARRAGLYM SKGKCTIQEL
ASNQFSQKYS VESFCHKHAP RGWQTSIEGI NKARKYFSLL STLQTETPQH NEANDRTNSK
FNKTIWKTPN QTPVAPHVFA EILQKVVDFF GLANPPAGAF DICKYWSMKR ELTGGTPLTA
CFENNSLGSL TEEQVQTRID FANDQLEDLY RLKELTTLVK KRTQASNSLS RSRKKVFDIV
KSPQKYLLKI NVLDIFIKSE QFKALERLVT EPKLLVILEK CKHCDFDTVQ IFKEEIMHFF
EVLETLPGAS RILQTVSSKA KEQVTNLIGL IEHVDIKKLL SRDFIINDDK IEERPWSGPV
IMEEEGLSDA EELSAGEHRM LKLILNSG
