YNG1_YEAST
ID YNG1_YEAST Reviewed; 219 AA.
AC Q08465; D6W2C7; O00025;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein YNG1;
DE AltName: Full=ING1 homolog 1;
GN Name=YNG1; OrderedLocusNames=YOR064C; ORFNames=YOR29-15;
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 [GENOMIC DNA].
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP NUA3 COMPLEX.
RX PubMed=12077334; DOI=10.1128/mcb.22.14.5047-5053.2002;
RA Howe L., Kusch T., Muster N., Chaterji R., Yates J.R. III, Workman J.L.;
RT "Yng1p modulates the activity of Sas3p as a component of the yeast NuA3
RT Hhistone acetyltransferase complex.";
RL Mol. Cell. Biol. 22:5047-5053(2002).
RN [6]
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 [7]
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 [8]
RP FUNCTION, INTERACTION WITH HISTONE H3, FUNCTION OF THE NUA3 COMPLEX,
RP IDENTIFICATION IN THE NUA3 COMPLEX, AND IDENTIFICATION BY MASS
RP 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 [9]
RP DOMAIN PHD-TYPE ZINC-FINGER, AND INTERACTION WITH HISTONES H3K4ME3 AND
RP H3K4ME2.
RX PubMed=16728974; DOI=10.1038/nature04835;
RA Shi X., Hong T., Walter K.L., Ewalt M., Michishita E., Hung T., Carney D.,
RA Pena P., Lan F., Kaadige M.R., Lacoste N., Cayrou C., Davrazou F., Saha A.,
RA Cairns B.R., Ayer D.E., Kutateladze T.G., Shi Y., Cote J., Chua K.F.,
RA Gozani O.;
RT "ING2 PHD domain links histone H3 lysine 4 methylation to active gene
RT repression.";
RL Nature 442:96-99(2006).
RN [10]
RP IDENTIFICATION BY 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: Histone-binding component of the NuA3 histone
CC acetyltransferase complex, that acetylates Lys-14 of histone H3.
CC Recruitment of NuA3 to nucleosomes requires methylated histone H3. In
CC conjunction with the FACT complex, NuA3 may be involved in
CC transcriptional regulation. YNG1 is required for the HAT activity of
CC NuA3 but not for its integrity. Mediates the interaction of SAS3 with
CC nucleosomes. {ECO:0000269|PubMed:12077334,
CC ECO:0000269|PubMed:17157260}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC Component of the NuA3 complex, composed of at least NTO1, SAS3, TAF14,
CC YNG1 and EAF6. Interacts with histone H3-K4 trimethylated.
CC {ECO:0000269|PubMed:12077334, ECO:0000269|PubMed:16728974,
CC ECO:0000269|PubMed:17157260}.
CC -!- INTERACTION:
CC Q08465; P61830: HHT2; NbExp=5; IntAct=EBI-31890, EBI-8098;
CC Q08465; P34218: SAS3; NbExp=5; IntAct=EBI-31890, EBI-16484;
CC Q08465; P35189: TAF14; NbExp=3; IntAct=EBI-31890, EBI-18920;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000269|PubMed:16728974}.
CC -!- MISCELLANEOUS: Present with 861 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
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DR EMBL; Z70678; CAA94549.1; -; Genomic_DNA.
DR EMBL; Z74972; CAA99257.1; -; Genomic_DNA.
DR EMBL; AY557753; AAS56079.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10843.1; -; Genomic_DNA.
DR PIR; S66947; S66947.
DR RefSeq; NP_014707.1; NM_001183483.1.
DR PDB; 2JMI; NMR; -; A=141-219.
DR PDB; 2JMJ; NMR; -; A=141-219.
DR PDBsum; 2JMI; -.
DR PDBsum; 2JMJ; -.
DR AlphaFoldDB; Q08465; -.
DR SMR; Q08465; -.
DR BioGRID; 34463; 153.
DR ComplexPortal; CPX-1810; NuA3 histone acetyltransferase complex.
DR DIP; DIP-3833N; -.
DR IntAct; Q08465; 6.
DR MINT; Q08465; -.
DR STRING; 4932.YOR064C; -.
DR iPTMnet; Q08465; -.
DR MaxQB; Q08465; -.
DR PaxDb; Q08465; -.
DR PRIDE; Q08465; -.
DR EnsemblFungi; YOR064C_mRNA; YOR064C; YOR064C.
DR GeneID; 854230; -.
DR KEGG; sce:YOR064C; -.
DR SGD; S000005590; YNG1.
DR VEuPathDB; FungiDB:YOR064C; -.
DR eggNOG; KOG1973; Eukaryota.
DR HOGENOM; CLU_074406_1_0_1; -.
DR InParanoid; Q08465; -.
DR OMA; RTLWTIQ; -.
DR BioCyc; YEAST:G3O-33604-MON; -.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-SCE-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-SCE-6811555; PI5P Regulates TP53 Acetylation.
DR EvolutionaryTrace; Q08465; -.
DR PRO; PR:Q08465; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08465; protein.
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:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0033698; C:Rpd3L complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IMP:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID50148; -.
DR InterPro; IPR028651; ING_fam.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10333; PTHR10333; 2.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..219
FT /note="Protein YNG1"
FT /id="PRO_0000240248"
FT ZN_FING 155..204
FT /note="PHD-type; degenerate"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 157
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 168
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 172
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 180
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:2JMI"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:2JMI"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2JMI"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:2JMI"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:2JMI"
SQ SEQUENCE 219 AA; 25350 MW; 5232A71839E2FDA4 CRC64;
MEHLANENSD SDIRYSFLST LDHLPCELIR SLRLMQTIDL FKNEEDEPGM ERACRDLLLV
ATYINDLVDD QIHFLKQHKK ELEIQKSVTK NFNSSLENIK SKLTLEEPGA YKEPKLLLKI
NLKKAKSRER KESITSPTIG INQGDVTEGN NNQEEVYCFC RNVSYGPMVA CDNPACPFEW
FHYGCVGLKQ APKGKWYCSK DCKEIANQRS KSKRQKRRK
