ID YNG2_YEAST Reviewed; 282 AA. AC P38806; D3DL42; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 12-OCT-2022, entry version 180. DE RecName: Full=Chromatin modification-related protein YNG2; DE AltName: Full=ESA1-associated factor 4; DE AltName: Full=ING1 homolog 2; GN Name=YNG2; Synonyms=EAF4, NBN1; OrderedLocusNames=YHR090C; 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=8091229; DOI=10.1126/science.8091229; RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., RA Waterston R., Wilson R., Vaudin M.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT VIII."; RL Science 265:2077-2082(1994). 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 FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE NUA4 COMPLEX. RX PubMed=10805724; DOI=10.1128/mcb.20.11.3807-3816.2000; RA Loewith R., Meijer M., Lees-Miller S.P., Riabowol K., Young D.; RT "Three yeast proteins related to the human candidate tumor suppressor RT p33(ING1) are associated with histone acetyltransferase activities."; RL Mol. Cell. Biol. 20:3807-3816(2000). RN [4] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11544250; DOI=10.1074/jbc.m102531200; RA Choy J.S., Tobe B.T.D., Huh J.H., Kron S.J.; RT "Yng2p-dependent NuA4 histone H4 acetylation activity is required for RT mitotic and meiotic progression."; RL J. Biol. Chem. 276:43653-43662(2001). RN [5] RP PROTEIN SEQUENCE OF 1-34; 62-70; 107-161; 171-180 AND 184-193, RP IDENTIFICATION IN THE NUA4 COMPLEX, AND FUNCTION. RX PubMed=11604499; DOI=10.1128/mcb.21.22.7629-7640.2001; RA Nourani A., Doyon Y., Utley R.T., Allard S., Lane W.S., Cote J.; RT "Role of an ING1 growth regulator in transcriptional activation and RT targeted histone acetylation by the NuA4 complex."; RL Mol. Cell. Biol. 21:7629-7640(2001). RN [6] RP FUNCTION. RX PubMed=12417725; DOI=10.1128/mcb.22.23.8215-8225.2002; RA Choy J.S., Kron S.J.; RT "NuA4 subunit Yng2 function in intra-S-phase DNA damage response."; RL Mol. Cell. Biol. 22:8215-8225(2002). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3; RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M., RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E., RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.; RT "Assigning function to yeast proteins by integration of technologies."; RL Mol. Cell 12:1353-1365(2003). RN [8] 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 [9] RP IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=15485911; DOI=10.1128/mcb.24.21.9424-9436.2004; RA Zhang H., Richardson D.O., Roberts D.N., Utley R.T., Erdjument-Bromage H., RA Tempst P., Cote J., Cairns B.R.; RT "The Yaf9 component of the SWR1 and NuA4 complexes is required for proper RT gene expression, histone H4 acetylation, and Htz1 replacement near RT telomeres."; RL Mol. Cell. Biol. 24:9424-9436(2004). RN [10] RP IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=15045029; DOI=10.1371/journal.pbio.0020131; RA Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., RA Jennings J.L., Link A.J., Madhani H.D., Rine J.; RT "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p RT deposits histone variant H2A.Z into euchromatin."; RL PLoS Biol. 2:587-599(2004). RN [11] RP IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=15353583; DOI=10.1073/pnas.0405753101; RA Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y., RA Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A., RA Buratowski S., Hieter P., Greenblatt J.F.; RT "Regulation of chromosome stability by the histone H2A variant Htz1, the RT Swr1 chromatin remodeling complex, and the histone acetyltransferase RT NuA4."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004). RN [12] 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; THR-185 AND SER-188, AND 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: Component of the NuA4 histone acetyltransferase complex which CC is involved in transcriptional activation of selected genes principally CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is CC also involved in DNA repair. Involved in cell cycle progression and CC meiosis. {ECO:0000269|PubMed:10805724, ECO:0000269|PubMed:11544250, CC ECO:0000269|PubMed:11604499, ECO:0000269|PubMed:12417725}. CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2. CC Component of the NuA4 histone acetyltransferase complex composed of at CC least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, CC ESA1, TRA1 and YNG2. {ECO:0000269|PubMed:10805724, CC ECO:0000269|PubMed:11604499, ECO:0000269|PubMed:15045029, CC ECO:0000269|PubMed:15353583, ECO:0000269|PubMed:15485911, CC ECO:0000269|PubMed:16728974}. CC -!- INTERACTION: CC P38806; P43572: EPL1; NbExp=10; IntAct=EBI-24622, EBI-22792; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10805724, CC ECO:0000269|PubMed:11544250, ECO:0000269|PubMed:14562095}. CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3. CC {ECO:0000269|PubMed:16728974}. CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00060; AAB68930.1; -; Genomic_DNA. DR EMBL; BK006934; DAA06786.1; -; Genomic_DNA. DR PIR; S46722; S46722. DR RefSeq; NP_011958.1; NM_001179220.1. DR PDB; 2MUM; NMR; -; A=222-271. DR PDB; 5J9Q; X-ray; 3.25 A; D/H/K=1-120. DR PDB; 5J9T; X-ray; 2.70 A; D/H/L=1-120. DR PDB; 5J9U; X-ray; 2.95 A; D/H/K=1-120. DR PDB; 5J9W; X-ray; 2.80 A; D/H/L=1-120. DR PDBsum; 2MUM; -. DR PDBsum; 5J9Q; -. DR PDBsum; 5J9T; -. DR PDBsum; 5J9U; -. DR PDBsum; 5J9W; -. DR AlphaFoldDB; P38806; -. DR BMRB; P38806; -. DR SMR; P38806; -. DR BioGRID; 36525; 597. DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex. DR ComplexPortal; CPX-3185; Piccolo NuA4 histone acetyltransferase complex. DR DIP; DIP-2095N; -. DR IntAct; P38806; 19. DR MINT; P38806; -. DR STRING; 4932.YHR090C; -. DR iPTMnet; P38806; -. DR MaxQB; P38806; -. DR PaxDb; P38806; -. DR PRIDE; P38806; -. DR EnsemblFungi; YHR090C_mRNA; YHR090C; YHR090C. DR GeneID; 856490; -. DR KEGG; sce:YHR090C; -. DR SGD; S000001132; YNG2. DR VEuPathDB; FungiDB:YHR090C; -. DR eggNOG; KOG1973; Eukaryota. DR GeneTree; ENSGT00940000156619; -. DR HOGENOM; CLU_031900_2_0_1; -. DR InParanoid; P38806; -. DR OMA; YEWFHWK; -. DR BioCyc; YEAST:G3O-31137-MON; -. DR Reactome; R-SCE-3899300; SUMOylation of transcription cofactors. DR Reactome; R-SCE-6811555; PI5P Regulates TP53 Acetylation. DR PRO; PR:P38806; -. DR Proteomes; UP000002311; Chromosome VIII. DR RNAct; P38806; protein. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD. DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:SGD. 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; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IDA:SGD. DR GO; GO:0006351; P:DNA-templated transcription; IC:ComplexPortal. DR GO; GO:0016573; P:histone acetylation; IDA:SGD. DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR028651; ING_fam. DR InterPro; IPR024610; ING_N_histone-binding. 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 PANTHER; PTHR10333; PTHR10333; 2. DR Pfam; PF12998; ING; 1. DR SMART; SM01408; ING; 1. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Chromatin regulator; Coiled coil; KW Direct protein sequencing; DNA damage; DNA repair; Meiosis; Metal-binding; KW Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1..282 FT /note="Chromatin modification-related protein YNG2" FT /id="PRO_0000212679" FT ZN_FING 222..271 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 123..217 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 35..86 FT /evidence="ECO:0000255" FT COMPBIAS 133..162 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 225 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT BINDING 227 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT BINDING 238 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT BINDING 243 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT BINDING 249 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT BINDING 252 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT BINDING 265 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT BINDING 268 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT SITE 224 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT SITE 235 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT SITE 239 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT SITE 247 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000250|UniProtKB:Q9UK53" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 185 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT HELIX 3..13 FT /evidence="ECO:0007829|PDB:5J9T" FT TURN 14..16 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 17..56 FT /evidence="ECO:0007829|PDB:5J9T" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 65..113 FT /evidence="ECO:0007829|PDB:5J9T" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:2MUM" FT TURN 250..254 FT /evidence="ECO:0007829|PDB:2MUM" FT HELIX 266..270 FT /evidence="ECO:0007829|PDB:2MUM" SQ SEQUENCE 282 AA; 32086 MW; 110E0A2536547D03 CRC64; MDPSLVLEQT IQDVSNLPSE FRYLLEEIGS NDLKLIEEKK KYEQKESQIH KFIRQQGSIP KHPQEDGLDK EIKESLLKCQ SLQREKCVLA NTALFLIARH LNKLEKNIAL LEEDGVLAPV EEDGDMDSAA EASRESSVVS NSSVKKRRAA SSSGSVPPTL KKKKTSRTSK LQNEIDVSSR EKSVTPVSPS IEKKIARTKE FKNSRNGKGQ NGSPENEEED KTLYCFCQRV SFGEMVACDG PNCKYEWFHY DCVNLKEPPK GTWYCPECKI EMEKNKLKRK RN //