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 14-OCT-2015, entry version 130. 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; OC Saccharomycetes; 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., RA Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., RA Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., RA Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., RA Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., RA Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., RA 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE NUA4 RP 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 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 [8] 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., RA Erdjument-Bromage H., Tempst P., Cote J., Cairns B.R.; RT "The Yaf9 component of the SWR1 and NuA4 complexes is required for RT proper gene expression, histone H4 acetylation, and Htz1 replacement RT near telomeres."; RL Mol. Cell. Biol. 24:9424-9436(2004). RN [9] 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 RT Swr1p deposits histone variant H2A.Z into euchromatin."; RL PLoS Biol. 2:587-599(2004). RN [10] 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, RT the Swr1 chromatin remodeling complex, and the histone RT acetyltransferase NuA4."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004). RN [11] 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., RA Carney D., Pena P., Lan F., Kaadige M.R., Lacoste N., Cayrou C., RA Davrazou F., Saha A., Cairns B.R., Ayer D.E., Kutateladze T.G., RA Shi Y., Cote J., Chua K.F., Gozani O.; RT "ING2 PHD domain links histone H3 lysine 4 methylation to active gene RT repression."; RL Nature 442:96-99(2006). RN [12] 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; THR-185 AND RP SER-188, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 RT insights into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex CC which is involved in transcriptional activation of selected genes CC principally by acetylation of nucleosomal histone H4 and H2A. The CC NuA4 complex is also involved in DNA repair. Involved in cell CC cycle progression and meiosis. {ECO:0000269|PubMed:10805724, CC ECO:0000269|PubMed:11544250, ECO:0000269|PubMed:11604499, CC ECO:0000269|PubMed:12417725}. CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with CC H3K4me2. Component of the NuA4 histone acetyltransferase complex CC composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, CC EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2. CC {ECO:0000269|PubMed:10805724, ECO:0000269|PubMed:11604499, CC ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15353583, CC ECO:0000269|PubMed:15485911, ECO:0000269|PubMed:16728974}. CC -!- INTERACTION: CC P43572:EPL1; NbExp=8; 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 -!- SIMILARITY: Contains 1 PHD-type zinc finger. {ECO:0000255|PROSITE- CC ProRule:PRU00146}. 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 PDBsum; 2MUM; -. DR ProteinModelPortal; P38806; -. DR SMR; P38806; 222-271. DR BioGrid; 36525; 286. DR DIP; DIP-2095N; -. DR IntAct; P38806; 18. DR MINT; MINT-561028; -. DR MaxQB; P38806; -. DR PaxDb; P38806; -. DR PeptideAtlas; P38806; -. DR EnsemblFungi; YHR090C; YHR090C; YHR090C. DR GeneID; 856490; -. DR KEGG; sce:YHR090C; -. DR EuPathDB; FungiDB:YHR090C; -. DR SGD; S000001132; YNG2. DR eggNOG; COG5034; -. DR GeneTree; ENSGT00550000074538; -. DR HOGENOM; HOG000000883; -. DR InParanoid; P38806; -. DR KO; K11396; -. DR OMA; TLTKHPK; -. DR OrthoDB; EOG7G1VHM; -. DR BioCyc; YEAST:G3O-31137-MONOMER; -. DR NextBio; 982194; -. DR PRO; PR:P38806; -. DR Proteomes; UP000002311; Chromosome VIII. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:SGD. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0016568; P:chromatin modification; IMP:SGD. DR GO; GO:0006281; P:DNA repair; IDA:SGD. DR GO; GO:0016573; P:histone acetylation; IDA:SGD. DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. 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; 1. DR Pfam; PF12998; 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 Complete proteome; Direct protein sequencing; DNA damage; DNA repair; KW Meiosis; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; KW Zinc; Zinc-finger. FT CHAIN 1 282 Chromatin modification-related protein FT YNG2. FT /FTId=PRO_0000212679. FT ZN_FING 222 271 PHD-type. {ECO:0000255|PROSITE- FT ProRule:PRU00146}. FT COILED 35 86 {ECO:0000255}. FT BINDING 224 224 Histone H3K4me3. {ECO:0000250}. FT BINDING 235 235 Histone H3K4me3. {ECO:0000250}. FT BINDING 239 239 Histone H3K4me3. {ECO:0000250}. FT BINDING 247 247 Histone H3K4me3. {ECO:0000250}. FT MOD_RES 183 183 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT MOD_RES 185 185 Phosphothreonine. FT {ECO:0000244|PubMed:19779198}. FT MOD_RES 188 188 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT STRAND 225 227 {ECO:0000244|PDB:2MUM}. FT TURN 250 254 {ECO:0000244|PDB:2MUM}. FT HELIX 266 270 {ECO:0000244|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 //