ID YNG2_YEAST STANDARD; PRT; 282 AA. AC P38806; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 07-MAR-2006, entry version 39. DE Chromatin modification-related protein YNG2 (ING1 homolog 2) (ESA1- DE associated factor 4). GN Name=YNG2; Synonyms=EAF4, NBN1; OrderedLocusNames=YHR090C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c / AB972; RX MEDLINE=94378003; PubMed=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 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 [3] 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 [4] 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 [5] 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 [6] RP SUBCELLULAR LOCATION. RX MEDLINE=22923954; 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 IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS 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 [8] RP IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS 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:E131-E131(2004). RN [9] RP IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS 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). 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. CC -!- SUBUNIT: 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 -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the ING family. CC -!- SIMILARITY: Contains 1 PHD-type zinc finger. 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 PIR; S46722; S46722. DR HSSP; Q14839; 1MM2. DR IntAct; P38806; -. DR GermOnline; 139407; -. DR TRANSFAC; T03507; -. DR Ensembl; YHR090C; Saccharomyces cerevisiae. DR GenomeReviews; U00093_GR; YHR090C. DR SGD; S000001132; YNG2. DR BioCyc; SCER-S28-01:SCER-S28-01-002722-MONOMER; -. DR LinkHub; P38806; -. DR GO; GO:0043189; C:H4/H2A histone acetyltransferase complex; IPI. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0008047; F:enzyme activator activity; IMP. DR GO; GO:0016568; P:chromatin modification; IMP. DR InterPro; IPR001965; Znf_PHD. DR Pfam; PF00628; PHD; 1. DR SMART; SM00249; PHD; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. KW Cell cycle; Chromatin regulator; Coiled coil; Complete proteome; KW Direct protein sequencing; DNA damage; DNA repair; Meiosis; KW Metal-binding; Nuclear protein; Zinc; Zinc-finger. FT CHAIN 1 282 Chromatin modification-related protein FT YNG2. FT /FTId=PRO_0000212679. FT ZN_FING 222 271 PHD-type. FT COILED 35 86 Potential. 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 //