ID BDF2_YEAST Reviewed; 638 AA. AC Q07442; D6VRS8; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-DEC-2019, entry version 152. DE RecName: Full=Bromodomain-containing factor 2; GN Name=BDF2; OrderedLocusNames=YDL070W; 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=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(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 DOMAIN BROMODOMAIN. RX PubMed=9175470; DOI=10.1016/s0968-0004(97)01042-6; RA Jeanmougin F., Wurtz J.-M., Le Douarin B., Chambon P., Losson R.; RT "The bromodomain revisited."; RL Trends Biochem. Sci. 22:151-153(1997). RN [4] RP INTERACTION WITH TAF7. RX PubMed=10783167; RA Matangkasombut O., Buratowski R.M., Swilling N.W., Buratowski S.; RT "Bromodomain factor 1 corresponds to a missing piece of yeast TFIID."; RL Genes Dev. 14:951-962(2000). RN [5] RP FUNCTION, AND INTERACTION WITH HISTONE H4. RX PubMed=12620224; DOI=10.1016/s1097-2765(03)00033-9; RA Matangkasombut O., Buratowski S.; RT "Different sensitivities of bromodomain factors 1 and 2 to histone H4 RT acetylation."; RL Mol. Cell 11:353-363(2003). 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 PHOSPHORYLATION BY THE CK2 PROTEIN KINASE COMPLEX. RX PubMed=15143168; DOI=10.1128/mcb.24.11.4734-4742.2004; RA Sawa C., Nedea E., Krogan N., Wada T., Handa H., Greenblatt J., RA Buratowski S.; RT "Bromodomain factor 1 (Bdf1) is phosphorylated by protein kinase CK2."; RL Mol. Cell. Biol. 24:4734-4742(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [10] 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 [11] 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: Transcription factor involved in the expression of a broad CC class of genes including snRNAs. Required for sporulation and DNA- CC damage repair. Prevents the spreading of SIR silencing at telomeres and CC protects histone H4, but not H3, from deacetylation (By similarity). CC {ECO:0000250, ECO:0000269|PubMed:12620224}. CC -!- SUBUNIT: Interacts with the TFIID subunit TAF7 and with histone H4. CC {ECO:0000269|PubMed:10783167, ECO:0000269|PubMed:12620224}. CC -!- INTERACTION: CC P35817:BDF1; NbExp=5; IntAct=EBI-37620, EBI-3493; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus CC {ECO:0000269|PubMed:14562095}. CC -!- PTM: Phosphorylated by the casein kinase CK2 complex. CC {ECO:0000269|PubMed:15143168}. CC -!- MISCELLANEOUS: Present with 2930 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; Z74119; CAA98636.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11788.1; -; Genomic_DNA. DR PIR; S67605; S67605. DR RefSeq; NP_010213.1; NM_001180129.1. DR SMR; Q07442; -. DR BioGrid; 31990; 196. DR DIP; DIP-1337N; -. DR IntAct; Q07442; 11. DR MINT; Q07442; -. DR STRING; 4932.YDL070W; -. DR iPTMnet; Q07442; -. DR MaxQB; Q07442; -. DR PaxDb; Q07442; -. DR PRIDE; Q07442; -. DR EnsemblFungi; YDL070W_mRNA; YDL070W; YDL070W. DR GeneID; 851488; -. DR KEGG; sce:YDL070W; -. DR EuPathDB; FungiDB:YDL070W; -. DR SGD; S000002228; BDF2. DR HOGENOM; HOG000248774; -. DR InParanoid; Q07442; -. DR KO; K11684; -. DR OMA; ATIARIY; -. DR BioCyc; YEAST:G3O-29482-MONOMER; -. DR PRO; PR:Q07442; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; Q07442; protein. DR GO; GO:0071944; C:cell periphery; HDA:SGD. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IC:SGD. DR GO; GO:0001047; F:core promoter binding; IDA:SGD. DR GO; GO:0042393; F:histone binding; IDA:SGD. DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:SGD. DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IPI:SGD. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0031452; P:negative regulation of heterochromatin assembly; IMP:SGD. DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW. DR Gene3D; 1.20.1270.220; -; 1. DR Gene3D; 1.20.920.10; -; 2. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR027353; NET_dom. DR InterPro; IPR038336; NET_sf. DR Pfam; PF17035; BET; 1. DR Pfam; PF00439; Bromodomain; 2. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 2. DR SUPFAM; SSF47370; SSF47370; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 2. DR PROSITE; PS51525; NET; 1. PE 1: Evidence at protein level; KW Bromodomain; Coiled coil; Cytoplasm; DNA damage; DNA repair; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Sporulation; Transcription; KW Transcription regulation. FT CHAIN 1..638 FT /note="Bromodomain-containing factor 2" FT /id="PRO_0000239629" FT DOMAIN 150..222 FT /note="Bromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 337..409 FT /note="Bromo 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 506..590 FT /note="NET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857" FT COILED 468..537 FT /evidence="ECO:0000255" FT MOD_RES 264 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17330950" SQ SEQUENCE 638 AA; 72513 MW; A85CC497190345AD CRC64; MSRTNMDTRH AHSALLAAPQ SATANSRSSN SSSESSSNKN NINVGVGDDS GNVSAVSIDD GPHFRDIFHY GHEENYKLAS SGITNLNSSS HAHQTLSPIS ISNASTPESF PEHPLGLERE TEPALEAEME AEELPPHQSK YLLSSIKATK RLKDARPFLK PVDPIALNIP HYFNYVQTPM DLSLIETKLQ GNVYHSVEQV TSDFKTMVDN CLNFNGPESS ISSMAKRIQK YFEKKLSAMP PRVLPASALK KTSRNRKKNE DMDSPLVIRR SVSTTNDNIG ESGNREGVSG GRPKRTIHPP KSKDLFDIYE NSKPKSKTLQ KKFRTCLKIL KVLMSKKNSD INFPFLQPVD PIALNLPNYF DVVKNPMDLG TISNNLMNWK YKTIDQFVDD LNLVFYNCFQ FNPEGNEVHS MGKKLKELFN FHWLENQDIL NEIETDSDLE EDNYSSSYSS DDEYDDEDIN ENDITNPAIQ YLEQKLKKME VELQQLKRQE LSKLSKERKR KHLGKTLLRR KAMKHSVDDL KKSITDKINE LSDLEMNGMI RIIKNSLPAD EILTSNEDEI EIDLDILDEA TIARIYERYF EKKNNNNSKR KLSGNYSTAP TNKKKKTLKF LEKDEIINNN NYSDSEEDSS DSSDSDSD //