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 09-DEC-2015, entry version 122. 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; 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=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., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA 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., 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 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., RA Dephoure N., 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 RT CK2."; RL Mol. Cell. Biol. 24:4734-4742(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION RP BY 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 RT phosphoproteome 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 RT insights into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Transcription factor involved in the expression of a CC broad class of genes including snRNAs. Required for sporulation CC and DNA-damage repair. Prevents the spreading of SIR silencing at CC telomeres and protects histone H4, but not H3, from deacetylation CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:12620224}. CC -!- SUBUNIT: Interacts with the TFIID subunit TAF7 and with histone CC H4. {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}. CC Nucleus {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 CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Contains 2 bromo domains. {ECO:0000255|PROSITE- CC ProRule:PRU00035}. CC -!- SIMILARITY: Contains 1 NET domain. {ECO:0000255|PROSITE- CC ProRule:PRU00857}. 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 ProteinModelPortal; Q07442; -. DR SMR; Q07442; 119-240, 303-428. DR BioGrid; 31990; 80. DR DIP; DIP-1337N; -. DR IntAct; Q07442; 10. DR MINT; MINT-410894; -. DR MaxQB; Q07442; -. DR EnsemblFungi; YDL070W; YDL070W; YDL070W. DR GeneID; 851488; -. DR KEGG; sce:YDL070W; -. DR EuPathDB; FungiDB:YDL070W; -. DR SGD; S000002228; BDF2. DR GeneTree; ENSGT00760000119206; -. DR HOGENOM; HOG000248774; -. DR InParanoid; Q07442; -. DR KO; K11684; -. DR OMA; ATIARIY; -. DR OrthoDB; EOG7Z69S1; -. DR BioCyc; YEAST:G3O-29482-MONOMER; -. DR Reactome; R-SCE-3371568; Attenuation phase. DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex. DR Reactome; R-SCE-6782135; Dual incision in TC-NER. DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR NextBio; 968816; -. DR PRO; PR:Q07442; -. DR Proteomes; UP000002311; Chromosome IV. 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 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:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.20.920.10; -; 2. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR027353; NET_dom. 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; Complete proteome; Cytoplasm; DNA damage; KW DNA repair; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Sporulation; Transcription; Transcription regulation. FT CHAIN 1 638 Bromodomain-containing factor 2. FT /FTId=PRO_0000239629. FT DOMAIN 150 222 Bromo 1. {ECO:0000255|PROSITE- FT ProRule:PRU00035}. FT DOMAIN 337 409 Bromo 2. {ECO:0000255|PROSITE- FT ProRule:PRU00035}. FT DOMAIN 506 590 NET. {ECO:0000255|PROSITE- FT ProRule:PRU00857}. FT COILED 468 537 {ECO:0000255}. FT MOD_RES 264 264 Phosphoserine. FT {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 //