BDF2_YEAST
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 03-AUG-2022, entry version 165.
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 Q07442; 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}.
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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 AlphaFoldDB; Q07442; -.
DR SMR; Q07442; -.
DR BioGRID; 31990; 200.
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 SGD; S000002228; BDF2.
DR VEuPathDB; FungiDB:YDL070W; -.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000176400; -.
DR HOGENOM; CLU_001499_4_0_1; -.
DR InParanoid; Q07442; -.
DR OMA; AQPDSQH; -.
DR BioCyc; YEAST:G3O-29482-MON; -.
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:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001046; F:core promoter sequence-specific DNA 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:0006338; P:chromatin remodeling; IBA:GO_Central.
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 REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 468..537
FT /evidence="ECO:0000255"
FT COMPBIAS 18..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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
