P35817 (BDF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bromodomain-containing factor 1

Gene names

Name:	BDF1
Ordered Locus Names:	YLR399C
ORF Names:	L8084.18

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	686 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor involved in the expression of a broad class of genes including snRNAs. Required for sporulation and DNA-damage repair. Prevents the spreading of SIR silencing at telomeres and protects histone H4, but not H3, from deacetylation. Ref.1 Ref.2 Ref.7 Ref.9 Ref.10 Ref.11 Ref.14 Ref.16
Subunit structure	Interacts with the TFIID subunit TAF7 and with acetylated histones H3 and H4. Ref.7 Ref.8 Ref.10 Ref.11
Subcellular location	Nucleus Ref.2 Ref.12.
Post-translational modification	Phosphorylated by the casein kinase CK2 complex. Ref.15
Miscellaneous	Present with 8100 molecules/cell in log phase SD medium.
Sequence similarities	Contains 2 bromo domains. Contains 1 NET domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair Sporulation Transcription Transcription regulation
Cellular component	Nucleus
Domain	Bromodomain Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from mutant phenotype Ref.2. Source: SGD chromatin remodeling Inferred from physical interaction PubMed 14690608. Source: SGD negative regulation of heterochromatin assembly Inferred from mutant phenotype PubMed 16239142. Source: SGD positive regulation of histone exchange Inferred from mutant phenotype PubMed 20332092. Source: SGD regulation of chromatin silencing at silent mating-type cassette Inferred from mutant phenotype Ref.11. Source: SGD regulation of chromatin silencing at telomere Inferred from mutant phenotype Ref.11. Source: SGD regulation of transcription by chromatin organization Inferred from mutant phenotype Ref.11. Source: SGD snRNA transcription Inferred from mutant phenotype Ref.1. Source: SGD sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Swr1 complex Inferred from direct assay PubMed 19088068. Source: SGD
Molecular_function	TFIID-class transcription factor binding Inferred from direct assay Ref.7. Source: SGD chromatin binding Inferred from direct assay Ref.11. Source: SGD core promoter binding Inferred from direct assay Ref.11PubMed 17526728. Source: SGD histone acetyl-lysine binding Inferred from direct assay Ref.10PubMed 20126658. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BDF2	Q07442	3	EBI-3493,EBI-37620
HHT2	P61830	2	EBI-3493,EBI-8098
HTZ1	Q12692	4	EBI-3493,EBI-8080
SWR1	Q05471	3	EBI-3493,EBI-22102
TAF1	P46677	3	EBI-3493,EBI-18855
TAF12	Q03761	2	EBI-3493,EBI-35097
TAF6	P53040	2	EBI-3493,EBI-18876
TAF7	Q05021	5	EBI-3493,EBI-27490
VPS71	Q03433	2	EBI-3493,EBI-27814
YAF9	P53930	3	EBI-3493,EBI-28841

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 686	686	Bromodomain-containing factor 1		PRO_0000211176
Regions
	Domain	165 – 237	73	Bromo 1
	Domain	332 – 404	73	Bromo 2
	Domain	518 – 598	81	NET
	Coiled coil	460 – 499	40	Potential
Amino acid modifications
	Modified residue	65	1	Phosphoserine Ref.21
	Modified residue	90	1	Phosphothreonine Ref.21
	Modified residue	92	1	Phosphoserine Ref.21
	Modified residue	269	1	Phosphoserine Ref.17 Ref.20 Ref.21
	Modified residue	270	1	Phosphoserine Ref.18 Ref.19 Ref.20 Ref.21
	Modified residue	429	1	Phosphoserine Ref.18
	Modified residue	612	1	Phosphoserine Ref.21
	Modified residue	613	1	Phosphoserine Ref.21
	Modified residue	615	1	Phosphoserine Ref.21
	Modified residue	617	1	Phosphothreonine Ref.21
	Modified residue	652	1	Phosphoserine Ref.21
	Modified residue	659	1	Phosphoserine Ref.21
Experimental info
	Mutagenesis	187	1	Y → F: Impairs interaction with histones H3 and H4; when associated with F-354. Ref.11
	Mutagenesis	354	1	Y → F: Impairs interaction with histones H3 and H4; when associated with F-187. Ref.11
	Sequence conflict	8	1	Q → LC in CAA79377. Ref.1
	Sequence conflict	93 – 94	2	GA → R in AAA89115. Ref.2
	Sequence conflict	94	1	A → P in CAA79377. Ref.1
	Sequence conflict	282	1	A → P in CAA79377. Ref.1
	Sequence conflict	385	1	D → E in CAA79377. Ref.1
	Sequence conflict	493	1	A → R in AAA35048. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P35817 [UniParc]. Last modified July 15, 1999. Version 3. Checksum: 8CCD52F41F91D0DA	FASTA	686	76,978
	10 20 30 40 50 60 MTDITPVQND VDVNGNNVND DVSSNLKRPI DQGDPSNGLA EEENPANNQL HLKKARLDGD 70 80 90 100 110 120 ALTSSPAGLA ENGIEGATLA ANGENGYNAT GSGAEDEQQG LKKEEGGQGT KQEDLDENSK 130 140 150 160 170 180 QELPMEVPKE PAPAPPPEPD MNNLPQNPIP KHQQKHALLA IKAVKRLKDA RPFLQPVDPV 190 200 210 220 230 240 KLDIPFYFNY IKRPMDLSTI ERKLNVGAYE VPEQITEDFN LMVNNSIKFN GPNAGISQMA 250 260 270 280 290 300 RNIQASFEKH MLNMPAKDAP PVIAKGRRSS AQEDAPIVIR RAQTHNGRPK RTIHPPKSKD 310 320 330 340 350 360 IYPYESKKPK SKRLQQAMKF CQSVLKELMA KKHASYNYPF LEPVDPVSMN LPTYFDYVKE 370 380 390 400 410 420 PMDLGTIAKK LNDWQYQTME DFERDVRLVF KNCYTFNPDG TIVNMMGHRL EEVFNSKWAD 430 440 450 460 470 480 RPNLDDYDSD EDSRTQGDYD DYESEYSESD IDETIITNPA IQYLEEQLAR MKVELQQLKK 490 500 510 520 530 540 QELEKIRKER RLARGSKKRG KRSKGRSGSK NASSKGRRDK KNKLKTVVTY DMKRIITERI 550 560 570 580 590 600 NDLPTSKLER AIDIIKKSMP NISEDDEVEL DLDTLDNHTI LTLYNTFFRQ YESSSGASNG 610 620 630 640 650 660 LDGTSGVTRD ASSLSPTSAG SRKRRSKALS QEEQSRQIEK IKNKLAILDS ASPLSQNGSP 670 680 GQIQSAAHNG FSSSSDDDVS SESEEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The yeast BDF1 gene encodes a transcription factor involved in the expression of a broad class of genes including snRNAs." Lygerou Z., Conesa C., Lesage P., Swanson R.N., Ruet A., Carlson M., Sentenac A., Seraphin B. Nucleic Acids Res. 22:5332-5340(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ATCC 204508 / S288c.
[2]	"Bdf1, a yeast chromosomal protein required for sporulation." Chua P., Roeder G.S. Mol. Cell. Biol. 15:3685-3696(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Evidence that the SKI antiviral system of Saccharomyces cerevisiae acts by blocking expression of viral mRNA." Widner W.R., Wickner R.B. Mol. Cell. Biol. 13:4331-4341(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 471-686.
[6]	"The bromodomain revisited." Jeanmougin F., Wurtz J.-M., Le Douarin B., Chambon P., Losson R. Trends Biochem. Sci. 22:151-153(1997) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN BROMODOMAIN.
[7]	"Bromodomain factor 1 corresponds to a missing piece of yeast TFIID." Matangkasombut O., Buratowski R.M., Swilling N.W., Buratowski S. Genes Dev. 14:951-962(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TAF7.
[8]	"Bromodomain factor 1 (Bdf1) protein interacts with histones." Pamblanco M., Poveda A., Sendra R., Rodriguez-Navarro S., Perez-Ortin J.E., Tordera V. FEBS Lett. 496:31-35(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HISTONES H3 AND H4.
[9]	"A genome-wide screen for methyl methanesulfonate-sensitive mutants reveals genes required for S phase progression in the presence of DNA damage." Chang M., Bellaoui M., Boone C., Brown G.W. Proc. Natl. Acad. Sci. U.S.A. 99:16934-16939(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Different sensitivities of bromodomain factors 1 and 2 to histone H4 acetylation." Matangkasombut O., Buratowski S. Mol. Cell 11:353-363(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HISTONES H3 AND H4.
[11]	"Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries." Ladurner A.G., Inouye C., Jain R., Tjian R. Mol. Cell 11:365-376(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ACETYLATED HISTONES H3 AND H4, MUTAGENESIS OF TYR-187 AND TYR-354.
[12]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[13]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]	"Precise nucleosome positioning and the TATA box dictate requirements for the histone H4 tail and the bromodomain factor Bdf1." Martinez-Campa C., Politis P., Moreau J.-L., Kent N., Goodall J., Mellor J., Goding C.R. Mol. Cell 15:69-81(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Bromodomain factor 1 (Bdf1) is phosphorylated by protein kinase CK2." Sawa C., Nedea E., Krogan N., Wada T., Handa H., Greenblatt J., Buratowski S. Mol. Cell. Biol. 24:4734-4742(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY THE CK2 PROTEIN KINASE COMPLEX.
[16]	"The bromodomain-containing protein Bdf1p acts as a phenotypic and transcriptional multicopy suppressor of YAF9 deletion in yeast." Bianchi M.M., Costanzo G., Chelstowska A., Grabowska D., Mazzoni C., Piccinni E., Cavalli A., Ciceroni F., Rytka J., Slonimski P.P., Frontali L., Negri R. Mol. Microbiol. 53:953-968(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, MASS SPECTROMETRY. Strain: YAL6B.
[18]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND SER-429, MASS SPECTROMETRY. Strain: ADR376.
[19]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, MASS SPECTROMETRY.
[20]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND SER-270, MASS SPECTROMETRY.
[21]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; THR-90; SER-92; SER-269; SER-270; SER-612; SER-613; SER-615; THR-617; SER-652 AND SER-659, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z18944 Genomic DNA. Translation: CAA79377.1. U18116 Genomic DNA. Translation: AAA89115.1. U19729 Genomic DNA. Translation: AAB82357.1. L13469 mRNA. Translation: AAA35048.1. BK006945 Genomic DNA. Translation: DAA09700.1.
PIR	S55955.
RefSeq	NP_013503.1. NM_001182287.1.
3D structure databases
ProteinModelPortal	P35817.
SMR	P35817. Positions 135-419, 517-592.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1624N.
IntAct	P35817. 29 interactions.
MINT	MINT-407031.
STRING	4932.YLR399C.
Proteomic databases
PaxDb	P35817.
PeptideAtlas	P35817.
PRIDE	P35817.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR399C; YLR399C; YLR399C.
GeneID	851115.
KEGG	sce:YLR399C.
Organism-specific databases
CYGD	YLR399c.
SGD	S000004391. BDF1.
Phylogenomic databases
eggNOG	COG5076.
GeneTree	ENSGT00700000104285.
HOGENOM	HOG000248774.
KO	K11684.
OMA	QETEIEL.
OrthoDB	EOG44TSHM.
Gene expression databases
Genevestigator	P35817.
GermOnline	YLR399C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.20.920.10. 2 hits.
InterPro	IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR027353. NET_dom. [Graphical view]
Pfam	PF00439. Bromodomain. 2 hits. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 2 hits. [Graphical view]
SUPFAM	SSF47370. Bromodomain. 2 hits.
PROSITE	PS00633. BROMODOMAIN_1. 2 hits. PS50014. BROMODOMAIN_2. 2 hits. PS51525. NET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967833.

Entry information

Entry name

BDF1_YEAST

Accession

Primary (citable) accession number: P35817
Secondary accession number(s): D6VZ34, Q06048

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	July 15, 1999
Last modified:	May 1, 2013
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program