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P35817 (BDF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bromodomain-containing factor 1
Gene names
Name:BDF1
Ordered Locus Names:YLR399C
ORF Names:L8084.18
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length686 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processDNA damage
DNA repair
Sporulation
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainBromodomain
Coiled coil
Repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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_componentSwr1 complex

Inferred from direct assay PubMed 19088068. Source: SGD

nuclear chromatin

Inferred from direct assay Ref.2. Source: SGD

   Molecular_functionTFIID-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

lysine-acetylated histone binding

Inferred from direct assay Ref.10PubMed 20126658. Source: SGD

protein binding

Inferred from physical interaction Ref.7PubMed 11805826PubMed 14690608PubMed 15045029PubMed 16429126PubMed 18719252PubMed 21179020PubMed 23452060. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 686686Bromodomain-containing factor 1
PRO_0000211176

Regions

Domain165 – 23773Bromo 1
Domain332 – 40473Bromo 2
Domain518 – 59881NET
Coiled coil460 – 49940 Potential

Amino acid modifications

Modified residue2701Phosphoserine Ref.18 Ref.21
Modified residue4291Phosphoserine Ref.18 Ref.21
Modified residue6151Phosphoserine Ref.20 Ref.21
Modified residue6591Phosphoserine Ref.20

Experimental info

Mutagenesis1871Y → F: Impairs interaction with histones H3 and H4; when associated with F-354. Ref.11
Mutagenesis3541Y → F: Impairs interaction with histones H3 and H4; when associated with F-187. Ref.11
Sequence conflict81Q → LC in CAA79377. Ref.1
Sequence conflict93 – 942GA → R in AAA89115. Ref.2
Sequence conflict941A → P in CAA79377. Ref.1
Sequence conflict2821A → P in CAA79377. Ref.1
Sequence conflict3851D → E in CAA79377. Ref.1
Sequence conflict4931A → R in AAA35048. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P35817 [UniParc].

Last modified July 15, 1999. Version 3.
Checksum: 8CCD52F41F91D0DA

FASTA68676,978
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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-615 AND SER-659, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-429 AND SER-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS55955.
RefSeqNP_013503.1. NM_001182287.1.

3D structure databases

ProteinModelPortalP35817.
SMRP35817. Positions 136-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31658. 174 interactions.
DIPDIP-1624N.
IntActP35817. 30 interactions.
MINTMINT-407031.
STRING4932.YLR399C.

Proteomic databases

MaxQBP35817.
PaxDbP35817.
PeptideAtlasP35817.
PRIDEP35817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR399C; YLR399C; YLR399C.
GeneID851115.
KEGGsce:YLR399C.

Organism-specific databases

CYGDYLR399c.
SGDS000004391. BDF1.

Phylogenomic databases

eggNOGCOG5076.
GeneTreeENSGT00730000110623.
HOGENOMHOG000248774.
KOK11684.
OMAPKSKDIY.
OrthoDBEOG7Z69S1.

Enzyme and pathway databases

BioCycYEAST:G3O-32463-MONOMER.

Gene expression databases

GenevestigatorP35817.

Family and domain databases

Gene3D1.20.920.10. 2 hits.
InterProIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR027353. NET_dom.
[Graphical view]
PfamPF00439. Bromodomain. 2 hits.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMSSF47370. SSF47370. 2 hits.
PROSITEPS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
PS51525. NET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967833.
PROP35817.

Entry information

Entry nameBDF1_YEAST
AccessionPrimary (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: July 9, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families