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P35817

- BDF1_YEAST

UniProt

P35817 - BDF1_YEAST

Protein

Bromodomain-containing factor 1

Gene

BDF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    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.8 Publications

    GO - Molecular functioni

    1. chromatin binding Source: SGD
    2. core promoter binding Source: SGD
    3. lysine-acetylated histone binding Source: SGD
    4. protein binding Source: IntAct
    5. TFIID-class transcription factor binding Source: SGD

    GO - Biological processi

    1. chromatin remodeling Source: SGD
    2. DNA repair Source: SGD
    3. negative regulation of heterochromatin assembly Source: SGD
    4. positive regulation of histone exchange Source: SGD
    5. regulation of chromatin silencing at silent mating-type cassette Source: SGD
    6. regulation of chromatin silencing at telomere Source: SGD
    7. regulation of transcription by chromatin organization Source: SGD
    8. snRNA transcription Source: SGD
    9. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Biological processi

    DNA damage, DNA repair, Sporulation, Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32463-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bromodomain-containing factor 1
    Gene namesi
    Name:BDF1
    Ordered Locus Names:YLR399C
    ORF Names:L8084.18
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR399c.
    SGDiS000004391. BDF1.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nuclear chromatin Source: SGD
    2. Swr1 complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi187 – 1871Y → F: Impairs interaction with histones H3 and H4; when associated with F-354. 1 Publication
    Mutagenesisi354 – 3541Y → F: Impairs interaction with histones H3 and H4; when associated with F-187. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 686686Bromodomain-containing factor 1PRO_0000211176Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei270 – 2701Phosphoserine3 Publications
    Modified residuei429 – 4291Phosphoserine3 Publications
    Modified residuei615 – 6151Phosphoserine3 Publications
    Modified residuei659 – 6591Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by the casein kinase CK2 complex.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP35817.
    PaxDbiP35817.
    PeptideAtlasiP35817.
    PRIDEiP35817.

    Expressioni

    Gene expression databases

    GenevestigatoriP35817.

    Interactioni

    Subunit structurei

    Interacts with the TFIID subunit TAF7 and with acetylated histones H3 and H4.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BDF2Q074425EBI-3493,EBI-37620
    HHT2P618302EBI-3493,EBI-8098
    HTZ1Q126924EBI-3493,EBI-8080
    SWR1Q054713EBI-3493,EBI-22102
    TAF1P466773EBI-3493,EBI-18855
    TAF12Q037612EBI-3493,EBI-35097
    TAF6P530402EBI-3493,EBI-18876
    TAF7Q050215EBI-3493,EBI-27490
    VPS71Q034332EBI-3493,EBI-27814
    YAF9P539303EBI-3493,EBI-28841

    Protein-protein interaction databases

    BioGridi31658. 174 interactions.
    DIPiDIP-1624N.
    IntActiP35817. 30 interactions.
    MINTiMINT-407031.
    STRINGi4932.YLR399C.

    Structurei

    3D structure databases

    ProteinModelPortaliP35817.
    SMRiP35817. Positions 136-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini165 – 23773Bromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini332 – 40473Bromo 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini518 – 59881NETPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili460 – 49940Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 2 bromo domains.PROSITE-ProRule annotation
    Contains 1 NET domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Bromodomain, Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG5076.
    GeneTreeiENSGT00730000110623.
    HOGENOMiHOG000248774.
    KOiK11684.
    OMAiPKSKDIY.
    OrthoDBiEOG7Z69S1.

    Family and domain databases

    Gene3Di1.20.920.10. 2 hits.
    InterProiIPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR027353. NET_dom.
    [Graphical view]
    PfamiPF00439. Bromodomain. 2 hits.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00297. BROMO. 2 hits.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 2 hits.
    PROSITEiPS00633. BROMODOMAIN_1. 2 hits.
    PS50014. BROMODOMAIN_2. 2 hits.
    PS51525. NET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P35817-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDITPVQND VDVNGNNVND DVSSNLKRPI DQGDPSNGLA EEENPANNQL    50
    HLKKARLDGD ALTSSPAGLA ENGIEGATLA ANGENGYNAT GSGAEDEQQG 100
    LKKEEGGQGT KQEDLDENSK QELPMEVPKE PAPAPPPEPD MNNLPQNPIP 150
    KHQQKHALLA IKAVKRLKDA RPFLQPVDPV KLDIPFYFNY IKRPMDLSTI 200
    ERKLNVGAYE VPEQITEDFN LMVNNSIKFN GPNAGISQMA RNIQASFEKH 250
    MLNMPAKDAP PVIAKGRRSS AQEDAPIVIR RAQTHNGRPK RTIHPPKSKD 300
    IYPYESKKPK SKRLQQAMKF CQSVLKELMA KKHASYNYPF LEPVDPVSMN 350
    LPTYFDYVKE PMDLGTIAKK LNDWQYQTME DFERDVRLVF KNCYTFNPDG 400
    TIVNMMGHRL EEVFNSKWAD RPNLDDYDSD EDSRTQGDYD DYESEYSESD 450
    IDETIITNPA IQYLEEQLAR MKVELQQLKK QELEKIRKER RLARGSKKRG 500
    KRSKGRSGSK NASSKGRRDK KNKLKTVVTY DMKRIITERI NDLPTSKLER 550
    AIDIIKKSMP NISEDDEVEL DLDTLDNHTI LTLYNTFFRQ YESSSGASNG 600
    LDGTSGVTRD ASSLSPTSAG SRKRRSKALS QEEQSRQIEK IKNKLAILDS 650
    ASPLSQNGSP GQIQSAAHNG FSSSSDDDVS SESEEE 686
    Length:686
    Mass (Da):76,978
    Last modified:July 15, 1999 - v3
    Checksum:i8CCD52F41F91D0DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81Q → LC in CAA79377. (PubMed:7816623)Curated
    Sequence conflicti93 – 942GA → R in AAA89115. (PubMed:7791775)Curated
    Sequence conflicti94 – 941A → P in CAA79377. (PubMed:7816623)Curated
    Sequence conflicti282 – 2821A → P in CAA79377. (PubMed:7816623)Curated
    Sequence conflicti385 – 3851D → E in CAA79377. (PubMed:7816623)Curated
    Sequence conflicti493 – 4931A → R in AAA35048. (PubMed:8321235)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS55955.
    RefSeqiNP_013503.1. NM_001182287.1.

    Genome annotation databases

    EnsemblFungiiYLR399C; YLR399C; YLR399C.
    GeneIDi851115.
    KEGGisce:YLR399C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S55955.
    RefSeqi NP_013503.1. NM_001182287.1.

    3D structure databases

    ProteinModelPortali P35817.
    SMRi P35817. Positions 136-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31658. 174 interactions.
    DIPi DIP-1624N.
    IntActi P35817. 30 interactions.
    MINTi MINT-407031.
    STRINGi 4932.YLR399C.

    Proteomic databases

    MaxQBi P35817.
    PaxDbi P35817.
    PeptideAtlasi P35817.
    PRIDEi P35817.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR399C ; YLR399C ; YLR399C .
    GeneIDi 851115.
    KEGGi sce:YLR399C.

    Organism-specific databases

    CYGDi YLR399c.
    SGDi S000004391. BDF1.

    Phylogenomic databases

    eggNOGi COG5076.
    GeneTreei ENSGT00730000110623.
    HOGENOMi HOG000248774.
    KOi K11684.
    OMAi PKSKDIY.
    OrthoDBi EOG7Z69S1.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32463-MONOMER.

    Miscellaneous databases

    NextBioi 967833.
    PROi P35817.

    Gene expression databases

    Genevestigatori P35817.

    Family and domain databases

    Gene3Di 1.20.920.10. 2 hits.
    InterProi IPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR027353. NET_dom.
    [Graphical view ]
    Pfami PF00439. Bromodomain. 2 hits.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00297. BROMO. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 2 hits.
    PROSITEi PS00633. BROMODOMAIN_1. 2 hits.
    PS50014. BROMODOMAIN_2. 2 hits.
    PS51525. NET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 204508 / S288c.
    4. 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. 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    13. 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].

    Entry informationi

    Entry nameiBDF1_YEAST
    AccessioniPrimary (citable) accession number: P35817
    Secondary accession number(s): D6VZ34, Q06048
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 8100 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3