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P32776

- TFB1_YEAST

UniProt

P32776 - TFB1_YEAST

Protein

RNA polymerase II transcription factor B subunit 1

Gene

TFB1

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 133 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Acts as component of the general transcription and DNA repair factor IIH (TFIIH) core, which is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase activity, and is essential for polymerase II transcription in vitro.2 Publications

    GO - Molecular functioni

    1. phosphatidylinositol-3-phosphate binding Source: SGD
    2. phosphatidylinositol-5-phosphate binding Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. nucleotide-excision repair Source: SGD
    2. phosphorylation of RNA polymerase II C-terminal domain Source: SGD
    3. transcription from RNA polymerase II promoter Source: SGD
    4. transcription from RNA polymerase I promoter Source: SGD

    Keywords - Biological processi

    DNA damage, DNA repair, Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29870-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA polymerase II transcription factor B subunit 1
    Alternative name(s):
    General transcription and DNA repair factor IIH subunit TFB1
    Short name:
    TFIIH subunit TFB1
    RNA polymerase II transcription factor B 73 kDa subunit
    RNA polymerase II transcription factor B p73 subunit
    Gene namesi
    Name:TFB1
    Ordered Locus Names:YDR311W
    ORF Names:D9740.3
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR311w.
    SGDiS000002719. TFB1.

    Subcellular locationi

    GO - Cellular componenti

    1. core TFIIH complex Source: SGD
    2. cytosol Source: SGD
    3. holo TFIIH complex Source: SGD
    4. nucleotide-excision repair factor 3 complex Source: SGD
    5. nucleus Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 642642RNA polymerase II transcription factor B subunit 1PRO_0000119261Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei150 – 1501Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32776.
    PaxDbiP32776.
    PeptideAtlasiP32776.

    Expressioni

    Gene expression databases

    GenevestigatoriP32776.

    Interactioni

    Subunit structurei

    Component of the TFIIH core complex, which is composed of RAD3, SSL1, SSL2, TFB1, TFB2, TFB4 and TFB5.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TFA1P361003EBI-19146,EBI-18903

    Protein-protein interaction databases

    BioGridi32364. 73 interactions.
    DIPiDIP-1702N.
    IntActiP32776. 21 interactions.
    MINTiMINT-387816.
    STRINGi4932.YDR311W.

    Structurei

    Secondary structure

    1
    642
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Beta strandi13 – 197
    Beta strandi21 – 244
    Beta strandi26 – 3510
    Beta strandi37 – 426
    Beta strandi48 – 503
    Beta strandi53 – 553
    Beta strandi56 – 649
    Beta strandi69 – 713
    Beta strandi75 – 773
    Beta strandi85 – 928
    Helixi94 – 11421

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y5ONMR-A1-115[»]
    2GS0NMR-A1-115[»]
    2K2UNMR-A1-115[»]
    2L2INMR-A2-115[»]
    2LOXNMR-A2-115[»]
    2M14NMR-A2-115[»]
    2MKRNMR-A1-115[»]
    ProteinModelPortaliP32776.
    SMRiP32776. Positions 2-115.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32776.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini165 – 22157BSD 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini243 – 29553BSD 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 BSD domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG315835.
    GeneTreeiENSGT00390000015066.
    HOGENOMiHOG000248691.
    KOiK03141.
    OMAiEFWARFF.
    OrthoDBiEOG7QRR3J.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR005607. BSD.
    IPR011993. PH_like_dom.
    IPR027079. Tfb1/p62.
    IPR013876. TFIIH_BTF_p62_N.
    [Graphical view]
    PANTHERiPTHR12856. PTHR12856. 1 hit.
    PfamiPF03909. BSD. 2 hits.
    PF08567. TFIIH_BTF_p62_N. 1 hit.
    [Graphical view]
    SMARTiSM00751. BSD. 2 hits.
    [Graphical view]
    PROSITEiPS50858. BSD. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32776-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHSGAAIFE KVSGIIAINE DVSPAELTWR STDGDKVHTV VLSTIDKLQA    50
    TPASSEKMML RLIGKVDESK KRKDNEGNEV VPKPQRHMFS FNNRTVMDNI 100
    KMTLQQIISR YKDADIYEEK RRREESAQHT ETPMSSSSVT AGTPTPHLDT 150
    PQLNNGAPLI NTAKLDDSLS KEKLLTNLKL QQSLLKGNKV LMKVFQETVI 200
    NAGLPPSEFW STRIPLLRAF ALSTSQKVGP YNVLSTIKPV ASSENKVNVN 250
    LSREKILNIF ENYPIVKKAY TDNVPKNFKE PEFWARFFSS KLFRKLRGEK 300
    IMQNDRGDVI IDRYLTLDQE FDRKDDDMLL HPVKKIIDLD GNIQDDPVVR 350
    GNRPDFTMQP GVDINGNSDG TVDILKGMNR LSEKMIMALK NEYSRTNLQN 400
    KSNITNDEED EDNDERNELK IDDLNESYKT NYAIIHLKRN AHEKTTDNDA 450
    KSSADSIKNA DLKVSNQQML QQLSLVMDNL INKLDLNQVV PNNEVSNKIN 500
    KRVITAIKIN AKQAKHNNVN SALGSFVDNT SQANELEVKS TLPIDLLESC 550
    RMLHTTCCEF LKHFYIHFQS GEQKQASTVK KLYNHLKDCI EKLNELFQDV 600
    LNGDGESMSN TCTAYLKPVL NSITLATHKY DEYFNEYNNN SN 642
    Length:642
    Mass (Da):72,894
    Last modified:October 1, 1993 - v1
    Checksum:iDAE369FE90A224F8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti209 – 2091F → L in AAU09707. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95750 Genomic DNA. Translation: AAA35143.1.
    U28374 Genomic DNA. Translation: AAB64747.1.
    AY723790 Genomic DNA. Translation: AAU09707.1.
    BK006938 Genomic DNA. Translation: DAA12150.1.
    PIRiS31285.
    RefSeqiNP_010597.3. NM_001180619.3.

    Genome annotation databases

    EnsemblFungiiYDR311W; YDR311W; YDR311W.
    GeneIDi851906.
    KEGGisce:YDR311W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95750 Genomic DNA. Translation: AAA35143.1 .
    U28374 Genomic DNA. Translation: AAB64747.1 .
    AY723790 Genomic DNA. Translation: AAU09707.1 .
    BK006938 Genomic DNA. Translation: DAA12150.1 .
    PIRi S31285.
    RefSeqi NP_010597.3. NM_001180619.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y5O NMR - A 1-115 [» ]
    2GS0 NMR - A 1-115 [» ]
    2K2U NMR - A 1-115 [» ]
    2L2I NMR - A 2-115 [» ]
    2LOX NMR - A 2-115 [» ]
    2M14 NMR - A 2-115 [» ]
    2MKR NMR - A 1-115 [» ]
    ProteinModelPortali P32776.
    SMRi P32776. Positions 2-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32364. 73 interactions.
    DIPi DIP-1702N.
    IntActi P32776. 21 interactions.
    MINTi MINT-387816.
    STRINGi 4932.YDR311W.

    Proteomic databases

    MaxQBi P32776.
    PaxDbi P32776.
    PeptideAtlasi P32776.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR311W ; YDR311W ; YDR311W .
    GeneIDi 851906.
    KEGGi sce:YDR311W.

    Organism-specific databases

    CYGDi YDR311w.
    SGDi S000002719. TFB1.

    Phylogenomic databases

    eggNOGi NOG315835.
    GeneTreei ENSGT00390000015066.
    HOGENOMi HOG000248691.
    KOi K03141.
    OMAi EFWARFF.
    OrthoDBi EOG7QRR3J.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29870-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32776.
    NextBioi 969921.
    PROi P32776.

    Gene expression databases

    Genevestigatori P32776.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR005607. BSD.
    IPR011993. PH_like_dom.
    IPR027079. Tfb1/p62.
    IPR013876. TFIIH_BTF_p62_N.
    [Graphical view ]
    PANTHERi PTHR12856. PTHR12856. 1 hit.
    Pfami PF03909. BSD. 2 hits.
    PF08567. TFIIH_BTF_p62_N. 1 hit.
    [Graphical view ]
    SMARTi SM00751. BSD. 2 hits.
    [Graphical view ]
    PROSITEi PS50858. BSD. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a subunit of yeast RNA polymerase II transcription factor b and CTD kinase."
      Gileadi O., Feaver W.J., Kornberg R.D.
      Science 257:1389-1392(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 314-322 AND 630-639.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "RNA polymerase transcription factor IIH holoenzyme from yeast."
      Svejstrup J.Q., Feaver W.J., LaPointe J., Kornberg R.D.
      J. Biol. Chem. 269:28044-28048(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF TFIIH IN RNA POLYMERASE II TRANSCRIPTION, IDENTIFICATION IN THE TFIIH COMPLEX.
    6. "Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3 and Rad25, in the incision step of nucleotide excision repair."
      Sung P., Guzder S.N., Prakash L., Prakash S.
      J. Biol. Chem. 271:10821-10826(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE TFIIH CORE COMPLEX IN DNA REPAIR.
    7. "Revised subunit structure of yeast transcription factor IIH (TFIIH) and reconciliation with human TFIIH."
      Takagi Y., Komori H., Chang W.-H., Hudmon A., Erdjument-Bromage H., Tempst P., Kornberg R.D.
      J. Biol. Chem. 278:43897-43900(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TFIIH CORE COMPLEX.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "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 THR-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTFB1_YEAST
    AccessioniPrimary (citable) accession number: P32776
    Secondary accession number(s): D6VSU0, E9P948
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 5150 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3