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P32776

- TFB1_YEAST

UniProt

P32776 - TFB1_YEAST

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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

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

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
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29870-MONOMER.
ReactomeiREACT_229646. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_233196. Formation of incision complex in GG-NER.
REACT_235070. Dual incision reaction in TC-NER.
REACT_236803. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_240372. mRNA Capping.
REACT_247354. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_249293. RNA Polymerase II Transcription Initiation.
REACT_249645. Formation of the Early Elongation Complex.
REACT_250453. Dual incision reaction in GG-NER.
REACT_250507. RNA Polymerase II Pre-transcription Events.
REACT_252915. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_257112. RNA Polymerase II Promoter Escape.

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
Complete GO annotation...

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. 74 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 – 119Combined sources
Beta strandi13 – 197Combined sources
Beta strandi21 – 244Combined sources
Beta strandi26 – 3510Combined sources
Beta strandi37 – 426Combined sources
Beta strandi48 – 503Combined sources
Beta strandi53 – 553Combined sources
Beta strandi56 – 649Combined sources
Beta strandi69 – 713Combined sources
Beta strandi75 – 773Combined sources
Beta strandi85 – 928Combined sources
Helixi94 – 11421Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP32776.
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

        10         20         30         40         50
MSHSGAAIFE KVSGIIAINE DVSPAELTWR STDGDKVHTV VLSTIDKLQA
60 70 80 90 100
TPASSEKMML RLIGKVDESK KRKDNEGNEV VPKPQRHMFS FNNRTVMDNI
110 120 130 140 150
KMTLQQIISR YKDADIYEEK RRREESAQHT ETPMSSSSVT AGTPTPHLDT
160 170 180 190 200
PQLNNGAPLI NTAKLDDSLS KEKLLTNLKL QQSLLKGNKV LMKVFQETVI
210 220 230 240 250
NAGLPPSEFW STRIPLLRAF ALSTSQKVGP YNVLSTIKPV ASSENKVNVN
260 270 280 290 300
LSREKILNIF ENYPIVKKAY TDNVPKNFKE PEFWARFFSS KLFRKLRGEK
310 320 330 340 350
IMQNDRGDVI IDRYLTLDQE FDRKDDDMLL HPVKKIIDLD GNIQDDPVVR
360 370 380 390 400
GNRPDFTMQP GVDINGNSDG TVDILKGMNR LSEKMIMALK NEYSRTNLQN
410 420 430 440 450
KSNITNDEED EDNDERNELK IDDLNESYKT NYAIIHLKRN AHEKTTDNDA
460 470 480 490 500
KSSADSIKNA DLKVSNQQML QQLSLVMDNL INKLDLNQVV PNNEVSNKIN
510 520 530 540 550
KRVITAIKIN AKQAKHNNVN SALGSFVDNT SQANELEVKS TLPIDLLESC
560 570 580 590 600
RMLHTTCCEF LKHFYIHFQS GEQKQASTVK KLYNHLKDCI EKLNELFQDV
610 620 630 640
LNGDGESMSN TCTAYLKPVL NSITLATHKY DEYFNEYNNN SN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 74 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.
InParanoidi P32776.
KOi K03141.
OMAi EFWARFF.
OrthoDBi EOG7QRR3J.

Enzyme and pathway databases

BioCyci YEAST:G3O-29870-MONOMER.
Reactomei REACT_229646. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_233196. Formation of incision complex in GG-NER.
REACT_235070. Dual incision reaction in TC-NER.
REACT_236803. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_240372. mRNA Capping.
REACT_247354. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_249293. RNA Polymerase II Transcription Initiation.
REACT_249645. Formation of the Early Elongation Complex.
REACT_250453. Dual incision reaction in GG-NER.
REACT_250507. RNA Polymerase II Pre-transcription Events.
REACT_252915. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_257112. RNA Polymerase II Promoter Escape.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 135 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