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Protein

Transcription initiation factor TFIID subunit 6

Gene

TAF6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a component of the DNA-binding general transcription factor complex TFIID and the regulatory transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.10 Publications

GO - Molecular functioni

  • chromatin binding Source: SGD
  • identical protein binding Source: IntAct
  • protein complex scaffold Source: SGD
  • RNA polymerase II activating transcription factor binding Source: SGD

GO - Biological processi

  • chromatin modification Source: SGD
  • histone acetylation Source: SGD
  • regulation of sequence-specific DNA binding transcription factor activity Source: InterPro
  • RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  • transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-30610-MONOMER.
ReactomeiR-SCE-674695. RNA Polymerase II Pre-transcription Events.
R-SCE-73776. RNA Polymerase II Promoter Escape.
R-SCE-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-SCE-75953. RNA Polymerase II Transcription Initiation.
R-SCE-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor TFIID subunit 6
Alternative name(s):
TBP-associated factor 6
TBP-associated factor 60 kDa
Short name:
TAFII-60
Short name:
TAFII60
Gene namesi
Name:TAF6
Synonyms:TAF60
Ordered Locus Names:YGL112C
ORF Names:G2985
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL112C.
SGDiS000003080. TAF6.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
  • SAGA complex Source: SGD
  • SLIK (SAGA-like) complex Source: SGD
  • transcription factor TFIID complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 516516Transcription initiation factor TFIID subunit 6PRO_0000118878Add
BLAST

Proteomic databases

MaxQBiP53040.

Interactioni

Subunit structurei

In TFIID, TAF6 heterodimerizes with TAF9, forming ultimately an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4 octamer. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-18876,EBI-18876
BDF1P358172EBI-18876,EBI-3493
HFI1Q120609EBI-18876,EBI-8287
TAF1P466778EBI-18876,EBI-18855
TAF10Q1203010EBI-18876,EBI-18889
TAF5P3812913EBI-18876,EBI-18868
TAF9Q0502710EBI-18876,EBI-27500

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein complex scaffold Source: SGD
  • RNA polymerase II activating transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi33139. 201 interactions.
DIPiDIP-981N.
IntActiP53040. 123 interactions.
MINTiMINT-405577.

Structurei

3D structure databases

ProteinModelPortaliP53040.
SMRiP53040. Positions 15-74, 217-400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 7570Histone-foldAdd
BLAST

Sequence similaritiesi

Belongs to the TAF6 family.Curated
Contains 1 histone-fold domain.Curated

Phylogenomic databases

GeneTreeiENSGT00640000091486.
HOGENOMiHOG000159894.
InParanoidiP53040.
KOiK03131.
OMAiFLDPYAS.
OrthoDBiEOG7SBP03.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR009072. Histone-fold.
IPR011442. TAF6_C.
IPR004823. TAF_TATA-bd.
[Graphical view]
PfamiPF02969. TAF. 1 hit.
PF07571. TAF6_C. 1 hit.
[Graphical view]
SMARTiSM00803. TAF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
SSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

P53040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTQQQSYTI WSPQDTVKDV AESLGLENIN DDVLKALAMD VEYRILEIIE
60 70 80 90 100
QAVKFKRHSK RDVLTTDDVS KALRVLNVEP LYGYYDGSEV NKAVSFSKVN
110 120 130 140 150
TSGGQSVYYL DEEEVDFDRL INEPLPQVPR LPTFTTHWLA VEGVQPAIIQ
160 170 180 190 200
NPNLNDIRVS QPPFIRGAIV TALNDNSLQT PVTSTTASAS VTDTGASQHL
210 220 230 240 250
SNVKPGQNTE VKPLVKHVLS KELQIYFNKV ISTLTAKSQA DEAAQHMKQA
260 270 280 290 300
ALTSLRTDSG LHQLVPYFIQ FIAEQITQNL SDLQLLTTIL EMIYSLLSNT
310 320 330 340 350
SIFLDPYIHS LMPSILTLLL AKKLGGSPKD DSPQEIHEFL ERTNALRDFA
360 370 380 390 400
ASLLDYVLKK FPQAYKSLKP RVTRTLLKTF LDINRVFGTY YGCLKGVSVL
410 420 430 440 450
EGESIRFFLG NLNNWARLVF NESGITLDNI EEHLNDDSNP TRTKFTKEET
460 470 480 490 500
QILVDTVISA LLVLKKDLPD LYEGKGEKVT DEDKEKLLER CGVTIGFHIL
510
KRDDAKELIS AIFFGE
Length:516
Mass (Da):57,902
Last modified:October 1, 1996 - v1
Checksum:i14B590E02C16F289
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97644 Genomic DNA. Translation: CAA66240.1.
L40145 Genomic DNA. Translation: AAA83389.1.
Z72634 Genomic DNA. Translation: CAA96819.1.
AY723809 Genomic DNA. Translation: AAU09726.1.
BK006941 Genomic DNA. Translation: DAA07996.1.
PIRiS64120.
RefSeqiNP_011403.1. NM_001180977.1.

Genome annotation databases

EnsemblFungiiYGL112C; YGL112C; YGL112C.
GeneIDi852766.
KEGGisce:YGL112C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97644 Genomic DNA. Translation: CAA66240.1.
L40145 Genomic DNA. Translation: AAA83389.1.
Z72634 Genomic DNA. Translation: CAA96819.1.
AY723809 Genomic DNA. Translation: AAU09726.1.
BK006941 Genomic DNA. Translation: DAA07996.1.
PIRiS64120.
RefSeqiNP_011403.1. NM_001180977.1.

3D structure databases

ProteinModelPortaliP53040.
SMRiP53040. Positions 15-74, 217-400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33139. 201 interactions.
DIPiDIP-981N.
IntActiP53040. 123 interactions.
MINTiMINT-405577.

Proteomic databases

MaxQBiP53040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL112C; YGL112C; YGL112C.
GeneIDi852766.
KEGGisce:YGL112C.

Organism-specific databases

EuPathDBiFungiDB:YGL112C.
SGDiS000003080. TAF6.

Phylogenomic databases

GeneTreeiENSGT00640000091486.
HOGENOMiHOG000159894.
InParanoidiP53040.
KOiK03131.
OMAiFLDPYAS.
OrthoDBiEOG7SBP03.

Enzyme and pathway databases

BioCyciYEAST:G3O-30610-MONOMER.
ReactomeiR-SCE-674695. RNA Polymerase II Pre-transcription Events.
R-SCE-73776. RNA Polymerase II Promoter Escape.
R-SCE-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-SCE-75953. RNA Polymerase II Transcription Initiation.
R-SCE-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Miscellaneous databases

PROiP53040.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR009072. Histone-fold.
IPR011442. TAF6_C.
IPR004823. TAF_TATA-bd.
[Graphical view]
PfamiPF02969. TAF. 1 hit.
PF07571. TAF6_C. 1 hit.
[Graphical view]
SMARTiSM00803. TAF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
SSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a TFIID-like multiprotein complex from Saccharomyces cerevisiae."
    Poon D., Bai Y., Campbell A.M., Bjorklund S., Kim Y.-J., Zhou S., Kornberg R.D., Weil P.A.
    Proc. Natl. Acad. Sci. U.S.A. 92:8224-8228(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 72-92; 99-132 AND 222-229.
    Strain: ATCC 76621 / YPH252.
  2. "The genes encoding the transcription factor yTAFII60, the G4p1 protein and a putative glucose transporter are contained in a 12.3 kb DNA fragment on the left arm of Saccharomyces cerevisiae chromosome VII."
    Paoluzi S., Minenkova O., Castagnoli L.
    Yeast 13:85-91(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family."
    Birck C., Poch O., Romier C., Ruff M., Mengus G., Lavigne A.C., Davidson I., Moras D.
    Cell 94:239-249(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TAF-TAF INTERACTION THROUGH HISTONE-FOLD DOMAIN.
  7. "A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation."
    Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C., Yates J.R. III, Workman J.L.
    Cell 94:45-53(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Expanded lysine acetylation specificity of Gcn5 in native complexes."
    Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.
    J. Biol. Chem. 274:5895-5900(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
  9. "Identification of two novel TAF subunits of the yeast Saccharomyces cerevisiae TFIID complex."
    Sanders S.L., Weil P.A.
    J. Biol. Chem. 275:13895-13900(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE TFIID COMPLEX.
  10. "Histone folds mediate selective heterodimerization of yeast TAF(II)25 with TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7."
    Gangloff Y.G., Sanders S.L., Romier C., Kirschner D.B., Weil P.A., Tora L., Davidson I.
    Mol. Cell. Biol. 21:1841-1853(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION IN TFIID AND SAGA.
  11. "The histone fold is a key structural motif of transcription factor TFIID."
    Gangloff Y.G., Romier C., Thuault S., Werten S., Davidson I.
    Trends Biochem. Sci. 26:250-257(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HISTONE-FOLD DOMAIN CHARACTERIZATION.
  12. "A histone fold TAF octamer within the yeast TFIID transcriptional coactivator."
    Selleck W., Howley R., Fang Q., Podolny V., Fried M.G., Buratowski S., Tan S.
    Nat. Struct. Biol. 8:695-700(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TAF OCTAMER FORMATION.
  13. "Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry."
    Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A.
    Mol. Cell. Biol. 22:4723-4738(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX.
  14. "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription."
    Sterner D.E., Belotserkovskaya R., Berger S.L.
    Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SALSA COMPLEX.
  15. "Molecular characterization of Saccharomyces cerevisiae TFIID."
    Sanders S.L., Garbett K.A., Weil P.A.
    Mol. Cell. Biol. 22:6000-6013(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TFIID STOICHIOMETRY.
  16. "The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway."
    Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L., Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.
    Mol. Cell. Biol. 22:8774-8786(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
  17. "Multi-protein complexes in eukaryotic gene transcription."
    Martinez E.
    Plant Mol. Biol. 50:925-947(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  19. "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation."
    Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.
    Nature 433:434-438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
  20. Cited for: 3D-STRUCTURE, ELECTRON MICROSCOPY OF TFIID.
  21. "Molecular architecture of the S. cerevisiae SAGA complex."
    Wu P.Y., Ruhlmann C., Winston F., Schultz P.
    Mol. Cell 15:199-208(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.

Entry informationi

Entry nameiTAF6_YEAST
AccessioniPrimary (citable) accession number: P53040
Secondary accession number(s): D6VU35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 147 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 6506 (+/-1290) molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.