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P38129 (TAF5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Transcription initiation factor TFIID subunit 5
Alternative name(s):
TAFII-90
TBP-associated factor 5
TBP-associated factor 90 kDa
Gene names
Name:TAF5
Synonyms:TAF90
Ordered Locus Names:YBR198C
ORF Names:YBR1410
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length798 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a component of the DNA-binding general transcription factor complex TFIID and the 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.14 Ref.15

Subunit structure

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. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.17

Subcellular location

Nucleus Probable.

Miscellaneous

Present with 14834 (+/-203) molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the WD repeat TAF5 family.

Contains 1 LisH domain.

Contains 6 WD repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainCoiled coil
Repeat
WD repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA polymerase II transcriptional preinitiation complex assembly

Inferred by curator Ref.9. Source: SGD

chromatin modification

Inferred from direct assay Ref.7. Source: SGD

histone acetylation

Inferred from direct assay Ref.7. Source: SGD

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.14PubMed 15448131. Source: SGD

   Cellular_componentSAGA complex

Inferred from direct assay Ref.7. Source: SGD

SLIK (SAGA-like) complex

Inferred from direct assay Ref.11. Source: SGD

transcription factor TFIID complex

Inferred from direct assay Ref.9PubMed 15448131. Source: SGD

   Molecular_functionchromatin binding

Inferred from direct assay PubMed 12600943. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 11805826Ref.14PubMed 21734642. Source: IntAct

protein binding

Inferred from physical interaction Ref.9PubMed 11805826PubMed 12582245PubMed 16429126PubMed 16888622PubMed 18719252PubMed 21734642PubMed 8083216. Source: IntAct

protein complex scaffold

Inferred from mutant phenotype PubMed 11585915. Source: SGD

ubiquitin binding

Inferred from direct assay PubMed 21070969. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 798798Transcription initiation factor TFIID subunit 5
PRO_0000051260

Regions

Domain56 – 8833LisH
Repeat464 – 50340WD 1
Repeat523 – 56240WD 2
Repeat565 – 60440WD 3
Repeat607 – 64640WD 4
Repeat649 – 68840WD 5
Repeat692 – 73140WD 6
Coiled coil329 – 34921 Potential
Compositional bias3 – 4846Gln-rich

Amino acid modifications

Modified residue2991Phosphoserine Ref.18
Modified residue4111Phosphoserine Ref.18
Modified residue4151Phosphoserine Ref.19
Modified residue7871Phosphoserine Ref.18

Secondary structure

........................ 798
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38129 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: B42315B8C752D0B6

FASTA79888,968
        10         20         30         40         50         60 
MSQKQSTNQN QNGTHQPQPV KNQRTNNAAG ANSGQQPQQQ SQGQSQQQGR SNGPFSASDL 

        70         80         90        100        110        120 
NRIVLEYLNK KGYHRTEAML RAESGRTLTP QNKQSPANTK TGKFPEQSSI PPNPGKTAKP 

       130        140        150        160        170        180 
ISNPTNLSSK RDAEGGIVSS GRLEGLNAPE NYIRAYSMLK NWVDSSLEIY KPELSYIMYP 

       190        200        210        220        230        240 
IFIYLFLNLV AKNPVYARRF FDRFSPDFKD FHGSEINRLF SVNSIDHIKE NEVASAFQSH 

       250        260        270        280        290        300 
KYRITMSKTT LNLLLYFLNE NESIGGSLII SVINQHLDPN IVESVTAREK LADGIKVLSD 

       310        320        330        340        350        360 
SENGNGKQNL EMNSVPVKLG PFPKDEEFVK EIETELKIKD DQEKQLNQQT AGDNYSGANN 

       370        380        390        400        410        420 
RTLLQEYKAM NNEKFKDNTG DDDKDKIKDK IAKDEEKKES ELKVDGEKKD SNLSSPARDI 

       430        440        450        460        470        480 
LPLPPKTALD LKLEIQKVKE SRDAIKLDNL QLALPSVCMY TFQNTNKDMS CLDFSDDCRI 

       490        500        510        520        530        540 
AAAGFQDSYI KIWSLDGSSL NNPNIALNNN DKDEDPTCKT LVGHSGTVYS TSFSPDNKYL 

       550        560        570        580        590        600 
LSGSEDKTVR LWSMDTHTAL VSYKGHNHPV WDVSFSPLGH YFATASHDQT ARLWSCDHIY 

       610        620        630        640        650        660 
PLRIFAGHLN DVDCVSFHPN GCYVFTGSSD KTCRMWDVST GDSVRLFLGH TAPVISIAVC 

       670        680        690        700        710        720 
PDGRWLSTGS EDGIINVWDI GTGKRLKQMR GHGKNAIYSL SYSKEGNVLI SGGADHTVRV 

       730        740        750        760        770        780 
WDLKKATTEP SAEPDEPFIG YLGDVTASIN QDIKEYGRRR TVIPTSDLVA SFYTKKTPVF 

       790 
KVKFSRSNLA LAGGAFRP 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II including BEM1, a new gene of the WD-40 repeat family and a new member of the KRE2/MNT1 family."
Mallet L., Bussereau F., Jacquet M.
Yeast 10:819-831(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"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.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Yeast TAFIIS in a multisubunit complex required for activated transcription."
Reese J.C., Apone L., Walker S.S., Griffin L.A., Green M.R.
Nature 371:523-527(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 726-747, CHARACTERIZATION.
Strain: Y57.
[6]"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: PROTEIN SEQUENCE OF 22-63 AND 726-752, CHARACTERIZATION.
Strain: ATCC 76621 / YPH252.
[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 IN 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 TFIID COMPLEX.
[10]"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 IN SAGA COMPLEX.
[11]"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.
[12]"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.
[13]"Mapping histone fold TAFs within yeast TFIID."
Leurent C., Sanders S.L., Ruhlmann C., Mallouh V., Weil P.A., Kirschner D.B., Tora L., Schultz P.
EMBO J. 21:3424-3433(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE, ELECTRON MICROSCOPY OF TFIID.
[14]"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.
[15]"Multi-protein complexes in eukaryotic gene transcription."
Martinez E.
Plant Mol. Biol. 50:925-947(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"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].
[17]"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.
[18]"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-299; SER-411 AND SER-787, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21487 Genomic DNA. Translation: CAA79685.1.
Z36067 Genomic DNA. Translation: CAA85160.1.
AY692890 Genomic DNA. Translation: AAT92909.1.
BK006936 Genomic DNA. Translation: DAA07314.1.
PIRS34023.
RefSeqNP_009757.1. NM_001178546.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J49X-ray2.30A147-290[»]
ProteinModelPortalP38129.
SMRP38129. Positions 149-282, 422-794.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32895. 304 interactions.
DIPDIP-740N.
IntActP38129. 197 interactions.
MINTMINT-475651.
STRING4932.YBR198C.

Proteomic databases

MaxQBP38129.
PaxDbP38129.
PeptideAtlasP38129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR198C; YBR198C; YBR198C.
GeneID852497.
KEGGsce:YBR198C.

Organism-specific databases

CYGDYBR198c.
SGDS000000402. TAF5.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00740000114860.
HOGENOMHOG000212424.
KOK03130.
OMARFRIEGR.
OrthoDBEOG7KQ29H.

Enzyme and pathway databases

BioCycYEAST:G3O-29139-MONOMER.

Gene expression databases

GenevestigatorP38129.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR007582. TFIID-su_WD40-assoc_reg.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF08513. LisH. 1 hit.
PF04494. TFIID_90kDa. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00667. LisH. 1 hit.
SM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 2 hits.
PROSITEPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38129.
NextBio971495.
PROP38129.

Entry information

Entry nameTAF5_YEAST
AccessionPrimary (citable) accession number: P38129
Secondary accession number(s): D6VQJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references