P38129 (TAF5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Coiled coil Repeat WD repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA polymerase II transcriptional preinitiation complex assembly Inferred by curator Ref.9. Source: SGD histone acetylation Inferred from direct assay Ref.7. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SAGA 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_function	chromatin binding Inferred from direct assay PubMed 12600943. Source: SGD protein complex scaffold Inferred from mutant phenotype PubMed 11585915. Source: SGD ubiquitin binding Inferred from direct assay PubMed 21070969. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		9	EBI-18868,EBI-18868
TAF2	P23255	10	EBI-18868,EBI-18862
TAF4	P50105	12	EBI-18868,EBI-11231
TAF6	P53040	14	EBI-18868,EBI-18876

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 798

798

Transcription initiation factor TFIID subunit 5

PRO_0000051260

Regions

Domain

56 – 88

33

LisH

Repeat

464 – 503

40

WD 1

Repeat

523 – 562

40

WD 2

Repeat

565 – 604

40

WD 3

Repeat

607 – 646

40

WD 4

Repeat

649 – 688

40

WD 5

Repeat

692 – 731

40

WD 6

Coiled coil

329 – 349

21

Potential

Compositional bias

3 – 48

46

Gln-rich

Amino acid modifications

Modified residue

67

1

Phosphotyrosine Ref.19

Modified residue

140

1

Phosphoserine Ref.19

Modified residue

299

1

Phosphoserine Ref.19

Modified residue

411

1

Phosphoserine Ref.18 Ref.19

Modified residue

414

1

Phosphoserine Ref.18

Modified residue

415

1

Phosphoserine Ref.18

Modified residue

787

1

Phosphoserine Ref.18 Ref.19

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

798

Helix Strand Turn

Details...

Helix

152 – 164

13

Turn

168 – 170

3

Helix

171 – 192

22

Helix

194 – 204

11

Helix

205 – 208

4

Helix

209 – 217

9

Turn

218 – 221

4

Helix

225 – 230

6

Helix

232 – 238

7

Beta strand

242 – 246

5

Helix

248 – 260

13

Helix

262 – 264

3

Helix

266 – 276

11

Beta strand

277 – 281

5

Sequences

	Sequence		Length	Mass (Da)
	P38129 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: B42315B8C752D0B6	FASTA	798	88,968
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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. , 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, 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]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-414; SER-415 AND SER-787, MASS SPECTROMETRY.
[19]	"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 TYR-67; SER-140; SER-299; SER-411 AND SER-787, MASS SPECTROMETRY.
[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.

PIR

S34023.

RefSeq

NP_009757.1. NM_001178546.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J49	X-ray	2.30	A	147-290	[»]

ProteinModelPortal

P38129.

SMR

P38129. Positions 149-282, 443-797.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-740N.

IntAct

P38129. 201 interactions.

MINT

MINT-475651.

STRING

4932.YBR198C.

Proteomic databases

PaxDb

P38129.

PeptideAtlas

P38129.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YBR198C; YBR198C; YBR198C.

GeneID

852497.

KEGG

sce:YBR198C.

Organism-specific databases

CYGD

YBR198c.

SGD

S000000402. TAF5.

Phylogenomic databases

eggNOG

COG2319.

GeneTree

ENSGT00700000104377.

HOGENOM

HOG000212424.

KO

K03130.

OMA

PNINYLA.

OrthoDB

EOG4S1XG9.

Gene expression databases

Genevestigator

P38129.

GermOnline

YBR198C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

2.130.10.10. 1 hit.

InterPro

IPR020472. 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]

Pfam

PF08513. LisH. 1 hit.
PF04494. TFIID_90kDa. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]

PRINTS

PR00320. GPROTEINBRPT.

SMART

SM00667. LisH. 1 hit.
SM00320. WD40. 6 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P38129.

NextBio

971495.

Entry information

Entry name

TAF5_YEAST

Accession

Primary (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:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program