Q12030 (TAF10_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription initiation factor TFIID subunit 10

Alternative name(s):
TAFII-23
Short name=TAFII23
TAFII-25
Short name=TAFII25
TBP-associated factor 10
TBP-associated factor 25 kDa
p25

Gene names

Name:	TAF10
Synonyms:	TAF23, TAF25
Ordered Locus Names:	YDR167W
ORF Names:	YD9489.02

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	206 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 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). 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.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
Subunit structure	In TFIID, TAF10 heterodimerizes with TAF3 and TAF8. 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 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.5 Ref.7 Ref.10 Ref.12 Ref.15
Subcellular location	Nucleus.
Miscellaneous	Present with 3400 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the TAF10 family. Contains 1 histone-fold domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA polymerase II transcriptional preinitiation complex assembly Inferred from mutant phenotype PubMed 12840001. Source: SGD histone acetylation Inferred from direct assay Ref.5. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SAGA complex Inferred from direct assay Ref.5. Source: SGD SLIK (SAGA-like) complex Inferred from direct assay Ref.12. Source: SGD transcription factor TFIID complex Inferred from direct assay Ref.7PubMed 15448131. Source: SGD
Molecular_function	chromatin binding Inferred from direct assay PubMed 10817999. Source: SGD protein complex scaffold Inferred from mutant phenotype PubMed 11940675. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-18889,EBI-18889
TAF11	Q04226	5	EBI-18889,EBI-18884
TAF12	Q03761	11	EBI-18889,EBI-35097
TAF13	P11747	8	EBI-18889,EBI-18897
TAF6	P53040	11	EBI-18889,EBI-18876
TAF8	Q03750	7	EBI-18889,EBI-27947

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 206	206	Transcription initiation factor TFIID subunit 10		PRO_0000118901
Regions
	Domain	47 – 194	148	Histone-fold
	Compositional bias	147 – 172	26	Gln-rich
Amino acid modifications
	Modified residue	58	1	Phosphoserine Ref.17 Ref.18
	Modified residue	146	1	Phosphoserine Ref.18

Sequences

	Sequence		Length	Mass (Da)
	Q12030 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A472CCA10DC3B495	FASTA	206	23,019
	10 20 30 40 50 60 MDFEEDYDAE FDDNQEGQLE TPFPSVAGAD DGDNDNDDSV AENMKKKQKR EAVVDDGSEN 70 80 90 100 110 120 AFGIPEFTRK DKTLEEILEM MDSTPPIIPD AVIDYYLTKN GFNVADVRVK RLLALATQKF 130 140 150 160 170 180 VSDIAKDAYE YSRIRSSVAV SNANNSQARA RQLLQGQQQP GVQQISQQQH QQNEKTTASK 190 200 VVLTVNDLSS AVAEYGLNIG RPDFYR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of TAF25, an essential yeast gene that encodes an RNA polymerase II-specific TATA-binding protein-associated factor." Klebanow E.R., Poon D., Zhou S., Weil P.A. J. Biol. Chem. 271:13706-13715(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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.
[5]	"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, MASS SPECTROMETRY.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[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 SAGA COMPLEX.
[11]	"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.
[12]	"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.
[13]	"Multi-protein complexes in eukaryotic gene transcription." Martinez E. Plant Mol. Biol. 50:925-947(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"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].
[15]	"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.
[16]	"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.
[17]	"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-58, MASS SPECTROMETRY.
[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-58 AND SER-146, MASS SPECTROMETRY.
[19]	"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	U51636 Genomic DNA. Translation: AAB07766.1. Z47813 Genomic DNA. Translation: CAA87798.1. BK006938 Genomic DNA. Translation: DAA12007.1.
PIR	S50913.
RefSeq	NP_010451.3. NM_001180474.3.
3D structure databases
ProteinModelPortal	Q12030.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-855N.
IntAct	Q12030. 44 interactions.
MINT	MINT-405873.
STRING	4932.YDR167W.
Proteomic databases
PaxDb	Q12030.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR167W; YDR167W; YDR167W.
GeneID	851745.
KEGG	sce:YDR167W.
Organism-specific databases
CYGD	YDR167w.
SGD	S000002574. TAF10.
Phylogenomic databases
eggNOG	COG5162.
GeneTree	ENSGT00390000009368.
HOGENOM	HOG000175811.
KO	K03134.
OMA	PPIIPDA.
OrthoDB	EOG4XPTR5.
Enzyme and pathway databases
BioCyc	YEAST:G3O-29756-MONOMER.
Gene expression databases
Genevestigator	Q12030.
GermOnline	YDR167W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003923. TFIID_30kDa. [Graphical view]
PANTHER	PTHR21242. PTHR21242. 1 hit.
Pfam	PF03540. TFIID_30kDa. 1 hit. [Graphical view]
PIRSF	PIRSF017246. TFIID_TAF10. 1 hit.
PRINTS	PR01443. TFIID30KDSUB.
ProtoNet	Search...
Other
NextBio	969490.

Entry information

Entry name

TAF10_YEAST

Accession

Primary (citable) accession number: Q12030
Secondary accession number(s): D6VSE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program