Reviewed, UniProtKB/Swiss-Prot Q03750 (TAF8_YEAST)

Names and origin

Protein names

Recommended name:
    Transcription initiation factor TFIID subunit 8
Alternative name(s):
    TBP-associated factor 8
    TBP-associated factor 65 kDa
    TAFII-65

Gene names

Name:	TAF8
Synonyms:	TAF65
Ordered Locus Names:	YML114C
ORF Names:	YM8339.05C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation 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. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7
Subunit structure	In TFIID, TAF8 heterodimerizes with TAF10. 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. Ref.3
Subcellular location	Nucleus.
Miscellaneous	Present with 4684 (+/-522) molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the TAF8 family. Contains 1 histone-fold domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	RNA polymerase II transcriptional preinitiation complex assembly Ref.3 Inferred by curator. Source: SGD general transcription from RNA polymerase II promoter Ref.6 Inferred from direct assay. Source: SGD regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	transcription factor TFIID complex Ref.3 Inferred from direct assay. Source: SGD
Molecular function	general RNA polymerase II transcription factor activity Ref.6 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TAF10	Q12030	2	EBI-27947,EBI-18889

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 510	510	Transcription initiation factor TFIID subunit 8		PRO_0000118887
Regions
	Domain	37 – 103	67	Histone-fold
	Coiled coil	142 – 165	24	Potential
	Coiled coil	346 – 383	38	Potential
Amino acid modifications
	Modified residue	269	1	Phosphoserine Ref.11
	Modified residue	317	1	Phosphoserine Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Q03750-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: A6393C86D0E890CE	FASTA	510	57,986
	10 20 30 40 50 60 MTSKTSESGT GTQSTIVQLR NLPDLTEISH LEIDAPVVEI LKKTVLFQLN SLNICISNFA 70 80 90 100 110 120 LDELVNLVTV QMDGMFRNLH NLTLLQRRSQ ASQADLKLLL REFNLDAPSL YQQFQASEFI 130 140 150 160 170 180 KSKHSTEYEK LMSWSSLAAL PHNEEDEEDE LNNIEEQQNE INVLLPPSNP LEKQIPSWLP 190 200 210 220 230 240 NFPPDHTYKF TPEFNHPITD LKTIKKEIVK ESQESEKALL NLNKSLSHIS SASNTPQPPG 250 260 270 280 290 300 LDDEDAIEQQ LEIWGNALEE RKPTITEKSF NENNIEQYAK YRVELARERV TKFEVNQLKR 310 320 330 340 350 360 TKNPFLKISE TLYLPESPHQ SHKTIQKTIE LQFRKSMTLF MHNLPKVQKL KKEKIRMAKE 370 380 390 400 410 420 ERAKSLKRRQ EELISQRTKR EQDEGHDLEL LLNNEHARDA ADDTTTPNAL NNSTIVINTN 430 440 450 460 470 480 AEDEDDDINL FGILGSSEDE NEMSSMPAEN LVAESEPPTM TAQDTTNTTP VAHNTTNIDA 490 500 510 TTSHSPHSTP NENAPTSPPA DIATDHDITM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"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: 9695952] [Abstract] Cited for: FUNCTION, TAF-TAF INTERACTION THROUGH HISTONE-FOLD DOMAIN.
[3]	"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: 10788514] [Abstract] Cited for: FUNCTION, SUBUNIT.
[4]	"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: 11238921] [Abstract] Cited for: FUNCTION, INTERACTION IN TFIID AND SAGA.
[5]	"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: 11295558] [Abstract] Cited for: FUNCTION, HISTONE-FOLD DOMAIN CHARACTERIZATION.
[6]	"Molecular characterization of Saccharomyces cerevisiae TFIID." Sanders S.L., Garbett K.A., Weil P.A. Mol. Cell. Biol. 22:6000-6013(2002) [PubMed: 12138208] [Abstract] Cited for: FUNCTION, TFIID STOICHIOMETRY.
[7]	"Multi-protein complexes in eukaryotic gene transcription." Martinez E. Plant Mol. Biol. 50:925-947(2002) [PubMed: 12516863] [Abstract] Cited for: FUNCTION.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"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: 12093743] [Abstract] Cited for: 3D-STRUCTURE, ELECTRON MICROSCOPY OF TFIID.
[11]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND SER-317, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z49210 Genomic DNA. Translation: CAA89104.1.
PIR	S53958.
RefSeq	NP_013593.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1954N.
IntAct	Q03750. 21 interactions.
STRING	Q03750.
Proteomic databases
PeptideAtlas	Q03750.
Genome annotation databases
Ensembl	YML114C; YML114C; YML114C; Saccharomyces cerevisiae. [Genome view]
GeneID	854926.
KEGG	sce:YML114C.
NMPDR	fig|4932.3.peg.4629.
Organism-specific databases
CYGD	YML114c.
SGD	S000004582. TAF8.
Phylogenomic databases
OMA	DHTYKFT
OrthoDB	EOG9283JK
Gene expression databases
ArrayExpress	Q03750.
Genevestigator	Q03750.
GermOnline	YML114C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR019473. TFIID_su8_C. [Graphical view]
Pfam	PF10406. TAF8_C. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	977947.

Entry information

Entry name

TAF8_YEAST

Accession

Primary (citable) accession number: Q03750

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 24, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)