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Q03750 (TAF8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 8
Alternative name(s):
TAFII-65
TBP-associated factor 65 kDa
TBP-associated factor 8
Gene names
Name:TAF8
Synonyms:TAF65
Ordered Locus Names:YML114C
ORF Names:YM8339.05C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length510 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. 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.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

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.4

Subcellular location

Nucleus Ref.9.

Miscellaneous

Present with 4684 (+/-522) molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the TAF8 family.

Contains 1 histone-fold domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TAF10Q120307EBI-27947,EBI-18889

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510Transcription initiation factor TFIID subunit 8
PRO_0000118887

Regions

Domain37 – 10367Histone-fold
Coiled coil142 – 16524 Potential
Coiled coil346 – 38338 Potential

Amino acid modifications

Modified residue2691Phosphoserine Ref.12

Sequences

Sequence LengthMass (Da)Tools
Q03750 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: A6393C86D0E890CE

FASTA51057,986
        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 

« Hide

References

« Hide '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. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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.
[4]"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, SUBUNIT.
[5]"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.
[6]"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.
[7]"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.
[8]"Multi-protein complexes in eukaryotic gene transcription."
Martinez E.
Plant Mol. Biol. 50:925-947(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]"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].
[11]"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.
[12]"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-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49210 Genomic DNA. Translation: CAA89104.1.
BK006946 Genomic DNA. Translation: DAA09784.1.
PIRS53958.
RefSeqNP_013593.1. NM_001182476.1.

3D structure databases

ProteinModelPortalQ03750.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35090. 179 interactions.
DIPDIP-1954N.
IntActQ03750. 21 interactions.
MINTMINT-405858.
STRING4932.YML114C.

Proteomic databases

PaxDbQ03750.
PeptideAtlasQ03750.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML114C; YML114C; YML114C.
GeneID854926.
KEGGsce:YML114C.

Organism-specific databases

CYGDYML114c.
SGDS000004582. TAF8.

Phylogenomic databases

eggNOGNOG267301.
KOK14649.
OMADHTYKFT.
OrthoDBEOG7KH9TV.

Enzyme and pathway databases

BioCycYEAST:G3O-32696-MONOMER.

Gene expression databases

GenevestigatorQ03750.

Family and domain databases

InterProIPR019473. TFIID_su8_C.
[Graphical view]
PfamPF10406. TAF8_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977947.

Entry information

Entry nameTAF8_YEAST
AccessionPrimary (citable) accession number: Q03750
Secondary accession number(s): D6W0H0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 103 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 XIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families