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Protein

Transcription initiation factor TFIID subunit 8

Gene

TAF8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  3. transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32696-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor TFIID subunit 8
Alternative name(s):
TAFII-65
TBP-associated factor 65 kDa
TBP-associated factor 8
Gene namesi
Name:TAF8
Synonyms:TAF65
Ordered Locus Names:YML114C
ORF Names:YM8339.05C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYML114c.
SGDiS000004582. TAF8.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. transcription factor TFIID complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510Transcription initiation factor TFIID subunit 8PRO_0000118887Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei269 – 2691Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03750.
PaxDbiQ03750.
PeptideAtlasiQ03750.

Expressioni

Gene expression databases

GenevestigatoriQ03750.

Interactioni

Subunit structurei

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 TAF14.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TAF10Q120307EBI-27947,EBI-18889

Protein-protein interaction databases

BioGridi35090. 179 interactions.
DIPiDIP-1954N.
IntActiQ03750. 21 interactions.
MINTiMINT-405858.
STRINGi4932.YML114C.

Structurei

3D structure databases

ProteinModelPortaliQ03750.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 10367Histone-foldAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili142 – 16524Sequence AnalysisAdd
BLAST
Coiled coili346 – 38338Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the TAF8 family.Curated
Contains 1 histone-fold domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG267301.
InParanoidiQ03750.
KOiK14649.
OMAiDHTYKFT.
OrthoDBiEOG7KH9TV.

Family and domain databases

InterProiIPR019473. TFIID_su8_C.
[Graphical view]
PfamiPF10406. TAF8_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03750-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSKTSESGT GTQSTIVQLR NLPDLTEISH LEIDAPVVEI LKKTVLFQLN
60 70 80 90 100
SLNICISNFA LDELVNLVTV QMDGMFRNLH NLTLLQRRSQ ASQADLKLLL
110 120 130 140 150
REFNLDAPSL YQQFQASEFI KSKHSTEYEK LMSWSSLAAL PHNEEDEEDE
160 170 180 190 200
LNNIEEQQNE INVLLPPSNP LEKQIPSWLP NFPPDHTYKF TPEFNHPITD
210 220 230 240 250
LKTIKKEIVK ESQESEKALL NLNKSLSHIS SASNTPQPPG LDDEDAIEQQ
260 270 280 290 300
LEIWGNALEE RKPTITEKSF NENNIEQYAK YRVELARERV TKFEVNQLKR
310 320 330 340 350
TKNPFLKISE TLYLPESPHQ SHKTIQKTIE LQFRKSMTLF MHNLPKVQKL
360 370 380 390 400
KKEKIRMAKE ERAKSLKRRQ EELISQRTKR EQDEGHDLEL LLNNEHARDA
410 420 430 440 450
ADDTTTPNAL NNSTIVINTN AEDEDDDINL FGILGSSEDE NEMSSMPAEN
460 470 480 490 500
LVAESEPPTM TAQDTTNTTP VAHNTTNIDA TTSHSPHSTP NENAPTSPPA
510
DIATDHDITM
Length:510
Mass (Da):57,986
Last modified:November 1, 1997 - v1
Checksum:iA6393C86D0E890CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49210 Genomic DNA. Translation: CAA89104.1.
BK006946 Genomic DNA. Translation: DAA09784.1.
PIRiS53958.
RefSeqiNP_013593.1. NM_001182476.1.

Genome annotation databases

EnsemblFungiiYML114C; YML114C; YML114C.
GeneIDi854926.
KEGGisce:YML114C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49210 Genomic DNA. Translation: CAA89104.1.
BK006946 Genomic DNA. Translation: DAA09784.1.
PIRiS53958.
RefSeqiNP_013593.1. NM_001182476.1.

3D structure databases

ProteinModelPortaliQ03750.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35090. 179 interactions.
DIPiDIP-1954N.
IntActiQ03750. 21 interactions.
MINTiMINT-405858.
STRINGi4932.YML114C.

Proteomic databases

MaxQBiQ03750.
PaxDbiQ03750.
PeptideAtlasiQ03750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML114C; YML114C; YML114C.
GeneIDi854926.
KEGGisce:YML114C.

Organism-specific databases

CYGDiYML114c.
SGDiS000004582. TAF8.

Phylogenomic databases

eggNOGiNOG267301.
InParanoidiQ03750.
KOiK14649.
OMAiDHTYKFT.
OrthoDBiEOG7KH9TV.

Enzyme and pathway databases

BioCyciYEAST:G3O-32696-MONOMER.

Miscellaneous databases

NextBioi977947.

Gene expression databases

GenevestigatoriQ03750.

Family and domain databases

InterProiIPR019473. TFIID_su8_C.
[Graphical view]
PfamiPF10406. TAF8_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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(1997) [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(1999) [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(2000) [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(2000) [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(2001) [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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. 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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTAF8_YEAST
AccessioniPrimary (citable) accession number: Q03750
Secondary accession number(s): D6W0H0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4684 (+/-522) molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.