Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P50105 (TAF4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. 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 4
Alternative name(s):
MPT-1
TAF suppressor gene 2 protein
TAFII-48
TBP-associated factor 4
TBP-associated factor 48 kDa
Gene names
Name:TAF4
Synonyms:MPT1, TAF48, TSG2
Ordered Locus Names:YMR005W
ORF Names:YM8270.07
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length388 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.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subunit structure

TAF4 heterodimerizes with TAF12, forming ultimately an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4 octamer. 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.5 Ref.8

Subcellular location

Nucleus Ref.11.

Miscellaneous

Present with 1900 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the TAF4 family.

Contains 1 histone-fold domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Transcription initiation factor TFIID subunit 4
PRO_0000118871

Regions

Domain193 – 26169Histone-fold
Coiled coil279 – 29719 Potential

Amino acid modifications

Modified residue361Phosphoserine Ref.14 Ref.15 Ref.16
Modified residue491Phosphoserine Ref.16
Modified residue801Phosphoserine Ref.16

Sequences

Sequence LengthMass (Da)Tools
P50105 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 7DFAC01C7AF07189

FASTA38842,336
        10         20         30         40         50         60 
MANSPKKPSD GTGVSASDTP KYQHTVPETK PAFNLSPGKA SELSHSLPSP SQIKSTAHVS 

        70         80         90        100        110        120 
STHNDAAGNT DDSVLPKNVS PTTNLRVESN GDTNNMFSSP AGLALPKKDD KKKNKGTSKA 

       130        140        150        160        170        180 
DSKDGKASNS SGQNAQQQSD PNKMQDVLFS AGIDVREEEA LLNSSINASK SQVQTNNVKI 

       190        200        210        220        230        240 
PNHLPFLHPE QVSNYMRKVG KEQNFNLTPT KNPEILDMMS SACENYMRDI LTNAIVISRH 

       250        260        270        280        290        300 
RRKAVKINSG RRSEVSAALR AIALIQKKEE ERRVKKRIAL GLEKEDYENK IDSEETLHRA 

       310        320        330        340        350        360 
SNVTAGLRAG SKKQYGWLTS SVNKPTSLGA KSSGKVASDI TARGESGLKF REAREEPGIV 

       370        380 
MRDLLFALEN RRNSVQTIIS KGYAKIRD 

« Hide

References

« Hide 'large scale' references
[1]Estey L.A., Douglas M.G.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DBY939.
[2]"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.
[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]"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.
[6]"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.
[7]"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.
[8]"A histone fold TAF octamer within the yeast TFIID transcriptional coactivator."
Selleck W., Howley R., Fang Q., Podolny V., Fried M.G., Buratowski S., Tan S.
Nat. Struct. Biol. 8:695-700(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[9]"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.
[10]"Multi-protein complexes in eukaryotic gene transcription."
Martinez E.
Plant Mol. Biol. 50:925-947(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"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].
[12]"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].
[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]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[15]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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-36; SER-49 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79240 Genomic DNA. Translation: CAA55822.1.
Z48613 Genomic DNA. Translation: CAA88520.1.
BK006946 Genomic DNA. Translation: DAA09904.1.
PIRS45013.
RefSeqNP_013718.1. NM_001182501.1.

3D structure databases

ProteinModelPortalP50105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35175. 81 interactions.
DIPDIP-789N.
IntActP50105. 33 interactions.
MINTMINT-647326.
STRING4932.YMR005W.

Proteomic databases

PaxDbP50105.
PeptideAtlasP50105.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR005W; YMR005W; YMR005W.
GeneID855017.
KEGGsce:YMR005W.

Organism-specific databases

CYGDYMR005w.
SGDS000004607. TAF4.

Phylogenomic databases

eggNOGNOG303189.
HOGENOMHOG000154501.
OMAEEPGIVM.
OrthoDBEOG7DFXNV.

Enzyme and pathway databases

BioCycYEAST:G3O-32716-MONOMER.

Gene expression databases

GenevestigatorP50105.

Family and domain databases

InterProIPR007900. TAF4.
[Graphical view]
PfamPF05236. TAF4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio978198.

Entry information

Entry nameTAF4_YEAST
AccessionPrimary (citable) accession number: P50105
Secondary accession number(s): D6VZI0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 113 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