Transcription initiation factor TFIID subunit 4 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P50105 (TAF4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 105. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	388 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. 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA polymerase II transcriptional preinitiation complex assembly Inferred by curator Ref.5. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	transcription factor TFIID complex Inferred from direct assay Ref.5 PubMed 15448131. Source: SGD
Molecular_function	DNA binding Inferred from direct assay PubMed 15601843. Source: UniProtKB RNA polymerase II activating transcription factor binding Inferred from direct assay PubMed 12501245. Source: SGD chromatin binding Inferred from direct assay PubMed 12600943. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
TAF1	P46677	7	EBI-11231,EBI-18855
TAF12	Q03761	8	EBI-11231,EBI-35097
TAF5	P38129	12	EBI-11231,EBI-18868
TAF9	Q05027	10	EBI-11231,EBI-27500

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 388

388

Transcription initiation factor TFIID subunit 4

PRO_0000118871

Regions

Domain

193 – 261

Histone-fold

Coiled coil

279 – 297

Potential

Amino acid modifications

Modified residue

Phosphoserine Ref.17

Modified residue

Phosphoserine Ref.15 Ref.16 Ref.17

Modified residue

Phosphoserine Ref.17

Modified residue

Phosphoserine Ref.17

Modified residue

Phosphoserine Ref.14 Ref.17

Modified residue

Phosphoserine Ref.17

Sequences

Sequence

Length

Mass (Da)

Tools

P50105 [UniParc].

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

388

42,336

        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' referencesShow '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. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, MASS SPECTROMETRY. Strain: YAL6B.
[15]	"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, MASS SPECTROMETRY. Strain: ADR376.
[16]	"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, MASS SPECTROMETRY.
[17]	"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-4; SER-36; SER-49; SER-51; SER-80 AND SER-89, MASS SPECTROMETRY.
+	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.
PIR	S45013.
RefSeq	NP_013718.1. NM_001182501.1.
3D structure databases
ProteinModelPortal	P50105.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-789N.
IntAct	P50105. 34 interactions.
MINT	MINT-647326.
STRING	4932.YMR005W.
Proteomic databases
PaxDb	P50105.
PeptideAtlas	P50105.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR005W; YMR005W; YMR005W.
GeneID	855017.
KEGG	sce:YMR005W.
Organism-specific databases
CYGD	YMR005w.
SGD	S000004607. TAF4.
Phylogenomic databases
eggNOG	NOG303189.
HOGENOM	HOG000154501.
OMA	EEPGIVM.
OrthoDB	EOG42592Z.
Gene expression databases
Genevestigator	P50105.
GermOnline	YMR005W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR007900. TAF4. [Graphical view]
Pfam	PF05236. TAF4. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	978198.

Entry information

Entry name

TAF4_YEAST

Accession

Primary (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 3, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents