P35189 (TAF14_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription initiation factor TFIID subunit 14

Alternative name(s):
Actin non-complementing mutant 1
Chromosome stability protein 10
SWI/SNF chromatin-remodeling complex subunit TAF14
SWI/SNF complex 29 kDa subunit
SWI/SNF complex subunit TAF14
TBP-associated factor 14
TBP-associated factor 30 kDa
Transcription factor G 30 kDa subunit
Transcription initiation factor TFIIF 30 kDa subunit

Gene names

Name:	TAF14
Synonyms:	ANC1, CST10, SWP29, TAF30, TFG3
Ordered Locus Names:	YPL129W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	244 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, the RNA polymerase II associated general transcription factor complex TFIIF, and the chromatin-remodeling complex SWI/SNF. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation 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. TFIIF is essential for the initiation of transcription by RNA polymerase II. TFIIF functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation. The TAF14 subunit has stimulatory activity. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. Component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation. Ref.8 Ref.9 Ref.11 Ref.12 Ref.15 Ref.17
Subunit structure	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. TFIIF is composed of three different subunits: TFG1/RAP74, TFG2/RAP30 and TAF14. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29. Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Component of the NuA3 complex, composed of at least NTO1, SAS3, TAF14, YNG1 and EAF6. Ref.9
Subcellular location	Nucleus.
Miscellaneous	TAF14 is the only non-essential TAF. Present with 3100 molecules/cell in log phase SD medium. Ref.16 There is no homolog of TAF14 present in the TFIIF complexes of higher eukaryotes.
Sequence similarities	Belongs to the TAF14 family. Contains 1 YEATS domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	RNA polymerase II transcriptional preinitiation complex assembly Inferred by curator Ref.9Ref.1. Source: SGD histone acetylation Inferred from direct assay Ref.6. Source: SGD nucleosome mobilization Inferred from direct assay Ref.13. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Ino80 complex Inferred from direct assay Ref.13. Source: SGD NuA3 histone acetyltransferase complex Inferred from direct assay Ref.6Ref.17. Source: SGD RSC complex Inferred from physical interaction. Source: SGD SWI/SNF complex Inferred from direct assay. Source: SGD mediator complex Inferred from physical interaction Ref.1. Source: SGD transcription factor TFIID complex Inferred from direct assay Ref.9. Source: SGD transcription factor TFIIF complex Inferred from direct assay Ref.1. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SAS3	P34218	2	EBI-18920,EBI-16484
SNF5	P18480	2	EBI-18920,EBI-17546
SNF6	P18888	4	EBI-18920,EBI-17550
YNG1	Q08465	3	EBI-18920,EBI-31890

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 244

244

Transcription initiation factor TFIID subunit 14

PRO_0000211241

Regions

Domain

8 – 115

108

YEATS

Experimental info

Sequence conflict

116

1

H → Q in CAA49192. Ref.5

Secondary structure

1

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244

Helix Strand Turn

Details...

Beta strand

6 – 17

12

Beta strand

30 – 37

8

Beta strand

53 – 58

6

Beta strand

66 – 71

6

Beta strand

74 – 78

5

Beta strand

86 – 90

5

Beta strand

92 – 94

3

Beta strand

99 – 103

5

Beta strand

107 – 119

13

Sequences

	Sequence		Length	Mass (Da)
	P35189 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 60EA5EC2474B1B9C	FASTA	244	27,440
	10 20 30 40 50 60 MVATVKRTIR IKTQQHILPE VPPVENFPVR QWSIEIVLLD DEGKEIPATI FDKVIYHLHP 70 80 90 100 110 120 TFANPNRTFT DPPFRIEEQG WGGFPLDISV FLLEKAGERK IPHDLNFLQE SYEVEHVIQI 130 140 150 160 170 180 PLNKPLLTEE LAKSGSTEET TANTGTIGKR RTTTNTTAEP KAKRAKTGSA STVKGSVDLE 190 200 210 220 230 240 KLAFGLTKLN EDDLVGVVQM VTDNKTPEMN VTNNVEEGEF IIDLYSLPEG LLKSLWDYVK KNTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TFIIF-TAF-RNA polymerase II connection." Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A., Kornberg R.D. Genes Dev. 8:2868-2878(1994) [PubMed: 7995524] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 189-222. Strain: ATCC 208279 / BJ926.
[2]	"A nuclear protein with sequence similarity to proteins implicated in human acute leukemias is important for cellular morphogenesis and actin cytoskeletal function in Saccharomyces cerevisiae." Welch M.D., Drubin D.G. Mol. Biol. Cell 5:617-632(1994) [PubMed: 7949419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"An essential yeast gene encoding a TTAGGG repeat-binding protein." Brigati C., Kurtz S., Balderes D., Vidali G., Shore D.M. Mol. Cell. Biol. 13:1306-1314(1993) [PubMed: 8423796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-244. Strain: LN224.
[6]	"The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex." John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L. Genes Dev. 14:1196-1208(2000) [PubMed: 10817755] [Abstract] Cited for: PROTEIN SEQUENCE OF 189-203, INTERACTION WITH SAS3.
[7]	"Purification and characterization of yeast RNA polymerase II general initiation factor g." Henry N.L., Sayre M.H., Kornberg R.D. J. Biol. Chem. 267:23388-23392(1992) [PubMed: 1331085] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Molecular genetics of the RNA polymerase II general transcriptional machinery." Hampsey M. Microbiol. Mol. Biol. Rev. 62:465-503(1998) [PubMed: 9618449] [Abstract] Cited for: FUNCTION, TAF14 IN TFIIF.
[9]	"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.
[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]	"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.
[12]	"Multi-protein complexes in eukaryotic gene transcription." Martinez E. Plant Mol. Biol. 50:925-947(2002) [PubMed: 12516863] [Abstract] Cited for: FUNCTION.
[13]	"Involvement of actin-related proteins in ATP-dependent chromatin remodeling." Shen X., Ranallo R., Choi E., Wu C. Mol. Cell 12:147-155(2003) [PubMed: 12887900] [Abstract] Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
[14]	"Structural analysis of the yeast SWI/SNF chromatin remodeling complex." Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L., Peterson C.L. Nat. Struct. Biol. 10:141-145(2003) [PubMed: 12524530] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, ELECTRON MICROSCOPY OF THE SWI/SNF COMPLEX.
[15]	"Recent advances in understanding chromatin remodeling by SWI/SNF complexes." Martens J.A., Winston F. Curr. Opin. Genet. Dev. 13:136-142(2003) [PubMed: 12672490] [Abstract] Cited for: FUNCTION, SWI/SNF STOICHIOMETRY.
[16]	"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].
[17]	"Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs." Taverna S.D., Ilin S., Rogers R.S., Tanny J.C., Lavender H., Li H., Baker L., Boyle J., Blair L.P., Chait B.T., Patel D.J., Aitchison J.D., Tackett A.J., Allis C.D. Mol. Cell 24:785-796(2006) [PubMed: 17157260] [Abstract] Cited for: FUNCTION OF THE NUA3 COMPLEX, IDENTIFICATION IN THE NUA3 COMPLEX, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U13017 Genomic DNA. Translation: AAA61644.1.
Z26040 Genomic DNA. Translation: CAA81125.1.
U43703 Genomic DNA. Translation: AAB68235.1.
X69394 Genomic DNA. Translation: CAA49192.1.
BK006949 Genomic DNA. Translation: DAA11304.1.

PIR

S38568.

RefSeq

NP_015196.1. NM_001183943.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L7E	NMR	-	A	1-123	[»]

ProteinModelPortal

P35189.

SMR

P35189. Positions 1-123.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1147N.

IntAct

P35189. 50 interactions.

MINT

MINT-646854.

STRING

P35189.

Proteomic databases

PeptideAtlas

P35189.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPL129W; YPL129W; YPL129W.

GeneID

855974.

KEGG

sce:YPL129W.

NMPDR

fig|4932.3.peg.6327.

Organism-specific databases

CYGD

YPL129w.

SGD

S000006050. TAF14.

Phylogenomic databases

eggNOG

fuNOG05577.

GeneTree

EFGT00050000002501.

HOGENOM

HBG329099.

OMA

HPTFANP.

OrthoDB

EOG4F4WM9.

Gene expression databases

ArrayExpress

P35189.

Genevestigator

P35189.

GermOnline

YPL129W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR016665. SAS_cplx_Sas5/TFIID_TAF14.
IPR005033. YEATS.
[Graphical view]

KO

K03140.

PANTHER

PTHR23195:SF2. PTHR23195:SF2. 1 hit.
PTHR23195. YEATS. 1 hit.

Pfam

PF03366. YEATS. 1 hit.
[Graphical view]

PIRSF

PIRSF016551. SAS5/TFIID_14. 1 hit.

PROSITE

PS51037. YEATS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

980795.

Entry information

Entry name

TAF14_YEAST

Accession

Primary (citable) accession number: P35189
Secondary accession number(s): D6W3N8, Q02460

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	December 14, 2011
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program