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YEAST:TAF14

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) TAF14 (synonyms: ANC1, CST10, SWP29, TAF30, TFG3)
Protein Name(s) Transcription initiation factor TFIID subunit 14

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

External Links
UniProt P35189
EMBL U13017
Z26040
U43703
X69394
BK006949
PIR S38568
RefSeq NP_015196.1
PDB 2L7E
3QRL
PDBsum 2L7E
3QRL
ProteinModelPortal P35189
SMR P35189
BioGrid 36052
DIP DIP-1147N
IntAct P35189
MINT MINT-646854
STRING 4932.YPL129W
MaxQB P35189
PaxDb P35189
PeptideAtlas P35189
EnsemblFungi [example_ID YPL129W]
GeneID 855974
KEGG sce:YPL129W
CYGD YPL129w
SGD S000006050
eggNOG COG5033
GeneTree ENSGT00530000068270
HOGENOM HOG000176324
InParanoid P35189
KO K03140
OMA HPTFANP
OrthoDB EOG76DV4G
BioCyc YEAST:G3O-34028-MONOMER
EvolutionaryTrace P35189
NextBio 980795
Proteomes UP000002311
Genevestigator P35189
GO GO:0031011
GO:0016592
GO:0033100
GO:1990467
GO:1990468
GO:0005634
GO:0016514
GO:0005669
GO:0005674
GO:0000991
GO:0006200
GO:0006338
GO:0016573
GO:0042766
GO:0001111
GO:0006357
GO:0051123
GO:0006368
GO:0006366
GO:0006367
GO:0001174
InterPro IPR016665
IPR005033
PANTHER PTHR23195
PTHR23195:SF2
Pfam PF03366
PIRSF PIRSF016551
PROSITE PS51037

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0005667

transcription factor complex

PMID:7995524[1]

ECO:0000314

C

Figure 4E shows the precipitates that were electrophoresed in a SDS-10% poly- acrylamide gel. It shows by the overlap that yeast TAFs can be immunoprecipitated by antibodies against Tfg3. Antibody against Tfg3 (lane 1) or mAb 12CA5 (lane 2) was used to immunoprecipitate yeast TAFs from a complex fraction.

complete
CACAO 9314

GO:0005674

transcription factor TFIIF complex

PMID:7995524[1]

ECO:0000314

C

Figure 5 Depicts region 4.2 showing the sequence homology between Tfg2 of bacterial cr factors. Alignment of the carboxy-terminal residues of Tfg2 with the carboxy-terminal residues of E. coli and Bacillus subtilis.

complete
CACAO 9315

part_of

GO:1990468

NuA3b histone acetyltransferase complex

PMID:25104842[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:1990467

NuA3a histone acetyltransferase complex

PMID:25104842[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0051123

RNA polymerase II preinitiation complex assembly

PMID:10788514[3]

ECO:0000305

curator inference used in manual assertion

GO:0005669

P

Seeded From UniProt

complete

involved_in

GO:0051123

RNA polymerase II preinitiation complex assembly

PMID:7995524[1]

ECO:0000305

curator inference used in manual assertion

GO:0005674

P

Seeded From UniProt

complete

involved_in

GO:0042766

nucleosome mobilization

PMID:12887900[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0033100

NuA3 histone acetyltransferase complex

PMID:10817755[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0033100

NuA3 histone acetyltransferase complex

PMID:17157260[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0031011

Ino80 complex

PMID:24034245[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P53115

C

Seeded From UniProt

complete

part_of

GO:0031011

Ino80 complex

PMID:12887900[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016592

mediator complex

PMID:7995524[1]

ECO:0000353

physical interaction evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0016573

histone acetylation

PMID:10817755[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016514

SWI/SNF complex

PMID:18644858[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

contributes_to

GO:0015616

DNA translocase activity

PMID:16455496[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

contributes_to

GO:0015616

DNA translocase activity

PMID:17918861[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

contributes_to

GO:0015616

DNA translocase activity

PMID:17188033[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006368

transcription elongation from RNA polymerase II promoter

PMID:7995524[1]

ECO:0000305

curator inference used in manual assertion

GO:0005674

P

Seeded From UniProt

complete

involved_in

GO:0006367

transcription initiation from RNA polymerase II promoter

PMID:1331084[12]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006366

transcription by RNA polymerase II

PMID:15448131[13]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006366

transcription by RNA polymerase II

PMID:12138208[14]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006338

chromatin remodeling

PMID:12887900[4]

ECO:0000305

curator inference used in manual assertion

GO:0031011

P

Seeded From UniProt

complete

involved_in

GO:0006338

chromatin remodeling

PMID:18644858[8]

ECO:0000305

curator inference used in manual assertion

GO:0016514

P

Seeded From UniProt

complete

part_of

GO:0005674

transcription factor TFIIF complex

PMID:15896708[15]

ECO:0000353

physical interaction evidence used in manual assertion

SGD:S000003418

C

Seeded From UniProt

complete

part_of

GO:0005674

transcription factor TFIIF complex

PMID:7995524[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005674

transcription factor TFIIF complex

PMID:15896708[15]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005674

transcription factor TFIIF complex

PMID:12242279[16]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005669

transcription factor TFIID complex

PMID:15448131[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005669

transcription factor TFIID complex

PMID:10788514[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:22932476[17]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0001174

transcriptional start site selection at RNA polymerase II promoter

PMID:7995524[1]

ECO:0000305

curator inference used in manual assertion

GO:0005674

P

Seeded From UniProt

complete

contributes_to

GO:0001139

RNA polymerase II complex recruiting activity

PMID:7995524[1]

ECO:0000305

curator inference used in manual assertion

GO:0005674

F

Seeded From UniProt

complete

involved_in

GO:0001111

promoter clearance from RNA polymerase II promoter

PMID:7995524[1]

ECO:0000305

curator inference used in manual assertion

GO:0005674

P

Seeded From UniProt

complete

contributes_to

GO:0016251

RNA polymerase II general transcription initiation factor activity

PMID:15448131[13]

ECO:0000305

curator inference used in manual assertion

GO:0005669

F

Seeded From UniProt

complete

enables

GO:0016251

RNA polymerase II general transcription initiation factor activity

PMID:14749386[18]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005033

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 Henry, NL et al. (1994) TFIIF-TAF-RNA polymerase II connection. Genes Dev. 8 2868-78 PubMed GONUTS page
  2. 2.0 2.1 Gilbert, TM et al. (2014) A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions. Mol. Cell Proteomics 13 2883-95 PubMed GONUTS page
  3. 3.0 3.1 Sanders, SL & Weil, PA (2000) Identification of two novel TAF subunits of the yeast Saccharomyces cerevisiae TFIID complex. J. Biol. Chem. 275 13895-900 PubMed GONUTS page
  4. 4.0 4.1 4.2 Shen, X et al. (2003) Involvement of actin-related proteins in ATP-dependent chromatin remodeling. Mol. Cell 12 147-55 PubMed GONUTS page
  5. 5.0 5.1 John, S et al. (2000) 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. Genes Dev. 14 1196-208 PubMed GONUTS page
  6. Taverna, SD et al. (2006) 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. Mol. Cell 24 785-96 PubMed GONUTS page
  7. Tosi, A et al. (2013) Structure and subunit topology of the INO80 chromatin remodeler and its nucleosome complex. Cell 154 1207-19 PubMed GONUTS page
  8. 8.0 8.1 Dechassa, ML et al. (2008) Architecture of the SWI/SNF-nucleosome complex. Mol. Cell. Biol. 28 6010-21 PubMed GONUTS page
  9. Lia, G et al. (2006) Direct observation of DNA distortion by the RSC complex. Mol. Cell 21 417-25 PubMed GONUTS page
  10. Fischer, CJ et al. (2007) Kinetic model for the ATP-dependent translocation of Saccharomyces cerevisiae RSC along double-stranded DNA. Biochemistry 46 12416-26 PubMed GONUTS page
  11. Zhang, Y et al. (2006) DNA translocation and loop formation mechanism of chromatin remodeling by SWI/SNF and RSC. Mol. Cell 24 559-68 PubMed GONUTS page
  12. Sayre, MH et al. (1992) Reconstitution of transcription with five purified initiation factors and RNA polymerase II from Saccharomyces cerevisiae. J. Biol. Chem. 267 23376-82 PubMed GONUTS page
  13. 13.0 13.1 13.2 Auty, R et al. (2004) Purification of active TFIID from Saccharomyces cerevisiae. Extensive promoter contacts and co-activator function. J. Biol. Chem. 279 49973-81 PubMed GONUTS page
  14. Sanders, SL et al. (2002) Molecular characterization of Saccharomyces cerevisiae TFIID. Mol. Cell. Biol. 22 6000-13 PubMed GONUTS page
  15. 15.0 15.1 Kabani, M et al. (2005) Anc1 interacts with the catalytic subunits of the general transcription factors TFIID and TFIIF, the chromatin remodeling complexes RSC and INO80, and the histone acetyltransferase complex NuA3. Biochem. Biophys. Res. Commun. 332 398-403 PubMed GONUTS page
  16. Krogan, NJ et al. (2002) RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach. Mol. Cell. Biol. 22 6979-92 PubMed GONUTS page
  17. Dastidar, RG et al. (2012) The nuclear localization of SWI/SNF proteins is subjected to oxygen regulation. Cell Biosci 2 30 PubMed GONUTS page
  18. Rani, PG et al. (2004) RNA polymerase II (Pol II)-TFIIF and Pol II-mediator complexes: the major stable Pol II complexes and their activity in transcription initiation and reinitiation. Mol. Cell. Biol. 24 1709-20 PubMed GONUTS page