P35189 · TAF14_YEAST
- ProteinTranscription initiation factor TFIID subunit 14
- GeneTAF14
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids244 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449).
Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449).
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 (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449).
TFIIF is essential for the initiation of transcription by RNA polymerase II (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449).
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 (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:30385749, PubMed:9618449).
TAF14 acts as a chromatin reader that specifically recognizes and binds histones that are acylated (PubMed:26341557, PubMed:27089029).
Recognizes and binds histone H3 acetylated or crotonylated at 'Lys-9' (H3K9ac and H3K9cr, respectively), with some preference for crotonylated lysine (PubMed:26341557, PubMed:27089029, PubMed:30385749).
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 (PubMed:12672490).
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 (PubMed:12672490).
Component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3 (PubMed:17157260).
In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation (PubMed:17157260).
Does not bind DNA (PubMed:30385749).
Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449).
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 (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449).
TFIIF is essential for the initiation of transcription by RNA polymerase II (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449).
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 (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:30385749, PubMed:9618449).
TAF14 acts as a chromatin reader that specifically recognizes and binds histones that are acylated (PubMed:26341557, PubMed:27089029).
Recognizes and binds histone H3 acetylated or crotonylated at 'Lys-9' (H3K9ac and H3K9cr, respectively), with some preference for crotonylated lysine (PubMed:26341557, PubMed:27089029, PubMed:30385749).
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 (PubMed:12672490).
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 (PubMed:12672490).
Component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3 (PubMed:17157260).
In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation (PubMed:17157260).
Does not bind DNA (PubMed:30385749).
Miscellaneous
TAF14 is the only non-essential TAF.
Present with 3100 molecules/cell in log phase SD medium.
There is no homolog of TAF14 present in the TFIIF complexes of higher eukaryotes.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 104 | Acylated histone binding | ||||
Sequence: D |
GO annotations
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscription initiation factor TFIID subunit 14
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP35189
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 24 | Does not affect binding to acylated histone H3. | ||||
Sequence: V → A | ||||||
Mutagenesis | 80 | Abolished binding to acylated histone H3. | ||||
Sequence: G → A | ||||||
Mutagenesis | 81 | Abolished binding to acetylated histone H3. | ||||
Sequence: W → A | ||||||
Mutagenesis | 82 | Does not affect ability to bind crotonylated lysines, while abolishing binding to acetylated lysines. | ||||
Sequence: G → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000211241 | 1-244 | Transcription initiation factor TFIID subunit 14 | |||
Sequence: MVATVKRTIRIKTQQHILPEVPPVENFPVRQWSIEIVLLDDEGKEIPATIFDKVIYHLHPTFANPNRTFTDPPFRIEEQGWGGFPLDISVFLLEKAGERKIPHDLNFLQESYEVEHVIQIPLNKPLLTEELAKSGSTEETTANTGTIGKRRTTTNTTAEPKAKRAKTGSASTVKGSVDLEKLAFGLTKLNEDDLVGVVQMVTDNKTPEMNVTNNVEEGEFIIDLYSLPEGLLKSLWDYVKKNTE | ||||||
Cross-link | 181 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
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.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P35189 | SAS3 P34218 | 3 | EBI-18920, EBI-16484 | |
BINARY | P35189 | SNF5 P18480 | 3 | EBI-18920, EBI-17546 | |
BINARY | P35189 | SNF6 P18888 | 5 | EBI-18920, EBI-17550 | |
BINARY | P35189 | YNG1 Q08465 | 3 | EBI-18920, EBI-31890 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-134 | YEATS | ||||
Sequence: MVATVKRTIRIKTQQHILPEVPPVENFPVRQWSIEIVLLDDEGKEIPATIFDKVIYHLHPTFANPNRTFTDPPFRIEEQGWGGFPLDISVFLLEKAGERKIPHDLNFLQESYEVEHVIQIPLNKPLLTEELAKS | ||||||
Region | 59-61 | Acylated histone binding | ||||
Sequence: HPT | ||||||
Region | 81-83 | Acylated histone binding | ||||
Sequence: WGG | ||||||
Compositional bias | 133-162 | Polar residues | ||||
Sequence: KSGSTEETTANTGTIGKRRTTTNTTAEPKA | ||||||
Region | 133-169 | Disordered | ||||
Sequence: KSGSTEETTANTGTIGKRRTTTNTTAEPKAKRAKTGS |
Domain
The YEATS domain specifically recognizes and binds acylated histones (acetylated and crotonylated) (PubMed:26341557, PubMed:27089029, PubMed:30385749).
Binds crotonylated lysine through a non-canonical pi-pi-pi stacking mechanism (PubMed:27089029, PubMed:30385749).
Binds crotonylated lysine through a non-canonical pi-pi-pi stacking mechanism (PubMed:27089029, PubMed:30385749).
Sequence similarities
Belongs to the TAF14 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length244
- Mass (Da)27,440
- Last updated1994-02-01 v1
- Checksum60EA5EC2474B1B9C
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 116 | in Ref. 5; CAA49192 | ||||
Sequence: H → Q | ||||||
Compositional bias | 133-162 | Polar residues | ||||
Sequence: KSGSTEETTANTGTIGKRRTTTNTTAEPKA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U13017 EMBL· GenBank· DDBJ | AAA61644.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z26040 EMBL· GenBank· DDBJ | CAA81125.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43703 EMBL· GenBank· DDBJ | AAB68235.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X69394 EMBL· GenBank· DDBJ | CAA49192.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006949 EMBL· GenBank· DDBJ | DAA11304.1 EMBL· GenBank· DDBJ | Genomic DNA |