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TAF14 (P35189) - Overview - Molecular Target Synopsis

Protein


TAF14, Transcription initiation factor TFIID subunit 14
UniProt P35189

Also Known as TAF14_YEAST, TAF14, ANC1, CST10, SWP29, TAF30, TFG3

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: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) (PubMed:26341557, PubMed:27089029). 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). 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.

6MIN
CRYSTAL STRUCTURE OF TAF14 YEATS DOMAIN G82A MUTANT IN COMPLEX WITH HISTONE H3K9CR
RCSB/PDB
Inspect Structure
See all 3D Structures for TAF14

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform
244P35189-1

Sub-cellular localization


Gene Copy Number Variation


In COSMIC - Cell Lines Project TAF14 has gain in 0 cell-lines, loss in 0 cell-lines and no signal in 0 cell-lines. (see details)

3D Structures


For TAF14 there are:
9 structures (9 chains) solved
2 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis