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, PubMed:30385749). 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). 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. 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). 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. Belongs to the TAF14 family.