ID TAF14_YEAST Reviewed; 244 AA. AC P35189; D6W3N8; Q02460; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 02-SEP-2026, entry version 209. DE RecName: Full=Transcription initiation factor TFIID subunit 14; DE AltName: Full=Actin non-complementing mutant 1; DE AltName: Full=Chromosome stability protein 10; DE AltName: Full=SWI/SNF chromatin-remodeling complex subunit TAF14; DE AltName: Full=SWI/SNF complex 29 kDa subunit; DE AltName: Full=SWI/SNF complex subunit TAF14; DE AltName: Full=TBP-associated factor 14; DE AltName: Full=TBP-associated factor 30 kDa; DE AltName: Full=Transcription factor G 30 kDa subunit; DE AltName: Full=Transcription initiation factor TFIIF 30 kDa subunit; GN Name=TAF14; Synonyms=ANC1, CST10, SWP29, TAF30, TFG3; GN OrderedLocusNames=YPL129W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 189-222. RC STRAIN=ATCC 208279 / BJ926; RX PubMed=7995524; DOI=10.1101/gad.8.23.2868; RA Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A., Kornberg R.D.; RT "TFIIF-TAF-RNA polymerase II connection."; RL Genes Dev. 8:2868-2878(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7949419; DOI=10.1091/mbc.5.6.617; RA Welch M.D., Drubin D.G.; RT "A nuclear protein with sequence similarity to proteins implicated in human RT acute leukemias is important for cellular morphogenesis and actin RT cytoskeletal function in Saccharomyces cerevisiae."; RL Mol. Biol. Cell 5:617-632(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; DOI=10.1038/387s103; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-244. RC STRAIN=LN224; RX PubMed=8423796; DOI=10.1128/mcb.13.2.1306-1314.1993; RA Brigati C., Kurtz S., Balderes D., Vidali G., Shore D.M.; RT "An essential yeast gene encoding a TTAGGG repeat-binding protein."; RL Mol. Cell. Biol. 13:1306-1314(1993). RN [6] RP PROTEIN SEQUENCE OF 189-203, AND INTERACTION WITH SAS3. RX PubMed=10817755; DOI=10.1101/gad.14.10.1196; RA John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L.; RT "The something about silencing protein, Sas3, is the catalytic subunit of RT NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 RT subunit of the yeast CP (Cdc68/Pob3)-FACT complex."; RL Genes Dev. 14:1196-1208(2000). RN [7] RP CHARACTERIZATION. RX PubMed=1331085; DOI=10.1016/s0021-9258(18)50103-4; RA Henry N.L., Sayre M.H., Kornberg R.D.; RT "Purification and characterization of yeast RNA polymerase II general RT initiation factor g."; RL J. Biol. Chem. 267:23388-23392(1992). RN [8] RP FUNCTION, AND TAF14 IN TFIIF. RX PubMed=9618449; DOI=10.1128/mmbr.62.2.465-503.1998; RA Hampsey M.; RT "Molecular genetics of the RNA polymerase II general transcriptional RT machinery."; RL Microbiol. Mol. Biol. Rev. 62:465-503(1998). RN [9] RP FUNCTION, AND SUBUNIT. RX PubMed=10788514; DOI=10.1074/jbc.275.18.13895; RA Sanders S.L., Weil P.A.; RT "Identification of two novel TAF subunits of the yeast Saccharomyces RT cerevisiae TFIID complex."; RL J. Biol. Chem. 275:13895-13900(2000). RN [10] RP 3D-STRUCTURE, AND ELECTRON MICROSCOPY OF TFIID. RX PubMed=12093743; DOI=10.1093/emboj/cdf342; RA Leurent C., Sanders S.L., Ruhlmann C., Mallouh V., Weil P.A., RA Kirschner D.B., Tora L., Schultz P.; RT "Mapping histone fold TAFs within yeast TFIID."; RL EMBO J. 21:3424-3433(2002). RN [11] RP FUNCTION, AND TFIID STOICHIOMETRY. RX PubMed=12138208; DOI=10.1128/mcb.22.16.6000-6013.2002; RA Sanders S.L., Garbett K.A., Weil P.A.; RT "Molecular characterization of Saccharomyces cerevisiae TFIID."; RL Mol. Cell. Biol. 22:6000-6013(2002). RN [12] RP FUNCTION. RX PubMed=12516863; DOI=10.1023/a:1021258713850; RA Martinez E.; RT "Multi-protein complexes in eukaryotic gene transcription."; RL Plant Mol. Biol. 50:925-947(2002). RN [13] RP IDENTIFICATION IN THE INO80 COMPLEX. RX PubMed=12887900; DOI=10.1016/s1097-2765(03)00264-8; RA Shen X., Ranallo R., Choi E., Wu C.; RT "Involvement of actin-related proteins in ATP-dependent chromatin RT remodeling."; RL Mol. Cell 12:147-155(2003). RN [14] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-181, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [15] RP 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, AND ELECTRON MICROSCOPY OF RP THE SWI/SNF COMPLEX. RX PubMed=12524530; DOI=10.1038/nsb888; RA Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L., RA Peterson C.L.; RT "Structural analysis of the yeast SWI/SNF chromatin remodeling complex."; RL Nat. Struct. Biol. 10:141-145(2003). RN [16] RP FUNCTION, AND SWI/SNF STOICHIOMETRY. RX PubMed=12672490; DOI=10.1016/s0959-437x(03)00022-4; RA Martens J.A., Winston F.; RT "Recent advances in understanding chromatin remodeling by SWI/SNF RT complexes."; RL Curr. Opin. Genet. Dev. 13:136-142(2003). RN [17] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [18] RP FUNCTION OF THE NUA3 COMPLEX, IDENTIFICATION IN THE NUA3 COMPLEX, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17157260; DOI=10.1016/j.molcel.2006.10.026; RA Taverna S.D., Ilin S., Rogers R.S., Tanny J.C., Lavender H., Li H., RA Baker L., Boyle J., Blair L.P., Chait B.T., Patel D.J., Aitchison J.D., RA Tackett A.J., Allis C.D.; RT "Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT RT activity at K14 of H3 and transcription at a subset of targeted ORFs."; RL Mol. Cell 24:785-796(2006). RN [19] RP SUBUNIT. RX PubMed=25104842; DOI=10.1074/mcp.m114.038224; RA Gilbert T.M., McDaniel S.L., Byrum S.D., Cades J.A., Dancy B.C., Wade H., RA Tackett A.J., Strahl B.D., Taverna S.D.; RT "A PWWP domain-containing protein targets the NuA3 acetyltransferase RT complex via histone H3 lysine 36 trimethylation to coordinate RT transcriptional elongation at coding regions."; RL Mol. Cell. Proteomics 13:2883-2895(2014). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-137, AND MUTAGENESIS OF TRP-81. RX PubMed=26341557; DOI=10.1101/gad.269977.115; RA Shanle E.K., Andrews F.H., Meriesh H., McDaniel S.L., Dronamraju R., RA DiFiore J.V., Jha D., Wozniak G.G., Bridgers J.B., Kerschner J.L., RA Krajewski K., Martin G.M., Morrison A.J., Kutateladze T.G., Strahl B.D.; RT "Association of Taf14 with acetylated histone H3 directs gene transcription RT and the DNA damage response."; RL Genes Dev. 29:1795-1800(2015). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-137, FUNCTION, DOMAIN, AND RP MUTAGENESIS OF VAL-24 AND GLY-80. RX PubMed=27089029; DOI=10.1038/nchembio.2065; RA Andrews F.H., Shinsky S.A., Shanle E.K., Bridgers J.B., Gest A., Tsun I.K., RA Krajewski K., Shi X., Strahl B.D., Kutateladze T.G.; RT "The Taf14 YEATS domain is a reader of histone crotonylation."; RL Nat. Chem. Biol. 12:396-398(2016). RN [22] {ECO:0007744|PDB:6MIN, ECO:0007744|PDB:6MIO, ECO:0007744|PDB:6MIP, ECO:0007744|PDB:6MIQ} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-137, FUNCTION, DOMAIN, AND RP MUTAGENESIS OF GLY-82. RX PubMed=30385749; DOI=10.1038/s41467-018-07072-6; RA Klein B.J., Vann K.R., Andrews F.H., Wang W.W., Zhang J., Zhang Y., RA Beloglazkina A.A., Mi W., Li Y., Li H., Shi X., Kutateladze A.G., RA Strahl B.D., Liu W.R., Kutateladze T.G.; RT "Structural insights into the pi-pi-pi stacking mechanism and DNA-binding RT activity of the YEATS domain."; RL Nat. Commun. 9:4574-4574(2018). CC -!- FUNCTION: Functions as a component of the DNA-binding general CC transcription factor complex TFIID, the RNA polymerase II associated CC general transcription factor complex TFIIF, and the chromatin- CC remodeling complex SWI/SNF (PubMed:10788514, PubMed:12138208, CC PubMed:12516863, PubMed:9618449). Binding of TFIID to a promoter (with CC or without TATA element) is the initial step in preinitiation complex CC (PIC) formation (PubMed:10788514, PubMed:12138208, PubMed:12516863, CC PubMed:9618449). TFIID plays a key role in the regulation of gene CC expression by RNA polymerase II through different activities such as CC transcription activator interaction, core promoter recognition and CC selectivity, TFIIA and TFIIB interaction, chromatin modification CC (histone acetylation by TAF1), facilitation of DNA opening and CC initiation of transcription (PubMed:10788514, PubMed:12138208, CC PubMed:12516863, PubMed:9618449). TFIIF is essential for the initiation CC of transcription by RNA polymerase II (PubMed:10788514, CC PubMed:12138208, PubMed:12516863, PubMed:9618449). TFIIF functions CC include the recruitment of RNA polymerase II to the promoter bound DNA- CC TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for CC non-specific DNA, allowing for the subsequent recruitment of TFIIE and CC TFIIH, and facilitating RNA polymerase II elongation (PubMed:10788514, CC PubMed:12138208, PubMed:12516863, PubMed:30385749, PubMed:9618449). CC TAF14 acts as a chromatin reader that specifically recognizes and binds CC histones that are acylated (PubMed:26341557, PubMed:27089029). CC Recognizes and binds histone H3 acetylated or crotonylated at 'Lys-9' CC (H3K9ac and H3K9cr, respectively), with some preference for CC crotonylated lysine (PubMed:26341557, PubMed:27089029, CC PubMed:30385749). Component of the SWI/SNF complex, an ATP-dependent CC chromatin-remodeling complex, is required for the positive and negative CC regulation of gene expression of a large number of genes CC (PubMed:12672490). It changes chromatin structure by altering DNA- CC histone contacts within a nucleosome, leading eventually to a change in CC nucleosome position, thus facilitating or repressing binding of gene- CC specific transcription factors (PubMed:12672490). Component of the NuA3 CC histone acetyltransferase complex (PubMed:17157260). The NuA3 HAT CC complex has 2 functionally distinct forms. NuA3a binds H3K4me3, through CC the PHD finger of YNG1, and acetylates H3K14 at the promoter region of CC actively transcribed genes to promote transcription initiation. NuA3b CC binds H3K36me3 at the coding regions of actively transcribed genes, CC through the PWWP domain of PDP3, and coordinates transcription CC elongation (PubMed:25104842). Does not bind DNA (PubMed:30385749). CC {ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:12138208, CC ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:12672490, CC ECO:0000269|PubMed:17157260, ECO:0000269|PubMed:25104842, CC ECO:0000269|PubMed:26341557, ECO:0000269|PubMed:27089029, CC ECO:0000269|PubMed:30385749, ECO:0000269|PubMed:9618449}. CC -!- SUBUNIT: The 1.2 MDa TFIID complex is composed of TATA binding protein CC (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, CC TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, CC TAF9, TAF10, TAF12, and three copies of TAF14. TFIIF is composed of CC three different subunits: TFG1/RAP74, TFG2/RAP30 and TAF14. Component CC of the SWI/SNF global transcription activator complex. The 1.14 MDa CC SWI/SNF complex is composed of 11 different subunits: one copy each of CC SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies CC each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29. CC Component of the chromatin-remodeling INO80 complex, at least composed CC of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, CC ACT1, IES2, IES5 and INO80. Component of the NuA3 histone CC acetyltransferase (HAT) complex. The NuA3 HAT complex has 2 CC functionally distinct forms that participate in transcription. The CC NuA3b HAT complex contains an additional subunit, PDP3. CC {ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:12887900, CC ECO:0000269|PubMed:17157260, ECO:0000269|PubMed:25104842}. CC -!- INTERACTION: CC P35189; P34218: SAS3; NbExp=3; IntAct=EBI-18920, EBI-16484; CC P35189; P18480: SNF5; NbExp=3; IntAct=EBI-18920, EBI-17546; CC P35189; P18888: SNF6; NbExp=5; IntAct=EBI-18920, EBI-17550; CC P35189; Q08465: YNG1; NbExp=3; IntAct=EBI-18920, EBI-31890; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DOMAIN: The YEATS domain specifically recognizes and binds acylated CC histones (acetylated and crotonylated) (PubMed:26341557, CC PubMed:27089029, PubMed:30385749). Binds crotonylated lysine through a CC non-canonical pi-pi-pi stacking mechanism (PubMed:27089029, CC PubMed:30385749). {ECO:0000269|PubMed:26341557, CC ECO:0000269|PubMed:27089029, ECO:0000269|PubMed:30385749}. CC -!- MISCELLANEOUS: TAF14 is the only non-essential TAF. CC -!- MISCELLANEOUS: Present with 3100 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- MISCELLANEOUS: There is no homolog of TAF14 present in the TFIIF CC complexes of higher eukaryotes. CC -!- SIMILARITY: Belongs to the TAF14 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U13017; AAA61644.1; -; Genomic_DNA. DR EMBL; Z26040; CAA81125.1; -; Genomic_DNA. DR EMBL; U43703; AAB68235.1; -; Genomic_DNA. DR EMBL; X69394; CAA49192.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11304.1; -; Genomic_DNA. DR PIR; S38568; S38568. DR RefSeq; NP_015196.1; NM_001183943.1. DR PDB; 2L7E; NMR; -; A=1-123. DR PDB; 3QRL; X-ray; 1.70 A; A=1-137. DR PDB; 5D7E; X-ray; 1.90 A; A=1-137. DR PDB; 5IOK; X-ray; 2.22 A; A=1-137. DR PDB; 5SVA; EM; 15.30 A; n=1-244. DR PDB; 6LQZ; NMR; -; A=174-244. DR PDB; 6MIN; X-ray; 1.90 A; A=1-137. DR PDB; 6MIO; X-ray; 1.85 A; A=1-137. DR PDB; 6MIP; X-ray; 2.00 A; A=1-137. DR PDB; 6MIQ; X-ray; 1.75 A; A=1-137. DR PDB; 7F4A; X-ray; 2.00 A; A=2-137. DR PDB; 7UHE; X-ray; 1.66 A; A/C=168-243. DR PDB; 8U77; X-ray; 1.93 A; A/C/E/G=176-243. DR PDB; 9UUO; EM; 3.68 A; E=1-244. DR PDB; 9UUS; EM; 3.20 A; E=1-244. DR PDB; 9VKW; EM; 3.13 A; E=1-244. DR AlphaFoldDB; P35189; -. DR BMRB; P35189; -. DR EMDB; EMD-64513; -. DR EMDB; EMD-64517; -. DR EMDB; EMD-65145; -. DR MDRepo; P35189; -. DR SMR; P35189; -. DR BioGRID; 36052; 337. DR ComplexPortal; CPX-1149; General transcription factor TFIIF complex. DR ComplexPortal; CPX-1150; SWI/SNF chromatin remodelling complex. DR ComplexPortal; CPX-1642; General transcription factor complex TFIID. DR ComplexPortal; CPX-1810; NuA3 histone acetyltransferase complex. DR ComplexPortal; CPX-863; INO80 chromatin remodeling complex. DR DIP; DIP-1147N; -. DR FunCoup; P35189; 624. DR IntAct; P35189; 79. DR MINT; P35189; -. DR STRING; 4932.YPL129W; -. DR iPTMnet; P35189; -. DR PaxDb; 4932-YPL129W; -. DR PeptideAtlas; P35189; -. DR DNASU; 855974; -. DR EnsemblFungi; YPL129W_mRNA; YPL129W; YPL129W. DR GeneID; 855974; -. DR KEGG; sce:YPL129W; -. DR AGR; SGD:S000006050; -. DR SGD; S000006050; TAF14. DR VEuPathDB; FungiDB:YPL129W; -. DR eggNOG; KOG3149; Eukaryota. DR HOGENOM; CLU_078004_0_0_1; -. DR InParanoid; P35189; -. DR OMA; GEFDMTI; -. DR OrthoDB; 1741717at2759; -. DR BioCyc; YEAST:G3O-34028-MONOMER; -. DR BioGRID-ORCS; 855974; 7 hits in 10 CRISPR screens. DR CD-CODE; BE14A044; Transcriptional condensate. DR EvolutionaryTrace; P35189; -. DR PRO; PR:P35189; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; P35189; protein. DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal. DR GO; GO:0031011; C:Ino80 complex; IDA:SGD. DR GO; GO:0016592; C:mediator complex; IDA:SGD. DR GO; GO:0033100; C:NuA3 histone acetyltransferase complex; IDA:SGD. DR GO; GO:1990467; C:NuA3a histone acetyltransferase complex; IDA:SGD. DR GO; GO:1990468; C:NuA3b histone acetyltransferase complex; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal. DR GO; GO:0016514; C:SWI/SNF complex; IDA:SGD. DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD. DR GO; GO:0005674; C:transcription factor TFIIF complex; IDA:SGD. DR GO; GO:0003677; F:DNA binding; IDA:SGD. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:SGD. DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal. DR GO; GO:0006281; P:DNA repair; NAS:ComplexPortal. DR GO; GO:0006351; P:DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:SGD. DR CDD; cd16905; YEATS_Taf14_like; 1. DR FunFam; 2.60.40.1970:FF:000006; Transcription initiation factor TFIID subunit 14; 1. DR Gene3D; 2.60.40.1970; YEATS domain; 1. DR IDEAL; IID50207; -. DR InterPro; IPR027353; NET_dom. DR InterPro; IPR016665; Sas5/TAF14. DR InterPro; IPR038704; YEAST_sf. DR InterPro; IPR005033; YEATS. DR InterPro; IPR055129; YEATS_dom. DR PANTHER; PTHR23195; YEATS DOMAIN; 1. DR Pfam; PF17035; BET; 1. DR Pfam; PF03366; YEATS; 1. DR PIRSF; PIRSF016551; SAS5/TFIID_14; 1. DR PROSITE; PS51037; YEATS; 1. DR PDBsum; 2L7E; -. DR PDBsum; 3QRL; -. DR PDBsum; 5D7E; -. DR PDBsum; 5IOK; -. DR PDBsum; 5SVA; -. DR PDBsum; 6LQZ; -. DR PDBsum; 6MIN; -. DR PDBsum; 6MIO; -. DR PDBsum; 6MIP; -. DR PDBsum; 6MIQ; -. DR PDBsum; 7F4A; -. DR PDBsum; 7UHE; -. DR PDBsum; 8U77; -. DR PDBsum; 9UUO; -. DR PDBsum; 9UUS; -. DR PDBsum; 9VKW; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Isopeptide bond; Nucleus; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..244 FT /note="Transcription initiation factor TFIID subunit 14" FT /id="PRO_0000211241" FT DOMAIN 1..134 FT /note="YEATS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376" FT REGION 59..61 FT /note="Acylated histone binding" FT /evidence="ECO:0000269|PubMed:26341557, FT ECO:0007744|PDB:5D7E" FT REGION 81..83 FT /note="Acylated histone binding" FT /evidence="ECO:0000269|PubMed:26341557, FT ECO:0007744|PDB:5D7E" FT REGION 133..169 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 143..157 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 104 FT /note="Acylated histone binding" FT /evidence="ECO:0000269|PubMed:26341557, FT ECO:0007744|PDB:5D7E" FT CROSSLNK 181 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 24 FT /note="V->A: Does not affect binding to acylated histone FT H3." FT /evidence="ECO:0000269|PubMed:27089029" FT MUTAGEN 80 FT /note="G->A: Abolished binding to acylated histone H3." FT /evidence="ECO:0000269|PubMed:27089029" FT MUTAGEN 81 FT /note="W->A: Abolished binding to acetylated histone H3." FT /evidence="ECO:0000269|PubMed:26341557" FT MUTAGEN 82 FT /note="G->A: Does not affect ability to bind crotonylated FT lysines, while abolishing binding to acetylated lysines." FT /evidence="ECO:0000269|PubMed:30385749" FT CONFLICT 116 FT /note="H -> Q (in Ref. 5; CAA49192)" FT /evidence="ECO:0000305" FT STRAND 3..17 FT /evidence="ECO:0007829|PDB:3QRL" FT STRAND 30..39 FT /evidence="ECO:0007829|PDB:3QRL" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:2L7E" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:5D7E" FT STRAND 51..57 FT /evidence="ECO:0007829|PDB:3QRL" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:3QRL" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:3QRL" FT STRAND 76..82 FT /evidence="ECO:0007829|PDB:3QRL" FT STRAND 86..92 FT /evidence="ECO:0007829|PDB:3QRL" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:3QRL" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:3QRL" FT STRAND 107..122 FT /evidence="ECO:0007829|PDB:3QRL" FT HELIX 125..131 FT /evidence="ECO:0007829|PDB:3QRL" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:3QRL" FT HELIX 179..188 FT /evidence="ECO:0007829|PDB:7UHE" FT HELIX 191..203 FT /evidence="ECO:0007829|PDB:7UHE" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:8U77" FT STRAND 211..214 FT /evidence="ECO:0007829|PDB:7UHE" FT TURN 215..218 FT /evidence="ECO:0007829|PDB:7UHE" FT STRAND 219..223 FT /evidence="ECO:0007829|PDB:7UHE" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:7UHE" FT HELIX 229..242 FT /evidence="ECO:0007829|PDB:7UHE" SQ SEQUENCE 244 AA; 27440 MW; 60EA5EC2474B1B9C CRC64; MVATVKRTIR IKTQQHILPE VPPVENFPVR QWSIEIVLLD DEGKEIPATI FDKVIYHLHP TFANPNRTFT DPPFRIEEQG WGGFPLDISV FLLEKAGERK IPHDLNFLQE SYEVEHVIQI PLNKPLLTEE LAKSGSTEET TANTGTIGKR RTTTNTTAEP KAKRAKTGSA STVKGSVDLE KLAFGLTKLN EDDLVGVVQM VTDNKTPEMN VTNNVEEGEF IIDLYSLPEG LLKSLWDYVK KNTE //