TAF14_YEAST
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 03-AUG-2022, entry version 190.
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;
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;
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 X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-137.
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 [20]
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 [21] {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:9618449, PubMed:30385749).
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
CC histone acetyltransferase NuA3 complex, that acetylates Lys-14 of
CC histone H3. Recruitment of NuA3 to nucleosomes requires methylated
CC histone H3 (PubMed:17157260). In conjunction with the FACT complex,
CC NuA3 may be involved in transcriptional regulation (PubMed:17157260).
CC Does not bind DNA (PubMed:30385749). {ECO:0000269|PubMed:10788514,
CC ECO:0000269|PubMed:12138208, ECO:0000269|PubMed:12516863,
CC ECO:0000269|PubMed:12672490, ECO:0000269|PubMed:17157260,
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 complex, composed of
CC at least NTO1, SAS3, TAF14, YNG1 and EAF6.
CC {ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:12887900,
CC ECO:0000269|PubMed:17157260}.
CC -!- INTERACTION:
CC P35189; P34218: SAS3; NbExp=3; IntAct=EBI-18920, EBI-16484;
CC P35189; P18480: SNF5; NbExp=2; IntAct=EBI-18920, EBI-17546;
CC P35189; P18888: SNF6; NbExp=4; 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}.
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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 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 AlphaFoldDB; P35189; -.
DR BMRB; P35189; -.
DR SMR; P35189; -.
DR BioGRID; 36052; 306.
DR ComplexPortal; CPX-1149; 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 IntAct; P35189; 53.
DR MINT; P35189; -.
DR STRING; 4932.YPL129W; -.
DR iPTMnet; P35189; -.
DR MaxQB; P35189; -.
DR PaxDb; P35189; -.
DR PRIDE; P35189; -.
DR DNASU; 855974; -.
DR EnsemblFungi; YPL129W_mRNA; YPL129W; YPL129W.
DR GeneID; 855974; -.
DR KEGG; sce:YPL129W; -.
DR SGD; S000006050; TAF14.
DR VEuPathDB; FungiDB:YPL129W; -.
DR eggNOG; KOG3149; Eukaryota.
DR GeneTree; ENSGT00940000176465; -.
DR HOGENOM; CLU_078004_0_0_1; -.
DR InParanoid; P35189; -.
DR OMA; GEFDMTI; -.
DR BioCyc; YEAST:G3O-34028-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR EvolutionaryTrace; P35189; -.
DR PRO; PR:P35189; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P35189; protein.
DR GO; GO:0000785; C:chromatin; IC: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:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:SGD.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
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: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:SGD.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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 from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 2.60.40.1970; -; 1.
DR IDEAL; IID50207; -.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR016665; Sas5/TAF14.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; PTHR23195; 1.
DR PANTHER; PTHR23195:SF2; PTHR23195:SF2; 1.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF03366; YEATS; 1.
DR PIRSF; PIRSF016551; SAS5/TFIID_14; 1.
DR PROSITE; PS51037; YEATS; 1.
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 133..162
FT /note="Polar residues"
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..186
FT /evidence="ECO:0007829|PDB:6LQZ"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6LQZ"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:6LQZ"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6LQZ"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:6LQZ"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:6LQZ"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6LQZ"
FT HELIX 229..243
FT /evidence="ECO:0007829|PDB:6LQZ"
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
